The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.
Belongs to the SRP receptor beta subunit family.
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex.
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
Component of an histone acetyltransferase complex.
Component of an histone acetyltransferase complex. Interacts with H3K4me3 and to a lesser extent with H3K4me2.
The PHD-type zinc finger mediates the binding to H3K4me3.
Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs.
Component of the endosomal sorting complex required for transport II (ESCRT-II).
Belongs to the major facilitator superfamily.
Does not affect the xanthocillin production.
Expressed in copper depleted conditions via the regulation of the macA transcription factor.
Major facilitator copper-regulated transporter; part of the crm gene cluster that mediates the biosynthesis of a yet unidentified copper-responsive metabolite.
Belongs to the glycosyl hydrolase 75 family.
Chitosanase catalyzing the endo-type cleavage of chitosan, the deacylated form of chitin. Chitosanase may be crucial in the degradation of the deacetylated portion of chitin in the fungal cell wall.
Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family.
Belongs to the group II decarboxylase family.
Belongs to the UPL family. K-HECT subfamily.
ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA.
Associates in the nucleolus with the 60S and pre-60S ribosomal subunits.
Belongs to the DEAD box helicase family. DDX18/HAS1 subfamily.
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER).
Although strongly related to the peptide:N-glycanase enzyme, it lacks the conserved active site Cys in position 261, which is replaced by a Val residue suggesting that it has no activity.
Belongs to the transglutaminase-like superfamily. PNGase family.
Belongs to the metallo-dependent hydrolases superfamily.
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
Belongs to the zinc-containing alcohol dehydrogenase family.
Xylitol dehydrogenase which catalyzes the conversion of xylitol to D-xylulose. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters pentose phosphate pathway.
Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair (By similarity).
Component of the NuA4 histone acetyltransferase complex.
As a target of azole drugs, plays a crucial role in azole susceptibility.
Expression is decreased upon exposure to voriconazole (PubMed:16622700). Expression is regulated by the GATA transcription factor sreA during hypoxia (PubMed:18721228, PubMed:22144905, PubMed:22006005).
In Aspergillus, the biosynthesis pathway of the sterol precursors leading to the prevalent sterol ergosterol differs from yeast. The ring system of lanosterol in S.cerevisiae is firstly demethylised in three enzymatic steps leading to the intermediate zymosterol and secondly a methyl group is added to zymosterol by the sterol 24-C-methyltransferase to form fecosterol. In Aspergillus, lanosterol is firstly transmethylated by the sterol 24-C-methyltransferase leading to the intermediate eburicol and secondly demethylated in three steps to form fecosterol.
Leads to the accumulation of eburicol (PubMed:18191972). Leads to decreased susceptibility to azoles, especially fluconazole and ketoconazole, as well as to itraconazole in an itraconazole-resistant strain.
Mutations of Gly-54 or Met-220 lead to the resistance to azoles, clinical drugs used to inhibit the activity and kill Aspergillus fumigatus cells during infections (PubMed:12543662, PubMed:12604551, PubMed:12709346, PubMed:15215142, PubMed:15563516, PubMed:15634974, PubMed:15695702). Duplication in tandem of a 34 bp sequence in the cyp51A promoter located at positions -288 and -322 from the start codon leads also to azole resistance, when associated with a mutation of Leu-98 (PubMed:17371828, PubMed:21907818).
Sterol 14alpha-demethylase, encoded by cyp51A and cyp51B, that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (PubMed:15215142, PubMed:9184358, PubMed:18191972, PubMed:26459890, PubMed:29439966). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity). In filamentous fungi, during the initial step of this module, lanosterol (lanosta-8,24-dien-3beta-ol) can be metabolized to eburicol (PubMed:18191972, PubMed:26459890, PubMed:29439966). Sterol 14alpha-demethylase catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of both these sterols in the form of formate, and converts eburicol and lanosterol to 14-demethyleburicol (4,4,24-trimethylergosta-8,14,24(28)-trienol) and 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, respectively, which are further metabolized by other enzymes in the pathway to ergosterol (PubMed:18191972, PubMed:26459890, PubMed:29439966). Can also use substrates not intrinsic to fungi, such as 24,25-dihydrolanosterol (DHL), producing 4,4'-dimethyl-8,14-cholestadien-3-beta-ol, but at lower rates than the endogenous substrates (By similarity).
The sterol 14-alpha demethylase activity is inhibited by azole compounds (PubMed:15142553, PubMed:15855543, PubMed:9184358, PubMed:26459890). Activity is inhibited by the novel and long-acting fungicidal azole, PC1244 (PubMed:29439966).
Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SETD6 subfamily.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates 60S ribosomal protein L42.
Belongs to the DASH complex DAD1 family.
Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.
Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate.
Belongs to the Mediator complex subunit 27 family.
Belongs to the putative lipase ROG1 family.
Belongs to the type-B carboxylesterase/lipase family.
Belongs to the glycosyl hydrolase 7 (cellulase C) family.
The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways.
Belongs to the neutral sphingomyelinase family.
Belongs to the glycosyl hydrolase 37 family.
Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family.
Belongs to the NADPH-dependent diflavin oxidoreductase NDOR1 family.
In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
In the N-terminal section; belongs to the flavodoxin family.
Interacts with dre2; as part of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery.
NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of dre2, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins. Positively controls H(2)O(2)-induced cell death.
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair.
Belongs to the XPG/RAD2 endonuclease family. EXO1 subfamily.
Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Belongs to the glycosyl hydrolase 61 family.
Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates.
Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.
Belongs to the ThrE exporter (TC 2.A.79) family.
Belongs to the universal ribosomal protein uS11 family.
Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites.
Belongs to the spermidine/spermine synthase family.
Belongs to the polyadenylate-binding protein type-1 family.
Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation. In the nucleus, involved in both mRNA cleavage and polyadenylation. Is also required for efficient mRNA export to the cytoplasm. Acts in concert with a poly(A)-specific nuclease (PAN) to affect poly(A) tail shortening, which may occur concomitantly with either nucleocytoplasmic mRNA transport or translational initiation. In the cytoplasm, stimulates translation initiation and regulates mRNA decay through translation termination-coupled poly(A) shortening, probably mediated by PAN (By similarity).
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. TRM7 subfamily.
Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs.
Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Belongs to the glycosyl hydrolase 12 (cellulase H) family.
Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues. Specific for xyloglucan and does not hydrolyze other cell wall components (By similarity).
Belongs to the helicase family. Dicer subfamily.
Dicer-like endonuclease involved in cleaving double-stranded RNA in the RNA interference (RNAi) pathway. Produces 21 to 25 bp dsRNAs (siRNAs) which target the selective destruction of homologous RNAs leading to sequence-specific suppression of gene expression, called post-transcriptional gene silencing (PTGS). Part of a broad host defense response against viral infection and transposons (By similarity).
Belongs to the glycosyltransferase 15 family.
Belongs to the deoxyhypusine synthase family.
Belongs to the aldehyde dehydrogenase family.
The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel.
Regulates the cell cycle in a nutrient dependent manner.
Component of the PEX2-PEX10-PEX12 retrotranslocation channel, composed of PEX2, PEX10 and PEX12.
Belongs to the flavin-dependent halogenase family.
Belongs to the IPP isomerase type 1 family.
Isopentenyl-diphosphate delta-isomerase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). Idi1 catalyzes the 1,3-allylic rearrangement of isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP) (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase erg12 (AFUA_4G07780) first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase erg8 (AFUA_5G10680). The diphosphomevalonate decarboxylase mvd1 (AFUA_4G07130) then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase idi1 (AFUA_6G11160) then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase erg20 (AFUA_5G02450) catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (PubMed:16110826, PubMed:22106303) (Probable).
Component of several multiprotein Golgi SNARE complexes.
Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor.
Belongs to the class-I aminoacyl-tRNA synthetase family.
Belongs to the copper/topaquinone oxidase family.
Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Belongs to the UbiA prenyltransferase family.
Polyprenyl transferase; part of the gene cluster that mediates the biosynthesis of pyripyropene A, a specific human acyl-coenzyme A:cholesterol acyltransferase 2 inhibitor (PubMed:20861902). The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase pyr1 (PubMed:20861902). Nicotinyl-CoA is then a substrate of polyketide synthase pyr2 to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase pyr6 to yield farnesyl-HPPO (PubMed:20861902). The next steps consist of an epoxidation of farnesyl-HPPO to epoxyfarnesyl-HPPO by FAD-dependent monooxygenase pyr5 and a cyclization of the terpenoid portion by the terpene cyclase pyr4 to yield deacetyl-pyripyropene E (PubMed:20861902). The 2 cytochrome P450 monooxygenases pyr3 and pyr9, and the 2 acetyltransferases pyr7 and pyr8 are involved in the conversion of deacetyl-pyripyropene E into pyripyropene A through several cycles of oxidation and acetylation steps (PubMed:20861902). Pyr7 acetylates deacetyl-pyripyropene E to pyripyropene E which is oxidized to 11-deacetyl-pyripyropene O by pyr3, which is in turn acetylated into pyripyropene O by pyr8 (PubMed:21224862, PubMed:26019565). Pyripyropene O is then oxidized to deacetyl-pyripyropene A by pyr9 (PubMed:21224862). Deacetyl-pyripyropene A is finally acetylated to pyripyropene A by pyr8 (PubMed:26019565).
Pyripyropene A and its derivatives have very unique characteristics of selectively inhibiting the acyl-coenzyme A:cholesterol acyltransferase 2 (ACAT2) isozyme (PubMed:18997389). Therefore, pyripyropenes are expected to be developed as a new type of anti-atherosclerotic agent (PubMed:18997389). Furthermore, pyripyropenes have been shown to exhibit anti-angiogenic activity against human umbilical vein endothelial cells (PubMed:19571395). Finally, pyripyropene A also exhibits insecticidal properties (PubMed:8534106).
Belongs to the PIGG/PIGN/PIGO family. PIGN subfamily.
Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor (By similarity).
Belongs to the 40S cdc5-associated complex (or cwf complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome.
Involved in mRNA splicing where it associates with cdc5 and the other cwf proteins as part of the spliceosome.
Belongs to the pyrroline-5-carboxylate reductase family.
Belongs to the 2-oxoacid dehydrogenase family.
Belongs to the lysine N-acyltransferase mbtK family.
Expression is induced during iron starvation (PubMed:17845073).
Hydroxyornithine transacylase; part of the siderophore biosynthetic pathway (PubMed:17845073, PubMed:23617799). Aspergillus fumigatus produces 4 types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake and intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial iron distribution and storage. TAFC consists of 3 N(2)-acetyl-N(5)-anhydromevalonyl-N(5)-hydroxyornithine residues cyclically linked by ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-(N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of all four siderophores depends on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA (PubMed:15504822, PubMed:16113265). Subsequently, the pathways for biosynthesis of extra- and intracellular siderophores split (PubMed:17845073). For biosynthesis of extracellular siderophores, the transacylase sidF transfers anhydromevalonyl to N(5)-hydroxyornithine (PubMed:17845073). The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by sidI and sidH respectively (PubMed:22106303). The acetylation of N(5)-hydroxyornithine for FC biosynthesis involves the constitutively expressed sidL (PubMed:21622789). FC is hydroxylated to HFC by an as yet uncharacterized enzyme during conidiation (PubMed:17845073). Assembly of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal peptide synthetases (NRPS), sidD and sidC respectively (PubMed:17845073). Subsequently, sidG catalyzes N2-acetylation of FsC for forming TAFC (PubMed:17845073). Both extra- and intracellular siderophores are crucial for growth during iron limitation and virulence (PubMed:16113265).
Prevents synthesis of TAFC and FsC without affecting FC production (PubMed:17845073).
Belongs to the eIF-2B alpha/beta/delta subunits family.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.
Mitogen-activated protein kinase kinase; part of the cell wall integrity (CWI) signaling pathway composed of pkcA, the bck1-mkk2-mpka MAPK cascade and the downstream rlmA transcription regulator (PubMed:19715768). The CWI signaling pathway regulates cell wall integrity and pyomelanin formation (PubMed:19715768). CWI controls also oxidative stress response, gliotoxin production, iron adaptation and asexual development (PubMed:21883519, PubMed:32005734). Finally, CWI is constitutively required for A.fumigatus to cope with the temperature increase found in the mammalian lung environment, during infection (PubMed:33010083). Mkk2 directly activates mpkA during vegetative growth and under cell wall stress conditions (PubMed:19715768).
Results in severe sensitivity against cell wall-disturbing compounds congo red or calcofluor white, and drastic alterations of the fungal morphology (PubMed:19715768). Impairs phosphorylation of mpkA (PubMed:19715768).
Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.
Belongs to the universal ribosomal protein uL24 family.
Belongs to the glycosyl hydrolase 33 family.
Expression is increased during conidial swelling and germination in presence of human serum.
Sialidase is able to release sialic acid from a wide variety of natural substrates including bovine salivary mucin, colominic acid, bovine fetuin, a serum glycoprotein containing both alpha-2-6 and alpha-2-3-linkages in a ratio of about 3:2, and glycoproteins and glycolipids from thermally denatured human lung epithelial cells. Does not show any trans-sialidase activity since it is able to remove terminal sialic acid residues but is unable to catalyze their transfer to the acceptor substrate. 2-keto-3-deoxynononic acid (KDN) is the preferred substrate and A.fumigatus can utilize KDN as a sole carbon source.
Belongs to the polysaccharide lyase 1 family.
Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity).
Belongs to the ATPase alpha/beta chains family.
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Both IUM domains are necessary for efficient binding to ubiquitin.
Component of the ESCRT-0 complex composed of HSE1 and VPS27.
Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane.
The FYVE domain is involved in the binding to phosphatidylinositol 3-phosphate (PtdIns(3)P) which is required for the association to endosomal membranes.
Vacuolar effluxer which mediate the efflux of amino acids resulting from autophagic degradation. The release of autophagic amino acids allows the maintenance of protein synthesis and viability during nitrogen starvation.
Belongs to the fungal hydrophobin family.
Belongs to the universal ribosomal protein uS15 family.
ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair.
Belongs to the SNF2/RAD54 helicase family.
Component of the INO80 chromatin-remodeling complex.
The DBINO region is involved in binding to DNA.
Belongs to the isocitrate and isopropylmalate dehydrogenases family.
Octamer of two non-identical subunits IDH1 and IDH2.
Lacks conserved residue(s) required for the propagation of feature annotation.
Belongs to the DPH1/DPH2 family. DPH2 subfamily.
Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the dph1 subunit.
Component of the 2-(3-amino-3-carboxypropyl)histidine synthase complex composed of dph1, dph2, dph3 and a NADH-dependent reductase, predominantly cbr1.
Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. Dph1 and dph2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising dph3 and a NADH-dependent reductase, predominantly cbr1 (By similarity). Facilitates the reduction of the catalytic iron-sulfur cluster found in the dph1 subunit (By similarity).
Belongs to the glycosyl hydrolase 43 family.
Belongs to the snRNP Sm proteins family.
Binds specifically to the 3'-terminal U-tract of U6 snRNA.
Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner, facilitating the efficient association of RNA processing factors with their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is thought to be involved in mRNA degradation by activating the decapping step in the 5'-to-3' mRNA decay pathway. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 di-snRNP, spliceosomal U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds directly to the 3'-terminal U-tract of U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. LSM2-LSM8 probably also is involved degradation of nuclear pre-mRNA by targeting them for decapping, and in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA.
Component of the heptameric LSM1-LSM7 complex, which consists of LSM1, LSM2, LSM3, LSM4, LSM5, LSM6 and LSM7. Component of the heptameric LSM2-LSM8 complex, which consists of LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8. The LSm subunits form a seven-membered ring structure with a doughnut shape.
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER).
Belongs to the DEAD box helicase family.
Belongs to the Orn/Lys/Arg decarboxylase class-II family.
Belongs to the acetate uptake transporter (AceTr) (TC 2.A.96) family.
Belongs to the class-II aminoacyl-tRNA synthetase family.
Belongs to the glycosyl hydrolase 32 family.
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates (By similarity).
Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (By similarity). Degrades cutin, a macromolecule that forms the structure of the plant cuticle.
Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. Degrades cutin, a macromolecule that forms the structure of the plant cuticle.
Belongs to the universal ribosomal protein uS12 family.
Belongs to the PPP phosphatase family. PP-6 (PP-V) subfamily.
Leads to decreased mpkA phosphorylation levels, increased sensitivity to cell wall-damaging agents, increased levels of beta-(1,3)-glucan and chitin, impaired in biofilm formation, and decreased protein kinase C activity (PubMed:25911225). Increases also sensitivity to several metals and ions, such as MnCl(2), CaCl(2), and LiCl, but it is more resistant to ZnSO(4) (PubMed:25911225). Impeairs the virulencein a murine model of invasive pulmonary aspergillosis and induces an augmented tumor necrosis factor alpha response in mouse macrophages (PubMed:25911225).
Protein phosphatase that acts as a modulator of pkcA/mpkA activity involved in the cell wall integrity pathway (PubMed:25911225). Plays an important role in regulation of adhesion, cell wall integrity, biofilm formation, and virulence (PubMed:25911225).
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family.
Belongs to the methyltransferase superfamily.
Expression is positively regulated by the fumisoquins biosynthesis specific transcription factor fsqA (PubMed:25582336).
Leads to complete abolishment of isoquinoline alkaloid production and accumulation of a series of benzyl pyrroles, including fumipyrrole.
N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the isoquinoline alkaloids fumisoquin A, fumisoquin B and fumisoquin C; as well as small amounts of fumipyrrole as a shunt metabolite (PubMed:25582336, PubMed:27065235). The products of the cluster lead to a brown coloration and are important for growth and conidiation (PubMed:25582336). The nonribosomal peptide synthetase-like protein fsqF, which lacks a canonical condensation domain, is required for addition of a serine-derived dehydroalanine moiety to activated tyrosine but is not essential for the subsequent steps leading to isoquinoline formation (PubMed:27065235). A different enzyme, most likely the ATP-grasp enzyme fsqD, is responsible for activation of tyrosine (Probable). Three additional enzymes encoded by the fsq cluster, the N-methyltransferase fsqC, the phenol 2-monooxygenase fsqG and the FAD-dependent oxidase fsqB, catalyze the formation of the isoquinoline ring system in the fumisoquins (PubMed:27065235, PubMed:30194285). FsqB converts the fspF thiolation domain-bound (2S,4S,5S)-2-amino-6-(3,4-dihydroxyphenyl)-4-hydroxy-5-(methylamino)hexanoyl into isoquinoline (PubMed:27065235, PubMed:30194285). The cyclization most likely proceeds via a two-step mechanism, beginning with FAD-dependent oxidation of the methyl group to an iminium species followed by electrophilic attack on the deprotonated phenol (Probable).
Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation (By similarity).
The C-terminus is required for mitochondrial localization, while the N-terminus is necessary for mitochondrial fission.
Belongs to the mitochondrion-specific ribosomal protein mS38 family.
May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Belongs to the glycosyl hydrolase 1 family.
Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Involved in nucleotide excision repair.
Component of the 66S pre-ribosomal particle.
Required for efficient assembly and nuclear export of the 60S ribosomal subunit.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family.
Expression is induced by the unfolded protein response (UPR) during ER stress.
Leads to osmotically suppressible basal growth defects and cationic tolerance associated with increased expression of calcineurin pathway genes (PubMed:20097742). Results in hypersensitivity to cell wall inhibitors but does not affect virulence (PubMed:20097742). Leads to severe polarity defect, hypersensitivity to ER stress, and attenuated virulence; when srcA is also deleted (PubMed:32487759).
Magnesium-dependent enzyme that catalyzes the hydrolysis of ATP coupled with the transport of calcium from the cytosol to the Golgi apparatus lumen (By similarity). Involved calcium homeostasis and both conidiation and polarized growth (PubMed:20097742, PubMed:32487759). Its activity is coupled to the unfolded protein response (UPR) and Ca(2+) import into the Golgi apparatus is important for virulence, cell wall biosynthesis, and resistance to antifungal compounds that inhibit Ca2+ signaling (PubMed:20097742).
Belongs to the enoyl-CoA hydratase/isomerase family.
Blocks TAFC biosynthesis, decreases resistance to oxidative stress, and attenuates virulence in a murine model of invasive pulmonary aspergillosis (PubMed:22106303).
Mevalonyl-coenzyme A hydratase; part of the siderophore biosynthetic pathway (PubMed:22106303). Aspergillus fumigatus produces 4 types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake and intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial iron distribution and storage. TAFC consists of 3 N(2)-acetyl-N(5)-anhydromevalonyl-N(5)-hydroxyornithine residues cyclically linked by ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-(N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of all four siderophores depends on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA (PubMed:15504822, PubMed:16113265). Subsequently, the pathways for biosynthesis of extra- and intracellular siderophores split (PubMed:17845073). For biosynthesis of extracellular siderophores, the transacylase sidF transfers anhydromevalonyl to N(5)-hydroxyornithine (PubMed:17845073). The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by sidI and sidH respectively (PubMed:22106303). The acetylation of N(5)-hydroxyornithine for FC biosynthesis involves the constitutively expressed sidL (PubMed:21622789). FC is hydroxylated to HFC by an as yet uncharacterized enzyme during conidiation (PubMed:17845073). Assembly of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal peptide synthetases (NRPS), sidD and sidC respectively (PubMed:17845073). Subsequently, sidG catalyzes N2-acetylation of FsC for forming TAFC (PubMed:17845073). Both extra- and intracellular siderophores are crucial for growth during iron limitation and virulence (PubMed:16113265).
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly. Required for cell wall integrity (By similarity).
Belongs to the protoporphyrinogen/coproporphyrinogen oxidase family. Protoporphyrinogen oxidase subfamily.
Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.
Belongs to the AB hydrolase superfamily. Lipase family.
Belongs to the prenylcysteine oxidase family.
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases L-arabinose from arabinoxylan.
Belongs to the glycosyl hydrolase 62 family.
Belongs to the ATPase gamma chain family.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c.
Belongs to the amino acid/polyamine transporter 2 family.
Belongs to the RNA polymerase beta' chain family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Belongs to the inositol monophosphatase superfamily.
Belongs to the aldolase class II family. MtnB subfamily.
Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Belongs to the NiCoT transporter (TC 2.A.52) family.
Leads to a reduced growth rate and a delayed conidiation.
Transcriptional regulator that forms a complex with somA to control biofilm formation.
Belongs to the universal ribosomal protein uS4 family.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.
Belongs to the glycosyltransferase 20 family.
Simultaneous disruption of tpsB abolishes trehalose biosynthesis during hyphal and conidia formation, and delays germination (PubMed:20439478). Simultaneous disruption of tpsB results in abnormal cell wall formation, sensitivity to caspofungin, calcofluor white, thermal stress and oxidative stress, and hypervirulence in a mouse model of aspergillosis (PubMed:20439478).
Synthase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-alpha-D-glucose in a two step process (PubMed:20439478). The disaccharide trehalose serves as a storage carbohydrate that is mobilized during conidial germination (PubMed:20439478). Regulates the level of trehalose as a protectant for cell integrity during thermal and oxidative stress (PubMed:20439478).
Belongs to the GTP cyclohydrolase I family.
Belongs to the glycosyl hydrolase 5 (cellulase A) family.
Belongs to the ubiquitin-conjugating enzyme family.
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Deletion of both erg4A and erg4B results in fluffy colonies with severely impaired conidiation and increased susceptibility to antifungal azoles itraconazole and voriconazole, but does not affect virulence (PubMed:27986720). The double deletion leads also to the loss of ergosterol production and accumulation of the ergosta-5,7,22,24(28)-tetraenol precursor (PubMed:27986720).
Delta(24(24(1)))-sterol reductase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:27986720). Catalyzes the last step of ergosterol biosynthesis by converting ergosta-5,7,22,24(28)-tetraen-3beta-ol into ergosterol (PubMed:27986720). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (PubMed:16110826, PubMed:18191972) (Probable).
Expression is induced in the absence of erg4A.
Inhibition of erg4A and erg4B might be an effective approach for alleviating A.fumigatus infection.
Belongs to the ABC transporter superfamily. ABCG family. PDR (TC 3.A.1.205) subfamily.
Exhibits enhanced susceptibility to itraconazole, however voriconazole susceptibility is less affected.
Expression is increased in clinical azole-resistant isolates.
Pleiotropic ABC efflux transporter involved in the basal level of azole susceptibility (PubMed:26933209). Confers resistance to fluconazole, itraconazole and voriconazole (PubMed:26933209).
Belongs to the STXBP/unc-18/SEC1 family.
Belongs to the small GTPase superfamily. SAR1 family.
COPII is composed of at least 5 proteins: the sec23/24 complex, the sec13/31 complex and sar1.
Small GTPase component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. Sar1 controls the coat assembly in a stepwise manner. Activated Sar1-GTP binds to membranes first and recruits the sec23/24 complex. These sec23/24-sar1 prebudding intermediates are then collected by the Sec13/31 complex as subunits polymerize to form coated transport vesicles. Conversion to sar1-GDP triggers coat release and recycles COPII subunits (By similarity).
Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Belongs to the proteasome subunit S1 family.
Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.
Belongs to the glycosyl hydrolase 15 family.
Belongs to the glycosyl hydrolase 47 family.
Involved in the maturation of Asn-linked oligosaccharides. Progressively trims alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The glutaminase domain produces the ammonia necessary for the cyclase domain to produce IGP and AICAR from PRFAR. The ammonia is channeled to the active site of the cyclase domain.
In the C-terminal section; belongs to the HisA/HisF family.
Binds 1 thiamine pyrophosphate per subunit.
Belongs to the low molecular weight phosphotyrosine protein phosphatase family.
Belongs to the Mediator complex subunit 18 family.
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.
Component of the srb8-11 complex, a regulatory module of the Mediator complex.
Component of the srb8-11 complex. The srb8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The srb8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The srb8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II (By similarity).
Belongs to the glycosyltransferase 34 family.
Belongs to the class-A beta-lactamase family.
Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes.
Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.
Expression is induced upon voriconazole treatment (PubMed:24123268). Expression is also induced in triazole-resistant isolates (PubMed:32209680).
Leads to decreased azole resistance, including itraconazole, posaconazole and voriconazole.
Pleiotropic ABC efflux transporter that confers resistance to structurally and functionally unrelated compounds including azoles such as itraconazole, posaconazole, and voriconazole.
The efflux inhibitor FK506 impairs the transport activity.
Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family.
Belongs to the glycosyl hydrolase 11 (cellulase G) family.
Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Belongs to the ammonia transporter channel (TC 1.A.11.2) family.
Belongs to the universal ribosomal protein uL11 family.
Belongs to the glycosyltransferase 8 family.
Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides.
Required for the maintenance of the structure of the mitochondrial inner membrane. Involved in mitochondrial morphology. Causes growth arrest when highly overexpressed (By similarity).
ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. Binds 90S pre-ribosomal particles and dissociates from pre-60S ribosomal particles after processing of 27SB pre-rRNA. Required for the normal formation of 18S rRNA through the processing of pre-rRNAs at sites A0, A1 and A2, and the normal formation of 25S and 5.8S rRNAs through the processing of pre-rRNAs at sites C1 and C2.
Belongs to the DEAD box helicase family. DDX55/SPB4 subfamily.
Component of pre-60S ribosomal complexes.
Belongs to the class I-like SAM-binding methyltransferase superfamily. BUD23/WBSCR22 family.
Belongs to the eukaryotic initiation factor 4E family.
Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures.
Belongs to the universal ribosomal protein uL16 family.
Belongs to the DNA mismatch repair MutL/HexB family.
Belongs to the mannitol dehydrogenase family.
Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway. Has a strong preference for NADH over NADPH.
Belongs to the glycosyl hydrolase 10 (cellulase F) family.
Expressed in presence of xylan and repressed by glucose.
Belongs to the proteasome subunit p27 family.
Involved in determination of the onset of polarized growth and morphogenesis. Plays a role in the regulation of branching in hyphae and spore formation (By similarity).
Belongs to the protein kinase superfamily.
Belongs to the Mediator complex subunit 1 family.
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Involved in determination of the onset of polarized growth and morphogenesis. Plays a role in the regulation of branching in hyphae and spore formation.
Component of the fork protection complex (FPC) consisting of tof1 and csm3.
Forms a fork protection complex (FPC) with tof1 and which is required for chromosome segregation during meiosis and DNA damage repair. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors (By similarity).
Belongs to the DNA/RNA non-specific endonuclease family.
Involved in the second step of GPI biosynthesis. De-N-acetylation of N-acetylglucosaminyl-phosphatidylinositol.
Belongs to the glycosyl hydrolase 18 family. Chitinase class V subfamily.
Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Alpha-1,2-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth mannose to trimannosyl-GPIs during GPI precursor assembly. The presence of a fourth mannose in GPI is essential in fungi (By similarity).
Belongs to the glycosyltransferase 22 family. PIGZ subfamily.
Component of the oligosaccharyltransferase (OST) complex.
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Belongs to the aconitase/IPM isomerase family.
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
Catalyzes the hydrolysis of ATP coupled with the transport of calcium.
Abolishes the expression of all cluster genes (PubMed:22046314). Impairs growth on L-tyrosine as the sole carbon source and affects homogentisic acid and pyomelanin formation (PubMed:19028908).
Transcription factor; part of the L-tyrosine degradation gene cluster that mediates the biosynthesis of the brownish pigment pyomelanin as an alternative melanin (PubMed:19028908, PubMed:22046314). Acts as a transcriptional activator for the genes of the tyrosine degradation cluster (PubMed:22046314).
Belongs to the universal ribosomal protein uL22 family.
Belongs to the peptidase M16 family. PreP subfamily.
Degrades mitochondrial transit peptides after their cleavage in the intermembrane space or in the matrix, and presequence peptides; clearance of these peptides is required to keep the presequence processing machinery running (By similarity). Preferentially cleaves the N-terminal side of paired basic amino acid residues (By similarity). Also degrades other unstructured peptides (By similarity). May function as an ATP-dependent peptidase as opposed to a metalloendopeptidase (By similarity).
Monomer and homodimer; homodimerization is induced by binding of the substrate.
Belongs to the major facilitator superfamily. Proton-dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
Activated by tyrosine and threonine phosphorylation.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily.
Dually phosphorylated on Thr-171 and Tyr-173, which activates the enzyme.
Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription of target genes (By similarity).
The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Has both phosphomonoesterase and phosphodiesterase activity. Cleaves a broad range of phosphate esters.
Inhibited by NaF, molybdate and vanadate.
The GPI-like anchor contains a phosphoceramide lipid group. The anchor position has not been determined.
Belongs to the uroporphyrinogen-III synthase family.
Expression is positively regulated by the cluster-specific transcription factor hmgR.
Fumarylacetoacetase; part of the L-tyrosine degradation gene cluster that mediates the biosynthesis of the brownish pigment pyomelanin as an alternative melanin (PubMed:19028908, PubMed:22046314). The 4-hydroxyphenylpyruvate dioxygenase hppD catalyzes the conversion of 4-hydroxyphenylpyruvate to homogentisic acid (HGA) (PubMed:19028908, PubMed:22046314). The protein hmgX is crucial for this conversion and thus, probably functions as an accessory factor to mediate specific activity of hppD (PubMed:22046314). The homogentisate 1,2-dioxygenase hmgA is then involved in the cleavage of the aromatic ring of HGA and its conversion to 4-maleylacetoacetate (PubMed:19028908, PubMed:19715768). When hmgA activity is lowered by the cell wall integrity (CWI) signaling pathway, HGA accumulates and leads to the production of pyomelanin through benzoquinone acetic acid after oxidation and polymerization (PubMed:19715768). On the opposite, in non-stress conditions, both hppD and hmgA activities are balanced and HGA is degraded into 4-maleylacetoacetate (PubMed:19715768). 4-maleylacetoacetate is further converted to 4-fumarylacetoacetate by the maleylacetoacetate isomerase maiA, which is degraded into fumarate and acetoacetate by the fumarylacetoacetase fahA (Probable).
Belongs to the anthranilate synthase component I family.
ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Belongs to the DEAD box helicase family. DDX31/DBP7 subfamily.
Present with 1460 molecules/cell in log phase SD medium.
Belongs to the CWC16 family. YJU2 subfamily.
Component of the spliceosome. Present in the activated B complex, the catalytically activated B* complex which catalyzes the branching, the catalytic step 1 C complex catalyzing the exon ligation, and the postcatalytic P complex containing the ligated exons (mRNA) and the excised lariat intron.
Part of the spliceosome which catalyzes two sequential transesterification reactions, first the excision of the non-coding intron from pre-mRNA and then the ligation of the coding exons to form the mature mRNA. Plays a role in stabilizing the structure of the spliceosome catalytic core and docking of the branch helix into the active site, producing 5'-exon and lariat intron-3'-intermediates.
Belongs to the universal ribosomal protein uL23 family.
Expression is also regulated by rsmA (PubMed:23671611).
Probable aminotransferase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). Gliotoxin contributes to pathogenesis during invasive aspergillosis (PubMed:17601876, PubMed:18199036). In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species (PubMed:17601876).
Belongs to the glycosyl hydrolase 13 family.
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Belongs to the GatB/GatE family. GatB subfamily.
Subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A, B and C subunits.
Belongs to the DNA2/NAM7 helicase family.
Key enzyme involved in DNA replication and DNA repair. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair by mediating the cleavage of 5'-ssDNA.
Belongs to the fungal Na(+)/H(+) exchanger family.
Blocks the ergot alkaloid pathway at festuclavine, and downstream products are eliminated (PubMed:26972831).
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:26972831). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:15870460). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482, PubMed:21409592). EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482). EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482). Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831). Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909).
Ergot alkaloids are known for their toxic effects on humans who consume contaminated grains or livestock that graze on grasses harboring ergot alkaloid-producing fungi (PubMed:19523108). Due to their strong affinity for monoamine neurotransmitter receptors they may also have clinical uses such as treatment of migraines, Parkinson's disease and cerebrovascular insufficiency (PubMed:19523108).
The expression of the ergot alkaloid synthesis cluster which leads to the synthesis of fumigaclavines is positively regulated by the brlA and stuA transcription factors (PubMed:19028996).
Belongs to the universal ribosomal protein uS17 family.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIA subfamily.
The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family.
Belongs to the glycosyltransferase 22 family. PIGB subfamily.
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI during GPI precursor assembly (By similarity).
Belongs to the carbohydrate esterase 1 (CE1) family. AxeA subfamily.
Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family.
Belongs to the histidine acid phosphatase family.
Catalyzes the hydrolysis of inorganic orthophosphate from phytate.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.
Belongs to the glycosyltransferase 32 family.
Belongs to the universal ribosomal protein uS14 family.
Has a role in a nucleosome assembly pathway that is required for the integrity of heterochromatin and proper chromosome segregation.
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
Heterodimer of an alpha and a beta chain.
The alpha and beta chains are autoproteolytically processed from a single precursor protein within the mitochondrion.
This protein may be expected to contain an N-terminal transit peptide but none has been predicted.
GPI-anchored cell wall protein involved in stabilizing the cell wall. Not implicated in virulence, heme uptake, and biofilm formation.
Increases susceptibility towards the chitin/beta-glucan-microfibril destabilizing compounds Congo red and calcofluor white.
The CFEM domain is involved in heme-binding and contains 8 cysteines and is found in proteins from several pathogenic fungi, including both human and plant pathogens (By similarity). The CFEM domain adopts a novel helical-basket fold that consists of six alpha-helices, and is uniquely stabilized by four disulfide bonds formed by its 8 signature cysteines (By similarity).
The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily.
Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan (By similarity).
Belongs to the glycosyl hydrolase 54 family.
Organized into two domains: an N-terminal catalytic domain and a C-terminal arabinose-binding domain (ABD).
Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan.
Required to generate and maintain the structure of the tubular endoplasmic reticulum network and the vacuole. Induces high curvature in membranes and causes membrane tubule formation. Involved in membrane/vesicle trafficking.
The short lumenal loops between transmembrane domains 1 and 2 and between transmembrane domains 3 and 4 may impart a wedge-like configuration, thus deforming membranes.
Component of the ER membrane protein complex (EMC).
Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins.
Belongs to the LDH/MDH superfamily. MDH type 1 family.
Belongs to the oligopeptide OPT transporter family.
Belongs to the TPT transporter family. SLC35D subfamily.
Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen.
Probable component of the endoplasmic reticulum-associated degradation (ERAD) pathway.
Belongs to the trans-sulfuration enzymes family.
Belongs to the oxygen-dependent FAD-linked oxidoreductase family.
FAD binding oxidoreductase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:23435153, PubMed:26972831). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:15870460). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482, PubMed:21409592, PubMed:23435153). EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482). EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482). Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831). Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909).
Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Belongs to the AB hydrolase superfamily.
Demethylates proteins that have been reversibly carboxymethylated. Demethylates the phosphatase PP2A catalytic subunit (By similarity).
Belongs to the tellurite-resistance/dicarboxylate transporter (TDT) family.
Belongs to the glycosyl hydrolase 3 family.
Belongs to the eukaryotic ribosomal protein eL15 family.
Belongs to the Tim17/Tim22/Tim23 family.
Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-dependent steps.
Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events (By similarity).
Involved in pre-mRNA splicing and cell cycle progression.
Belongs to the DHHC palmitoyltransferase family. SWF1 subfamily.
Palmitoyltransferase that targets several endosomal SNAREs. Palmitoylates the SNAREs at cysteine residues close to the cytoplasmic end of their transmembrane domain. May have a role in the cellular quality control of transmembrane domain-containing proteins (By similarity).
The DHHC domain is required for palmitoyltransferase activity.
Acts as component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. The NOT protein subcomplex negatively regulates the basal and activated transcription of many genes. Preferentially affects TC-type TATA element-dependent transcription. Could directly or indirectly inhibit component(s) of the general transcription machinery.
Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.
Involved in nuclear export, actin cytoskeleton organization and vesicular transport.
Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Arp2/3 complex plays a critical role in the control of cell morphogenesis via the modulation of cell polarity development.
Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (By similarity). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs (By similarity). Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1) (By similarity).
Belongs to the FPP/GGPP synthase family.
Belongs to the mitochondrion-specific ribosomal protein mL49 family.
Belongs to the CND3 (condensin subunit 3) family.
Belongs to the folylpolyglutamate synthase family.
DNA-dependent RNA polymerase which catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Belongs to the complex I NDUFB11 subunit family.
Belongs to the proteasome subunit S9 family.
Belongs to the phosphohexose mutase family.
Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, which is a biosynthetic precursor of chitin and also supplies the amino sugars for N-linked oligosaccharides of glycoproteins.
A pair of annexin repeats may form one binding site for calcium and phospholipid.
Belongs to the glycosyl hydrolase 2 family. Beta-mannosidase A subfamily.
Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of beta-mannosidic oligosaccharides of various complexity and length. Involved in the degradation of polymeric mannan and galactomannan (By similarity).
Belongs to the eukaryotic ribosomal protein eL27 family.
Adds the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(1)Man(9)GlcNAc(2)-PP-Dol.
Belongs to the ALG6/ALG8 glucosyltransferase family.
Belongs to the universal ribosomal protein uS7 family.
Belongs to the DASH complex SPC19 family.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.
TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity.
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.
Protein kinase C; part of cell wall integrity (CWI) signaling pathway composed of pkcA, the bck1-mkk2-mpka MAPK cascade and the downstream rlmA transcription regulator (PubMed:26295576, PubMed:27473315). The CWI signaling pathway regulates cell wall integrity and pyomelanin formation (PubMed:26295576). CWI controls also oxidative stress response, gliotoxin production, iron adaptation and asexual development (PubMed:26295576, PubMed:32005734). Finally, CWI is constitutively required for A.fumigatus to cope with the temperature increase found in the mammalian lung environment, during infection (PubMed:33010083). Modulates the expression of fumiquinazoline cluster during conidiogenesis (PubMed:33705521).
Required for nuclear membrane fusion during karyogamy.
Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
Belongs to the peptidase S26 family. IMP2 subfamily.
Belongs to the aldo/keto reductase family.
Catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters pentose phosphate pathway (By similarity).
Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.
Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation.
Component of the heptameric LSM1-LSM7 complex that forms a seven-membered ring structure with a donut shape.
Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. May be involved in protection from the host during host infection.
Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.
Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme.
Belongs to the complex I 20 kDa subunit family.
Increases radial growth, remediates the germination defect of a laeA deletion, and increases virulence in the G. mellonella model of invasive aspergillosis.
Transcription factor that mediates stress and developmental response.
Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Acts as a membrane receptor for soluble get3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol.
RNA-binding nucleolar protein required for pre-rRNA processing. Involved in production of 18S rRNA and assembly of small ribosomal subunit.
Probable adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
Catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters pentose phosphate pathway.
Belongs to the glucosamine/galactosamine-6-phosphate isomerase family.
Involved in DNA double-strand break repair (DSBR). Possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity. Also involved in meiotic DSB processing.
Belongs to the methyltransferase superfamily. Arsenite methyltransferase family.
Belongs to the pseudouridine synthase TruB family.
May associate with the eukaryotic translation initiation factor 3 (eIF-3) complex.
mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.
Belongs to the diphosphomevalonate decarboxylase family.
Diphosphomevalonate decarboxylase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). Mvd1 converts diphosphomevalonate into isopentenyl diphosphate (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase erg12 (AFUA_4G07780) first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase erg8 (AFUA_5G10680). The diphosphomevalonate decarboxylase mvd1 (AFUA_4G07130) then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase idi1 (AFUA_6G11160) then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase erg20 (AFUA_5G02450) catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (PubMed:16110826, PubMed:22106303) (Probable).
Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type I sub-subfamily.
Binds 1 pyruvoyl group covalently per subunit.
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine.
Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.
Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Belongs to the V-ATPase E subunit family.
Rnase which modulates cell survival under stress conditions. Released from the vacuole to the cytoplasm during stress to promote tRNA and rRNA cleavage and to activate separately a downstream pathway that promotes cell death. Involved in cell size, vacuolar morphology and growth at high temperatures and high salt concentration (By similarity).
Belongs to the asaB hydroxylase/desaturase family.
Belongs to the mitochondrial carrier (TC 2.A.29) family.
Catalyzes the exchange of ADP and ATP across the membrane.
Multidomain protein; including a starter unit:ACP transacylase (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a product template (PT) domain that controls the immediate cyclization regioselectivity of the reactive polyketide backbone; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm (By similarity).
Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of neosartoricin, a prenylated anthracenone that exhibits T-cell antiproliferative activity, suggestive of a physiological role as an immunosuppressive agent (PubMed:23758576, PubMed:23368997). The non-reducing polyketide synthase nscA probably synthesizes and cyclizes the decaketide backbone (PubMed:23368997). The hydrolase nscB then mediates the product release through hydrolysis followed by spontaneous decarboxylation (PubMed:23368997). The prenyltransferase nscD catalyzes the addition of the dimethylallyl group to the aromatic C5 (PubMed:23368997). The FAD-dependent monooxygenase nscC is then responsible for the stereospecific hydroxylation at C2 (PubMed:23368997). There is no gene encoding O-acetyltransferase in the nsc gene cluster; thus, the last step of 2-O-acetylation leading to neosartoricin may be catalyzed by an unidentified O-acetyltransferase (PubMed:23368997).
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
The active site is a redox-active disulfide bond.
Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter.
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
Belongs to the dynactin 150 kDa subunit family.
Belongs to the glycosyl hydrolase 18 family. Chitinase class III subfamily.
GPI-anchored chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Required to reshape the cell wall at the sites where cell wall remodeling and/or cell wall maturation actively take place such as sites of conidia formation.
Belongs to the glycosyl hydrolase 35 family.
Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Forms a redox cycle with ERV1 that involves a disulfide relay system. Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria. The oxidized form of MIA40 forms a transient intermolecular disulfide bridge with the reduced precursor protein, resulting in oxidation of the precursor protein that now contains an intramolecular disulfide bond and is able to undergo folding in the IMS (By similarity).
The CHCH domain contains a conserved twin Cys-X(9)-Cys motif which is required for import and stability of MIA40 in mitochondria.
In the 2nd section; belongs to the type-I 3-dehydroquinase family.
In the N-terminal section; belongs to the shikimate kinase family.
Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Belongs to the beta-class carbonic anhydrase family.
Belongs to the eukaryotic ribosomal protein eS28 family.
Belongs to the pyridoxine kinase family.
Completely abolishes the production of fumagillin but leads to the accumulation of the intermediate prefumagillin (PubMed:24082142, PubMed:24568283).
Expression is controlled by the fumagillin biosynthesis cluster regulator fumR (PubMed:24082142). Expression is also under the control of the developmental and secondary metabolism regulator veA (PubMed:24116213).
Fumagillin and its derivatives have been intensely studied for their potential use in the treatment of amebiasis, microsporidiosis and rheumatoid arthritis (PubMed:14913169, PubMed:12075057, PubMed:18209961). They have also interesting antiangiogenic properties by the irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) (PubMed:9177176).
Monooxygenase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) (PubMed:23488861, PubMed:24568283). Within the pathway, the monooxygenase af470 catalyzes the oxidative cleavage of prefumagillin to yield the final compound of the pathway, fumagillin (PubMed:24568283). The pathway begins with the conversion of farnesyl pyrophosphate (FPP) to beta-trans-bergamotene by the membrane-bound beta-trans-bergamotene synthase af520. The multifunctional cytochrome P450 monooxygenase af510 then converts beta-trans-bergamotene into 5-keto-demethoxyfumagillol via several oxydation steps. 5-keto-demethoxyfumagillol is then subjected to successive C-6 hydroxylation and O-methylation by the dioxygenase af480 and O-methyltransferase af390-400, respectively, to yield 5-keto-fumagillol, which is then stereoselectively reduced by the keto-reductase af490 to 5R-hydroxy-seco-sesquiterpene. The next step is the polyketide transferase af380-catalyzed transfer of a dodecapentaenoyl group synthesized by the polyketide synthase af370 onto 5R-hydroxy-seco-sesquiterpene which leads to the production of prefumagillin. Finally, oxidative cleavage by the monooxygenase af470 converts prefumagillin to fumagillin (PubMed:24568283) (Probable).
Belongs to the universal ribosomal protein uL29 family.
Component of the mitochondrial large ribosomal subunit. Mature mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S subunit contains at least 33 different proteins and 1 molecule of RNA (15S). The 54S subunit contains at least 45 different proteins and 1 molecule of RNA (21S) (By similarity).
Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
Belongs to the fungal fatty acid synthetase subunit beta family.
[Alpha(6)beta(6)] hexamers of two multifunctional subunits (alpha and beta).
Belongs to the universal ribosomal protein uS2 family.
Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (25S, 5.8S and 5S). Interacts with rps21.
Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits.
Belongs to the carbon-nitrogen hydrolase superfamily. Nitrilase family.
Belongs to the V-ATPase G subunit family.
Glutathione S-transferase-like protein; part of the gene cluster that mediates the biosynthesis of trypacidin, a mycotoxin with antiprotozoal activity and that plays a role in the infection process (PubMed:26278536, PubMed:26242966). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) tpcC (PubMed:26242966). The atrochrysone carboxyl ACP thioesterase tpcB then breaks the thioester bond and releases the atrochrysone carboxylic acid from tpcC (PubMed:26242966). The decarboxylase tpcK converts atrochrysone carboxylic acid to atrochrysone which is further reduced into emodin anthrone (PubMed:26242966). The next step is performed by the emodin anthrone oxygenase tpcL that catalyzes the oxidation of emodinanthrone to emodin (PubMed:26242966). Emodin O-methyltransferase encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin to form questin (PubMed:26242966). Ring cleavage of questin by questin oxidase tpcI leads to desmethylsulochrin via several intermediates including questin epoxide (By similarity). Another methylation step catalyzed by tpcM leads to the formation of sulochrin which is further converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes the conversion of monomethylsulfochrin to trypacidin (PubMed:26242966). Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)), thus triggering host necrotic cell death (PubMed:22319557). The trypacidin pathway is also able to produce endocrocin via a distinct route from the endocrocin Enc pathway (PubMed:26242966).
Specifically expressed in conidia (PubMed:22319557).
ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA (By similarity).
Belongs to the DEAD box helicase family. DDX48/FAL1 subfamily.
Component of the RIX1 complex required for processing of ITS2 sequences from 35S pre-rRNA.
Component of the RIX1 complex, composed of ipi1, rix1/ipi2 and ipi3 in a 1:2:2 stoichiometry. The complex interacts (via rix1) with mdn1 (via its hexameric AAA ATPase ring) and the pre-60S ribosome particles.
Belongs to the DASH complex SPC34 family.
Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of endocrocin, a simple anthraquinone interesting for many biotechnological applications (PubMed:22492455, PubMed:23592999). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) encA (PubMed:22492455). The atrochrysone carboxyl ACP thioesterase encB then breaks the thioester bond and releases the atrochrysone carboxylic acid from encA (PubMed:22492455). The atrochrysone carboxylic acid is then converted to endocrocin anthrone which is further oxidized into endocrocin by the anthrone oxygenase encC (PubMed:22492455). The exact function of encD has not been identified yet, but it negatively regulates endocrocin production, likely through the modification of endocrocin itself (PubMed:22492455).
Belongs to the anthrone oxygenase family.
Endocrocin and related anthraquinones compounds have interesting activities for medicinal uses, including anti-inflammatory activity (PubMed:20379952).
Endocrocin is specifically produced in conidia.
Expression is positively regulated by the transcription factors brlA and laeA (PubMed:26242966).
Leads to unstable anthrone production and abolishes the production of endocrocin (PubMed:22492455).
Belongs to the transferase hexapeptide repeat family.
Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint.
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for l- to d- amino acid conversion) are present within the NRP synthetase. NRPS6 has the following architecture: A-T-C.
Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence.
Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family.
Dipeptidase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). Gliotoxin contributes to pathogenesis during invasive aspergillosis (PubMed:17601876, PubMed:18199036). In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species (PubMed:17601876).
Belongs to the adenylate kinase family. AK3 subfamily.
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon GTP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent GTP hydrolysis.
Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities.
Belongs to the AAA ATPase family. BCS1 subfamily.
Belongs to the Mrp/NBP35 ATP-binding proteins family.
Belongs to the phosphoglycerate kinase family.
Belongs to the DASH complex ASK1 family.
Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
Component of complex II composed of four subunits: a flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a large and a small subunit.
Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Expression is induced by the cAMP-dependent protein kinase A signaling pathway (PubMed:25582336).
Leads to reduced growth and sporulation, but does not affect virulence in infected mice (PubMed:25582336). Impairs the production of isoquinolines (PubMed:27065235).
Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of the isoquinoline alkaloids fumisoquin A, fumisoquin B and fumisoquin C; as well as small amounts of fumipyrrole as a shunt metabolite (PubMed:25582336, PubMed:27065235). The products of the cluster lead to a brown coloration and are important for growth and conidiation (PubMed:25582336).
Belongs to the acetyltransferase family. GNAT subfamily.
Belongs to the reverse transcriptase family. Telomerase subfamily.
Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Belongs to the DNA polymerase type-B family.
Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)) (By similarity).
The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.
Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family.
High-conductance magnesium-selective channel that mediates the influx of magnesium into the mitochondrial matrix. Essential for the splicing of mRNA group II introns in mitochondria by affecting mitochondrial magnesium concentrations, which are critical for group II intron splicing. It also suppresses a variety of mitochondrial intron mutations and its absence may disturb the assembly of mitochondrial membrane complexes.
Homopentamer. Forms homooligomers. Interacts with MFM1.
Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A subfamily.
Belongs to the sterol desaturase family. SCS7 subfamily.
Belongs to the inositol phosphokinase (IPK) family.
Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Belongs to the eukaryotic release factor 1 family.
Belongs to the Mediator complex subunit 8 family.
In the C-terminal section; belongs to the DHPS family.
Pleiotropic ABC efflux transporter that shows a strong substrate specificity for the azole class of drugs such as lotrimazole (CLT), fluconazole (FLC), itraconazole (ITC), ketoconazole (KTC), posaconazole (POS), econazole (ECON), metconazole (MET), miconazole (MCZ), prochloraz (PCLZ), and tebuconazole (TEBZ).
Belongs to the PheA/TfdB FAD monooxygenase family.
Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Belongs to the cytidine and deoxycytidylate deaminase family.
Belongs to the prokaryotic/mitochondrial release factor family.
Belongs to the NUP186/NUP192/NUP205 family.
Belongs to the V-ATPase 116 kDa subunit family.
Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Belongs to the transcriptional coactivator PC4 family.
Belongs to the GTP cyclohydrolase II family.
Belongs to the iron/ascorbate-dependent oxidoreductase family.
Chanoclavine-I dehydrogenase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:26972831). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:15870460). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482, PubMed:21409592). EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482). EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482). Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831). Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909).
Belongs to the peroxiredoxin family. Prx5 subfamily.
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Belongs to the eukaryotic ribosomal protein eL42 family.
Heterodimers with gpn1 or gpn2. Binds to RNA polymerase II (RNAPII).
Small GTPase required for proper nuclear import of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import.
Plays an essential role in initiation of the G0 program by preventing the degradation of specific nutrient-regulated mRNAs via the 5'-3' mRNA decay pathway.
Belongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family.
Catalyzes the second two steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylmonomethylethanolamine (PMME) to phosphatidyldimethylethanolamine (PDME) and of PDME to phosphatidylcholine (PC).
Belongs to the universal ribosomal protein uL30 family.
Belongs to the ATP-dependent AMP-binding enzyme family.
Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).
Belongs to the small GTPase superfamily. Arf family.
GTP-binding protein involved in protein trafficking; modulates vesicle budding and uncoating within the Golgi apparatus.
May be involved in a process influencing telomere capping.
Belongs to the acyl-CoA dehydrogenase family.
Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Belongs to the mitochondrion-specific ribosomal protein mL54 family.
Positively regulates the expression of genes involved in the catabolism of certain amides, omega amino acids, and lactams.
Belongs to the archaeal Rpo12/eukaryotic RPC10 RNA polymerase subunit family.
Belongs to the HMG-CoA reductase family.
Expression is induced during iron starvation.
HMG-CoA reductase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (PubMed:22106303, PubMed:30940706). Hmg1 and hmg2 catalyze the reduction of hydroxymethylglutaryl-CoA (HMG-CoA) to mevalonate (PubMed:22106303) (Probable). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase erg10B that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases erg13A and erg13B then condense acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases hmg1 and hmg2. Mevalonate is also a precursor for the extracellular siderophore triacetylfusarinine C (TAFC) (PubMed:16110826, PubMed:22106303) (Probable).
Mutations of Phe-262, Ser-305, Pro-320 or Ile-412 are associated to acquired resistance to azoles, clinical drugs used to inhibit the activity and kill Aspergillus fumigatus cells during infections.
In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.
Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family.
Belongs to the universal ribosomal protein uS10 family.
Vacuolar effluxer which mediate the efflux of amino acids resulting from autophagic degradation. The release of autophagic amino acids allows the maintenance of protein synthesis and viability during nitrogen starvation (By similarity).
In the C-terminal section; belongs to the peptidase M41 family.
In the N-terminal section; belongs to the AAA ATPase family.
May be involved in vacuolar sorting and osmoregulation.
Belongs to the HAD-like hydrolase superfamily. S-2-haloalkanoic acid dehalogenase family.
Acts as a sulfur carrier required for molybdopterin biosynthesis. Component of the molybdopterin synthase complex that catalyzes the conversion of precursor Z into molybdopterin by mediating the incorporation of 2 sulfur atoms into precursor Z to generate a dithiolene group. In the complex, serves as sulfur donor by being thiocarboxylated (-COSH) at its C-terminus by UBA4. After interaction with MOCS2B, the sulfur is then transferred to precursor Z to form molybdopterin.
Belongs to the MoaD family. MOCS2A subfamily.
C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of UBA4, then thiocarboxylated (-COSH) via the rhodanese domain of UBA4.
Heterotetramer; composed of 2 small (MOCS2A) and 2 large (MOCS2B) subunits.
Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane (By similarity).
Belongs to the G-alpha family. G(q) subfamily.
Part of the gene cluster that mediates the biosynthesis of the isocyanide xanthocillin and its derivatives (PubMed:29844112). The first step of the pathway consists in the conversion of tyrosine into a vinyl-isonitrile intermediate by the isocyanide synthase xanB (PubMed:29844112). Subsequent oxidative dimerization of this intermediate to form xanthocillin may involve the cytochrome P450 monooxygenase xanG, whose expression is coregulated with that of XanB (PubMed:29844112). Xanthocillin can be further modified by the isonitrile hydratase-like protein xanA which introduces N-formyl groups and the methyltransferase xanE which introduces methyl groups, leading to the production of several derivatives including fumiformamide (PubMed:29844112). Finally, fumiformamide can be subject to both oxidative and reductive cyclization to yield melanocins E and F, respectively (PubMed:29844112).
8-formyl-7-hydroxy-4-methylcoumarin inhibits the endonuclease activity and prebvent the splicing if the hacA mRNA (PubMed:33087521). The kinase domain is activated by trans-autophosphorylation (By similarity). Kinase activity is required for activation of the endoribonuclease domain (By similarity).
Autophosphorylated mainly on serine residues.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Homodimer; in response to the accumulation of unfolded proteins.
Leads to avirulence in a mouse model of invasive aspergillosis (PubMed:22028661). Results in severe defects in the expression of multiple virulence-related traits, including reduced thermotolerance, decreased nutritional versatility, impaired growth under hypoxia, altered cell wall and membrane composition, and increased susceptibility to azole antifungals (PubMed:22028661).
Senses unfolded proteins in the lumen of the endoplasmic reticulum (ER) via its N-terminal domain which leads to enzyme auto-activation (By similarity). The active endoribonuclease domain responds by cleaving an intron from the downstream cytoplasmic mRNA hacA, allowing for the translation of a transcription factor that coordinates a series of adaptive responses that are collectively known as the unfolded protein response (UPR) (PubMed:33087521). In the absence of ER stress, ireA controls dual signaling circuits that are both hacA-dependent and hacA-independent and which contribute to the expression of traits that are essential for virulence (PubMed:22028661).
Belongs to the NFYA/HAP2 subunit family.
Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes.
Belongs to the actin-binding proteins ADF family. Twinfilin subfamily.
Belongs to the flavin monoamine oxidase family.
Exoribonuclease involved in ribosome biosynthesis. Involved in the processing of ITS1, the internal transcribed spacer localized between the 18S and 5.8S rRNAs (By similarity).
Belongs to the complex I 24 kDa subunit family.
Belongs to the terpene cyclase/mutase family.
Belongs to the chloride channel (TC 2.A.49) family.
Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type II sub-subfamily.
Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit. Interacts with pstB2. This interaction may be a means to structurally tether the donor membrane (ER) harboring PstB2 to acceptor membranes (Golgi/endosomes) harboring PSD2 during PtdSer transport to the site of PtdEtn synthesis.
The C2 domains have an essential, but non-catalytic function. They may facilitate interactions with other proteins and are required for lipid transport function.
ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives.
Belongs to the carbohydrate kinase PfkB family.
Belongs to the ribonucleoside diphosphate reductase small chain family.
Belongs to the GMC oxidoreductase family.
Belongs to the copper transporter (Ctr) (TC 1.A.56) family. SLC31A subfamily.
Putative copper transporter; part of the crm gene cluster that mediates the biosynthesis of a yet unidentified copper-responsive metabolite (PubMed:29844112). Probably involved in the transport of copper, even if it does not act as a major copper transporter (PubMed:25281782).
Expression is up-regulated during co-cultivation of A.fumigatus with Streptomyces rapamycinicus that triggersthe production of the polyketide fumigermin during the bacterial-fungal interaction.
Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of fumigermin that inhibits germination of spores of the inducing S.rapamycinicus, and thus helps the fungus to defend resources in the shared habitat against a bacterial competitor (PubMed:32083553). The partially reducing polyketide synthase fngA alone is sufficient for the production of fumigermin (PubMed:32083553). FgnA catalyzes the condensation of 3 malonyl-CoA units to an acetyl-CoA starter, and 3 methylations to yield fumigermin (PubMed:32083553). It is remarkable that the five cluster genes including fgnA are conserved in distantly related fungi, supporting the assumption of a fumigermin cluster; it is thus possible that originally all five genes were functional, but that the genes encoding tailoring enzymes became inactive from mutations, similar to the case of the fgnA gene in strains A1163 and Af293 (Probable).
Belongs to the ribose-phosphate pyrophosphokinase family.
Belongs to the glycosyl hydrolase 2 family.
Required for exosome-dependent processing of pre-rRNA and small nucleolar RNA (snRNA) precursors. Involved in processing of 35S pre-rRNA at the A0, A1 and A2 sites.
Belongs to the nucleoporin NSP1/NUP62 family.
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Belongs to the complex I NDUFA1 subunit family.
Belongs to the succinate/malate CoA ligase beta subunit family.
Heterodimer of an alpha and a beta subunit.
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Involved in pre-mRNA splicing and cell cycle control.
Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Belongs to the class I-like SAM-binding methyltransferase superfamily.
S-methyltransferase that catalyzes the irreversible conversion of the secondary metabolite gliotoxin to bis(methylthio)gliotoxin (BmGT). Gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins, is characterized by a disulfide bridged cyclic dipeptide. Its thiol groups are essential for bioactivity, as they conjugate to sulfur-containing proteins, disturb the intracellular redox equilibrium, and generate reactive oxygen species by cycling between reduced and oxidized states. The enzyme prevents self-intoxication of the fungus by irreversible conversion of the toxic gliotoxin to a biologically inactive bis-thiomethylated derivative. Appears to negatively regulate gliotoxin biosynthesis.
ATP-dependent DNA helicase important for chromosome transmission and normal cell cycle progression in G(2)/M (By similarity). May have a role in changing DNA topology to allow the loading of proteins involved in maintaining sister chromatid cohesion in the vicinity of the centromeres (By similarity). Has a specific role in chromosome segregation during meiosis II (By similarity).
Belongs to the DEAD box helicase family. DEAH subfamily. DDX11/CHL1 sub-subfamily.
Belongs to the D-glutamate cyclase family.
Belongs to the eukaryotic/archaeal RNase P protein component 3 family.
Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.
Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.
Component of the origin recognition complex (ORC).
Belongs to the carotenoid oxygenase family.
Component of the pre-66S ribosomal particle.
Involved in the biogenesis of the 60S ribosomal subunit.
Belongs to the DPH1/DPH2 family. DPH1 subfamily.
Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase, predominantly CBR1.
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37.
Belongs to the SIMIBI class G3E GTPase family. ZNG1 subfamily.
Belongs to the universal ribosomal protein uS8 family.
Carboxylation allows a single lysine to coordinate two nickel ions.
In the C-terminal section; belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.
Belongs to the major facilitator superfamily. DHA1 family. Polyamines/proton antiporter (TC 2.A.1.2.16) subfamily.
Exhibits enhanced susceptibility to voriconazole, however itraconazole susceptibility is less affected.
Expression is up-regulated by exposure to human monocyte-derived immature dendritic cells (PubMed:21264256). Expression is increased in clinical azole-resistant isolates (PubMed:26933209).
MFS transporter involved in the basal level of azole susceptibility (PubMed:26933209). Confers resistance to voriconazole and, to a lesser extent, to fluconazole (PubMed:26933209).
Belongs to the GST superfamily. Kappa family.
Belongs to the TRAPP small subunits family.
Part of the multisubunit transport protein particle (TRAPP) complex.
Component of the cytosolic Fe/S protein assembly machinery. Required for maturation of extramitochondrial Fe/S proteins. May play a role in the transfer of pre-assembled Fe/S clusters to target apoproteins (By similarity).
Involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles.
Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm. Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix.
Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration.
Belongs to the RecA family. DMC1 subfamily.
Belongs to the ribonucleoside diphosphate reductase large chain family.
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Belongs to the glycosyl hydrolase 25 family.
Belongs to the small heat shock protein (HSP20) family.
Forms a homotrimer with a solvated central pore, which is connected laterally to the cytosol through the cavity within each protomer. Acts as a lipid scramblase that uses its central pore to function: the central pore opens laterally to accommodate lipid headgroups, thereby enabling lipid flipping and redistribution of lipids added to the outer leaflet of atg9-containing vesicles, thereby enabling growth into autophagosomes.
Homotrimer; forms a homotrimer with a central pore that forms a path between the two membrane leaflets.
Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through atg2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Required for mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking.
Phosphorylated by atg1. Atg1 phosphorylation is required for preautophagosome elongation.
Expressed at high levels in the presence of carboxymethylcellulose and repressed in the presence of glucose.
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CHEK2 subfamily.
Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
Cooperates with the reticulon proteins and tubule-shaping DP1 family proteins to generate and maintain the structure of the tubular endoplasmic reticulum network. Has GTPase activity, which is required for its function in ER organization.
Belongs to the eukaryotic ribosomal protein eL31 family.
Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
Belongs to the helicase family. RecQ subfamily.
Plays a role in the regulation of membrane potential. Could mediate a proton leak (By similarity).
Expression is induced upon voriconazole treatment (PubMed:16622700). Expression is up-regulated by exposure to human monocyte-derived immature dendritic cells (PubMed:21264256). Expression is also up-regulated in conidia exposed to human neutrophils (PubMed:18648542).
Major facilitator superfamily transporter that may be involved in A.fumigatus adaptation to azoles such as vorizonazole.
Endoplasmic reticulum-Golgi intermediate compartment membrane
Plays a role in transport between endoplasmic reticulum and Golgi.
Belongs to the mitochondrion-specific ribosomal protein mL67 family.
Belongs to the two pore domain potassium channel (TC 1.A.1.8) family.
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.
Belongs to the dynein light chain family.
Cytoplasmic dynein consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits which present intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs).
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
Belongs to the glycosyl hydrolase 6 (cellulase B) family.
Has a modular structure: a carbohydrate-binding module (CBM) at the N-terminus, a linker rich in threonines, and a C-terminal exocellobiohydrolase catalytic module. The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Belongs to the indoleamine 2,3-dioxygenase family.
Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. Dph1 and dph2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising dph3 and a NADH-dependent reductase, predominantly cbr1. Acts as an electron donor to reduce the Fe-S cluster in dph1-dph2 keeping the [4Fe-4S] clusters in the active and reduced state. Restores iron to dph1-dph2 iron-sulfur clusters which have degraded from [4Fe-4S] to [3Fe-4S] by donating an iron atom to reform [4Fe-4S] clusters, in a manner dependent on the presence of elongation factor 2 and SAM. Associates with the elongator complex and is required for tRNA Wobble base modifications mediated by the elongator complex. The elongator complex is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine).
The DPH-type metal-binding (MB) domain can also bind zinc. However, iron is the physiological binding partner as zinc binding impairs the protein electron donor function.
Expression is up-regulated by laeA during mycelial growth in a liquid medium but laeA is not involved in alb1 regulation during conidial morphogenesis (PubMed:17630330). Expression is, at least in part, controlled by the cAMP/PKA signal transduction pathway (PubMed:16110796).
Impairs the production of melanin and leads to an albino phenotype (PubMed:9620950, PubMed:15321679, PubMed:15812003, PubMed:17343676, PubMed:19156203, PubMed:26701308). Blocks the synthesis of the intermediate 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) (PubMed:9620950). Results in an altered conidial surface with masked surface rodlet layer, leaky cell wall allowing the deposition of proteins on the cell surface and exposing the otherwise-masked cell wall polysaccharides at the surface (PubMed:19703288, PubMed:24818666, PubMed:26972005). Results also in a dramatic reduction of virulence in a mice models of infections (pulmonary and cutanous) with efficient complement component C3 binding on conidial surfaces and increased neutrophil-mediated phagocytosis (PubMed:9620950, PubMed:9832321, PubMed:12464010, PubMed:20145078, PubMed:21501368, PubMed:21747802, PubMed:21573171, PubMed:24836942). Decreases also the protection of conidia against amoeba predation (PubMed:25684622). Decreases significantly the ability of conidia to activate platelets and to induce platelet aggregation (PubMed:25810442). Causes enhanced insect mortality compared to the parent strain in a wax moth Galleria mellonella infection model, probably through exacerbated immune response of the wax moth (PubMed:19156203).
Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment and a structural component of the conidial wall (PubMed:9620950, PubMed:10515939, PubMed:18539819, PubMed:19156203). The first step of the pathway is the production of the heptaketide naphtopyrone YWA1 by the polyketide synthase alb1 though condensation of acetyl-CoA with malonyl-CoA (PubMed:9620950, PubMed:11040426). The naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase ayg1 though chain-length shortening (PubMed:10515939, PubMed:11350964). 1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to yield scytalone (PubMed:10515939). The scytalone dehydratase arp1 then reduces scytalone to 1,3,8-THN (PubMed:10515939). 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to yield vermelone (PubMed:10515939). Vermelone is further converted by the multicopper oxidase abr1 to 1,8-DHN (PubMed:10515939). Finally the laccase abr2 transforms 1,8-DHN to DHN-melanin (PubMed:10515939). DHN-melanin biosynthesis appears to be initiated in endosomes where early enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to melanin deposition on the cell surface where late enzymes (abr1 and abr2) localize (PubMed:26972005). DHN-melanin is an important structural component of the outer cell wall and is required for the presence of conidial surface hydrophobins (PubMed:19703288). DHN-melanin also plays a crucial role in fungal virulence, including a protective role against the host's immune defenses (PubMed:9620950, PubMed:9832321, PubMed:12464010, PubMed:16110796, PubMed:20145078, PubMed:21501368, PubMed:21747802, PubMed:21573171, PubMed:24818666, PubMed:24836942, PubMed:25810442, PubMed:26972005). DHN-melanin protects also conidia against amoeba predation (PubMed:25684622).
The C-terminal region is involved in Claisen-type cyclization of the second ring of naphthopyrone.
Belongs to the methyltransferase superfamily. LaeA methyltransferase family.
Component of the heterotrimeric velvet complex composed of laeA, veA and velB; VeA acting as a bridging protein between laeA and velB (By similarity).
Expression is induces in response to antifungal activity produced by Lactobacillus plantarum (PubMed:23876797).
Methyltransferase that performs automethylation (By similarity). No other methyl-accepting substrate has been identified yet (By similarity). Component of the velvet transcription factor complex that acts as a global regulator for secondary metabolite gene expression (PubMed:15075281, PubMed:17630330, PubMed:19843884, PubMed:24082142, PubMed:24116213). Positively controls expression of 20% to 40% of major classes of secondary metabolite biosynthesis genes such as nonribosomal peptide synthetases, polyketide synthases, and P450 monooxygenases (PubMed:17432932). Controls the expression of the gliotoxin gene cluster (PubMed:15075281, PubMed:17630330, PubMed:19843884). Controls the expression of the fumitremorgin, fumagillin, and pseurotin gene clusters, where genes for fumagillin and pseurotin are physically intertwined in a single supercluster (PubMed:24082142). Regulates the biosynthetic genes required for endocrocin production (PubMed:22492455). Secondary metabolites under the transcriptional regulation of laeA are necessary for inhibition of angiogenesis during invasive infection in mice (PubMed:19843884). Controls the expression of cell surface rodA, a hydrophobin that acts as an antiphagocytic molecule (PubMed:19917717). Regulates also the expression of genes involved in conidial biosynthesis (PubMed:16151250).
Reduces the production of the immunotoxin gliotoxin (PubMed:15075281, PubMed:16151250, PubMed:17630330). Reduces the production of endocrocin (PubMed:22492455). Affects transcription of numerous secondary metabolite biosynthesis genes (PubMed:17432932). Decreases spore formation and germination (PubMed:23022264). Reduces virulence in a murine pulmonary infection model through increased phagocytosis by host macrophages (PubMed:16151250, PubMed:19917717).
Acts as the tether and is essential for anchoring of Woronin bodies at the septal pore (PubMed:23869404). In damaged hyphae, Woronin bodies occlude septal pores in order to separate intact from damaged compartments (PubMed:23869404).
Binds directly or indirectly to the Woronin body major protein hexA.
The N-terminal domain binds to Woronin bodies in the cytoplasm and on either side of the septal pore, whereas the C-terminal domain binds to the septal pore.
Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the universal ribosomal protein uL2 family.
Component of the spt4-spt5 complex. Interacts with RNA polymerase II (By similarity).
The spt4-spt5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene (By similarity).
Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family.
Belongs to the mitochondrial carrier (TC 2.A.29) family. SLC25A38 subfamily.
Mitochondrial glycine transporter that imports glycine into the mitochondrial matrix. Plays an important role in providing glycine for the first enzymatic step in heme biosynthesis, the condensation of glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the mitochondrial matrix.
Heterohexamer; composed of 3 copies of TIM9 and 3 copies of TIM10, named soluble 70 kDa complex. Associates with the TIM22 complex, whose core is composed of TIM22 and TIM54. Interacts with the transmembrane regions of multi-pass transmembrane proteins in transit (By similarity).
Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity).
The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIM9 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity).
Converts proline to delta-1-pyrroline-5-carboxylate.
Belongs to the Mediator complex subunit 17 family.
Belongs to the tryptophan dimethylallyltransferase family.
Prenyltransferase; part of the gene cluster that mediates the biosynthesis of neosartoricin, a prenylated anthracenone that exhibits T-cell antiproliferative activity, suggestive of a physiological role as an immunosuppressive agent (PubMed:23758576, PubMed:23368997). The non-reducing polyketide synthase nscA probably synthesizes and cyclizes the decaketide backbone (PubMed:23368997). The hydrolase nscB then mediates the product release through hydrolysis followed by spontaneous decarboxylation (PubMed:23368997). The prenyltransferase nscD catalyzes the addition of the dimethylallyl group to the aromatic C5 (PubMed:23368997). The FAD-dependent monooxygenase nscC is then responsible for the stereospecific hydroxylation at C2 (PubMed:23368997). There is no gene encoding O-acetyltransferase in the nsc gene cluster; thus, the last step of 2-O-acetylation leading to neosartoricin may be catalyzed by an unidentified O-acetyltransferase (PubMed:23368997).
Belongs to the eIF-2B gamma/epsilon subunits family.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.
Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily.
Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of Fe/S cluster precursors synthesized by nfs1 and other mitochondrial proteins (By similarity). Hydrolyzes ATP (By similarity). Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound (By similarity).
Belongs to the SMC family. SMC2 subfamily.
Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Plays a role in both the assembly of the exocyst and the polarization of this complex to specific sites of the plasma membrane for exocytosis. Also involved in assembly of the spliceosome (By similarity).
Belongs to the RecA family. RAD51 subfamily.
Required both for recombination and for the repair of DNA damage caused by X-rays.
Essential component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. Required for the maturation of extramitochondrial Fe/S proteins.
Belongs to the eukaryotic ribosomal protein eS1 family.
Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (25S, 5.8S and 5S).
GPI-anchored cell wall protein involved in stabilizing the cell wall. Not implicated in virulence, heme uptake and biofilm formation.
The GPI-like anchor contains a phosphoceramide lipid group.
Belongs to the multicopper oxidase family.
Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER.
Divalent metal ions. Mg(2+) is the most effective.
Belongs to the glycosyl hydrolase 16 family. CRH1 subfamily.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity).
Component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs).
Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ("psi") residues may serve to stabilize the conformation of rRNAs.
Belongs to the steroid 5-alpha reductase family.
Component of the EKC/KEOPS complex composed of at least BUD32, CGI121, GON7, KAE1 and PCC1; the whole complex dimerizes.
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily.
Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.
Belongs to the dermatan-sulfate isomerase family.
Belongs to the complex I NDUFS4 subunit family.
Belongs to the bZIP family. ATF subfamily.
Expression is induced in during osmotic stress and repressed in the absence of the mitogen-activated protein kinase sakA (PubMed:27706915). Expression is also highly induced at low and high caspofungin concentrations (PubMed:27706915).
Increases sensitivity to osmotic and oxidative stresses, but also to cell wall-damaging agents such as Congo red or iprodione (PubMed:27706915). Shows increased resistance to low caspofungin concentrations, but is more sensitive to higher caspofungin concentrations (PubMed:27706915). Leads to attenuated virulence (PubMed:27706915).
Transcription factor that acts as a key player in the regulatory circuit that integrates secondary metabolism and cellular response to oxidative stress (By similarity). Regulates the genes involved in development, as well as osmotic, oxidative, and cell wall stresses (PubMed:27706915). Participates in the caspofungin paradoxical effect (CPE), where fungi grow beyond the minimum inhibitory concentration of caspofungin (PubMed:27706915). Plays a role in virulence (PubMed:27706915).
RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Required for the delivery of cortical endoplasmic reticulum into the emerging bud.
Component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. Required to prevent the proteolysis of the CreB deubiquitinating enzyme in the absence of carbon catabolite repression. CreB deubiquitinating enzyme stabilized in a complex with the CreC leads to the expression of genes such as those in the proline and quinate pathways (By similarity).
Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.
Interacts with PCNA. Three molecules of fen1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Phosphorylated. Phosphorylation upon DNA damage induces relocalization to the nuclear plasma.
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family.
Has a role in promoting intracellular calcium ion sequestration via the exchange of calcium ions for hydrogen ions across the vacuolar membrane. Involved also in manganese ion homeostasis via its uptake into the vacuole.
Belongs to the proteasome subunit S14 family.
Belongs to the kynurenine formamidase family.
Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.
The main chain amide nitrogen atoms of the second glycine and its adjacent residue in the HGGXW motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
May be involved in protection from oxidative damage.
Gamma-glutamyl cyclotransferase-like protein; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). Gliotoxin contributes to pathogenesis during invasive aspergillosis (PubMed:17601876, PubMed:18199036). In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species (PubMed:17601876).
Impairs gliotoxin biosynthesis and accumulates ergothioneine (PubMed:22903976, PubMed:26150413). Leads also to attenuated gliT abundance (PubMed:22903976, PubMed:26150413).
Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family.
Belongs to the chromate ion transporter (CHR) (TC 2.A.51) family.
Belongs to the DDOST 48 kDa subunit family.
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER).
Belongs to the universal ribosomal protein uL6 family.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
Belongs to the LIMR family. LMBRD1 subfamily.
Probable lysosomal cobalamin transporter. Required to export cobalamin from lysosomes allowing its conversion to cofactors (By similarity).
Belongs to the purine-cytosine permease (2.A.39) family.
Belongs to the actin-binding proteins ADF family. GMF subfamily.
Belongs to the myo-inositol 1-phosphate synthase family.
Associates with the pre-60S ribosomal particle.
Belongs to the universal ribosomal protein uL10 family.
Component of the ribosome assembly machinery. Nuclear paralog of the ribosomal protein P0, it binds pre-60S subunits at an early stage of assembly in the nucleolus, and is replaced by P0 in cytoplasmic pre-60S subunits and mature 80S ribosomes.
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Belongs to the WD repeat DDB2/WDR76 family.
DNA-binding protein that binds to both single- and double-stranded DNA. Binds preferentially to UV-damaged DNA. May be involved in DNA-metabolic processes.
Belongs to the xanthine dehydrogenase family.
Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Belongs to the acetyltransferase family. GNA1 subfamily.
In the N-terminal section; belongs to the glycosyltransferase 20 family.
Belongs to the GTP-binding SRP family. SRP54 subfamily.
Fungal signal recognition particle consists of a 7S RNA molecule (scR1) and at least six protein subunits: srp72, srp68, srp54, sec65, srp21 and srp14.
Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the arrest of nascent chain elongation during membrane targeting. SRP54 binds to the signal sequence of presecretory protein when they emerge from the ribosomes. SRP54 interacts with the scR1 RNA and mediates the association of the resulting SRP-RNC complex with the signal recognition particle receptor (SR) via its alpha subunit SRP101. Both, SRP54 and SRP101, are locked in their GTP bound forms in the SRP-RNC-SR complex, which dissociates upon transferring the signal sequence to the protein-conducting channel (translocon). After signal sequence transfer, SRP54 and SRP101 act as reciprocal GTPase-activating proteins (GAPs), thereby resolving their association.
The M domain binds the 7SL RNA and the signal sequence of presecretory proteins.
The NG domain, also named G domain, is a special guanosine triphosphatase (GTPase) domain, which binds GTP and forms a guanosine 5'-triphosphate (GTP)-dependent complex with a homologous NG domain in the SRP receptor subunit srp101. The two NG domains undergo cooperative rearrangements upon their assembly, which culminate in the reciprocal activation of the GTPase activity of one another. SRP receptor compaction upon binding with cargo-loaded SRP and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER.
Belongs to the complex I 51 kDa subunit family.
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Belongs to the adaptor complexes small subunit family.
Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits.
The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
Transcriptional activator of the xylanolytic system. Involved in the regulation of extracellular cellulolytic and xylanolytic genes and in the regulation of the intracellular activities of D-xylose catabolic genes in the pentose catabolic pathway (PCP) in response to the presence of D-xylose (By similarity).
Major facilitator transporter involved in triacetylfusarinine C (TAFC) uptake (PubMed:22903978, PubMed:36125294). Can also transport ferricrocin and coprogen, but not ferrichrysin (PubMed:22903978). MirB plays a crucial role for virulence in a murine model of pulmonary aspergillosis, indicating that TAFC-mediated iron uptake plays a dominant role during infection (PubMed:36125294).
Catalyzes the covalent attachment of ubiquitin to other proteins. Plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation. Also involved in postreplication repair of UV-damaged DNA, in N-end rule-dependent protein degradation and in sporulation.
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for l- to d- amino acid conversion) are present within the NRP synthetase. NRPS5 has the following architecture: A-T-C-A-T-C-T.
Belongs to the glycosyltransferase 28 family.
Heterodimer with alg14 to form a functional enzyme.
Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity).
Belongs to the WD repeat DCAF13/WDSOF1 family.
Belongs to the ATP phosphoribosyltransferase family.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
Aldehyde reductase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:22453123). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:15870460). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482, PubMed:21409592). EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482). EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482). Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831). Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909).
Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.
Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin. Active against paranitrophenyl-acetate, methyl ferulate and wheat arabinoxylan.
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1), a complex that is involved in endosomal cargo sorting.
Belongs to the eukaryotic ribosomal protein eL8 family.
Common component of the spliceosome and rRNA processing machinery.
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PDPK1 subfamily.
Belongs to the peptidase S8 family. Furin subfamily.
Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily.
Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose (By similarity).
Belongs to the CDP-alcohol phosphatidyltransferase class-II family.
Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Belongs to the DEAD box helicase family. DDX52/ROK1 subfamily.
Interacts with the U3 snoRNA and is associated with the 90S and 40S pre-ribosomes.
Required for proper homologous chromosome pairing and efficient cross-over and intragenic recombination during meiosis.
Interacts with the 40S ribosomal subunit.
The SUI1 domain may be involved in RNA binding.
Belongs to the ATP-dependent DNA ligase family.
In the C-terminal section; belongs to the Cu-Zn superoxide dismutase family.
Belongs to the WD repeat MET30/SCONB/SCON-2 family.
Component of the SCF(sconB) E3 ubiquitin ligase complex involved in the regulation of sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor.
Component of the SCF(sconB) E3 ubiquitin ligase complex.
Belongs to the PDK/BCKDK protein kinase family.
Belongs to the eukaryotic ribosomal protein eS8 family. Ribosome biogenesis protein NSA2 subfamily.
Component of the pre-66S ribosomal particle. Interacts with nop7 and rrp1. Interacts with rsa4 (via WD repeats).
Involved in the biogenesis of the 60S ribosomal subunit. May play a part in the quality control of pre-60S particles (By similarity).
Belongs to the protein kinase superfamily. RIO-type Ser/Thr kinase family.
Divalent metal cations. Prefers magnesium or manganese.
Belongs to the cytidylyltransferase family.
Belongs to the glycosyl hydrolase 36 family.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).
During iron-replete conditions, partially derepresses synthesis of triacetylfusarinine C (TAFC) and uptake of iron resulting in increased cellular accumulation of both iron and ferricrocin (FC) (PubMed:18721228). Increases sensitivity to iron and oxidative stress (PubMed:18721228).
Expression is repressed by the zinc cluster transcription factor acuM in order to stimulate expression of genes involved in both reductive iron assimilation and siderophore-mediated iron uptake (PubMed:21062375).
GATA-type transcription repressor that regulates iron- acquisition genes through specific binding the GATA sequence element 5'-ATCWGATAA-3' of target promoters (PubMed:18721228). Iron acquisition regulation is critical for survival under both iron-limiting conditions (to acquire essential iron) and iron-replete conditions (to limit iron toxicity) (PubMed:18721228). SreA targets include genes encoding a number of key iron-regulated factors such as those involved in siderophore biosynthesis (PubMed:18721228).
The conserved cystein-rich region (CRR) localized between the zinc fingers is also involved in DNA-binding and transcription repressor activity (By similarity).
Belongs to the HAD-like hydrolase superfamily. SerB family.
Acetylated once deposited into chromatin.
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. H2A or its variant H2A.Z forms a heterodimer with H2B. H2A.Z associates with the vps72/swc2 subunit of the SWR1 chromatin remodeling complex. Interacts also with rbp1/DNA-directed RNA polymerase II largest subunit (By similarity).
Variant histone H2A which can replace H2A in some nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. This variant is enriched at promoters, it may keep them in a repressed state until the appropriate activation signal is received. Near telomeres, it may counteract gene silencing caused by the spread of heterochromatin proteins. Required for the RNA polymerase II and spt15/TBP recruitment to the target genes. Involved in chromosome stability (By similarity).
Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle.
Belongs to the ACC deaminase/D-cysteine desulfhydrase family.
Mitogen-activated protein kinase required for growth on media where sorbitol or mannitol is the sole carbon source.
Belongs to the phosphoenolpyruvate carboxykinase (ATP) family.
Belongs to the eukaryotic RPA43 RNA polymerase subunit family.
By Zn(2+) (PubMed:8188335). Expression is controlled by the prtT transcription factor (PubMed:19564390, PubMed:19564385).
Causes an allergic reaction in human. Recombinant protein binds to IgE in 93% of the 54 patients tested suffering with allergic bronchopulmonary aspergillosis (ABPA). Recombinant protein binds to IgE in 74% of the 35 A.fumigatus-allergic patients tested without ABPA.
Completely inhibited by metalloprotease inhibitors EDTA, 1,10-phenanthroline, and phosphoramidon, but not by inhibitors specific for serine, cysteine, and aspartate proteases, such as PMSF, antipain, leupeptin, chymostatin, and pepstatin. Zn(2+) and, to a lesser extent, Co(2+) reversed the inhibition of 1,10-phenanthroline.
Not glycosylated according to PubMed:8188335, but glycosylated according to PubMed:24100314.
Secreted metalloproteinase that allows assimilation of proteinaceous substrates and probably acts as a virulence factor (By similarity). Catalyzes the hydrolysis of elastin (PubMed:7927676, PubMed:8188335). Hydrolyzes azocasein, synthetic fluorigenic substrate Abz-Ala-Ala-Phe-Phe-pNA, and His-Leu, Ala-Leu, Tyr-Leu, Gly-Phe, and Phe-Phe peptide bonds in the B chain of insulin (PubMed:8188335).
Component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes.
Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor (By similarity).
Belongs to the complex I NDUFB3 subunit family.
Ceramide-binding protein that may transfer ceramides from the endoplasmic reticulum membrane to the cis-Golgi network membrane, and is thereby required for the biosynthesis of complex sphingolipids.
Belongs to the glycosyl hydrolase 76 family.
Belongs to the cyclophilin-type PPIase family. CWC27 subfamily.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in pre-mRNA splicing (By similarity).
Belongs to the acetolactate synthase small subunit family.
Causes an allergic reaction in human. Binds to IgE (By similarity).
Chitosanase catalyzing the endo-type cleavage of chitosan, the deacylated form of chitin. Chitosanase may be crucial in the degradation of the deacetylated portion of chitin in the fungal cell wall. Chitoolisaccharides produced by the hydrolysis of partially N-acetylated chitosan are known to have many biological activities, including antibacterial activity, immune-enhancing effects, and elicitor activity. The chitosans with higher degrees of deacetylation were shown to be the better substrates. Chitodimer, chitotrimer, and chitotetramer are the major products but monoacetyl chitodimer, monoacetyl chitotrimer, and monoacetyl chitotetramer are also produced (By similarity).
Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
Belongs to the gamma-glutamylcyclotransferase family.
Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
Belongs to the acetyltransferase family. MAK3 subfamily.
Belongs to the eukaryotic ribosomal protein eS12 family.
Belongs to the glycosyl hydrolase 72 family.
Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall morphogenesis.
Cell wall protein regularly arranged in interwoven fascicules of clustered proteinaceous microfibrils, or rodlets, to form the outer spore coat protein. It is involved in resistance to environmental stress and may well be associated with conidial hydrophobicity. It is important in the morphogenesis of the dispersible conidia.
Expression is limited to the developmental stages in which maturing conidiophores are present.
Belongs to the peroxisomal membrane protein PXMP2/4 family.
Belongs to the RNA 3'-terminal cyclase family. Type 2 subfamily.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type V subfamily.
Component of the nascent polypeptide-associated complex (NAC), a dynamic component of the ribosomal exit tunnel, protecting the emerging polypeptides from interaction with other cytoplasmic proteins to ensure appropriate nascent protein targeting. The NAC complex also promotes mitochondrial protein import by enhancing productive ribosome interactions with the outer mitochondrial membrane and blocks the inappropriate interaction of ribosomes translating non-secretory nascent polypeptides with translocation sites in the membrane of the endoplasmic reticulum. Egd2 may also be involved in transcription regulation (By similarity).
Part of the nascent polypeptide-associated complex (NAC), consisting of egd2 and egd1. NAC associates with ribosomes via egd1 (By similarity).
Necessary for protein synthesis in mitochondria. Functions as a ribosome recycling factor in mitochondria.
Belongs to the acid sphingomyelinase family.
Belongs to the snRNP core protein family.
Belongs to the class II fructose-bisphosphate aldolase family.
Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution.
Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.
Accessory subunit of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis.
Belongs to the DNA polymerase alpha subunit B family.
Belongs to the choline monooxygenase family.
Catalyzes the first step of the osmoprotectant glycine betaine synthesis.
Changes the gray-green conidial pigment to a brown color and reduces the ornamentation of conidia (PubMed:16988817, PubMed:26972005). Reduces overall laccase activity only during sporulation, but not during vegetative growth (PubMed:16988817). Causes enhanced insect mortality compared to the parent strain in a wax moth Galleria mellonella infection model, probably through exacerbated immune response of the wax moth (PubMed:19156203).
Expression is up-regulated upon hyphal competency and drastically increased during conidiation (PubMed:16988817, PubMed:24123270). Expression is controlled by brlA, the master regulator of conidiophore development, and is responsive to the copper level in the medium (PubMed:24123270).
Laccase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment and a structural component of the conidial wall (PubMed:10515939, PubMed:14970241, PubMed:19156203). The first step of the pathway is the production of the heptaketide naphtopyrone YWA1 by the polyketide synthase alb1 though condensation of acetyl-CoA with malonyl-CoA (PubMed:10515939). The naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase ayg1 though chain-length shortening (PubMed:10515939). 1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to yield scytalone (PubMed:10515939). The scytalone dehydratase arp1 then reduces scytalone to 1,3,8-THN (PubMed:10515939). 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to yield vermelone (PubMed:10515939). Vermelone is further converted by the multicopper oxidase abr1 to 1,8-DHN (PubMed:10515939). Finally the laccase abr2 transforms 1,8-DHN to DHN-melanin (PubMed:10515939). DHN-melanin biosynthesis appears to be initiated in endosomes where early enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to melanin deposition on the cell surface where late enzymes (abr1 and abr2) localize (PubMed:26972005). DHN-melanin is an important structural component of the outer cell wall and is required for the presence of conidial surface hydrophobins (PubMed:19703288). DHN-melanin also plays a crucial role in fungal virulence, including a protective role against the host's immune defenses (PubMed:19156203, PubMed:20145078, PubMed:21747802, PubMed:21573171, PubMed:24818666). DHN-melanin protects also conidia against amoeba predation (PubMed:25684622).
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA.
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
Belongs to the Dus family. Dus3 subfamily.
Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U47 in cytoplasmic tRNAs (By similarity). Catalyzes the synthesis of dihydrouridine in some mRNAs, thereby affecting their translation.
Probable mitochondrial mRNA stabilization factor.
RNA-binding nucleolar protein required for pre-rRNA processing. Involved in production of 18S rRNA and assembly of small ribosomal subunit (By similarity).
Belongs to the glycosyl hydrolase 27 family.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. GDP-mannose 4,6-dehydratase subfamily.
Abolishes the production of pseurotin (PubMed:24082142, PubMed:24939566).
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of pseurotin A, a competitive inhibitor of chitin synthase and an inducer of nerve-cell proliferation (PubMed:24082142, PubMed:24939566). The PKS-NRPS hybrid synthetase psoA is responsible for the biosynthesis of azaspirene, one of the first intermediates having the 1-oxa-7-azaspiro[4,4]-non-2-ene-4,6-dione core of pseurotin, via condensation of one acetyl-CoA, 4 malonyl-CoA, and a L-phenylalanine molecule (PubMed:24082142, PubMed:24939566). The dual-functional monooxygenase/methyltransferase psoF seems to be involved in the addition of the C3 methyl group onto the pseurotin scaffold (PubMed:24939566). Azaspirene is then converted to synerazol through 4 steps including oxidation of C17 by the cytochrome P450 monooxygenase psoD, O-methylation of the hydroxy group of C8 by the methyltransferase psoC, and the trans-to-cis isomerization of the C13 olefin by the glutathione S-transferase psoE (PubMed:24939566). The fourth step of synerazol production is performed by the dual-functional monooxygenase/methyltransferase psoF which seems to catalyze the epoxidation of the intermediate deepoxy-synerazol (PubMed:24939566). Synerazol can be attacked by a water molecule nonenzymatically at two different positions to yield two diol products, pseurotin A and pseurotin D (PubMed:24939566).
Expression is induced under hypoxic conditions (PubMed:21388144).
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the MICOS complex subunit Mic60 family.
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway (By similarity).
Component of the mitochondrial contact site and cristae organizing system (MICOS) complex.
Involved in the first step of pre-mRNA splicing. Required for cell growth and cell cycle control. Plays a role in the levels of the U1, U4, U5 and U6 snRNAs and the maintenance of the U4/U6 snRNA complex. May provide the link between the 'nineteen complex' NTC spliceosome protein complex and the spliceosome through the U6 snRNA. Associates predominantly with U6 snRNAs in assembled active spliceosomes. Binds directly to the internal stem-loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cycle (By similarity).
The C-terminal RRM domain and the zinc finger motif are necessary for RNA-binding.
Forms a chaperone-bound H2A.Z-H2B complex that acts as a source for SWR1 complex-dependent H2A to H2A.Z histone replacement in chromatin.
Forms a heterotrimer with H2A.Z-H2B, stabilizing the association of the histone dimer. Also, with a lower affinity, forms a heterotrimer with H2A-H2B (By similarity).
Highly expressed under low-iron conditions and down-regulated under high-iron conditions (PubMed:26929401). Expression is regulated by hapX under low-iron conditions (PubMed:26929401).
Leads to lower ferrichrome (FC) uptake activity, which is reduced to approximately 60% of the wild-type activity (PubMed:26929401).
Major facilitator transporter involved in ferrichrome (FC) uptake (PubMed:26929401).
Belongs to the polysaccharide monooxygenase AA13 family.
Decreased prostaglandin (PG) production in triple ppoA/ppoB/ppoC mutants. The triple mutant is hypervirulent in the invasive pulmonary aspergillosis murine model system and shows increased tolerance to hydrogen peroxide stress.
Responsible for the synthesis of various fatty acid-derived oxylipins. Oxidizes linoleic acid primarily to 10R-hydroperoxy-8,12-octadecadienoic acid (10R-HPODE) and, to a lesser extent, 8R-hydroperoxylinoleic acid (8R-HPODE). Also synthesizes 10-hydroxy-octadeca-8,12-dienoic acid (10-HODE) from linoleic acid and primarily 8R-hydroxy-octadeca-9-monoenoic acid (8-HOME, also known as psiB beta) from oleic acid. 8-HOME forms part of psi factor, a mixture of oxylipins that regulates the balance between sexual and asexual spore production. Displays epoxyalcohol synthase activity. Plays a role in the synthesis of prostaglandins which may be required for pathogenicity.
Belongs to the ABC transporter superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201) subfamily.
Expression is induced upon voriconazole treatment (PubMed:16622700). Expression is up-regulated in sreA deficiency strains, probably in response to accumulation of toxic compounds (PubMed:18721228). Expression is up-regulated during biofilm growth (PubMed:21724936). Expression is increased in clinical azole-resistant isolates (PubMed:15504870).
Pleiotropic ABC efflux transporter that may be involved in A.fumigatus adaptation to azoles such as vorizonazole.
Methyltransferase; part of the gene cluster that mediates the biosynthesis of trypacidin, a mycotoxin with antiprotozoal activity and that plays a role in the infection process (PubMed:26278536, PubMed:26242966). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) tpcC (PubMed:26242966). The atrochrysone carboxyl ACP thioesterase tpcB then breaks the thioester bond and releases the atrochrysone carboxylic acid from tpcC (PubMed:26242966). The decarboxylase tpcK converts atrochrysone carboxylic acid to atrochrysone which is further reduced into emodin anthrone (PubMed:26242966). The next step is performed by the emodin anthrone oxygenase tpcL that catalyzes the oxidation of emodinanthrone to emodin (PubMed:26242966). Emodin O-methyltransferase encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin to form questin (PubMed:26242966). Ring cleavage of questin by questin oxidase tpcI leads to desmethylsulochrin via several intermediates including questin epoxide (By similarity). Another methylation step catalyzed by tpcM leads to the formation of sulochrin which is further converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes the conversion of monomethylsulfochrin to trypacidin (PubMed:26242966). Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)), thus triggering host necrotic cell death (PubMed:22319557). The trypacidin pathway is also able to produce endocrocin via a distinct route from the endocrocin Enc pathway (PubMed:26242966).
Belongs to the WD repeat NOL10/ENP2 family.
Belongs to the cyclin family. Cyclin C subfamily.
Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The SRB8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II.
Belongs to the cyclic nucleotide phosphodiesterase family.
Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
Belongs to the peptidase C2 family. PalB/RIM13 subfamily.
Activated by C-terminal proteolytic cleavage by signaling protease (probably palB/RIM13) at neutral to alkaline ambient pH.
Transcription factor that mediates regulation of both acid- and alkaline-expressed genes in response to ambient pH. At alkaline ambient pH, activates transcription of alkaline-expressed genes (including pacC itself) and represses transcription of acid-expressed genes (By similarity).
Self-assembles into detergent-resistant oligomers and forms a complex with hexA assemblies.
Woronin sorting complex protein involved in both Woronin bodies (WB) formation and inherence (PubMed:23869404). Localizes to large peroxisome membranes where it self-assembles into detergent-resistant oligomers that envelop hex-1 assemblies, producing asymmetrical nascent WBs (By similarity). These structures are then delivered to the cell cortex, which permits partitioning of the nascent WB and WB inheritance (By similarity).
Belongs to the adenylyl cyclase class-3 family.
Plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP.
Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions, but also accepts a lysine residue in the P1 position, leading to the activation of trypsinogen and chymotrypsinogen A (By similarity). Can catalyze hydrolysis of the major structural proteins of basement membrane, elastin, collagen, and laminin. Thought to play a significant role in virulence (PubMed:7558282).
Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family. Azg-like subfamily.
Belongs to the glycosyl hydrolase 31 family.
Belongs to the carnitine/choline acetyltransferase family.
This promotes the activity of RNA polymerase II.
Acts in the GPI biosynthetic pathway between GlcNAc-PI synthesis and GPI transfer to protein.
Belongs to the palmitoyl-protein thioesterase family.
Belongs to the SLC35F solute transporter family.
Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm.
Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family.
L-ornithine N(5)-monooxygenase; part of the siderophore biosynthetic pathway (PubMed:15504822, PubMed:16113265, PubMed:17845073, PubMed:20614882, PubMed:20650894, PubMed:22465572). Aspergillus fumigatus produces four types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake; and intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial iron distribution and storage. TAFC consists of three N(2)-acetyl-N(5)-anhydromevalonyl-N(5)-hydroxyornithine residues cyclically linked by ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-(N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of all four siderophores depends on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA (PubMed:15504822, PubMed:16113265, PubMed:20614882, PubMed:20650894, PubMed:22465572). SidA is highly specific for its substrate, only hydrolyzing l-ornithine, and has preference for NADPH over NADH, NADPH playing a role in stabilization of the C4a-hydroperoxyflavin intermediate (PubMed:20614882, PubMed:22465572). Subsequently, the pathways for biosynthesis of extra- and intracellular siderophores split (PubMed:17845073). For biosynthesis of extracellular siderophores, the transacylase sidF transfers anhydromevalonyl to N(5)-hydroxyornithine (PubMed:17845073). The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by sidI and sidH respectively (PubMed:22106303). The acetylation of N(5)-hydroxyornithine for FC biosynthesis involves the constitutively expressed sidL (PubMed:21622789). FC is hydroxylated to HFC by an as yet uncharacterized enzyme during conidiation (PubMed:17845073). Assembly of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal peptide synthetases (NRPS), sidD and sidC respectively (PubMed:17845073). Subsequently, sidG catalyzes N2-acetylation of FsC for forming TAFC (PubMed:17845073). Both extra- and intracellular siderophores are crucial for growth during iron limitation and virulence (PubMed:16113265).
Moderately reduced growth rate during iron starvation and in iron replete conditions. Only displays 1% of wild-type conidiospore production in iron-depleted and replete conditions. Completely attenuates virulence in a mouse model of invasive pulmonary aspergillosis.
Belongs to the nitrate reductase family.
Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily.
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Belongs to the CoA-transferase III family.
Belongs to the bacterial ribosomal protein bL34 family.
Completely abolishes the production of fumagillin but leads to the accumulation of the intermediate beta-trans-bergamotene (PubMed:24082142, PubMed:24568283).
Expression is controlled by the fumagillin biosynthesis cluster regulator fumR (PubMed:24082142). Expression is also under the control of the developmental and secondary metabolism regulator veA (PubMed:24116213). Expression is significantly up-regulated during infection (PubMed:30251593).
Multifunctional cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) (PubMed:23488861, PubMed:24568283). Within the pathway, the multifunctional cytochrome P450 monooxygenase af510 acts as a 2,4,6-trichlorophenol monooxygenase that first performs the C-H hydroxylation at the bridgehead C5 position to yield 5R-hydroxyl-beta-trans-bergamotene (PubMed:24568283). Subsequently, a four electron oxidation initiated at C-9 coupled to cleavage of the cyclobutane C5-C8 bond of the bicyclo[3.1.1] core yields the epoxyketone intermediate 5-keto-cordycol (PubMed:24568283). An additional epoxidation reaction also catalyzed by af510 then furnishes the characteristic bisepoxide ketone 5-keto-demethoxyfumagillol (PubMed:24568283). The pathway begins with the conversion of farnesyl pyrophosphate (FPP) to beta-trans-bergamotene by the membrane-bound beta-trans-bergamotene synthase af520. The multifunctional cytochrome P450 monooxygenase af510 then converts beta-trans-bergamotene into 5-keto-demethoxyfumagillol via several oxydation steps. 5-keto-demethoxyfumagillol is then subjected to successive C-6 hydroxylation and O-methylation by the dioxygenase af480 and O-methyltransferase af390-400, respectively, to yield 5-keto-fumagillol, which is then stereoselectively reduced by the keto-reductase af490 to 5R-hydroxy-seco-sesquiterpene. The next step is the polyketide transferase af380-catalyzed transfer of a dodecapentaenoyl group synthesized by the polyketide synthase af370 onto 5R-hydroxy-seco-sesquiterpene which leads to the production of prefumagillin. Finally, oxidative cleavage by the monooxygenase af470 converts prefumagillin to fumagillin (PubMed:24568283) (Probable).
Belongs to the ketopantoate reductase family.
Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
In contrast to other NRP synthetases, deletion of NRPS8 significantly increases the virulence, probably through aberrant innate immune recognition of the fungus.
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for l- to d- amino acid conversion) are present within the NRP synthetase. NRPS8 has the following architecture: A-T-C-A-T-E-C-A-T-C-T-E-C-A-T-C-A-T-C-A-T-E-C.
Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence. However, contarary to other nonribosomal peptide synthases, NRPS8 does not encode a secreted peptide, but has more a structural role since it is involved in germ tube formation.
Belongs to the eukaryotic ribosomal protein eL21 family.
Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.
Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 3 respiratory subunits cytochrome b, cytochrome c1 and Rieske protein, 2 core protein subunits, and additional low-molecular weight protein subunits. The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with cytochrome c oxidase (complex IV, CIV).
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Involved in the proteasome-dependent degradation of fructose-1,6-bisphosphatase.
Belongs to the glutamine synthetase family.
Component of the ribosomal small subunit (SSU) processome.
Involved in nucleolar processing of pre-18S ribosomal RNA.
Belongs to the snRNP Sm proteins family. SmF/LSm6 subfamily.
Belongs to the MICOS complex subunit Mic12 family.
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Belongs to the MIP/aquaporin (TC 1.A.8) family.
Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall morphogenesis (By similarity).
Involved in the initiation of assembly of the COPII coat required for the formation of transport vesicles from the endoplasmic reticulum (ER) and the selection of cargo molecules. Also involved in autophagy (By similarity).
Belongs to the transient receptor potential (TRP) ion channel family.
Component of the TIM22 complex, whose core is composed of TIM22 and TIM54, associated with the 70 kDa heterohexamer composed of TIM9 and TIM10 (or TIM8 and TIM13).
Essential component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as external driving force (By similarity).
Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs.
Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.
Probable helicase, member of the UBC2/RAD6 epistasis group. Functions with DNA repair protein RAD18 in error-free postreplication DNA repair. Involved in the maintenance of wild-type rates of instability of simple repetitive sequences such as poly(GT) repeats. Seems to be involved in maintaining a balance which acts in favor of error-prone non-homologous joining during DNA double-strand breaks repairs (By similarity).
Belongs to the WD repeat G protein beta family. Ribosomal protein RACK1 subfamily.
In the central section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily.
Belongs to the eukaryotic ribosomal protein eL22 family.
Belongs to the V-ATPase V0D/AC39 subunit family.
Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments. This subunit is a non-integral membrane component of the membrane pore domain and is required for proper assembly of the V0 sector. Might be involved in the regulated assembly of V1 subunits onto the membrane sector or alternatively may prevent the passage of protons through V0 pores.
V-ATPase is a heteromultimeric enzyme made up of two complexes: the ATP-hydrolytic V1 complex and the proton translocation V0 complex.
Belongs to the DEAD box helicase family. DDX54/DBP10 subfamily.
Putative mitochondrial redox protein which could be involved in the reduction of small toxic molecules.
Consists of at least two heavy chains and a number of intermediate and light chains.
Golgi membrane protein involved in vesicular trafficking.
Belongs to the methyltransferase superfamily. Trimethylguanosine synthase family.
Belongs to the XPG/RAD2 endonuclease family.
Acetyltransferase; part of the gene cluster that mediates the biosynthesis of pyripyropene A, a specific human acyl-coenzyme A:cholesterol acyltransferase 2 inhibitor (PubMed:20861902). The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase pyr1 (PubMed:20861902). Nicotinyl-CoA is then a substrate of polyketide synthase pyr2 to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase pyr6 to yield farnesyl-HPPO (PubMed:20861902). The next steps consist of an epoxidation of farnesyl-HPPO to epoxyfarnesyl-HPPO by FAD-dependent monooxygenase pyr5 and a cyclization of the terpenoid portion by the terpene cyclase pyr4 to yield deacetyl-pyripyropene E (PubMed:20861902). The 2 cytochrome P450 monooxygenases pyr3 and pyr9, and the 2 acetyltransferases pyr7 and pyr8 are involved in the conversion of deacetyl-pyripyropene E into pyripyropene A through several cycles of oxidation and acetylation steps (PubMed:20861902). Pyr7 acetylates deacetyl-pyripyropene E to pyripyropene E which is oxidized to 11-deacetyl-pyripyropene O by pyr3, which is in turn acetylated into pyripyropene O by pyr8 (PubMed:21224862, PubMed:26019565). Pyripyropene O is then oxidized to deacetyl-pyripyropene A by pyr9 (PubMed:21224862). Deacetyl-pyripyropene A is finally acetylated to pyripyropene A by pyr8 (PubMed:26019565).
Expression is regulated by the AcuK and AcuM transcription factors.
Results in increased resistance to the chitin synthesis inhibitor nikkomycin Z and causes increased damage to pulmonary epithelial cells and vascular endothelial cells, as well as increased pulmonary epithelial cell cytokine gene expression.
Transcription factor that seems to function as negative regulators of virulence by affecting the capacity to damage host cells and to stimulate a pro-inflammatory response.
Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of fumigermin that inhibits germination of spores of the inducing S.rapamycinicus, and thus helps the fungus to defend resources in the shared habitat against a bacterial competitor (PubMed:32083553). The partially reducing polyketide synthase fngA alone is sufficient for the production of fumigermin (PubMed:32083553). FgnA catalyzes the condensation of 3 malonyl-CoA units to an acetyl-CoA starter, and 3 methylations to yield fumigermin (PubMed:32083553). It is remarkable that the five cluster genes including fgnA are conserved in distantly related fungi, supporting the assumption of a fumigermin cluster; it is thus possible that originally all five genes were functional, but that the genes encoding tailoring enzymes became inactive from mutations, similar to the case of the fgnA gene in strains A1163 and Af293 (Probable).
Belongs to the GTR/RAG GTP-binding protein family.
GTPase involved in activation of the TORC1 signaling pathway, which promotes growth and represses autophagy in nutrient-rich conditions.
Belongs to the pseudouridine synthase TruD family.
Belongs to the glycosyltransferase 2 family.
Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans as well as the feruloyl-galactose and feruloyl-arabinose ester bonds in pectin.
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly (By similarity).
Vacuolar aspartic endopeptidase which is probably also secreted and contributes to virulence.
Belongs to the eukaryotic ribosomal protein eL36 family.
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. This subunit can bind 18S rRNA.
Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration.
Belongs to the adaptor complexes large subunit family.
Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA (By similarity).
Belongs to the DNA polymerase epsilon subunit B family.
Component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Belongs to the imidazoleglycerol-phosphate dehydratase family.
Belongs to the TrkH potassium transport family.
Belongs to the eukaryotic ATPase epsilon family.
Belongs to the WD repeat CDC20/Fizzy family.
Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Belongs to the ferric reductase (FRE) family.
Expression is repressed by iron in a sreA- and acuM-mediated way (PubMed:21062375, PubMed:21840411).
Ferric reductase involved in adaptation to iron starvation and which is most likely part of the reductive iron assimilatory system (RIA), a siderophore-independent high affinity iron uptake mechanism (PubMed:21840411).
Reduces ferrireductase activity and decreases biomass production during iron starvation but not during iron and copper sufficiency and copper starvation (PubMed:21840411). Increases sensitivity to hydrogen peroxide (PubMed:21840411).
Component of the ESCRT-I complex (endosomal sorting complex required for transport I), a regulator of vesicular trafficking process.
Belongs to the glycosyl hydrolase 16 family.
Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
Belongs to the type IB topoisomerase family.
Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
Decreases the virulence, increases the susceptibility to oxidative stress and exhibites altered conidial morphology and hydrophobicity.
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for l- to d- amino acid conversion) are present within the NRP synthetase. NRPS1 has the following architecture: A-T-E-C-A-C-A-T-C-A-T-E-C-T-C-T.
Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence. Contributes to improved fungal tolerance against oxidative stress, during the infection process.
The thiolation domains are 4'-phosphopantetheinylated.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
Atrochrysone carboxyl ACP thioesterase; part of the gene cluster that mediates the biosynthesis of trypacidin, a mycotoxin with antiprotozoal activity and that plays a role in the infection process (PubMed:26278536, PubMed:26242966). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) tpcC (PubMed:26242966). The atrochrysone carboxyl ACP thioesterase tpcB then breaks the thioester bond and releases the atrochrysone carboxylic acid from tpcC (PubMed:26242966). The decarboxylase tpcK converts atrochrysone carboxylic acid to atrochrysone which is further reduced into emodin anthrone (PubMed:26242966). The next step is performed by the emodin anthrone oxygenase tpcL that catalyzes the oxidation of emodin anthrone to emodin (PubMed:26242966). Emodin O-methyltransferase encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin to form questin (PubMed:26242966). Ring cleavage of questin by questin oxidase tpcI leads to desmethylsulochrin via several intermediates including questin epoxide (By similarity). Another methylation step catalyzed by tpcM leads to the formation of sulochrin which is further converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes the conversion of monomethylsulfochrin to trypacidin (PubMed:26242966). Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)), thus triggering host necrotic cell death (PubMed:22319557). The trypacidin pathway is also able to produce endocrocin via a distinct route from the endocrocin Enc pathway (PubMed:26242966).
Belongs to the metallo-beta-lactamase superfamily.
Impairs the production of trypacidin and pathway intermediates including questin (PubMed:26278536, PubMed:26242966).
Belongs to the polysaccharide lyase 4 family.
Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone of pectin (By similarity).
Cell surface ferroxidase; part of the reductive iron assimilatory system (RIA), a siderophore-independent high affinity iron uptake mechanism (PubMed:15504822). Required to oxidize Fe(2+) and release it from the transporter (By similarity).
Expression is up-regulated during iron starvation and is controlled by the GATA-type transcription factor sreA (PubMed:15504822, PubMed:18721228).
DNA helicase which participates in several chromatin remodeling complexes, including the SWR1 and the INO80 complexes. The SWR1 complex mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. The INO80 complex remodels chromatin by shifting nucleosomes and is involved in DNA repair. Also involved in pre-rRNA processing (By similarity).
May form heterododecamers with RVB1. Component of the SWR1 chromatin remodeling complex, the INO80 chromatin remodeling complex, and of the R2TP complex (By similarity).
Belongs to the transaldolase family. Type 1 subfamily.
Catalyzes the rate-limiting step of the non-oxidative phase in the pentose phosphate pathway. Catalyzes the reversible conversion of sedheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into erythrose-4-phosphate and beta-D-fructose 6-phosphate.
Non-catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments.
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex attached to an integral membrane V0 proton pore complex.
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for l- to d- amino acid conversion) are present within the NRP synthetase. NRPS7 has the following architecture: A-T-C-A-T-C.
Belongs to the eukaryotic ribosomal protein eS25 family.
Exhibits a reduced copper content and leads to cell decolorization due to lower laccase activity, when ctrA2 is also deleted.
Expression is up-regulated by copper deficiency and decreased dramatically when the copper concentration increases (PubMed:25281782). Expression is up-regulated by the deletion of ctrA2 (PubMed:25281782).
High-affinity copper transporter of plasma membrane that mediates copper uptake under low copper conditions (PubMed:25281782). The mechanism driving the transmembrane transport of copper has still to be determined (Probable). Acts as a potential virulence factor (PubMed:25281782).
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Belongs to the V-ATPase F subunit family.
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments.
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and VOA1).
Required for correct functioning of the GINS complex, a complex that plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex seems to bind preferentially to single-stranded DNA.
The GINS complex plays an essential role in the initiation of DNA replication.
Involved in the small subunit (SSU) processome assembly and function, and in the 18S rRNA synthesis. Required for the early cleavages at sites A0, A1 and A2 (By similarity).
Component of the NOP7 complex, composed of erb1, nop7 and ytm1. The complex is held together by erb1, which interacts with nop7 via its N-terminal domain and with ytm1 via a high-affinity interaction between the seven-bladed beta-propeller domains of the 2 proteins. The NOP7 complex associates with the 66S pre-ribosome.
Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome.
Belongs to the RNA cytidine acetyltransferase family. NAT10 subfamily.
RNA cytidine acetyltransferase with specificity toward both 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine (ac4C) in 18S rRNA. Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis. Catalyzes the formation of ac4C in serine and leucine tRNAs. Requires the tRNA-binding adapter protein TAN1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation.
Plays a role in determining ER morphology.
The C4-type zinc finger motif is necessary both for its ER three-way tubular junction localization and formation.
Belongs to the cyclophilin-type PPIase family.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Component of the SWR1 chromatin-remodeling complex and of the NuA4 histone acetyltransferase complex.
Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4 and H2A. The NuA4 complex is also involved in DNA repair. Yaf9 may also be required for viability in conditions in which the structural integrity of the spindle is compromised (By similarity).
The coiled-coil domain is required for assembly into the NuA4 complex.
Belongs to the RNA polymerase beta chain family.
Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs (By similarity).
Belongs to the major facilitator superfamily. EmrB family.
Expression is induced upon voriconazole treatment (PubMed:16622700). Expression is also induced during germination (PubMed:18796135).
Catalyzes the reversible hydration of cis-homoaconitate to (2R,3S)-homoisocitrate, a step in the alpha-aminoadipate pathway for lysine biosynthesis.
Expression is slightly increased during growth on ethanol.
Major secreted chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Plays a role in the morphogenesis and autolysis (By similarity).
Methylxanthine drugs surch as theophylline, caffeine and pentoxifylline, as well as the two cyclic peptide natural products argifin and argadin, act as specific inhibitors.
This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds.
Catalyzes the synthesis of activated sulfate.
AFL adopts the six-bladed beta-propeller fold and contains 6 binding sites per monomer, each located between two adjacent blades (PubMed:25760594). The 6 binding sites that are non-equivalent, and owing to minor differences in amino-acid composition they exhibit a marked difference in specific ligand recognition (PubMed:24340081, PubMed:25760594).
Belongs to the fungal fucose-specific lectin family.
Expressed in conidia (PubMed:27058347, PubMed:24340081).
Increases lung infection and lung injury by A.fumigatus (PubMed:27058347).
Lectins have particular value as specific probes for investigating the distribution, structure and biological function of carbohydrate chains on the cell surface of animal, plant, and microorganism because of their specificity for defined carbohydrate structures. AFL is suitable for detecting core fucose on cell surface glycoproteins (PubMed:25760594).
Multispecific lectin that is able to recognize L-fucose in all possible linkages (PubMed:23695231, PubMed:27058347, PubMed:24340081, PubMed:25760594). These could be found not only in decomposed plant matter in soil, which is the natural environment for A.fumigatus, but also in various epitopes on human tissues (PubMed:25760594). Mediates binding of A.fumigatus conidia to airway mucin in a fucose dependent manner (PubMed:27058347). Stimulates IL-8 production by human bronchial cells in a dose-dependent manner, contributing to the inflammatory response observed upon the exposure of a patient to A.fumigatus, and thus might be an important virulence factor involved in an early stage of A.fumigatus infection (PubMed:24340081).
E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 and ATG8 for its conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production.
Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly.
Interacts with histone H3 and histone H4.
Completely abolishes the production of fumagillin but leads to the accumulation of the intermediate 6-demethoxyfumagillin (PubMed:24082142, PubMed:24568283).
Dioxygenase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) (PubMed:23488861, PubMed:24568283). Within the pathway, the dioxygenase af480 acts as a 5-dehydro-6-demethoxyfumagillol dioxygenase that hydroylates 5-keto-demethoxyfumagillol at position C-6 (PubMed:24568283). The pathway begins with the conversion of farnesyl pyrophosphate (FPP) to beta-trans-bergamotene by the membrane-bound beta-trans-bergamotene synthase af520. The multifunctional cytochrome P450 monooxygenase af510 then converts beta-trans-bergamotene into 5-keto-demethoxyfumagillol via several oxydation steps. 5-keto-demethoxyfumagillol is then subjected to successive C-6 hydroxylation and O-methylation by the dioxygenase af480 and O-methyltransferase af390-400, respectively, to yield 5-keto-fumagillol, which is then stereoselectively reduced by the keto-reductase af490 to 5R-hydroxy-seco-sesquiterpene. The next step is the polyketide transferase af380-catalyzed transfer of a dodecapentaenoyl group synthesized by the polyketide synthase af370 onto 5R-hydroxy-seco-sesquiterpene which leads to the production of prefumagillin. Finally, oxidative cleavage by the monooxygenase af470 converts prefumagillin to fumagillin (PubMed:24568283) (Probable).
Belongs to the glycosyl hydrolase 38 family.
Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport.
ATP-dependent rRNA helicase required for pre-ribosomal RNA processing. Involved in the maturation of the 35S-pre-rRNA and to its cleavage to mature 18S rRNA.
Belongs to the DEAD box helicase family. DDX47/RRP3 subfamily.
Resulted in loss of trypacidin production (PubMed:26278536, PubMed:26242966).
Transcriptional coactivator; part of the gene cluster that mediates the biosynthesis of trypacidin, a mycotoxin with antiprotozoal activity and that plays a role in the infection process (PubMed:26278536, PubMed:26242966). With tpcE, coregulates the production of trypacidin (PubMed:26278536, PubMed:26242966).
Belongs to the SSU72 phosphatase family.
Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Ssu72 is required for 3'-end formation of snoRNAs (By similarity).
Component of the cleavage and polyadenylation factor (CPF) complex.
Processively dephosphorylates Ser-5 of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (rpb1).
Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
May mediate the reduction of outer membrane cytochrome b5.
Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA polymerase subunit family.
Microtubule binding protein that promotes the stabilization of dynamic microtubules. Required for mitotic spindle formation (By similarity).
In the N-terminal section; belongs to the cytochrome P450 family.
Belongs to the aerobic coproporphyrinogen-III oxidase family.
Belongs to the polyketide transferase af380 family.
Belongs to the FIT family. Fungal FIT2B/SCS3 subfamily.
Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate. Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen. This catalytic activity is required for maintaining ER structure and for lipid droplets (LDs) biogenesis, which are lipid storage organelles involved in maintaining lipid and energy homeostasis. May directly bind to diacylglycerol (DAGs) and triacylglycerol, which is also important for LD biogenesis. May support directional budding of nacent LDs from the ER into the cytosol by reducing DAG levels at sites of LD formation. May play a role in the regulation of cell morphology and cytoskeletal organization. Involved in phospholipid biosynthesis.
Belongs to the concentrative nucleoside transporter (CNT) (TC 2.A.41) family.
Belongs to the NAD(P)-dependent epimerase/dehydratase family.
The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
The glycine cleavage system is composed of four proteins: P, T, L and H.
Belongs to the WD repeat MDV1/CAF4 family.
Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Belongs to the Mediator complex subunit 31 family.
Acyltransferase; part of the siderophore biosynthetic pathway (PubMed:21622789). Aspergillus fumigatus produces 4 types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake and intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial iron distribution and storage. TAFC consists of 3 N(2)-acetyl-N(5)-anhydromevalonyl-N(5)-hydroxyornithine residues cyclically linked by ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-(N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of all four siderophores depends on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA (PubMed:15504822, PubMed:16113265). Subsequently, the pathways for biosynthesis of extra- and intracellular siderophores split (PubMed:17845073). For biosynthesis of extracellular siderophores, the transacylase sidF transfers anhydromevalonyl to N(5)-hydroxyornithine (PubMed:17845073). The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by sidI and sidH respectively (PubMed:22106303). The acetylation of N(5)-hydroxyornithine for FC biosynthesis involves the constitutively expressed sidL (PubMed:21622789). FC is hydroxylated to HFC by an as yet uncharacterized enzyme during conidiation (PubMed:17845073). Assembly of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal peptide synthetases (NRPS), sidD and sidC respectively (PubMed:17845073). Subsequently, sidG catalyzes N2-acetylation of FsC for forming TAFC (PubMed:17845073). Both extra- and intracellular siderophores are crucial for growth during iron limitation and virulence (PubMed:16113265).
Decreases ferricrocin (FC) biosynthesis during iron starvation and completely blocks FC biosynthesis during iron-replete growth (PubMed:21622789). Blocks conidial accumulation of FC-derived hydroxyferricrocin (HFC) under iron-replete conditions, which delays germination and decreases the size of conidia and their resistance to oxidative stress (PubMed:21622789).
Expression is not affected by iron availability and is not regulated by the iron regulator sreA (PubMed:21622789).
Alpha/beta hydrolase; part of the gene cluster that mediates the biosynthesis of pseurotin A, a competitive inhibitor of chitin synthase and an inducer of nerve-cell proliferation (PubMed:24082142, PubMed:24939566). The PKS-NRPS hybrid synthetase psoA is responsible for the biosynthesis of azaspirene, one of the first intermediates having the 1-oxa-7-azaspiro[4,4]-non-2-ene-4,6-dione core of pseurotin, via condensation of one acetyl-CoA, 4 malonyl-CoA, and a L-phenylalanine molecule (PubMed:24082142, PubMed:24939566). The dual-functional monooxygenase/methyltransferase psoF seems to be involved in the addition of the C3 methyl group onto the pseurotin scaffold (PubMed:24939566). Azaspirene is then converted to synerazol through 4 steps including oxidation of C17 by the cytochrome P450 monooxygenase psoD, O-methylation of the hydroxy group of C8 by the methyltransferase psoC, and the trans-to-cis isomerization of the C13 olefin by the glutathione S-transferase psoE (PubMed:24939566). The fourth step of synerazol production is performed by the dual-functional monooxygenase/methyltransferase psoF which seems to catalyze the epoxidation of the intermediate deepoxy-synerazol (PubMed:24939566). Synerazol can be attacked by a water molecule nonenzymatically at two different positions to yield two diol products, pseurotin A and pseurotin D (PubMed:24939566).
Belongs to the AB hydrolase superfamily. FUS2 hydrolase family.
Results in significant reduction of pseurotin production (PubMed:24082142).
Belongs to the polysaccharide lyase 3 family.
Belongs to the eukaryotic ribosomal protein eL29 family.
Component of the GINS complex which is a heterotetramer of sld5, psf1, psf2 and psf3.
Belongs to the peroxiredoxin family. Prx6 subfamily.
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively.
Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family.
ATP-binding RNA helicase involved in 40S ribosomal subunit biogenesis and is required for the normal formation of 18S rRNAs through pre-rRNA processing at A0, A1 and A2 sites. Required for vegetative growth (By similarity).
Belongs to the DEAD box helicase family. DDX49/DBP8 subfamily.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Not involved in the GTP-dependent ribosomal translocation step during translation elongation.
Acetyl-CoA acetyltransferase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (Ref.6). Erg10B catalyzes the formation of acetoacetyl-CoA from acetyl-CoA (Ref.6). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase erg10B that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases erg13A and erg13B then condense acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases hmg1 and hmg2. Mevalonate is also a precursor for the extracellular siderophore triacetylfusarinine C (TAFC) (PubMed:16110826, PubMed:22106303) (Probable).
Activity is increased by monovalent cations such as K(+), Rb(+) or Cs(+).
Belongs to the thiolase-like superfamily. Thiolase family.
Even though it is not involved in catalysis directly, the Cl(-) anion stabilizes the catalytic site via both direct and water-mediated hydrogen bonds to catalytic residues and residues adjacent.
Belongs to the triosephosphate isomerase family.
Belongs to the damage-control phosphatase family. Sugar phosphate phosphatase III subfamily.
Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism.
Subfamily III proteins have a conserved RTxK motif about 40-50 residues from the C-terminus; the threonine may be replaced by serine or cysteine.
Belongs to the AB hydrolase superfamily. MetX family.
Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family.
Belongs to the galactose-1-phosphate uridylyltransferase type 1 family.
Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.
Belongs to the eukaryotic NMN adenylyltransferase family.
Positive regulator of phosphatidylinositol 4,5-bisphosphate turnover and negatively regulates signaling through the cell integrity pathway. Involved in rDNA silencing (By similarity).
Belongs to the sterol desaturase family.
Delta(7)-sterol 5(6)-desaturase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:16436696, PubMed:18191972). Erg3C is a minor delta(7)-sterol 5(6)-desaturase within the ergosterol pathway, erg3B being the major one (PubMed:16436696, PubMed:18191972). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (PubMed:16110826, PubMed:18191972) (Probable).
The histidine box domains may contain the active site and/or be involved in metal ion binding.
Abolishes the production of endocrocin (PubMed:22492455, PubMed:23592999). Leads to attenuated virulence in a toll-deficient Drosophila invasive aspergillosis model (PubMed:23592999).
Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of endocrocin, a simple anthraquinone interesting for many biotechnological applications (PubMed:22492455, PubMed:23592999). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) encA (PubMed:22492455). The atrochrysone carboxyl ACP thioesterase encB then breaks the thioester bond and releases the atrochrysone carboxylic acid from encA (PubMed:22492455). The atrochrysone carboxylic acid is then converted to endocrocin anthrone which is further oxidized into endocrocin by the anthrone oxygenase encC (PubMed:22492455). The exact function of encD has not been identified yet, but it negatively regulates endocrocin production, likely through the modification of endocrocin itself (PubMed:22492455).
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.
Component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation (By similarity). Controls the production of several secondary metabolites, including gliotoxin, but does not contribute to pathogenicity (PubMed:23638376).
Impairs tri- and dimethylation of H3K4 (PubMed:23638376). Results in sensitivity to 6-azauracil (PubMed:23638376). Leads to increased production of several secondary metabolites, including gliotoxin (PubMed:23638376). Does not affect pathogenicity in a murine model and the Toll-deficient Drosophila model of invasive aspergillosis (PubMed:23638376).
Belongs to the complex I 23 kDa subunit family.
Components of the endosome-vacuole trafficking pathway that regulates nutrient transport. May be involved in processes which determine whether plasma membrane proteins are degraded or routed to the plasma membrane.
Belongs to the NADH dehydrogenase family.
Second step of mRNA capping. Transfer of the GMP moiety of GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction intermediate.
Involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs.
Belongs to the DHHC palmitoyltransferase family. AKR/ZDHHC17 subfamily.
Palmitoyltransferase specific for casein kinase 1.
Belongs to the metallo-dependent hydrolases superfamily. NagA family.
Binds 1 divalent metal cation per subunit.
Belongs to the threonine aldolase family.
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the isocyanide xanthocillin and its derivatives (PubMed:29844112). The first step of the pathway consists in the conversion of tyrosine into a vinyl-isonitrile intermediate by the isocyanide synthase xanB (PubMed:29844112). Subsequent oxidative dimerization of this intermediate to form xanthocillin may involve the cytochrome P450 monooxygenase xanG, whose expression is coregulated with that of XanB (PubMed:29844112). Xanthocillin can be further modified by the isonitrile hydratase-like protein xanA which introduces N-formyl groups and the methyltransferase xanE which introduces methyl groups, leading to the production of several derivatives including fumiformamide (PubMed:29844112). Finally, fumiformamide can be subject to both oxidative and reductive cyclization to yield melanocins E and F, respectively (PubMed:29844112).
Belongs to the eukaryotic ribosomal protein eL18 family.
Belongs to the bacterial ribosomal protein bL17 family.
Involved in the organization of the mitochondrial membranes and the global structure of the mitochondria. Also required for mitochondrial distribution and mobility as well as for the maintenance of mitochondrial DNA nucleoids structures.
Associates with the respiratory chain complex III/complex IV supercomplex.
Cytochrome c oxidase subunit which plays a role in assembly of respiratory supercomplexes.
Belongs to the paxM FAD-dependent monooxygenase family.
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of pyripyropene A, a specific human acyl-coenzyme A:cholesterol acyltransferase 2 inhibitor (PubMed:20861902). The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase pyr1 (PubMed:20861902). Nicotinyl-CoA is then a substrate of polyketide synthase pyr2 to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase pyr6 to yield farnesyl-HPPO (PubMed:20861902). The next steps consist of an epoxidation of farnesyl-HPPO to epoxyfarnesyl-HPPO by FAD-dependent monooxygenase pyr5 and a cyclization of the terpenoid portion by the terpene cyclase pyr4 to yield deacetyl-pyripyropene E (PubMed:20861902). The 2 cytochrome P450 monooxygenases pyr3 and pyr9, and the 2 acetyltransferases pyr7 and pyr8 are involved in the conversion of deacetyl-pyripyropene E into pyripyropene A through several cycles of oxidation and acetylation steps (PubMed:20861902). Pyr7 acetylates deacetyl-pyripyropene E to pyripyropene E which is oxidized to 11-deacetyl-pyripyropene O by pyr3, which is in turn acetylated into pyripyropene O by pyr8 (PubMed:21224862, PubMed:26019565). Pyripyropene O is then oxidized to deacetyl-pyripyropene A by pyr9 (PubMed:21224862). Deacetyl-pyripyropene A is finally acetylated to pyripyropene A by pyr8 (PubMed:26019565).
Belongs to the bZIP family. YAP subfamily.
Contains two cysteine rich domains (CRD), referred to as the N- and C-terminal CRD's, n-CRD and c-CRD, respectively. A nuclear export signal is embedded in the c-CRD, with which the nuclear export proteins interact only in the absence of disulfide bonds (or otherwise oxidized cysteines) within the c-CRD or between the c-CRD and the n-CRD.
Depending on the oxidative stress inducing agent, yap1 can undergo two distinct conformational changes, both involving disulfide bond formation, and both masking the nuclear export signal, thus abolishing nuclear export.
Leads to increased sensitivity against H(2)O(2) and menadione (PubMed:17921349, PubMed:27748436). Attenuates antifungal susceptibility to voriconazole (PubMed:20376564). Does not show attenuated virulence in a murine model of Aspergillus infection (PubMed:17921349, PubMed:18608886).
Transcription activator involved in oxidative stress response and redox homeostasis (PubMed:17921349, PubMed:18608886, PubMed:18651311, PubMed:20376564, PubMed:27748436). Regulates the transcription of genes encoding antioxidant enzymes and components of the cellular thiol-reducing pathways, including thioredoxin peroxidase (aspF3), cytochrome peroxidase, and the protein AFUA_3G00730, which appears to belong to the glutathione S-transferase family (PubMed:17921349, PubMed:18651311). Proteins of the protein degradation pathway are also regulated by yap1, as well the p-nitroreductase family protein AFUA_5G09910 (PubMed:17921349). May be involved in antifungal resistance to voriconazole (PubMed:20376564).
Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity.
Belongs to the peptidase M24 family. SPT16 subfamily.
Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II (By similarity).
Forms a stable heterodimer with pob3. The spt16-pob3 dimer weakly associates with multiple molecules of nhp6 to form the FACT complex (By similarity).
Belongs to the PIGG/PIGN/PIGO family. PIGO subfamily.
Belongs to the methyltransferase superfamily. Fibrillarin family.
Belongs to the actin-binding proteins ADF family.
Belongs to the WD repeat BOP1/ERB1 family.
Long-chain fatty alcohol oxidase involved in the omega-oxidation pathway of lipid degradation.
Belongs to the Mediator complex subunit 6 family.
Belongs to the eukaryotic ribosomal protein eL28 family.
ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes (By similarity).
Belongs to the DEAD box helicase family. DDX3/DED1 subfamily.
HMG-CoA reductase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity). Hmg1 and hmg2 catalyze the reduction of hydroxymethylglutaryl-CoA (HMG-CoA) to mevalonate (By similarity). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase erg10B that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases erg13A and erg13B then condense acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases hmg1 and hmg2. Mevalonate is also a precursor for the extracellular siderophore triacetylfusarinine C (TAFC) (PubMed:16110826, PubMed:22106303) (Probable).
Belongs to the actin family. ARP4 subfamily.
Chromatin interaction component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Is required for NuA4 complex integrity. Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair (By similarity).
Component of the NuA4 histone acetyltransferase complex, of the INO80 chromatin remodeling complex, and of the SWR1 chromatin remodeling complex.
Belongs to the precorrin methyltransferase family.
Belongs to the Necrosis inducing protein (NPP1) family.
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.
Belongs to the lysophospholipase family.
Catalyzes the release of fatty acids from lysophospholipids.
Transcription factor involved in RNA polymerase II transcription regulation. May function in both SPT15/TBP post-recruitment and recruitment steps of transcription (By similarity).
Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase (By similarity).
Belongs to the RNase HII family. Eukaryotic subfamily.
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Belongs to the alpha-IPM synthase/homocitrate synthase family. Homocitrate synthase LYS20/LYS21 subfamily.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. uL10 forms part of the P stalk that participates in recruiting G proteins to the ribosome.
Prenyltransferase that catalyzes reverse prenylation at position N-1 of tryptophan-containing cyclic dipeptides (PubMed:17525915, PubMed:35767141, PubMed:18383240, PubMed:19113967, PubMed:19421461, PubMed:33643664). Accepts only dimethylallyl diphosphate (DMAPP) as the prenyl donor but shows broad substrate specificities toward its aromatic substrates (PubMed:17525915, PubMed:18383240, PubMed:19113967, PubMed:19421461, PubMed:33643664, PubMed:35767141). Shows also tryptophan aminopeptidase activity with preference for linear peptides containing a tryptophanyl moiety at the N-terminus (PubMed:18635009).
Belongs to the gluconokinase GntK/GntV family.
Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
Belongs to the glycosyltransferase 39 family.
Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Belongs to the Mediator complex subunit 21 family.
Involved in the lipid remodeling steps of GPI-anchor maturation.
Histone methyltransferase that trimethylates histone H3 'Lys-36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression.
Belongs to the DHHC palmitoyltransferase family. PFA3 subfamily.
Palmitoyltransferase specific for VAC8. Palmitoylates VAC8 at one or more of its N-terminal cysteine residues, which is required for its proper membrane localization (By similarity).
Belongs to the Mediator complex subunit 13 family.
Component of the SRB8-11 complex, which itself associates with the Mediator complex.
Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex.
Interacts with missfolded ER lumenal proteins.
Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation (By similarity).
Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.
In the C-terminal section; belongs to the MoeA family.
Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are bound between subunits.
Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Belongs to the peptidase M67A family. CSN6 subfamily.
Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes.
Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function.
Belongs to the endopolyphosphatase PPN1 family.
Catalyzes the hydrolysis of inorganic polyphosphate (polyP) chains of many hundreds of phosphate residues into shorter lengths.
Required for synthesis of 60S ribosomal subunits and the transport of pre-ribosomes from the nucleoplasm to the cytoplasm.
Belongs to the WD repeat LIS1/nudF family.
Dimerization mediated by the LisH domain may be required to activate dynein.
Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for nuclear migration during vegetative growth as well as development. Required for retrograde early endosome (EE) transport from the hyphal tip. Required for localization of dynein to the mitotic spindle poles. Recruits additional proteins to the dynein complex at SPBs.
Self-associates. Interacts with nudE and dynein.
Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
Completely abolishes the production of fumagillin (PubMed:24082142).
Polyketide transferase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) (PubMed:23488861, PubMed:24568283). Within the pathway, the polyketide transferase af380 catalyzes the transfer of a dodecapentaenoyl group synthesized by the polyketide synthase af370 onto 5R-hydroxy-seco-sesquiterpene to produce prefumagillin (PubMed:23488861). The pathway begins with the conversion of farnesyl pyrophosphate (FPP) to beta-trans-bergamotene by the membrane-bound beta-trans-bergamotene synthase af520. The multifunctional cytochrome P450 monooxygenase af510 then converts beta-trans-bergamotene into 5-keto-demethoxyfumagillol via several oxydation steps. 5-keto-demethoxyfumagillol is then subjected to successive C-6 hydroxylation and O-methylation by the dioxygenase af480 and O-methyltransferase af390-400, respectively, to yield 5-keto-fumagillol, which is then stereoselectively reduced by the keto-reductase af490 to 5R-hydroxy-seco-sesquiterpene. The next step is the polyketide transferase af380-catalyzed transfer of a dodecapentaenoyl group synthesized by the polyketide synthase af370 onto 5R-hydroxy-seco-sesquiterpene which leads to the production of prefumagillin. Finally, oxidative cleavage by the monooxygenase af470 converts prefumagillin to fumagillin (PubMed:24568283) (Probable).
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Homohexamer or homoheptamer. Organized in a ring with a central cavity.
Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
Irreversibly catalyzes the reduction of fumarate to succinate.
Impairs the production of trypacidin and pathway intermediates including questin (PubMed:26278536, PubMed:26242966). Leads to enhanced phagocytosis ratio by macrophages and amoebae (PubMed:26278536).
Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of trypacidin, a mycotoxin with antiprotozoal activity and that plays a role in the infection process (PubMed:26278536, PubMed:26242966). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) tpcC (PubMed:26242966). The atrochrysone carboxyl ACP thioesterase tpcB then breaks the thioester bond and releases the atrochrysone carboxylic acid from tpcC (PubMed:26242966). The decarboxylase tpcK converts atrochrysone carboxylic acid to atrochrysone which is further reduced into emodin anthrone (PubMed:26242966). The next step is performed by the emodin anthrone oxygenase tpcL that catalyzes the oxidation of emodin anthrone to emodin (PubMed:26242966). Emodin O-methyltransferase encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin to form questin (PubMed:26242966). Ring cleavage of questin by questin oxidase tpcI leads to desmethylsulochrin via several intermediates including questin epoxide (By similarity). Another methylation step catalyzed by tpcM leads to the formation of sulochrin which is further converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes the conversion of monomethylsulfochrin to trypacidin (PubMed:26242966). Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)), thus triggering host necrotic cell death (PubMed:22319557). The trypacidin pathway is also able to produce endocrocin via a distinct route from the endocrocin Enc pathway (PubMed:26242966).
Belongs to the PI3/PI4-kinase family. Type III PI4K subfamily.
Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis.
Catalyzes the isomerization of citrate to isocitrate via cis-aconitate, a step in the citric acid cycle. Also catalyzes the reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine biosynthesis.
Constitutively expressed on glucose medium and increased expression on ethanol.
The fermenting yeast S.cerevisiae has 2 aconitases, ACO1 essential for the citric acid cycle, and ACO2 specifically and exclusively contributing to lysine biosynthesis. In contrast, in respiring filamentous fungi the ACO2 homologs (acoB) seem enzymatically inactive and the ACO1 homolog (acoA) is solely responsible for these functions.
Belongs to the 6-phosphogluconate dehydrogenase family.
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Belongs to the proteasome subunit S3 family.
Belongs to the bacterial ribosomal protein bS6 family.
Belongs to the alkaline ceramidase family.
Expression is under the control of StuA, which is responsible for transcriptional activation during acquisition of developmental competence.
In contrast to other A.fumigatus strains, strain ATCC MYA-4609 does not produce indole alkaloids such as fumitremorgins and verruculogen. While the biosynthetic pathway is complete, a variation in the O-methyltransferase FtmD (AC Q4WAW6) abolishes production of the tryprostatin A intermediate (PubMed:23649274).
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for l- to d- amino acid conversion) are present within the NRP synthetase. NRPS13 has the following architecture: A-T-C-A-T-C.
Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities (PubMed:16755625, PubMed:23649274). The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA (PubMed:16755625, PubMed:17464044). Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B (PubMed:16000710, PubMed:21105662, PubMed:23090579). The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively (PubMed:19226505). The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B (PubMed:18683158). Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties (PubMed:19763315). In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Belongs to the enhancer of polycomb family.
Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Involved in gene silencing by neighboring heterochromatin, blockage of the silencing spreading along the chromosome, and required for cell cycle progression through G2/M (By similarity).
Belongs to the intradiol ring-cleavage dioxygenase family.
Belongs to the casein kinase 2 subunit beta family.
Regulatory subunit of casein kinase II/CK2 (By similarity). As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine.
Regulatory subunit of casein kinase II/CK2. As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine.
Tetramer of two alpha and two beta subunits.
Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization (By similarity).
Component of the PAN1 actin cytoskeleton-regulatory complex.
Component of a multi-subunit COQ enzyme complex, composed of at least coq3, coq4, coq5, coq6, coq7 and coq9.
Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides.
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation.
Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes.
Regulates also the sphingolipid metabolism.
Delta(7)-sterol 5(6)-desaturase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:16436696, PubMed:18191972). Erg3A is a minor delta(7)-sterol 5(6)-desaturase within the ergosterol pathway, erg3B being the major one (PubMed:16436696, PubMed:18191972). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (PubMed:16110826, PubMed:18191972) (Probable).
Does not affect the susceptibility to amphotericin B, itraconazole, fluconazole, voriconazole, and ketoconazole.
In the 2nd section; belongs to the EPSP synthase family.
In the 3rd section; belongs to the shikimate kinase family.
In the 4th section; belongs to the type-I 3-dehydroquinase family.
In the C-terminal section; belongs to the shikimate dehydrogenase family.
In the N-terminal section; belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.
The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis.
Belongs to the class I-like SAM-binding methyltransferase superfamily. METTL21 family. EFM6 subfamily.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 1-alpha.
Belongs to the glycosyltransferase 22 family.
Belongs to the mitochondrion-specific ribosomal protein mL40 family.
Belongs to the nucleoporin Nup85 family.
Component of the nuclear pore complex (NPC).
Functions as a component of the nuclear pore complex (NPC).
In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.
Belongs to the cyclophilin-type PPIase family. PPIase B subfamily.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
Belongs to the alkaline phosphatase family.
Belongs to the band 7/mec-2 family. Flotillin subfamily.
Belongs to the NtaA/SnaA/DszA monooxygenase family.
Belongs to the glycosyl hydrolase 28 family.
Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall (By similarity).
Belongs to the AB hydrolase superfamily. LDAH family.
Belongs to the DNA polymerase delta/II small subunit family.
Secreted tripeptidyl-peptidase which degrades proteins at acidic pHs and is involved in virulence.
Activated by threonine and tyrosine phosphorylation.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily.
Belongs to the cysteine dioxygenase family.
Belongs to the MsrB Met sulfoxide reductase family.
Belongs to the GHMP kinase family. GalK subfamily.
Involved in vacuolar transport and vacuole pH homeostasis. Also required for cytokinesis (By similarity).
Belongs to the eukaryotic ribosomal protein eL14 family.
Expression is positively regulated by the atrR transcription factor (PubMed:28052140). Expression is induced upon voriconazole treatment (PubMed:16622700, PubMed:24123268). Expression is increased in clinical azole-resistant isolates (PubMed:23580559, PubMed:32209680). In particular F20140, F18304 and F18454 show over 25-fold greater basal expression levels, whereas F19980 (7.2-fold), F20063 (6.5-fold), F20451 (3.6-fold), F18454 (5.1-fold) and F15483 (2.1-fold) also show significantly raised levels of basal expression (PubMed:23580559).
Pleiotropic ABC efflux transporter that shows a strong substrate specificity for the azole class of drugs such as lotrimazole (CLT), fluconazole (FLC), itraconazole (ITC), ketoconazole (KTC), posaconazole (POS), tebuconazole (TEBZ), and voriconazole (VRC) (Probable) (PubMed:22509997, PubMed:23580559, PubMed:24123268, PubMed:28264842, PubMed:32209680). Is also able to transport rhodamine 6G (R-6G), a known substrate for many ABC transporters (PubMed:32209680). Required for normal pathogenesis in a Galleria mellonella (greater wax moth) infection model (PubMed:24123268).
Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.
Belongs to the protein-tyrosine phosphatase family. Non-receptor class CDC14 subfamily.
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Associates with the NTC complex (or PRP19-associated complex). The NTC complex associates with the spliceosome after the release of the U1 and U4 snRNAs and forms the CWC spliceosome subcomplex reminiscent of a late-stage spliceosome.
Involved in pre-mRNA splicing. May function at or prior to the first catalytic step of splicing at the catalytic center of the spliceosome. May do so by stabilizing the catalytic center or the position of the RNA substrate (By similarity).
Belongs to the cytochrome c oxidase subunit 5A family.
Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of a catalytic core of 3 subunits and several supernumerary subunits.
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar4-20 subfamily.
Histone methyltransferase that trimethylates 'Lys-20' of histone H4 to form H4K20me3.
Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome.
Small GTPase required for proper nuclear import of RNA polymerase II (RNAPII). May act at an RNAP assembly step prior to nuclear import.
Belongs to the radical SAM superfamily. Biotin synthase family.
Belongs to the heat shock protein 70 family.
Belongs to the glycosyl hydrolase 53 family.
Endogalactanase involved in the degradation of plant cell wall polysaccharides, and more particularly of hairy regions of pectin.
Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan (By similarity).
In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily.
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and mocs2a to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards urm1 and mocs2a. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; nfs1 probably acting as a sulfur donor for thiocarboxylation reactions (By similarity).
Belongs to the class I-like SAM-binding methyltransferase superfamily. UbiG/COQ3 family.
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Belongs to the glutathione peroxidase family.
Impairs the production of ergot alkaloids including festuclavine, fumigaclavine A, fumigaclavine B and fumigaclavine C (PubMed:15933009).
Tryptophan dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:23435153, PubMed:26972831). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:15870460, PubMed:23435153). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482, PubMed:21409592). EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482). EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482). Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831). Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909).
Interacts with newly synthesized monoglucosylated glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity).
C-8 sterol isomerase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:16110826) (Probable). Erg2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (PubMed:16110826, PubMed:18191972) (Probable).
4-hydroxyphenylpyruvate dioxygenase; part of the L-tyrosine degradation gene cluster that mediates the biosynthesis of the brownish pigment pyomelanin as an alternative melanin (PubMed:19028908, PubMed:22046314). The 4-hydroxyphenylpyruvate dioxygenase hppD catalyzes the conversion of 4-hydroxyphenylpyruvate to homogentisic acid (HGA) (PubMed:19028908, PubMed:22046314). The protein hmgX is crucial for this conversion and thus, probably functions as an accessory factor to mediate specific activity of hppD (PubMed:22046314). The homogentisate 1,2-dioxygenase hmgA is then involved in the cleavage of the aromatic ring of HGA and its conversion to 4-maleylacetoacetate (PubMed:19028908, PubMed:19715768). When hmgA activity is lowered by the cell wall integrity (CWI) signaling pathway, HGA accumulates and leads to the production of pyomelanin through benzoquinone acetic acid after oxidation and polymerization (PubMed:19715768). On the opposite, in non-stress conditions, both hppD and hmgA activities are balanced and HGA is degraded into 4-maleylacetoacetate (PubMed:19715768). 4-maleylacetoacetate is further converted to 4-fumarylacetoacetate by the maleylacetoacetate isomerase maiA, which is degraded into fumarate and acetoacetate by the fumarylacetoacetase fahA (Probable).
Expression is induced by L-tyrosine (PubMed:19028908). Expression is positively regulated by the cluster-specific transcription factor hmgR (PubMed:22046314).
Impairs growth on L-tyrosine as the sole carbon source and affects homogentisic acid and pyomelanin formation (PubMed:19028908, PubMed:19715768). Leads to increased sensitivity to reactive oxygen intermediates (PubMed:19028908).
Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation.
Required for multiple vacuole delivery pathways including the cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and endocytosis.
Belongs to the EF-1-beta/EF-1-delta family.
Belongs to the succinate/malate CoA ligase alpha subunit family.
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
During the catalytic reaction, a sulfide is transferred from Cys-221 to a reaction intermediate, generating a dehydroalanine residue.
Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance.
Belongs to the mitochondrion-specific ribosomal protein mL43 family.
Belongs to the sirtuin family. Class I subfamily.
Belongs to the TRAPP small subunits family. BET3 subfamily.
Belongs to the dolichyldiphosphatase family.
Required for efficient N-glycosylation. Necessary for maintaining optimal levels of dolichol-linked oligosaccharides. Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl monophosphate at a much lower rate. Does not act on phosphatidate.
Belongs to the fluoride channel Fluc/FEX (TC 1.A.43) family.
Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
In the C-terminal section; belongs to the AIR carboxylase family. Class I subfamily.
Belongs to the SEC23/SEC24 family. SEC23 subfamily.
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity).
The COPII coat is composed of at least 5 proteins: the sec23/24 complex, the sec13/31 complex, and the protein sar1.
In the C-terminal section; belongs to the NRP synthetase family.
In the N-terminal section; belongs to the isocyanide synthase family.
Isocyanide synthase-NRPS hybrid; part of the crm gene cluster that mediates the biosynthesis of a yet unidentified copper-responsive metabolite.
Component of the ER-mitochondria encounter structure (ERMES) or MDM complex, composed of mmm1, mdm10, mdm12 and mdm34. Associates with the mitochondrial outer membrane sorting assembly machinery SAM(core) complex.
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. mdm10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the tom40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of tom40 with the receptor tom22 and small TOM proteins. Can associate with the SAM(core) complex as well as the mdm12-mmm1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the tom40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme.
Belongs to the PNP/MTAP phosphorylase family.
The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
Over-expressed in azole-resistant clinical isolates.
Sterol 14alpha-demethylase, encoded by cyp51A and cyp51B, that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (PubMed:9184358, PubMed:18191972, PubMed:26459890, PubMed:29439966, PubMed:26269599). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity). In filamentous fungi, during the initial step of this module, lanosterol (lanosta-8,24-dien-3beta-ol) can be metabolized to eburicol (PubMed:18191972, PubMed:26459890, PubMed:29439966). Sterol 14alpha-demethylase catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of both these sterols in the form of formate, and converts eburicol and lanosterol to 14-demethyleburicol (4,4,24-trimethylergosta-8,14,24(28)-trienol) and 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, respectively, which are further metabolized by other enzymes in the pathway to ergosterol (PubMed:18191972, PubMed:26459890, PubMed:29439966, PubMed:26269599, PubMed:28461309). Can also use substrates not intrinsic to fungi, such as 24,25-dihydrolanosterol (DHL), producing 4,4'-dimethyl-8,14-cholestadien-3-beta-ol, but at lower rates than the endogenous substrates (By similarity).
The activity is completely inhibited by miconazole and reduced by voriconazole (6% substrate conversion), posaconazole (10%), itraconazole (16%), (R)-N-(1-(2,4-dichlorophenyl)-2-(1H-imidazol-1-yl)ethyl)-4-(5-phenyl-1,3,4-oxadiazol-2-yl)benzamide (VNI) (20%), and (R)-N-(1-(3,4'-difluorobiphenyl-4-yl)-2-(1H-imidazol-1-yl)ethyl)-4-(5-phenyl-1,3,4-oxadiazol-2-yl)benzamide (VFV) (31%). The weakest inhibitory effect is observed with fluconazole (PubMed:26459890, PubMed:26269599, PubMed:28461309). Activity is also inhibited by ketoconazole, as well as by the azole-based drug candidates VT-1161 and VT-1598 (PubMed:28461309). Activity is inhibited by the novel and long-acting fungicidal azole PC1244 (PubMed:29439966).
Expression is induced by voriconazole exposure in vitro and in mice (PubMed:21321135). Expression is increased in clinical azole-resistant isolates and by the presence of itraconazole (PubMed:12709346, PubMed:15504870). Expression is also up-regulated during biofilm growth (PubMed:21724936). Expression is repressed by iron in an SreA-dependent manner (PubMed:18721228). Expression is down-regulated by tetrandrine and posaconazole in a synergistic manner (PubMed:28080217).
Pleiotropic ABC efflux transporter that confers resistance to azoles such as itraconazole and voriconazole.
Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
Belongs to the glutamate--cysteine ligase type 3 family.
6-hydroxytryprostatin B O-methyltransferase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities (PubMed:23649274). The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA (PubMed:16755625). Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B (PubMed:16000710, PubMed:21105662, PubMed:23090579). The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively (PubMed:19226505). The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B (PubMed:18683158). Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties (PubMed:19763315). In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family.
In contrast to other A.fumigatus strains, strain ATCC MYA-4609 does not produce indole alkaloids such as fumitremorgins and verruculogen. While the biosynthetic pathway is complete, a variation in this enzyme abolishes production of the tryprostatin A intermediate. The weak methyltransferase activity is probably due to the presence of Leu-202 instead of an Arg residue that affects the binding of 6-hydroxytryprostatin B (PubMed:23649274).
Eliminates TAFC production and increases FsC production about 10-fold (PubMed:17845073). Does not affect the production of FC (PubMed:17845073).
FsC-acetyl coenzyme A-N(2)-transacetylase; part of the siderophore biosynthetic pathway (PubMed:21622789). Aspergillus fumigatus produces 4 types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake and intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial iron distribution and storage. TAFC consists of 3 N(2)-acetyl-N(5)-anhydromevalonyl-N(5)-hydroxyornithine residues cyclically linked by ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-(N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of all four siderophores depends on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA (PubMed:15504822, PubMed:16113265). Subsequently, the pathways for biosynthesis of extra- and intracellular siderophores split (PubMed:17845073). For biosynthesis of extracellular siderophores, the transacylase sidF transfers anhydromevalonyl to N(5)-hydroxyornithine (PubMed:17845073). The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by sidI and sidH respectively (PubMed:22106303). The acetylation of N(5)-hydroxyornithine for FC biosynthesis involves the constitutively expressed sidL (PubMed:21622789). FC is hydroxylated to HFC by an as yet uncharacterized enzyme during conidiation (PubMed:17845073). Assembly of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal peptide synthetases (NRPS), sidD and sidC respectively (PubMed:17845073). Subsequently, sidG catalyzes N2-acetylation of FsC for forming TAFC (PubMed:17845073). Both extra- and intracellular siderophores are crucial for growth during iron limitation and virulence (PubMed:16113265).
Belongs to the complex I NDUFA12 subunit family.
Belongs to the phosphatase 2A regulatory subunit B family.
Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration.
Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM7 family.
S-adenosyl-L-methionine-dependent protein methyltransferase that trimethylates the N-terminal glycine 'Gly-2' of elongation factor 1-alpha, before also catalyzing the mono- and dimethylation of 'Lys-3'.
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The mdm12-mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The mdm10-mdm12-mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the mdm12-mmm1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Homodimer. Component of the ER-mitochondria encounter structure (ERMES) or MDM complex, composed of mmm1, mdm10, mdm12 and mdm34. A mmm1 homodimer associates with one molecule of mdm12 on each side in a pairwise head-to-tail manner, and the SMP-LTD domains of mmm1 and mdm12 generate a continuous hydrophobic tunnel for phospholipid trafficking.
The SMP-LTD domain is a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers.
Belongs to the tRNA pseudouridine synthase TruA family.
Belongs to the arylamine N-acetyltransferase family.
Belongs to the ubiquitin-activating E1 family.
Binds 1 heme c group covalently per subunit.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily.
Expression is positively regulated by the brlA and abaA transcription factors (PubMed:26032501).
O-methyltransferase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). Gliotoxin contributes to pathogenesis during invasive aspergillosis (PubMed:17601876, PubMed:18199036). In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species (PubMed:17601876).
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins.
Vacuolar carboxypeptidase involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate (By similarity).
Forms a heterodimer with the catalytic subunit trm8.
Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
Belongs to the eukaryotic RPC7 RNA polymerase subunit family.
Component of the RNA polymerase III (Pol III) complex.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
Belongs to the protein prenyltransferase subunit alpha family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.
The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits.
RNA-binding component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Involved in poly(A) site recognition. May be involved in coupling transcription termination and mRNA 3'-end formation (By similarity).
Belongs to the universal ribosomal protein uL3 family.
Causes an allergic reaction in human. Binds to IgE and IgG.
The L3 protein is a component of the large subunit of cytoplasmic ribosomes.
Mitochondrial acetyl-CoA acetyltransferase that catalyzes both the formation and degradation of acetoacetyl-CoA (PubMed:32005728). Has no overlapping function with erg10B and seems not to be involved in ergosterol biosynthesis (PubMed:32005728). Plays an important role in growth, morphogenesis and maintaining mitochondrial function including the response to oxidative stresses (PubMed:32005728).
Mitochondrial erg10A is essential for A.fumigatus cell viability and might be a potential drug target to feed the antifungal drug development pipeline.
Involved in the assembly of the cytochrome c oxidase complex.
Involved in protein synthesis. Involved in microtubule stabilization (By similarity).
Belongs to the universal ribosomal protein uL1 family.
Belongs to the DNA mismatch repair MutS family. MSH3 subfamily.
Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with msh2 to form MutS beta, which binds to DNA mismatches thereby initiating DNA repair. Msh3 provides substrate-binding and substrate specificity to the complex. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. Acts mainly to repair insertion-deletion loops (IDLs) from 2 to 13 nucleotides in size, but can also repair base-base and single insertion-deletion mismatches that occur during replication. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions (By similarity).
Heterodimer consisting of msh2-msh3 (MutS beta). Forms a ternary complex with MutL alpha (mlh1-pms1) (By similarity).
Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity.
Component of the NDC80 complex, which consists of at least ndc80, nuf2 and spc24.
Belongs to the complex I NDUFB7 subunit family.
Involved in the regulation of telomere length, clustering and has a specific role in telomere position effect (TPE).
Component of the SWR1 chromatin remodeling complex.
Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Involved in chromosome stability (By similarity).
Belongs to the eukaryotic GSH synthase family.
Highly specific phosphatase involved in the metabolism of ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of tRNA splicing.
Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN).
Component of the Golgi-associated retrograde protein (GARP) complex.
ATP-dependent RNA helicase involved spliceosome assembly and in nuclear splicing. Catalyzes an ATP-dependent conformational change of U2 snRNP. Bridges U1 and U2 snRNPs and enables stable U2 snRNP association with intron RNA (By similarity).
Belongs to the DEAD box helicase family. DDX46/PRP5 subfamily.
Associates with DNA double-strand breaks.
Belongs to the PI3/PI4-kinase family. ATM subfamily.
Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of DNA damage, involved in the regulation of DNA damage response mechanism. Required for the control of telomere length and genome stability (By similarity).
Belongs to the GcvT family. CAF17 subfamily.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.
Catalytic tRNA acetyltransferase subunit of the elongator complex, which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs.
Belongs to the 3-oxoacid CoA-transferase family.
Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate.
Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of neosartoricin, a prenylated anthracenone that exhibits T-cell antiproliferative activity, suggestive of a physiological role as an immunosuppressive agent (PubMed:23758576, PubMed:23368997). The non-reducing polyketide synthase nscA probably synthesizes and cyclizes the decaketide backbone (PubMed:23368997). The hydrolase nscB then mediates the product release through hydrolysis followed by spontaneous decarboxylation (PubMed:23368997). The prenyltransferase nscD catalyzes the addition of the dimethylallyl group to the aromatic C5 (PubMed:23368997). The FAD-dependent monooxygenase nscC is then responsible for the stereospecific hydroxylation at C2 (PubMed:23368997). There is no gene encoding O-acetyltransferase in the nsc gene cluster; thus, the last step of 2-O-acetylation leading to neosartoricin may be catalyzed by an unidentified O-acetyltransferase (PubMed:23368997).
Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans.
Belongs to the shaker potassium channel beta subunit family.
Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.
Component of the homotypic vacuole fusion and vacuole protein sorting (HOPS) complex. Component of the class C core vacuole/endosome tethering (CORVET) complex.
Belongs to the TFIIF alpha subunit family.
TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation.
Belongs to the eIF-5A family. Hex1 subfamily.
Forms oligomers (By similarity). Self-assembles into hexagonal rods (By similarity). Binds directly or indirectly to the Woronin body tether lah (Probable).
Leads to an increased sensitivity to stressors that affect the integrity of the cell wall and membrane, such as SDS, the antifungal agent fludioxonil, the acyclic sesquiterpene alcohol farnesol and the cell wall perturbing agents Calcofluor White and Congo Red (PubMed:23869404). Does not affect the resistance to hypo-osmotic stress but leads to a higher sensitivity to physical damage (PubMed:23869404). Results in the lack of Woronin bodies (PubMed:23869404). Attenuates virulence in a murine model of infection (PubMed:23869404).
Major component of Woronin bodies, fungal-specific organelles that occlude septal pores in order to separate intact from damaged compartments (PubMed:23332467, PubMed:23869404). HexA binds directly or indirectly to the Woronin body tether that in turn is anchored at the rim of the septal pore (PubMed:23869404). Woronin bodies are important for stress resistance and virulence (PubMed:23869404).
Belongs to the histone deacetylase family. HD Type 1 subfamily.
Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Festuclavine dehydrogenase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:22453123). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:15870460). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482, PubMed:21409592). EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482). EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482). Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831). Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909).
Acyl-CoA ligase; part of the siderophore biosynthetic pathway (PubMed:22106303). Aspergillus fumigatus produces 4 types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake and intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial iron distribution and storage. TAFC consists of 3 N(2)-acetyl-N(5)-anhydromevalonyl-N(5)-hydroxyornithine residues cyclically linked by ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-(N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of all four siderophores depends on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA (PubMed:15504822, PubMed:16113265). Subsequently, the pathways for biosynthesis of extra- and intracellular siderophores split (PubMed:17845073). For biosynthesis of extracellular siderophores, the transacylase sidF transfers anhydromevalonyl to N(5)-hydroxyornithine (PubMed:17845073). The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by sidI and sidH respectively (PubMed:22106303). The acetylation of N(5)-hydroxyornithine for FC biosynthesis involves the constitutively expressed sidL (PubMed:21622789). FC is hydroxylated to HFC by an as yet uncharacterized enzyme during conidiation (PubMed:17845073). Assembly of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal peptide synthetases (NRPS), sidD and sidC respectively (PubMed:17845073). Subsequently, sidG catalyzes N2-acetylation of FsC for forming TAFC (PubMed:17845073). Both extra- and intracellular siderophores are crucial for growth during iron limitation and virulence (PubMed:16113265).
Repressed under nutrient-rich culture conditions.
Secreted aspartic-type endopeptidase which is secreted and contributes to virulence.
Cell surface beta-glucosidase involved in cell wall biosynthesis and septation, and thus required for normal growth and correct hyphal morphogenesis. Has hydrolytic activity on linear (1->3)-beta-D-glucans such as laminaribiose and other laminarioligosaccharides. Has also a minor transferase activity.
Expression was detected 4h after the initiation of spore germination and during mycelial growth.
Leads to smaller colonies and swollen and vacuolated hyphae with double cell wall and leaky tips. Leads also to decreased conidiation.
Belongs to the proteasome subunit S5A family.
Involved in pre-mRNA splicing. Facilitates the cooperative formation of U2/U6 helix II in association with stem II in the spliceosome. Binds to RNA (By similarity).
Belongs to the SMC family. SMC5 subfamily.
Heterotetramer of erg25, erg26, erg27 and erg28 (By similarity). Erg28 acts as a scaffold to tether erg27 and other 4,4-demethylation-related enzymes, forming a demethylation enzyme complex, in the endoplasmic reticulum (By similarity).
Sterol-C4-methyl oxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (By similarity). Erg26 is a catalytic component of the C-4 demethylation complex that catalyzes the conversion of 4,4-dimethylfecosterol into fecosterol via 4-methylfecosterol (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (PubMed:18191972) (Probable).
Belongs to the prefoldin subunit beta family.
Histones H3 and H4 chaperone involved in the nucleosome formation and heterochromatin silencing. Required for the deposition of H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role in the transcriptional regulation of the cell-cycle dependent histone genes by creating a repressive structure at the core histone gene promoter (By similarity).
Belongs to the eukaryotic/archaeal RNase P protein component 1 family.
ATP-binding RNA helicase involved in mitochondrial RNA metabolism. Required for maintenance of mitochondrial DNA (By similarity).
Belongs to the DEAD box helicase family. MRH4 subfamily.
Belongs to the thiolase-like superfamily. Fungal fatty acid synthetase subunit alpha family.
E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation.
Belongs to the universal ribosomal protein uL4 family.
Belongs to the eIF-2B alpha/beta/delta subunits family. MtnA subfamily.
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Involved in rRNA-processing at A0, A1 and A2 sites and regulates negatively telomerase.
Involved in the catabolism of quinolinic acid (QA).
Belongs to the major facilitator superfamily. Nitrate/nitrite porter (TC 2.A.1.8) family.
Involved in ds DNA break repair. Has a role in non-homologous integration (NHI) pathways where it is required in the final step of non-homologous end-joining.
Converts protoheme IX and farnesyl diphosphate to heme O.
Belongs to the glycosyltransferase 48 family.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
As part of the replication protein A (RPA/RP-A), a single-stranded DNA-binding heterotrimeric complex, may play an essential role in DNA replication, recombination and repair. Binds and stabilizes single-stranded DNA intermediates, preventing complementary DNA reannealing and recruiting different proteins involved in DNA metabolism.
Belongs to the replication factor A protein 1 family.
Component of the heterotrimeric canonical replication protein A complex (RPA).
Belongs to the eukaryotic ribosomal protein eL32 family.
Leads to lower ferrichrome (FC) and ferrioxamine B (FOB) uptake activities, which are reduced to approximately 60% and 50% of the wild-type activities, respectively (PubMed:26929401).
Major facilitator transporter involved in ferrichrome (FC) and ferrioxamine B (FOB) uptake (PubMed:26929401).
Belongs to the activator 1 small subunits family.
Belongs to the PHP hydrolase family. HisK subfamily.
GPI-anchored chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Required to reshape the cell wall at the sites where cell wall remodeling and/or cell wall maturation actively take place such as sites of conidia formation (By similarity).
The cyclic peptide natural product argifin acts as a specific inhibitor.
Belongs to the clathrin light chain family.
Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Causes an allergic reaction in human. Binds to IgE. May promote colonization through cytotoxic activity and by causing inflammatory reactions involving IgE antibodies. Binds also to IgG.
This purine-specific ribonuclease cleaves 28S RNA in eukaryotic ribosomes, inhibits protein synthesis, and shows antitumor activity.
Belongs to the Mediator complex subunit 5 family.
Belongs to the chitin synthase family. Class VI subfamily.
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Belongs to the DODA-type extradiol aromatic ring-opening dioxygenase family.
Belongs to the histidinol dehydrogenase family.
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Nonessential protein required for the fusion of transport vesicles derived from the endocytic pathway with the Golgi complex.
Catalyzes the reversible interconversion of glucose 1-phosphate and glucose 6-phosphate. Key enzyme in hexose metabolism. The reverse reaction is an essential step for biosynthesis because glucose 1-phosphate is the starting point for the synthesis of UDP-glucose, which acts as a precursor for the synthesis of oligosaccharides and trehalose.
Expression is under the control of the developmental and secondary metabolism regulators laeA and veA (PubMed:24082142, PubMed:24116213).
Results in silencing of the fumagillin gene cluster and elimination of fumagillin biosynthesis (PubMed:24116213).
Transcription factor that regulates the expression of the gene clusters that mediate the biosynthesis of pseurotin and fumagillin (PubMed:24116213).
Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Involved in ribosomal large subunit assembly.
Ubiquitin-protein ligase which is mainly involved pre-mRNA splicing and DNA repair. Required for pre-mRNA splicing as component of the spliceosome.
Belongs to the prefoldin subunit alpha family.
Belongs to the proteasome subunit S11 family.
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Components of the endosome-vacuole trafficking pathway that regulates nutrient transport. May be involved in processes which determine whether plasma membrane proteins are degraded or routed to the plasma membrane (By similarity).
Belongs to the peptidase M28 family. M28E subfamily.
Extracellular aminopeptidase that allows assimilation of proteinaceous substrates and which contributes to pathogenicity.
Belongs to the ubiquitin-activating E1 family. ULA1 subfamily.
Regulatory subunit of the dimeric UBA3-ULA1 E1 enzyme.
Component of the ER-mitochondria encounter structure (ERMES) or MDM complex, composed of mmm1, mdm10, mdm12 and mdm34.
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. Mdm34 is required for the interaction of the ER-resident membrane protein mmm1 and the outer mitochondrial membrane-resident beta-barrel protein mdm10.
Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.
Component of the dolichol-phosphate mannose (DPM) synthase complex.
Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins.
Belongs to the PAPS reductase family. CysH subfamily.
Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase subunit family.
Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in association with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1.
Belongs to the fumigaclavine B O-acetyltransferase family.
O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of pyripyropene A, a specific human acyl-coenzyme A:cholesterol acyltransferase 2 inhibitor (PubMed:20861902). The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase pyr1 (PubMed:20861902). Nicotinyl-CoA is then a substrate of polyketide synthase pyr2 to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase pyr6 to yield farnesyl-HPPO (PubMed:20861902). The next steps consist of an epoxidation of farnesyl-HPPO to epoxyfarnesyl-HPPO by FAD-dependent monooxygenase pyr5 and a cyclization of the terpenoid portion by the terpene cyclase pyr4 to yield deacetyl-pyripyropene E (PubMed:20861902). The 2 cytochrome P450 monooxygenases pyr3 and pyr9, and the 2 acetyltransferases pyr7 and pyr8 are involved in the conversion of deacetyl-pyripyropene E into pyripyropene A through several cycles of oxidation and acetylation steps (PubMed:20861902). Pyr7 acetylates deacetyl-pyripyropene E to pyripyropene E which is oxidized to 11-deacetyl-pyripyropene O by pyr3, which is in turn acetylated into pyripyropene O by pyr8 (PubMed:21224862, PubMed:26019565). Pyripyropene O is then oxidized to deacetyl-pyripyropene A by pyr9 (PubMed:21224862). Deacetyl-pyripyropene A is finally acetylated to pyripyropene A by pyr8 (PubMed:26019565).
Belongs to the bacterial ribosomal protein bL28 family.
Has a dual role in the assembly of mitochondrial ATPase. Acts as a protease that removes N-terminal residues of mitochondrial ATPase CF(0) subunit 6 at the intermembrane space side. Also involved in the correct assembly of the membrane-embedded ATPase CF(0) particle, probably mediating association of subunit 6 with the subunit 9 ring (By similarity).
Belongs to the eukaryotic ribosomal protein eL37 family.
Specific in hydrolyzing the terminal glycosidic bond of polygalacturonic acid and oligogalacturonates.
LSm subunits form a heteromer with a doughnut shape.
Plays a role in U6 snRNP assembly and function. Binds to the 3' end of U6 snRNA.
Belongs to the AAA ATPase family. PCH2 subfamily.
Leads to complete abolishment of isoquinoline alkaloid production but accumulates a series of benzyl pyrroles, including fumipyrrole.
Phenol 2-monooxygenase; part of the gene cluster that mediates the biosynthesis of the isoquinoline alkaloids fumisoquin A, fumisoquin B and fumisoquin C; as well as small amounts of fumipyrrole as a shunt metabolite (PubMed:25582336, PubMed:27065235). The products of the cluster lead to a brown coloration and are important for growth and conidiation (PubMed:25582336). The nonribosomal peptide synthetase-like protein fsqF, which lacks a canonical condensation domain, is required for addition of a serine-derived dehydroalanine moiety to activated tyrosine but is not essential for the subsequent steps leading to isoquinoline formation (PubMed:27065235). A different enzyme, most likely the ATP-grasp enzyme fsqD, is responsible for activation of tyrosine (Probable). Three additional enzymes encoded by the fsq cluster, the N-methyltransferase fsqC, the phenol 2-monooxygenase fsqG and the FAD-dependent oxidase fsqB, catalyze the formation of the isoquinoline ring system in the fumisoquins (PubMed:27065235, PubMed:30194285). FsqB converts the fspF thiolation domain-bound (2S,4S,5S)-2-amino-6-(3,4-dihydroxyphenyl)-4-hydroxy-5-(methylamino)hexanoyl into isoquinoline (PubMed:27065235, PubMed:30194285). The cyclization most likely proceeds via a two-step mechanism, beginning with FAD-dependent oxidation of the methyl group to an iminium species followed by electrophilic attack on the deprotonated phenol (Probable).
Belongs to the eukaryotic ribosomal protein eS10 family.
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with ncs6 that ligates sulfur from thiocarboxylated urm1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.
Impairs the ability to undergo asexual reproduction with abnormal morphology of conidiophores and only small numbers of dysmorphic conidia exhibiting precocious germination (PubMed:16207816, PubMed:19028996). Displayed reduced expression of the catalase gene cat1 and hypersusceptibility to hydrogen peroxide (PubMed:16207816). Impairs the production of ergot alkaloids such as chanoclavine-I, festuclavine, fumigaclavine A, fumigaclavine B, and fumigaclavine C (PubMed:23925951). Impairs A.fumigatus immunoglobulin E-independent mast cell degranulation induction (PubMed:19527167).
Induced at the onset of developmental competence and highly expressed in competent hyphae (PubMed:16207816).
Transcription factor that regulates asexual reproduction (PubMed:16207816, PubMed:19028996). Binds the StuA-response elements (StRE) with the consensus sequence 5'-(A/T)CGCG(T/A)N(A/C)-3' at the promoters of target genes (By similarity). Controls the expression of 6 secondary metabolite biosynthetic clusters including 2 involved in the synthesis of alkaloids (fumigaclavine and fumitremorgen), 2 clusters of the ETP class (gliotoxin and an unknown ETP-like toxin), a cluster predicted to produce pseurotin A, and the product of the last cluster is unknown (PubMed:19028996). Controls the production of ergot alkaloids during conidiophore development (PubMed:23925951). Controls expression of sspA and gliP (PubMed:18490465). Involved in the induction of immunoglobulin E-independent mast cell degranulation (PubMed:19527167).
Belongs to the DASH complex DAM1 family.
Nuclear serine protease which mediates apoptosis.
Belongs to the ferroportin (FP) (TC 2.A.100) family. SLC40A subfamily.
May be involved in iron transport and iron homeostasis.
Belongs to the universal ribosomal protein uL14 family.
Nicotinic acid-CoA ligase; part of the gene cluster that mediates the biosynthesis of pyripyropene A, a specific human acyl-coenzyme A:cholesterol acyltransferase 2 inhibitor (PubMed:20861902). The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase pyr1 (PubMed:20861902). Nicotinyl-CoA is then a substrate of polyketide synthase pyr2 to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase pyr6 to yield farnesyl-HPPO (PubMed:20861902). The next steps consist of an epoxidation of farnesyl-HPPO to epoxyfarnesyl-HPPO by FAD-dependent monooxygenase pyr5 and a cyclization of the terpenoid portion by the terpene cyclase pyr4 to yield deacetyl-pyripyropene E (PubMed:20861902). The 2 cytochrome P450 monooxygenases pyr3 and pyr9, and the 2 acetyltransferases pyr7 and pyr8 are involved in the conversion of deacetyl-pyripyropene E into pyripyropene A through several cycles of oxidation and acetylation steps (PubMed:20861902). Pyr7 acetylates deacetyl-pyripyropene E to pyripyropene E which is oxidized to 11-deacetyl-pyripyropene O by pyr3, which is in turn acetylated into pyripyropene O by pyr8 (PubMed:21224862, PubMed:26019565). Pyripyropene O is then oxidized to deacetyl-pyripyropene A by pyr9 (PubMed:21224862). Deacetyl-pyripyropene A is finally acetylated to pyripyropene A by pyr8 (PubMed:26019565).
Belongs to the chitin synthase family. Class III subfamily.
O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the isocyanide xanthocillin and its derivatives (PubMed:29844112). The first step of the pathway consists in the conversion of tyrosine into a vinyl-isonitrile intermediate by the isocyanide synthase xanB (PubMed:29844112). Subsequent oxidative dimerization of this intermediate to form xanthocillin may involve the cytochrome P450 monooxygenase xanG, whose expression is coregulated with that of XanB (PubMed:29844112). Xanthocillin can be further modified by the isonitrile hydratase-like protein xanA which introduces N-formyl groups and the methyltransferase xanE which introduces methyl groups, leading to the production of several derivatives including fumiformamide (PubMed:29844112). Finally, fumiformamide can be subject to both oxidative and reductive cyclization to yield melanocins E and F, respectively (PubMed:29844112).
Plays a central role as a glucosyl donor in cellular metabolic pathways.
Belongs to the glutamate synthase family.
Belongs to the MsrA Met sulfoxide reductase family.
Probable aspartic-type endopeptidase which contributes to virulence.
Belongs to the cytochrome c oxidase VIIc family.
Exhibits an altered cell wall organization in addition to defects related to vegetative growth and tolerance to cell wall-perturbing agents (PubMed:27473315). Results in attenuated virulence in a neutropenic murine model of invasive pulmonary aspergillosis (PubMed:27473315). Leads to reduced conidiation during asexual differentiation (PubMed:32005734). Reduces conidial pigment DHN-melanin formation (PubMed:27393422). Strongly decreases the production of fumiquinazoline C (PubMed:33705521).
Expression is induced during cell wall stress (PubMed:27473315). Also induced during asexual development (PubMed:32005734).
Phosphorylation during asexual development.
Transcription factor; part of cell wall integrity (CWI) signaling pathway composed of pkcA, the bck1-mkk2-mpka MAPK cascade and the downstream rlmA transcription regulator (PubMed:16372009). The CWI signaling pathway regulates cell wall integrity and pyomelanin formation (PubMed:19715768). CWI controls also oxidative stress response, gliotoxin production, iron adaptation and asexual development (PubMed:21883519, PubMed:32005734). Finally, CWI is constitutively required for A.fumigatus to cope with the temperature increase found in the mammalian lung environment, during infection (PubMed:33010083). Positively regulates the phosphorylation of mpkA (PubMed:27473315). Involved in tolerance to oxidative damage and transcriptional regulation of genes related to oxidative stress adaptation (PubMed:27473315). Finally, CWI is constitutively required for A.fumigatus to cope with the temperature increase found in the mammalian lung environment, during infection (PubMed:33010083). Directly regulates the expression of regulators of conidiation, including flbB, flbC, brlA, abaA, and rasB, as well as genes involved in cell wall synthesis and remodeling (PubMed:32005734). Specifically associates with the target fumiquinazoline (fmq) cluster genes promoters at conserved motifs (5'-TAWWWWTA-3') during conidiation to supplement mature conidia with fumiquinazoline C (PubMed:33705521). Controls also the DHN-melanin production via binding the promoter of pksP (PubMed:27393422).
Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA polymerase subunit family.
Belongs to the isocyanide synthase family.
Isocyanide synthase involved in the biosynthesis of isocyanides (or isonitriles), a class of microbial secondary metabolites. The presence of an isonitrile moiety within a compound imparts unique biological (cytotoxic, antibacterial, and antiprotozoal) and chemical (transition metal coordination) properties and enables synthetic and biochemical applications.
Very low expression levels near the detection limit.
Belongs to the PPP phosphatase family. PP-5 (PP-T) subfamily.
Belongs to the membrane magnesium transporter (TC 1.A.67) family.
Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.
Belongs to the MICOS complex subunit Mic10 family.
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of neosartoricin, a prenylated anthracenone that exhibits T-cell antiproliferative activity, suggestive of a physiological role as an immunosuppressive agent (PubMed:23758576, PubMed:23368997). The non-reducing polyketide synthase nscA probably synthesizes and cyclizes the decaketide backbone (PubMed:23368997). The hydrolase nscB then mediates the product release through hydrolysis followed by spontaneous decarboxylation (PubMed:23368997). The prenyltransferase nscD catalyzes the addition of the dimethylallyl group to the aromatic C5 (PubMed:23368997). The FAD-dependent monooxygenase nscC is then responsible for the stereospecific hydroxylation at C2 (PubMed:23368997). There is no gene encoding O-acetyltransferase in the nsc gene cluster; thus, the last step of 2-O-acetylation leading to neosartoricin may be catalyzed by an unidentified O-acetyltransferase (PubMed:23368997).
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IID subfamily.
Belongs to the nucleosome assembly protein (NAP) family.
Belongs to the JHDM1 histone demethylase family.
Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code.
The JmjC domain mediates the demethylation activity.
Belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family.
Responsible for methylating the 5'-cap structure of mRNAs.
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Belongs to the metallo-beta-lactamase superfamily. RNA-metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
Component of the cleavage factor I (CF I) involved in pre-mRNA 3'-end processing.
Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.
Belongs to the adenylate kinase family. AK6 subfamily.
Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has also ATPase activity. May be involved in rRNA maturation and transcription regulation.
Belongs to the ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily.
Expression is induced upon voriconazole treatment.
ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon (By similarity).
Belongs to the DEAD box helicase family. eIF4A subfamily.
Component of the eIF4F complex, which composition varies with external and internal environmental conditions. It is composed of at least eIF4A, eIF4E and eIF4G (By similarity).
MAP4K component of the MAPK pathway required for the mating pheromone response and the regulation of cell polarity and cell cycle.
Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.
Mediator of diverse signals that repress RNA polymerase III transcription. Inhibits the de novo assembly of TFIIIB onto DNA.
Component of the 60S subunit of the ribosome.
In the C-terminal section; belongs to the eukaryotic ribosomal protein eL40 family.
In the N-terminal section; belongs to the ubiquitin family.
Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Contributes to pathogenicity (By similarity).
Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.
In the C-terminal section; belongs to the trehalose phosphatase family.
May be involved in cellular response to stress. Required to maintain mitochondrial DNA (mtDNA) integrity and stability (By similarity).
Mitogen-activated protein kinase kinase kinase; part of cell wall integrity (CWI) signaling pathway composed of pkcA, the bck1-mkk2-mpka MAPK cascade and the downstream rlmA transcription regulator (PubMed:19715768). The CWI signaling pathway regulates cell wall integrity and pyomelanin formation (PubMed:19715768). CWI controls also oxidative stress response, gliotoxin production, iron adaptation and asexual development (PubMed:21883519, PubMed:32005734). Finally, CWI is constitutively required for A.fumigatus to cope with the temperature increase found in the mammalian lung environment, during infection (PubMed:33010083).
Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine. May be involved in virulence (By similarity).
Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription.
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid (PubMed:19415934, PubMed:19216560, PubMed:29158519). Protostadienol synthase helA cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol)(PubMed:19415934, PubMed:19216560, PubMed:29158519). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid (PubMed:19216560). Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton (PubMed:29158519). This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid (PubMed:19415934, PubMed:19216560, PubMed:29158519). Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order (PubMed:29158519). The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21 (PubMed:29158519). C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation (PubMed:19415934, PubMed:29158519). The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC (PubMed:19415934, PubMed:29158519).
Expression is under the control of the secondary metabolism regulator laeA (PubMed:17432932).
May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi.
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Sec13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity).
The COPII coat is composed of at least 5 proteins: the sec23/24 complex, the sec13/31 complex, and the protein sar1. Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof.
Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate).
The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Belongs to the cyclophilin-type PPIase family. PPIL4 subfamily.
Expression is reduced by up to 90 percent under iron-depleted conditions.
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for l- to d- amino acid conversion) are present within the NRP synthetase. NRPS3 has the following architecture: A-T-C-A-T-C.
Nonribosomal peptide synthase; part of the siderophore biosynthetic pathway (PubMed:17845073). Aspergillus fumigatus produces four types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake and intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial iron distribution and storage. TAFC consists of three N(2)-acetyl-N(5)-anhydromevalonyl-N(5)-hydroxyornithine residues cyclically linked by ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-(N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of all four siderophores depends on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA (PubMed:15504822, PubMed:16113265). Subsequently, the pathways for biosynthesis of extra- and intracellular siderophores split (PubMed:17845073). For biosynthesis of extracellular siderophores, the transacylase sidF transfers anhydromevalonyl to N(5)-hydroxyornithine (PubMed:17845073). The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by sidI and sidH respectively (PubMed:22106303). The acetylation of N(5)-hydroxyornithine for FC biosynthesis involves the constitutively expressed sidL (PubMed:21622789). FC is hydroxylated to HFC by an as yet uncharacterized enzyme during conidiation (PubMed:17845073). Assembly of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal peptide synthetases (NRPS), sidD and sidC respectively (PubMed:17845073). Subsequently, sidG catalyzes N2-acetylation of FsC for forming TAFC (PubMed:17845073). Both extra- and intracellular siderophores are crucial for growth during iron limitation and virulence (PubMed:16113265).
Belongs to the eukaryotic ribosomal protein eS6 family.
Belongs to the GPI inositol-deacylase family.
Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.
Belongs to the eukaryotic ribosomal protein eL43 family.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. APG1/unc-51/ULK1 subfamily.
Homodimer. Forms a ternary complex with ATG13 and ATG17.
Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates. Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes phosphorylation of ATG4, decreasing the interaction between ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of ATG8.
Belongs to the AP endonuclease 2 family.
Expression is under the control of the secondary metabolism regulator laeA (PubMed:17432932). Expression is down-regulated when gliT is deleted and up-regulated upon exposure to exogenous gliotoxin (PubMed:25311525).
Protostadienol synthase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid (PubMed:19415934, PubMed:19216560, PubMed:19951700, PubMed:29158519). Protostadienol synthase helA cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol)(PubMed:19415934, PubMed:19216560, PubMed:19951700, PubMed:29158519). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid (PubMed:19216560). Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton (PubMed:29158519). This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid (PubMed:19415934, PubMed:19216560, PubMed:29158519). Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order (PubMed:29158519). The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21 (PubMed:29158519). C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation (PubMed:19415934, PubMed:29158519). The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC (PubMed:19415934, PubMed:29158519).
Catalyzes the ferrous insertion into protoporphyrin IX.
Involved in amino sugar synthesis (formation of chitin, supplies the amino sugars of asparagine-linked oligosaccharides of glycoproteins).
Necessary for the splicing of pre-mRNA. Has a role in the recognition of the branch site (5'-UACUAAC-3'), the pyrimidine tract and the 3'-splice site at the 3'-end of introns (By similarity).
Belongs to the diphthine synthase family.
S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis.
Contains a large substrate-binding pocket that recognizes alpha-helical transmembranes, which alternately faces the endoplasmic reticulum lumen and cytosol, while remaining accessible to the lipid bilayer through a lateral opening (By similarity). The translocase alternates between two conformations: inward-open (E1) and outward-open (E2) states (By similarity). Undergoes a series of conformational changes with ATP-binding, phosphorylation of the Asp active site and subsequent dephosphorylation in a Post-Albers cycle (i.e., E1 -> E1-ATP -> E1P-ADP -> E1P -> E2P -> E2-Pi -> E1) (By similarity). A substrate transmembrane helix with a short, preferentially positively charged lumenal segment binds to the outward-open pocket and the E2P-to-E1 transition flips the transmembrane by a switch from the outward-open to inward-open conformation (By similarity).
Endoplasmic reticulum (ER) translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum (By similarity). Acts as a dislocase that mediates the ATP-dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane (By similarity). Works in concert with the ER Ca(2+) pump srcA to support ER homeostasis (PubMed:34663092). With srcA, supports also redox homeostasis and virulence (PubMed:34663092).
Expression is induced by ER stress in a UPR-dependent manner (PubMed:34663092). Leads to the down-regulation of genes largely associated with the metabolism of carbohydrates, amino acids, nitrogen, and sulfur; as well as genes that encode abundantly secreted proteins (PubMed:34663092).
The ATPase activity is stimulated by phosphatidylinositol 4-phosphate (PI4P).
Pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase.
Belongs to the glycosyl hydrolase 18 family.
Dioxygenase that cleaves the interphenyl C-alpha-C-beta double bond of resveratrol to yield 3,5-dihydroxybenzaldehyde and 4-hydroxybenzaldehyde (PubMed:21073977). Cleaves also piceatannol, a compound that differs from resveratrol only in the occurrence of an additional hydroxyl group, which leads to the production of 3,4-dihydroxybenzaldehyde and 3,5-hydroxybenzaldehyde (By similarity).
Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity.
Belongs to the ATPase delta chain family.
Belongs to the proteasome inhibitor PI31 family.
Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28.
Belongs to the XRCC4-XLF family. XLF subfamily.
DNA polymerase II participates in chromosomal DNA replication.
Heterotetramer. Consists of 4 subunits: pol2, dpb2, dpb3 and dpb4 (By similarity).
The CysA-type zinc finger is required for PCNA-binding.
The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes.
Belongs to the splicing factor SR family.
Acetylated by esa1 to form H2AK4ac and H2AK7ac.
Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
In contrast to vertebrates and insects, its C-terminus is not monoubiquitinated.
Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases mec1/ATR and tel1/ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint (By similarity).
The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.
To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H2AK4ac = acetylated Lys-5; H2AK7ac = acetylated Lys-9; H2AS128ph = phosphorylated Ser-130.
Belongs to the F-actin-capping protein beta subunit family.
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments (By similarity).
Forms the NCT transcriptional regulatory complex with nctA and mot1.
Leads to a multidrug-resistance phenotype, including the azoles (itraconazole, voriconazole and posaconazole), as well as the salvage therapeutic amphotericin B and terbinafine, an agent used in the treatment of chronic and allergic disease (PubMed:31969561). Leads also to transcriptional derepression of cdr1B and its over-production (PubMed:31969561). Results also in a notable increase in the immunogenic properties of Aspergillus fumigatus, but does not result in loss of virulence (PubMed:31969561).
Part of the NCT transcriptional regulatory complex that acts as a key regulator of ergosterol biosynthesis and the azole exporter cdr1B (PubMed:31969561). The NCT complex binds the promoters of genes linked to azole susceptibility, and especially represses the expression of cdr1B transporter (PubMed:31969561).
Belongs to the protein prenyltransferase subunit beta family.
Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX.
Belongs to the eukaryotic ribosomal protein eS26 family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Belongs to the DHHC palmitoyltransferase family. ERF2/ZDHHC9 subfamily.
Palmitoyltransferase specific for Ras proteins.
Belongs to the UPL family. TOM1/PTR1 subfamily.
Xylitol dehydrogenase which catalyzes the conversion of xylitol to D-xylulose. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters pentose phosphate pathway (By similarity).
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of an adenine present in helix 65 in 25S rRNA.
Belongs to the alpha-ketoglutarate dehydrogenase family.
Belongs to the adenylate kinase family. AK2 subfamily.
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Belongs to the DASH complex DUO1 family.
Expression is induced during iron starvation (PubMed:15953695, PubMed:17845073).
Leads to a delay in both conidial swelling and germ tube production during iron-depleted conditions (PubMed:17845073).
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for L- to D- amino acid conversion) are present within the NRP synthetase. NRPS2 has the following architecture: A-T-C-A-T-C-A-T-C-T-C-T-C.
Nonribosomal peptide synthase; part of the siderophore biosynthetic pathway (PubMed:17845073). Aspergillus fumigatus produces four types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake; and intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial iron distribution and storage. TAFC consists of three N(2)-acetyl-N(5)-anhydromevalonyl-N(5)-hydroxyornithine residues cyclically linked by ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-(N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of all four siderophores depends on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA (PubMed:15504822, PubMed:16113265). Subsequently, the pathways for biosynthesis of extra- and intracellular siderophores split (PubMed:17845073). For biosynthesis of extracellular siderophores, the transacylase sidF transfers anhydromevalonyl to N(5)-hydroxyornithine (PubMed:17845073). The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by sidI and sidH respectively (PubMed:22106303). The acetylation of N(5)-hydroxyornithine for FC biosynthesis involves the constitutively expressed sidL (PubMed:21622789). FC is hydroxylated to HFC by an as yet uncharacterized enzyme during conidiation (PubMed:17845073). Assembly of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal peptide synthetases (NRPS), sidD and sidC respectively (PubMed:15953695, PubMed:17845073, PubMed:17464044). Subsequently, sidG catalyzes N2-acetylation of FsC for forming TAFC (PubMed:17845073). Both extra- and intracellular siderophores are crucial for growth during iron limitation and virulence (PubMed:16113265).
Terpene cyclase; part of the gene cluster that mediates the biosynthesis of pyripyropene A, a specific human acyl-coenzyme A:cholesterol acyltransferase 2 inhibitor (PubMed:20861902). The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase pyr1 (PubMed:20861902). Nicotinyl-CoA is then a substrate of polyketide synthase pyr2 to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase pyr6 to yield farnesyl-HPPO (PubMed:20861902). The next steps consist of an epoxidation of farnesyl-HPPO to epoxyfarnesyl-HPPO by FAD-dependent monooxygenase pyr5 and a cyclization of the terpenoid portion by the terpene cyclase pyr4 to yield deacetyl-pyripyropene E (PubMed:20861902). The 2 cytochrome P450 monooxygenases pyr3 and pyr9, and the 2 acetyltransferases pyr7 and pyr8 are involved in the conversion of deacetyl-pyripyropene E into pyripyropene A through several cycles of oxidation and acetylation steps (PubMed:20861902). Pyr7 acetylates deacetyl-pyripyropene E to pyripyropene E which is oxidized to 11-deacetyl-pyripyropene O by pyr3, which is in turn acetylated into pyripyropene O by pyr8 (PubMed:21224862, PubMed:26019565). Pyripyropene O is then oxidized to deacetyl-pyripyropene A by pyr9 (PubMed:21224862). Deacetyl-pyripyropene A is finally acetylated to pyripyropene A by pyr8 (PubMed:26019565).
Belongs to the peptidase M28 family. M28A subfamily.
Extracellular aminopeptidase that releases a wide variety of amino acids from natural peptides and contributes to pathogenicity.
Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome.
Belongs to the eukaryotic-type primase large subunit family.
DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.
Belongs to the G-protein coupled receptor 4 family.
Belongs to the nonaspanin (TM9SF) (TC 9.A.2) family.
Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity).
Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to cysteines occuring in specific C-terminal amino acid sequences.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair (By similarity).
Belongs to the glycosyl hydrolase 17 family.
Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase.
Belongs to the protein-tyrosine phosphatase family.
Sterol glycosyltransferase responsible for the glycosylation of ergosterol to form ergosterol-glucoside.
The GRAM and PH domains are required for the localization of ATG26 to the preautophagosomal structure (PAS) and are involved in autophagy (By similarity).
Belongs to the mitochondrion-specific ribosomal protein mS37 family.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Component of the mitochondrial small ribosomal subunit.
Belongs to the helicase family. RAD25/XPB subfamily.
Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Belongs to the PA-phosphatase related phosphoesterase family.
Hydroxynaphthalene reductase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment and a structural component of the conidial wall (PubMed:10515939, PubMed:19156203). The first step of the pathway is the production of the heptaketide naphtopyrone YWA1 by the polyketide synthase alb1 though condensation of acetyl-CoA with malonyl-CoA (PubMed:10515939). The naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase ayg1 though chain-length shortening (PubMed:10515939). 1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to yield scytalone (PubMed:10515939). The scytalone dehydratase arp1 then reduces scytalone to 1,3,8-THN (PubMed:10515939). 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to yield vermelone (PubMed:10515939). Vermelone is further converted by the multicopper oxidase abr1 to 1,8-DHN (PubMed:10515939). Finally the laccase abr2 transforms 1,8-DHN to DHN-melanin (PubMed:10515939). DHN-melanin biosynthesis appears to be initiated in endosomes where early enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to melanin deposition on the cell surface where late enzymes (abr1 and abr2) localize (PubMed:26972005). DHN-melanin is an important structural component of the outer cell wall and is required for the presence of conidial surface hydrophobins (PubMed:19703288). DHN-melanin also plays a crucial role in fungal virulence, including a protective role against the host's immune defenses (PubMed:19156203, PubMed:20145078, PubMed:21747802, PubMed:21573171, PubMed:24818666). DHN-melanin protects also conidia against amoeba predation (PubMed:25684622).
Results in brownish conidial phenotype (PubMed:19703288, PubMed:26972005). Results in an altered conidial surface with masked surface rodlet layer, leaky cell wall allowing the deposition of proteins on the cell surface and exposing the otherwise-masked cell wall polysaccharides at the surface (PubMed:24818666).
Tricyclazole and pyroquilon inhibit arp2 hydroxynaphtalene reductase activity (PubMed:19703288).
Belongs to the WD repeat WDR12/YTM1 family.
Component of the NOP7 complex, composed of erb1, nop7 and ytm1. The complex is held together by erb1, which interacts with nop7 via its N-terminal domain and with ytm1 via a high-affinity interaction between the seven-bladed beta-propeller domains of the 2 proteins. The NOP7 complex associates with the 66S pre-ribosome. Interacts (via UBL domain) with mdn1 (via VWFA/MIDAS domain).
tRNA nucleus export receptor which facilitates tRNA translocation across the nuclear pore complex. Involved in pre-tRNA splicing, probably by affecting the interaction of pre-tRNA with splicing endonuclease.
Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.
Belongs to the archaeal/bacterial/fungal opsin family.
Belongs to the Clp1 family. Clp1 subfamily.
Component of a pre-mRNA cleavage factor complex. Interacts directly with PCF11.
May lack the polyribonucleotide 5'-hydroxyl-kinase and polynucleotide 5'-hydroxyl-kinase activities that are characteristic of the human ortholog.
Required for endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation.
Belongs to the eukaryotic ribosomal protein eL34 family.
Belongs to the ZIP transporter (TC 2.A.5) family.
Catalyzes the hydration of cyanide to formamide. Degradation of cyanide may be important for plant pathogenic fungi in infection of cyanogenic plants.
Oligomer of dimers, forming left-handed helical fibers.
Belongs to the class-I DAHP synthase family.
Belongs to the DEAD box helicase family. DDX24/MAK5 subfamily.
Belongs to the adaptor complexes medium subunit family.
May act as a negative regulator of salt tolerance.
Belongs to the eukaryotic ribosomal protein P1/P2 family.
P1 and P2 exist as dimers at the large ribosomal subunit.
Plays an important role in the elongation step of protein synthesis.
Catalytic subunit of the slx1-slx4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Component of the ribosome quality control complex (RQC).
E3 ubiquitin-protein ligase. Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation.
In the central section; belongs to the inositol 1,4,5-trisphosphate 5-phosphatase family.
Belongs to the phosphosulfolactate synthase family.
Abolishes completely conidiation (PubMed:17030990). Results in production of bristle-like structures instead of conidiophores and conidia and fails to produce ergot alkaloids (PubMed:18333504). Reduces significantly expression of gliotoxin biosynthetic gene cluster including gliM, gliP, gliT, and gliZ (PubMed:26032501). Impairs down-regulation of genes encoding ribosomal proteins under nitrogen-limiting, but not carbon-limiting, conditions (PubMed:19028996). Abolishes the production of fumiquinazoline C (PubMed:24612080).
BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (PubMed:17030990). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (By similarity). Binds promoters of target genes at brlA response elements (BREs) containing the conserved sequence 5'-(C/A)(A/G)AGGG(G/A)-3' (By similarity). Positively regulates expression of the gliotoxin biosynthetic gene cluster in actively growing vegetative cells, and likely bridges morphological and chemical development during the life-cycle (PubMed:26032501). Regulates (directly or indirectly) the ergot cluster genes (PubMed:18333504). Positively regulates expression of the fumiquinazoline C biosynthetic gene cluster (PubMed:24612080). Positively regulates expression of the melanin biosynthetic gene cluster (PubMed:24123270). Mediates repression of ribosomal protein gene expression in response to nitrogen depletion (PubMed:19028996).
Expression increases dramatically during the synchronous asexual development (PubMed:18298443). Expression is positively regulated by hsp90 (PubMed:22822234). Expression is controlled by upstream regulators fluG and flbA (PubMed:17030990). Expression is controlled by the histone methyltransferase clrD (PubMed:18849468). Expression is decreased by 2',4'-Dihydroxychalcone (2',4'-DHC) (PubMed:26190922).
Belongs to the ribulose-phosphate 3-epimerase family.
Belongs to the bacterial ribosomal protein bL19 family.
ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5'-splice site duplex to permit an effective competition for the 5'-splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5'-splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/U5 snRNP, facilitating the first covalent step of splicing (By similarity).
Belongs to the DEAD box helicase family. DDX23/PRP28 subfamily.
Causes an allergic reaction in human. Binds to IgE (PubMed:9412580, PubMed:10756236). Shares common IgE-binding epitopes with allergen Cand b 2 of Candida boidinii (PubMed:9412580).
Homodimer; disulfide-linked, upon oxidation.
Renders cells sensitive to reactive oxygen species. Renders A.fumigatus avirulent in a mouse model of pulmonary aspergillosis.
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys Prx, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Required for virulence.
Belongs to the fungal surface NADase family.
Conidial surface nicotinamide adenine dinucleotide glycohydrolase that cleave NAD(+) and NADP(+) but not their reduced counterparts, NADH and NADPH (PubMed:33712585). Lacks both ADP-ribosyl cyclase and base exchange activity and does not mediate synthesis of calcium messengers cADPR or NAADP (PubMed:33712585). Plays a role in pathogenicity by depleting the host's NAD(+) pool (PubMed:33712585).
Expression is up-regulated during conidiation of A.fumigatus strains displaying high adherence to pulmonary epithelial cells.
The C-terminus contains also a calcium binding site (residues 215-224) that might be involved in NADase activity regulation (PubMed:33712585). The calcium-binding site is not alweays present since it emerged in the order Eurotiales, which includes Aspergillus species (PubMed:33712585).
The catalytic activity is positively regulated by calcium via its binding to the calcium-binding site.
Belongs to the ETF alpha-subunit/FixB family.
The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).
Belongs to the iron/manganese superoxide dismutase family.
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Results in a hypersensitivity to the azole drugs fluconazole, miconazole, and itraconazole (PubMed:28052140). In addition to the medical azoles, shows also hypersensitivity to widely used azole fungicides, bromuconazole, tebuconazole, difenoconazole, and propiconazole (PubMed:28052140). Impairs growth under hypoxic conditions and attenuation of virulence in murine infection model for aspergillosis (PubMed:28052140). Cures azole resistant phenotype in a clinical strain with cyp51A G54E mutation (PubMed:28052140).
Transcription factor that regulates expression of the genes related to ergosterol biosynthesis, including erg3B, erg24A, erg25A, as well as cyp51A that encodes a target protein of azoles (PubMed:30862750, PubMed:28052140). In coordination with ffmA and ncaA, is responsible for the expression of the ABC transporter abcC/cdr1B/abcG1 related to azole resistance (PubMed:28052140, PubMed:30862750, PubMed:36374043, PubMed:35138125). Directly binds both the cyp51A and abcC/cdr1B/abcG1 promoters at a conserved 34 bp region called the atrR response element (ATRE) (PubMed:30862750, PubMed:35575535, PubMed:35467427, PubMed:28052140). AtrR also binds to the promoter regions of both the sterol response transcription factor srbA and atrR genes themselves, the latter suggesting the possibility that atrR is autoregulated (PubMed:30862750). Regulates also iron uptake, most likely via cooperation with SrbA (PubMed:37093084). AtrR is necessary for hypoxia adaptation and virulence (PubMed:28052140).
Activated by a monovalent cation that binds near, but not in, the active site. The most likely occupant of the site in vivo is potassium. Ion binding induces a conformational change that may alter substrate affinity.
Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.
Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Proteolytically removes the C-terminal three residues of farnesylated proteins.
Has a role in the initiation of DNA replication. Required at S-phase checkpoint (By similarity).
Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. ku70, of the ku70/ku80 heterodimer, binds to the stem loop of tlc1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching (By similarity).
Belongs to the calcineurin regulatory subunit family.
Composed of a catalytic subunit (A) and a regulatory subunit (B).
Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.
Belongs to the DEAD box helicase family. DDX5/DBP2 subfamily.
Allosterically inhibited by 3'-phosphoadenosine 5'-phosphosulfate (PAPS).
Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.
In the C-terminal section; belongs to the APS kinase family.
In the N-terminal section; belongs to the sulfate adenylyltransferase family.
The adenylyl-sulfate kinase (APS kinase) is non-functional. It is involved in allosteric regulation by PAPS. PAPS binding induces a large rotational rearrangement of domains lowering the substrate affinity of the enzyme.
Binds to both phosphatidylinositol (PI) and phosphatidylinositol 3,5-bisphosphate (PIP2).
Lipase which is essential for lysis of subvacuolar cytoplasm to vacuole targeted bodies and intravacuolar autophagic bodies. Involved in the lysis of intravacuolar multivesicular body (MVB) vesicles. The intravacuolar membrane disintegration by atg15 is critical to life span extension (By similarity).
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER.
Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle. Required for growth on ethanol or acetate, but dispensable when fermentable carbon sources are available. Acts also on 2-methylisocitrate.
Involved in spliceosome maturation and the first step of pre-mRNA splicing.
Constituent of COPII-coated endoplasmic reticulum-derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum (By similarity).
Belongs to the methyltransferase superfamily. METL family.
S-adenosyl-L-methionine-dependent methyltransferase.
Lanosterol synthase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (By similarity). ERG7A and ERG7B catalyze the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (PubMed:16110826, PubMed:18191972) (Probable).
Belongs to the DNA polymerase type-B-like family.
Belongs to the cyclophilin-type PPIase family. PPIase D subfamily.
Belongs to the proteasome subunit p55 family.
Interacts with eme1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI) (By similarity).
Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Acts only on small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides (By similarity).
Belongs to the glycosyl hydrolase 51 family.
Belongs to the PPP phosphatase family. PP-2B subfamily.
Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.
Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity.
Belongs to the nucleotide-sugar transporter family. SLC35B subfamily.
May be involved in specific transport of UDP-Gal from the cytosol to the Golgi lumen. Involved in the maintenance of optimal conditions for the folding of secretory pathway proteins in the endoplasmic reticulum (By similarity).
Probably involved in the biogenesis of the COX complex.
Belongs to the acetyl-CoA hydrolase/transferase family.
Heterotetramer; composed of two copies of TRM6 and two copies of TRM61.
Substrate-binding subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA.
Increases sensitivity calcium and to oxidative stress factors, such as paraquat and H(2)O(2) (PubMed:22345349). Leads to attenuated virulence in a murine model of invasive pulmonary aspergillosis through increased killing by the murine alveolar macrophages (PubMed:22345349). Increases the expression of the fumiquinazoline (fmq) cluster and leads to overproduction of fumiquinazoline C (PubMed:33705521).
Transcription factor that is involved in the response to heat shock, oxidative stress, and poor nutrient conditions (PubMed:22345349). Controls expression of oxidative stress response genes such as ccp1, cat1, cat2, sod2; as well as of heat shock genes such as hsf1, hsp30 and hsp90 (PubMed:22345349). Negatively controls the expression of the fumiquinazoline (fmq) cluster via binding to the STRE motifs at the fmqA-D promoters (PubMed:33705521). Plays a role in virulence (PubMed:22345349, PubMed:33705521).
C-22 sterol desaturase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:16110826) (Probable). Erg5 converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (PubMed:16110826, PubMed:18191972) (Probable).
Belongs to the small GTPase superfamily. Rho family. CDC42 subfamily.
Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state.
Belongs to the ABC transporter superfamily. ABCB family. Mitochondrial peptide exporter (TC 3.A.1.212) subfamily.
Expression is up-regulated during biofilm growth (PubMed:21724936). Expression is also induced upon amphotericin B treatment (PubMed:18838595). Expression is down-regulated by tetrandrine and posaconazole in a synergistic manner (PubMed:28080217). Expression is increased in clinical azole-resistant isolates (PubMed:15504870).
Pleiotropic ABC efflux transporter that may be involved in A.fumigatus adaptation to azoles.
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of pyripyropene A, a specific human acyl-coenzyme A:cholesterol acyltransferase 2 inhibitor (PubMed:20861902). The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase pyr1 (PubMed:20861902). Nicotinyl-CoA is then a substrate of polyketide synthase pyr2 to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase pyr6 to yield farnesyl-HPPO (PubMed:20861902). The next steps consist of an epoxidation of farnesyl-HPPO to epoxyfarnesyl-HPPO by FAD-dependent monooxygenase pyr5 and a cyclization of the terpenoid portion by the terpene cyclase pyr4 to yield deacetyl-pyripyropene E (PubMed:20861902). The 2 cytochrome P450 monooxygenases pyr3 and pyr9, and the 2 acetyltransferases pyr7 and pyr8 are involved in the conversion of deacetyl-pyripyropene E into pyripyropene A through several cycles of oxidation and acetylation steps (PubMed:20861902). Pyr7 acetylates deacetyl-pyripyropene E to pyripyropene E which is oxidized to 11-deacetyl-pyripyropene O by pyr3, which is in turn acetylated into pyripyropene O by pyr8 (PubMed:21224862, PubMed:26019565). Pyripyropene O is then oxidized to deacetyl-pyripyropene A by pyr9 (PubMed:21224862). Deacetyl-pyripyropene A is finally acetylated to pyripyropene A by pyr8 (PubMed:26019565).
Allosterically activated by ATP (By similarity). ATP binding is a prerequisite to magnesium and substrate binding. ATP binds to 2 of the subunits in the homotetramer inducing a closure of these 2 subunits and the release of the C-terminal loop, thereby activating the enzyme (By similarity).
IMP-specific 5'-nucleotidase involved in IMP (inositol monophosphate) degradation.
Belongs to the eukaryotic ribosomal protein eS7 family.
Belongs to the Mediator complex subunit 19 family.
Belongs to the fungal cytochrome c oxidase subunit 7a family.
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation.
Belongs to the eukaryotic RPB4 RNA polymerase subunit family.
Plays a role in vesicular protein sorting.
Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of DNA damage, involved in the regulation of DNA damage response mechanism. Required for the control of telomere length and genome stability.
Belongs to the phospholipid scramblase family.
Belongs to the Mediator complex subunit 14 family.
The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity.
Despite the presence of this enzyme, this enzyme may not be involved in verruculogen synthesis in vivo. In contrast to other A.fumigatus strains, strain ATCC MYA-4609 does not produce indole alkaloids such as fumitremorgins and verruculogen. While the biosynthetic pathway is complete, a variation in the O-methyltransferase FtmD (AC Q4WAW6) abolishes production of the tryprostatin A intermediate (PubMed:23649274).
Verruculogen synthase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities (PubMed:19763315, PubMed:23649274, PubMed:31117657). The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA (PubMed:16755625). Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B (PubMed:16000710, PubMed:21105662, PubMed:23090579). The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively (PubMed:19226505). The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B (PubMed:18683158). Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties (PubMed:19763315, PubMed:31117657). In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Belongs to the protein disulfide isomerase family.
Activated by threonine and tyrosine phosphorylation by the upstreamm MAPKK mkk2.
Expression is induced by cell wall-disturbing compounds.
Interacts with flbB, flbC, brlA, and rasB (PubMed:32005734). Interacts with fmqA and fmqC (PubMed:33705521). Interacts with hsp90 (PubMed:33010083).
Mitogen-activated protein kinase; part of cell wall integrity (CWI) signaling pathway composed of pkcA, the bck1-mkk2-mpka MAPK cascade and the downstream rlmA transcription regulator (PubMed:19715768). The CWI signaling pathway regulates cell wall integrity and pyomelanin formation (PubMed:19715768). CWI controls also oxidative stress response, gliotoxin production, iron adaptation and asexual development (PubMed:21883519, PubMed:32005734). Finally, CWI is constitutively required for A.fumigatus to cope with the temperature increase found in the mammalian lung environment, during infection (PubMed:33010083). MpkA positively modulates the expression of fumiquinazoline cluster during conidiogenesis and directly phosphorylates fmqC, and perhaps also fmqA (PubMed:33705521).
Phosphorylated by the upstreamm MAPKK mkk2 (PubMed:19715768). Phosphorylation is induced during asexual development (PubMed:25911225, PubMed:32005734). Phosphorylation is regulated by rlmA (PubMed:27473315).
Results in severe sensitivity against cell wall-disturbing compounds congo red or calcofluor white, and drastic alterations of the fungal morphology (PubMed:19715768). Leads to reduced conidiation during asexual differentiation (PubMed:32005734). Abolishes the production of fumiquinazoline C (PubMed:33705521).
Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Belongs to the mitochondrion-specific ribosomal protein mL46 family.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family.
Belongs to the VPS10-related sortilin family.
Functions as a sorting receptor in the Golgi compartment required for the intracellular sorting and delivery of soluble vacuolar proteins, like carboxypeptidase Y (CPY) and proteinase A. Executes multiple rounds of sorting by cycling between the late Golgi and a prevacuolar endosome-like compartment (By similarity).
Belongs to the threonine synthase family.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. TRM10 family.
S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Involved in ubiquitin-mediated protein degradation. Regulatory factor in the ubiquitin/proteasome pathway that controls the turnover of proteasome substrates. Targets proteasomes to the nucleus and facilitates the degradation of nuclear proteins (By similarity).
Belongs to the ATPase epsilon chain family.
Belongs to the fatty acid desaturase type 1 family. DEGS subfamily.
In the C-terminal section; belongs to the NAD synthetase family.
Belongs to the histidine acid phosphatase family. VIP1 subfamily.
Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, may regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, and exocytosis. Phosphorylates inositol hexakisphosphate (InsP6).
The glycine cleavage system catalyzes the degradation of glycine.
Nuclear chaperone required for maturation and nuclear export of pre-60S ribosome subunits.
Belongs to the glycosyl hydrolase 81 family.
Belongs to the CND2 (condensin subunit 2) family.
Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes.
Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis.
Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
Catalytic component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling.
Component of the SWR1 chromatin-remodeling complex.
Delta(14)-sterol reductase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:33475797). Catalyzes the reduction of the C14=C15 double bond within 4,4,24-trimethyl ergosta-8,14,24(28)-trienolto produce 4,4-dimethylfecosterol (PubMed:33475797). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (PubMed:16110826, PubMed:18191972) (Probable).
Results in decreased hyphal growth and virulence; as well as to hypersensitivity to azole drugs (PubMed:33475797). Deletion of both erg24A and erg24B affects ergosterol biosynthesis and leads to the accumulation of the intermediate 4,4-dimethylcholesta-8,12,24-trienol (PubMed:33475797).
Highly specific D-xylulose kinase which participates in the catabolism of xylose. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters pentose phosphate pathway (By similarity).
Belongs to the class-II aminoacyl-tRNA synthetase family. Alax-L subfamily.
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Alpha-glucuronidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases 4-O-methylglucuronic acid from xylan (By similarity).
Belongs to the glycosyl hydrolase 67 family.
Belongs to the vitamin-B12 independent methionine synthase family.
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Required for 3'-end cleavage and polyadenylation of pre-mRNAs. Also involved in chromosome segregation where it has a role in chromosome attachment to the mitotic spindle (By similarity).
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. MOCOS subfamily.
Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
Component of the 7-subunit TFIIH core complex composed of XPB/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is active in NER. The core complex associates with the 3-subunit CTD-kinase module TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription.
Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily.
Belongs to the protein kinase superfamily. PAN3 family.
Contains a pseudokinase domain. The protein kinase domain is predicted to be catalytically inactive because some of the residues important for catalytic activity are substituted and it lacks the equivalent of the binding site for a peptide substrate. However, it has retained an ATP-binding site and ATP-binding is required for mRNA degradation, stimulating the activity of the pan2 nuclease in vitro. The nucleotide-binding site is juxtaposed to the RNase active site of pan2 in the complex and may actually bind nucleosides of a poly(A) RNA rather than ATP, feeding the poly(A)-tail to the active site of the deadenylase and thus increasing the efficiency with which this distributive enzyme degrades oligo(A) RNAs.
Homodimer. Forms a heterotrimer with a catalytic subunit pan2 to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts (via PAM-2 motif) with poly(A)-binding protein pab1 (via PABC domain), conferring substrate specificity of the enzyme complex.
Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein pab1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by xrn1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. pan3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit pan2 to mRNA via its interaction with RNA and with pab1.
The N-terminal zinc finger binds to poly(A) RNA.
The pseudokinase domain, the coiled-coil (CC), and C-terminal knob domain (CK) form a structural unit (PKC) that forms an extensive high-affinity interaction surface for pan2.
Belongs to the amino acid-polyamine-organocation (APC) superfamily. YAT (TC 2.A.3.10) family.
Belongs to the eukaryotic AdoMetDC family.
Belongs to the sphingosine N-acyltransferase family.
Functions as a nucleotide exchange factor (NEF) for Hsp70 chaperones which accelerates the release of ADP. Required for fully efficient Hsp70-mediated folding of proteins (By similarity).
Belongs to the clathrin heavy chain family.
Involved in cell death (apoptosis) (By similarity). Required for the apoptotic-like loss of membrane phospholipid asymmetry at stationary phase and facilitates growth under conditions of endoplasmic reticulum stress.
Belongs to the nucleoporin Nup133 family.
Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. Acts on lutean, pustulan and 1,6-oligo-beta-D-glucosides (By similarity).
Chaperone required for the export of the chitin synthase chs3 from the endoplasmic reticulum.
Trifunctional enzyme bearing the Gln amidotransferase (GATase) domain of anthranilate synthase, indole-glycerolphosphate synthase, and phosphoribosylanthranilate isomerase activities.
Belongs to the phage and mitochondrial RNA polymerase family.
Stereoselective keto-reductase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) (PubMed:23488861, PubMed:24568283). Within the pathway, the keto-reductase af490 acts as a 5-dehydrofumagillol 5-reductase that stereoselectively reduces 5-keto-fumagillol to 5R-hydroxy-seco-sesquiterpene (PubMed:24568283). The pathway begins with the conversion of farnesyl pyrophosphate (FPP) to beta-trans-bergamotene by the membrane-bound beta-trans-bergamotene synthase af520. The multifunctional cytochrome P450 monooxygenase af510 then converts beta-trans-bergamotene into 5-keto-demethoxyfumagillol via several oxydation steps. 5-keto-demethoxyfumagillol is then subjected to successive C-6 hydroxylation and O-methylation by the dioxygenase af480 and O-methyltransferase af390-400, respectively, to yield 5-keto-fumagillol, which is then stereoselectively reduced by the keto-reductase af490 to 5R-hydroxy-seco-sesquiterpene. The next step is the polyketide transferase af380-catalyzed transfer of a dodecapentaenoyl group synthesized by the polyketide synthase af370 onto 5R-hydroxy-seco-sesquiterpene which leads to the production of prefumagillin. Finally, oxidative cleavage by the monooxygenase af470 converts prefumagillin to fumagillin (PubMed:24568283) (Probable).
Strongly decreases the production of fumagillin (PubMed:24568283).
Was first identified as a pseudogene since it seemed to be altered polyketide synthase with only the dehydratase (DH) and ketoreductase (KR) domains remaining (PubMed:23488861). Further study showed it encoded indeed for a functional keto-reductase involved in fumagillin biosynthesis (PubMed:24568283).
Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.
Forms a fork protection complex (FPC) with csm3 and which is required for chromosome segregation during meiosis and DNA damage repair. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors (By similarity).
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Cgi121 acts as an allosteric effector that regulates the t(6)A activity of the complex. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators. Cgi121 is not required for tRNA modification (By similarity).
Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus.
Component of the TIM23 complex, at least composed of TIM23/timX, TIM17/timQ, tim50 and TIM21/timU.
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Required to keep the TOM and the TIM23 complexes in close contact. At some point, it is released from the TOM23 complex to allow protein translocation into the mitochondrial matrix (By similarity).
Supercomplex made of cofactors A to E. Cofactors A and D function by capturing and stabilizing tubulin in a quasi-native conformation. Cofactor E binds to the cofactor D-tubulin complex; interaction with cofactor C then causes the release of tubulin polypeptides that are committed to the native state.
Leads to reduced capacity for protease secretion and impairs growth when challenged to assimilate nutrients from complex substrates (PubMed:19132084). In addition, exhibits increased susceptibility to antifungal agents that disrupt the membrane or cell wall and shows attenuated virulence in multiple mouse models of invasive aspergillosis (PubMed:19132084, PubMed:22028661, PubMed:21217201). Affects the expression of only a small amount of genes (PubMed:22028661). Leads to hypersensitivity to agents that block calcineurin-dependent signaling (PubMed:32487759). Impairs the UPR-dependent induction of spfA (PubMed:34663092).
Master transcriptional regulator of the unfolded protein response (UPR) that recognizes and binds to the UPR element (UPRE) in the promoter of UPR-regulated genes (PubMed:19132084, PubMed:22028661, PubMed:21217201). In the canonical UPR pathway, the ireA RNase splices the cytoplasmic mRNA hacA, which alters the reading frame to allow translation of the bZIP transcription factor hacA (PubMed:19132084, PubMed:33087521). Induces the expression of pmrA, scrA and spfA in response to UPR (PubMed:32487759, PubMed:34663092).
Not translated. The unspliced HAC1 mRNA is stable, located in the cytoplasm, and is associated with polyribosomes, yet does not produce protein. Translational attenuation is due to basepairing of the intron with the 5'-UTR of the mRNA.
Belongs to the eukaryotic ribosomal protein eS8 family.
Belongs to the protein-tyrosine phosphatase family. Non-receptor class myotubularin subfamily.
Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Involved in nucleotide metabolism via production of dUMP, the immediate precursor of thymidine nucleotides, and decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Belongs to the archaeal rpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family.
Belongs to the GHMP kinase family. Homoserine kinase subfamily.
Belongs to the V-ATPase C subunit family.
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity.
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex.
Belongs to the eukaryotic ribosomal protein eL19 family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family.
Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle.
Changes the gray-green conidial pigment to a brown color (PubMed:26972005).
Expression is up-regulated upon hyphal competency and drastically increased during conidiation (PubMed:24123270). Expression is controlled by brlA, the master regulator of conidiophore development, and is responsive to the copper level in the medium (PubMed:24123270).
Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment and a structural component of the conidial wall (PubMed:10515939, PubMed:14970241, PubMed:19156203). The first step of the pathway is the production of the heptaketide naphtopyrone YWA1 by the polyketide synthase alb1 though condensation of acetyl-CoA with malonyl-CoA (PubMed:10515939). The naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase ayg1 though chain-length shortening (PubMed:10515939). 1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to yield scytalone (PubMed:10515939). The scytalone dehydratase arp1 then reduces scytalone to 1,3,8-THN (PubMed:10515939). 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to yield vermelone (PubMed:10515939). Vermelone is further converted by the multicopper oxidase abr1 to 1,8-DHN (PubMed:10515939). Finally the laccase abr2 transforms 1,8-DHN to DHN-melanin (PubMed:10515939). DHN-melanin biosynthesis appears to be initiated in endosomes where early enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to melanin deposition on the cell surface where late enzymes (abr1 and abr2) localize (PubMed:26972005). DHN-melanin is an important structural component of the outer cell wall and is required for the presence of conidial surface hydrophobins (PubMed:19703288). DHN-melanin also plays a crucial role in fungal virulence, including a protective role against the host's immune defenses (PubMed:19156203, PubMed:20145078, PubMed:21747802, PubMed:21573171, PubMed:24818666). DHN-melanin protects also conidia against amoeba predation (PubMed:25684622).
Component of a fungal signal recognition particle (SRP) complex that consists of a 7SL RNA molecule (scR1) and at least six protein subunits: SRP72, SRP68, SRP54, SEC65, SRP21 and SRP14.
ABC efflux transporter that seems not to be able to transport azoles, nor rhodamine 6G (R-6G), a known substrate for many ABC transporters.
GTPase-activating protein for the ADP ribosylation factor family.
SNARE required for protein transport between the ER and the Golgi complex.
Belongs to the pantothenate synthetase family.
Belongs to the thioesterase PaaI family.
Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
Belongs to the eukaryotic ribosomal protein eL20 family.
Belongs to the queuine tRNA-ribosyltransferase family. QTRT2 subfamily.
Heterodimer of a catalytic subunit and an accessory subunit.
Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Belongs to the adaptor complexes medium subunit family. Delta-COP subfamily.
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network.
Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with atg5 through a ubiquitin-like conjugating system involving also atg7 as an E1-like activating enzyme and atg10 as an E2-like conjugating enzyme, is essential for its function. The atg12-atg5 conjugate functions as an E3-like enzyme which is required for lipidation of atg8 and atg8 association to the vesicle membranes (By similarity).
Belongs to the U2 small nuclear ribonucleoprotein A family.
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
Leads to reduced levels of beta-1,3-glucan in the cell wall and impairs pathogenicity in an experimental murine model of invasive pulmonary aspergillosis (PubMed:18456861, PubMed:18298443, PubMed:19015336). Increases sensitivity to heat shock (PubMed:18298443).
Transcription factor involved in the regulation of calcium ion homeostasis (PubMed:18298443). Regulates genes encoding calcium transporters, transcription factors and genes that could be directly or indirectly involved in calcium metabolism (PubMed:20078882). Supports especially pmcA, pmcB and pmcC expression encoding for calcium-translocating P-type ATPases (PubMed:18298443, PubMed:22649543). Binds target promoters at motif A[GT][CG]CA[AC][AG] (PubMed:25196896). Plays an essential role germination, radial growth, and asexual development (PubMed:18456861, PubMed:18298443). Also plays a major role in proper chitin and glucan incorporation into the cell wall (PubMed:19015336). Involved in the high-osmolarity glycerol response (HOG) signaling pathway (PubMed:25196896). Required for pathogenicity in an experimental murine model of invasive pulmonary aspergillosis (PubMed:18456861, PubMed:18298443, PubMed:22649543, PubMed:25196896).
Essential role in pre-mRNA splicing. Also essential for entry into mitosis (G2/M progression) as well as for chromosome segregation during mitosis.
Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization.
Belongs to the cyclophilin-type PPIase family. PPIase H subfamily.
May negatively regulate the snf1 kinase.
The RNA gate region regulates mRNA cap recognition to prevent promiscuous mRNA-binding before assembly of eif3d into the full eukaryotic translation initiation factor 3 (eIF-3) complex.
mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
Mediates the transfer of lipids between membranes at organelle contact sites. May play a role in mitochondrial lipid homeostasis.
Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.
Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family.
Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone.
In contrast to other lysine histone methyltransferases, it does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones.
Ubiquitination of histone H2B to form H2BK123ub1 is required for efficient DOT1 methyltransferase activity on histone H3.
Belongs to the GST superfamily. Zeta family.
Maleylacetoacetate isomerase; part of the L-tyrosine degradation gene cluster that mediates the biosynthesis of the brownish pigment pyomelanin as an alternative melanin (PubMed:19028908, PubMed:22046314). The 4-hydroxyphenylpyruvate dioxygenase hppD catalyzes the conversion of 4-hydroxyphenylpyruvate to homogentisic acid (HGA) (PubMed:19028908, PubMed:22046314). The protein hmgX is crucial for this conversion and thus, probably functions as an accessory factor to mediate specific activity of hppD (PubMed:22046314). The homogentisate 1,2-dioxygenase hmgA is then involved in the cleavage of the aromatic ring of HGA and its conversion to 4-maleylacetoacetate (PubMed:19028908, PubMed:19715768). When hmgA activity is lowered by the cell wall integrity (CWI) signaling pathway, HGA accumulates and leads to the production of pyomelanin through benzoquinone acetic acid after oxidation and polymerization (PubMed:19715768). On the opposite, in non-stress conditions, both hppD and hmgA activities are balanced and HGA is degraded into 4-maleylacetoacetate (PubMed:19715768). 4-maleylacetoacetate is further converted to 4-fumarylacetoacetate by the maleylacetoacetate isomerase maiA, which is degraded into fumarate and acetoacetate by the fumarylacetoacetase fahA (Probable).
Causes an allergic reaction in human. Binds to IgE.
Belongs to the SAICAR synthetase family.
Belongs to the glycosyl hydrolase 2 family. Beta-mannosidase B subfamily.
Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of beta-mannosidic oligosaccharides of various complexity and length. Prefers mannobiose over mannotriose and has no activity against polymeric mannan. Is also severely restricted by galactosyl substitutions at the +1 subsite (By similarity).
In contrast to clade A beta-mannosidases, which are likely secreted, clade B proteins appear to be intracellular.
Belongs to the polyprenol kinase family.
Expression is induced by L-tyrosine (PubMed:22046314). Expression is positively regulated by the cluster-specific transcription factor hmgR (PubMed:22046314).
Impairs growth on L-tyrosine as the sole carbon source and affects homogentisic acid and pyomelanin formation.
Part of the L-tyrosine degradation gene cluster that mediates the biosynthesis of the brownish pigment pyomelanin as an alternative melanin (PubMed:19028908, PubMed:22046314). The 4-hydroxyphenylpyruvate dioxygenase hppD catalyzes the conversion of 4-hydroxyphenylpyruvate to homogentisic acid (HGA) (PubMed:19028908, PubMed:22046314). The protein hmgX is crucial for this conversion and thus, probably functions as an accessory factor to mediate specific activity of hppD (PubMed:22046314). The homogentisate 1,2-dioxygenase hmgA is then involved in the cleavage of the aromatic ring of HGA and its conversion to 4-maleylacetoacetate (PubMed:19028908, PubMed:19715768). When hmgA activity is lowered by the cell wall integrity (CWI) signaling pathway, HGA accumulates and leads to the production of pyomelanin through benzoquinone acetic acid after oxidation and polymerization (PubMed:19715768). On the opposite, in non-stress conditions, both hppD and hmgA activities are balanced and HGA is degraded into 4-maleylacetoacetate (PubMed:19715768). 4-maleylacetoacetate is further converted to 4-fumarylacetoacetate by the maleylacetoacetate isomerase maiA, which is degraded into fumarate and acetoacetate by the fumarylacetoacetase fahA (Probable).
May participate in the translocation of oligosaccharide from the cytoplasmic side to the lumenal side of the endoplasmic reticulum membrane.
Monomer. Component of the 2-(3-amino-3-carboxypropyl)histidine synthase complex composed of dph1, dph2, dph3 and a NADH-dependent reductase, predominantly cbr1.
NADH-dependent reductase for dph3 and cytochrome b5. Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. Dph1 and dph2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising dph3 and a NADH-dependent reductase, predominantly cbr1. By reducing dph3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes.
Belongs to the glycosyltransferase group 1 family.
Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
The AWS and SET domains are necessary for transcription repression.
4-dimethylallyltryptophan N-methyltransferase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:23435153, PubMed:26972831). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:15870460). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482, PubMed:21409592). EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482). EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482). Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831). Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909).
Belongs to the universal ribosomal protein uS9 family.
Beta-trans-bergamotene synthase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) (PubMed:23488861, PubMed:24568283, PubMed:34829223). Within the pathway, the membrane-bound fumagillin beta-trans-bergamotene synthase af520 converts farnesyl pyrophosphate (FPP) to beta-trans-bergamotene (PubMed:23488861). The pathway begins with the conversion of FPP to beta-trans-bergamotene by af520. The multifunctional cytochrome P450 monooxygenase af510 then converts beta-trans-bergamotene into 5-keto-demethoxyfumagillol via several oxydation steps. 5-keto-demethoxyfumagillol is then subjected to successive C-6 hydroxylation and O-methylation by the dioxygenase af480 and O-methyltransferase af390-400, respectively, to yield 5-keto-fumagillol, which is then stereoselectively reduced by the keto-reductase af490 to 5R-hydroxy-seco-sesquiterpene. The next step is the polyketide transferase af380-catalyzed transfer of a dodecapentaenoyl group synthesized by the polyketide synthase af370 onto 5R-hydroxy-seco-sesquiterpene which leads to the production of prefumagillin. Finally, oxidative cleavage by the monooxygenase af470 converts prefumagillin to fumagillin (PubMed:24568283) (Probable).
Completely abolishes the production of fumagillin and decreases virulence.
Belongs to the BPG-independent phosphoglycerate mutase family.
Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Required for the function of coenzyme Q in the respiratory chain. May serve as a chaperone or may be involved in the transport of Q6 from its site of synthesis to the catalytic sites of the respiratory complexes.
Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Belongs to the ALG10 glucosyltransferase family.
Belongs to the universal ribosomal protein uS3 family.
Required for replication-independent chromatin assembly and for the periodic repression of histone gene transcription during the cell cycle.
Belongs to the UTP23/FCF1 family. FCF1 subfamily.
Belongs to the eukaryotic ribosomal protein eL24 family.
Required for growth under high-pressure and low-temperature conditions.
FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via a ferredoxin/ferredoxin reductase system to COQ6.
Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes.
Belongs to the aldo/keto reductase family. Glutamate--cysteine ligase light chain subfamily.
Heterodimer of a catalytic heavy chain and a regulatory light chain.
Mg(2+) is required for catalysis and for stabilizing the dimer.
Expression is induced by gliotoxin (PubMed:20548963). Expression is controlled by veA (PubMed:23087369). Expression is controlled by brlA and abaA (PubMed:26032501). Expression is also regulated by rsmA (PubMed:23671611). Expression is also influenced by SfaD and GpgA (PubMed:19915845).
Impairs the expression of the majority of genes in the gliotoxin cluster with the exception of gliT (PubMed:17030582, PubMed:20548963, PubMed:21612254).
Transcription factor that regulates gliotoxin production and contributes to virulence (PubMed:15979823, PubMed:17030582, PubMed:20548963, PubMed:21612254).
Belongs to the DNA repair enzymes AP/ExoA family.
Probably binds two magnesium or manganese ions per subunit.
Maintains high levels of reduced glutathione in the cytosol.
Belongs to the cAMP-dependent kinase regulatory chain family.
Tetramer, composed of 2 regulatory (R) and 2 catalytic (C) subunits. In the presence of cAMP it dissociates into 2 active monomeric C subunits and an R dimer (By similarity).
May form heterododecamers with RVB2. Component of the SWR1 chromatin remodeling complex, the INO80 chromatin remodeling complex, and of the R2TP complex (By similarity).
Belongs to the universal ribosomal protein uL5 family.
Required for proper folding and/or the stability of a subset of proteins in the endoplasmic reticulum. Component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the mannosyltransferase gpi14 (By similarity).
First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.
Heterodimer. The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an mRNA 5'-triphosphate monophosphatase.
Belongs to the eukaryotic ribosomal protein eL38 family.
Belongs to the uroporphyrinogen decarboxylase family.
Integral membrane transporter that imports quinic acid to be catabolized as a carbon source.
Ubiquitinated. Deubiquitinated by creB, probably to control its activity or amount.
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site.
Belongs to the bacterial ribosomal protein bL12 family.
In the C-terminal section; belongs to the eukaryotic ribosomal protein eS31 family.
Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment.
Belongs to the Mediator complex subunit 22 family.
Belongs to the complex I LYR family. SDHAF3 subfamily.
Interacts with the iron-sulfur protein subunit within the SDH catalytic dimer.
Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. May act together with SDHAF1.
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in endosomal cargo sorting.
Belongs to the DNA photolyase class-1 family.
Expression is induced by gliotoxin, but appears to be independently regulated compared to all other cluster components (PubMed:20548963). Expression is positively regulated by the brlA and abaA transcription factors (PubMed:26032501). Expression is also regulated by rsmA (PubMed:23671611).
Impairs gliotoxin oxidation, leading to unchecked methylation and subsequent significant S-adenosylmethionine (SAM) depletion and S-adenosylhomocysteine (SAH) overproduction which in turn significantly contributes to hypersensitivity to gliotoxin of gliT-deficient A.fumigatus (PubMed:26150413). Results in altered expression of over 200 genes involved in many functions (PubMed:25311525).
Thioredoxin reductase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). GliT is required for self-protection against gliotoxin (PubMed:20548963, PubMed:26150413). GliT plays a role in preventing dysregulation of the methyl/methionine cycle to control intracellular S-adenosylmethionine (SAM) depletion and S-adenosylhomocysteine (SAH) homeostasis during gliotoxin biosynthesis and exposure (PubMed:26150413).
Belongs to the nucleoporin Nup84/Nup107 family.
Belongs to the eukaryotic ribosomal protein eL33 family.
Belongs to the cytochrome c oxidase subunit 6B family.
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate.
Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 2 subfamily.
Belongs to the acetyltransferase family. NAA40 subfamily.
tRNA nucleus export receptor which facilitates tRNA translocation across the nuclear pore complex. Involved in pre-tRNA splicing, probably by affecting the interaction of pre-tRNA with splicing endonuclease (By similarity).
Assembly factor required for Rieske Fe-S protein RIP1 incorporation into the cytochrome b-c1 (CIII) complex. Functions as a chaperone, binding to this subunit within the mitochondrial matrix and stabilizing it prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane. Modulates the mitochondrial matrix zinc pool (By similarity).
Belongs to the complex I LYR family. MZM1 subfamily.
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Belongs to the CSN7/EIF3M family. CSN7 subfamily.
Belongs to the eukaryotic RPA49/POLR1E RNA polymerase subunit family.
Belongs to the complex I 30 kDa subunit family.
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). Gliotoxin contributes to pathogenesis during invasive aspergillosis (PubMed:17601876, PubMed:18199036). In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species (PubMed:17601876).
Required for the assembly of cytochrome c oxidase.
Belongs to the adenylosuccinate synthetase family.
Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
The GINS complex plays an essential role in the initiation of DNA replication. Has a role in chromosome segregation (By similarity).
Belongs to the methyltransferase superfamily. LCMT family.
Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Belongs to the complex I NDUFA13 subunit family.
Complex I functions in the transfer of electrons from NADH to the respiratory chain. Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis.
Expression is increased in clinical azole-resistant isolates and by the presence of itraconazole (PubMed:12709346, PubMed:15504870, PubMed:29124846). Expression is down-regulated by tetrandrine and posaconazole in a synergistic manner (PubMed:28080217). Expression is also induced upon amphotericin B treatment (PubMed:18838595).
Major facilitator superfamily transporter that confers resistance to azoles such as itraconazole.
Belongs to the acireductone dioxygenase (ARD) family.
Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes an acireductone dioxygenase reaction producing 2-keto-4-methylthiobutyrate, while nickel-binding promotes an acireductone dioxygenase reaction producing 3-(methylsulfanyl)propanoate.
Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose.
ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity).
Associates with the nuclear pore complex.
Belongs to the DEAD box helicase family. DDX19/DBP5 subfamily.
This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand.
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
Belongs to the thymidylate kinase family.
Belongs to the methyltransferase superfamily. RRP8 family.
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of adenine in helix 25.1 in 25S rRNA. Required both for ribosomal 40S and 60S subunits biogenesis. Required for efficient pre-rRNA cleavage at site A2.
Acetylation of histone H3 leads to transcriptional activation. H3K14ac formation by gcn5 is promoted by H3S10ph. H3K14ac can also be formed by esa1. H3K56ac formation occurs predominantly in newly synthesized H3 molecules during G1, S and G2/M of the cell cycle and may be involved in DNA repair (By similarity).
Mono-, di- and trimethylated by the COMPASS complex to form H3K4me1/2/3. H3K4me activates gene expression by regulating transcription elongation and plays a role in telomere length maintenance. H3K4me enrichment correlates with transcription levels, and occurs in a 5' to 3' gradient with H3K4me3 enrichment at the 5'-end of genes, shifting to H3K4me2 and then H3K4me1. Methylated by set2 to form H3K36me. H3K36me represses gene expression. Methylated by dot1 to form H3K79me. H3K79me is required for association of SIR proteins with telomeric regions and for telomeric silencing. The COMPASS-mediated formation of H3K4me2/3 and the dot1-mediated formation of H3K79me require H2BK123ub1 (By similarity).
Phosphorylated to form H3S10ph. H3S10ph promotes subsequent H3K14ac formation and is required for transcriptional activation through TBP recruitment to the promoters (By similarity).
To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H3K4me1/2/3 = mono-, di- and trimethylated Lys-5; H3K9ac = acetylated Lys-10; H3K9me1 = monomethylated Lys-10; H3S10ph = phosphorylated Ser-11; H3K14ac = acetylated Lys-15; H3K14me2 = dimethylated Lys-15; H3K18ac = acetylated Lys-19; H3K18me1 = monomethylated Lys-19; H3K23ac = acetylated Lys-24; H3K23me1 = monomethylated Lys-24; H3K27ac = acetylated Lys-28; H3K27me1/2/3 = mono-, di- and trimethylated Lys-28; H3K36ac = acetylated Lys-37; H3K36me1/2/3 = mono-, di- and trimethylated Lys-37; H3K56ac = acetylated Lys-57; H3K64ac = acetylated Lys-65; H3K79me1/2/3 = mono-, di- and trimethylated Lys-80.
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for l- to d- amino acid conversion) are present within the NRP synthetase. NRPS9 has the following architecture: C-A-T-C.
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities (PubMed:19226505, PubMed:23649274). The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA (PubMed:16755625). Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B (PubMed:16000710, PubMed:21105662, PubMed:23090579). The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively (PubMed:19226505). The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B (PubMed:18683158). Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties (PubMed:19763315). In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate.
Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate.
Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
Belongs to the MPDU1 (TC 2.A.43.3) family.
Belongs to the class-II DAHP synthase family.
Binds 1 divalent cation per subunit. The enzyme is active with manganese, cobalt or cadmium ions.
Belongs to the helicase family. UvrD subfamily.
Autoacetylation at Lys-295 is required for proper function.
Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z (By similarity). Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac (By similarity). The NuA4 complex is involved in the DNA damage response and is required for chromosome segregation. The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) through homologous recombination (By similarity). Recruitment to promoters depends on H3K4me. Also acetylates non-histone proteins (By similarity). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-hydroxyisobutyrylation and crotonylation, respectively (By similarity).
The ESA1-RPD3 motif is common to ESA1 and RPD3 and is required for ESA1 histone acetyl-transferase (HAT) activity and RPD3 histone deacetylase (HDAC) activity.
Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.
Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and dUMP as phosphate acceptors, but can also use CMP, dCMP and AMP.
Belongs to the universal ribosomal protein uL18 family.
E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of atg8. The atg12-atg5 conjugate plays a role of an E3 and promotes the transfer of atg8 from atg3 to phosphatidylethanolamine (PE). This step is required for the membrane association of atg8. The formation of the atg8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity).
Monomer. Interacts with atg8 through an intermediate thioester bond through the C-terminal Gly of atg8. Also interacts with the 40 amino acid C-terminal region of the E1-like atg7 enzyme. Interacts also with the atg12-atg5 conjugate.
The flexible region (FR) is required for atg7-binding.
The handle region (HR) contains the atg8 interaction motif (AIM) and mediates binding to atg8. It is crucial for the cytoplasm-to-vacuole targeting pathway (By similarity).
Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks.
ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Also required for efficient mitochondrial translation (By similarity).
Expression is controlled by the transcriptional regulator srbA.
Leads to the accumulation of 4-methyl fecosterol and 4,4-dimethyl fecosterol.
Sterol-C4-methyl oxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:25107308). Erg25B is a catalytic component of the C-4 demethylation complex that catalyzes the conversion of 4,4-dimethylfecosterol into fecosterol via 4-methylfecosterol (PubMed:25107308). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (PubMed:16110826, PubMed:18191972) (Probable).
Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family.
Pyridoxal 5'-phosphate (PLP)-binding protein, which may be involved in intracellular homeostatic regulation of pyridoxal 5'-phosphate (PLP), the active form of vitamin B6.
Glucosidase involved in the degradation of cellulosic biomass. Has both alpha- and beta-glucosidase activity (By similarity).
Required for proper 27S pre-rRNA processing and 60S ribosome subunit assembly.
Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
Forms the NCT transcriptional regulatory complex with nctA and nctB.
Regulates transcription in association with TATA binding protein (TBP). Removes TBP from the TATA box via its C-terminal ATPase activity. Both transcription activation and repression require its ATPase activity (By similarity). Part of the NCT transcriptional regulatory complex that acts as a key regulator of ergosterol biosynthesis and the azole exporter cdr1B (PubMed:31969561). The NCT complex binds the promoters of genes linked to azole susceptibility, and especially represses the expression of cdr1B transporter (PubMed:31969561).
Catalyzes the intermembrane transfer of phosphatidylglycerol and phosphatidylinositol.
Belongs to the SIMIBI class G3E GTPase family. UreG subfamily.
Belongs to the complex I NDUFA2 subunit family.
Belongs to the cytochrome c-type heme lyase family.
Lyase that catalyzes the covalent linking of the heme group to the cytochrome C apoprotein to produce the mature functional cytochrome.
Belongs to the arsenical resistance-3 (ACR3) (TC 2.A.59) family.
Belongs to the mitochondrion-specific ribosomal protein mS41 family.
ABC efflux transporter that is able to transport rhodamine 6G (R-6G), a known substrate for many ABC transporters, but seems not to transport azoles.
Expression is induced in triazole-resistant isolates.
Belongs to the homoserine dehydrogenase family.
Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine at position 1191 (Psi1191) in 18S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA.
Belongs to the TDD superfamily. TSR3 family.
Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Belongs to the glycosyl hydrolase 30 family.
Endoglucanase that has highest activity on the linear beta-1,6-glucan pustulan and lower activity against laminarin (beta-1,3-glucans with beta-1,6-branches). Is active on C.albicans cell walls allowing the release of a previously described cell wall proteins.
Belongs to the FKBP-type PPIase family. FKBP2 subfamily.
This enzyme is required for electron transfer from NADP to cytochrome P450.
Transcription factor that controls the expression of genes related to the process of conidiation and adherence and regulates biofilm formation (PubMed:26529322). Controls conidiation and adhesion primarily by affecting the expression of the three regulatory genes flbB, stuA and medA (PubMed:26529322). Required for virulence in an egg and a mouse infection model (PubMed:26529322).
Belongs to the universal ribosomal protein uS5 family.
Belongs to the PPP phosphatase family. PP-Z subfamily.
Belongs to the cyclophilin-type PPIase family. PPIL3 subfamily.
Belongs to the oligoribonuclease family.
ATP-dependent DNA helicase important for chromosome transmission and normal cell cycle progression in G(2)/M (By similarity). May have a role in changing DNA topology to allow the loading of proteins involved in maintaining sister chromatid cohesion in the vicinity of the centromeres (By similarity). Has a specific role in chromosome segregation during meiosis II.
Belongs to the helicase family. RAD3/XPD subfamily.
Belongs to the uracil-DNA glycosylase (UDG) superfamily. UNG family.
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Acts as catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover (By similarity). Ccr4 has 3'-5' RNase activity with a strong preference for polyadenylated substrates and also low exonuclease activity towards single-stranded DNA (By similarity).
Belongs to the peroxidase family. Cytochrome c peroxidase subfamily.
Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Binds ubiquitin and polyubiquitinated proteins.
Probable aspartic protease. May be involved in the regulation of exocytosis. Acts as a linker between the 19S proteasome and polyubiquitinated proteins via UBA domain interactions with ubiquitin for their subsequent degradation. Required for S-phase checkpoint control.
Component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. May be involved in signaling by recognizing appropriately phosphorylated substrates via its arrestin domains and then recruit a HECT-type ubiquitin ligase such as hulA, leading to ubiquitination of the substrate, providing a link between ubiquitination and phosphorylation in protein regulation and stability (By similarity).
Belongs to the class V-like SAM-binding methyltransferase superfamily.
Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.
Component of the COMPASS (Set1C) complex.
Belongs to the cyclophilin-type PPIase family. PPIL2 subfamily.
May catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins. May also function as a chaperone, playing a role in intracellular transport of proteins. May also have a protein ubiquitin ligase activity acting as an E3 ubiquitin protein ligase or as a ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on proteins.
Associates with 90S and pre-40S pre-ribosomal particles.
Component of the 90S pre-ribosome involved in the maturation of rRNAs. Required for early cleavages of the pre-RNAs in the 40S ribosomal subunit maturation pathway (By similarity).
Belongs to the WD repeat PRL1/PRL2 family.
Involved in pre-mRNA splicing and required for cell cycle progression at G2/M.
Required for pre-18S rRNA processing. May bind microtubules (By similarity).
Abolishes the production of pseurotin (PubMed:17722120, PubMed:24082142).
Expression is under the control of StuA, which is responsible for transcriptional activation during acquisition of developmental competence (PubMed:16207816). Expression is also induced under hypoxic conditions (PubMed:21388144).
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module (PubMed:17464044). Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product (PubMed:17464044). Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for l- to d- amino acid conversion) are present within the NRP synthetase (PubMed:17464044). NRPS14 contains also a ketoacyl synthase domain (KS), an acyl transferase domain (AT), a dehydratase domain (DH), and 2 ketoreductase domains (KR) (PubMed:17464044). NRPS14 has the following architecture: KS-AT-DH-KR-T-C-A-T-KR (PubMed:17464044).
PKS-NRPS hybrid synthetase; part of the gene cluster that mediates the biosynthesis of pseurotin A, a competitive inhibitor of chitin synthase and an inducer of nerve-cell proliferation (PubMed:17722120, PubMed:17464044, PubMed:24082142, PubMed:24939566). The PKS-NRPS hybrid synthetase psoA is responsible for the biosynthesis of azaspirene, one of the first intermediates having the 1-oxa-7-azaspiro[4,4]-non-2-ene-4,6-dione core of pseurotin, via condensation of one acetyl-CoA, 4 malonyl-CoA, and a L-phenylalanine molecule (PubMed:24082142, PubMed:24939566). The dual-functional monooxygenase/methyltransferase psoF seems to be involved in the addition of the C3 methyl group onto the pseurotin scaffold (PubMed:24939566). Azaspirene is then converted to synerazol through 4 steps including oxidation of C17 by the cytochrome P450 monooxygenase psoD, O-methylation of the hydroxy group of C8 by the methyltransferase psoC, and the trans-to-cis isomerization of the C13 olefin by the glutathione S-transferase psoE (PubMed:24939566). The fourth step of synerazol production is performed by the dual-functional monooxygenase/methyltransferase psoF which seems to catalyze the epoxidation of the intermediate deepoxy-synerazol (PubMed:24939566). Synerazol can be attacked by a water molecule nonenzymatically at two different positions to yield two diol products, pseurotin A and pseurotin D (PubMed:24939566).
Transcriptional coactivator that stimulates GCN4-dependent transcriptional activity by bridging the DNA-binding region of GCN4 and TBP (SPT15), thereby recruiting TBP to GCN4-bound promoters. Involved in induction of the ribosome quality control (RQC) pathway; a pathway that degrades nascent peptide chains during problematic translation. Required to prevent stalled ribosomes from frameshifting.
Acts as a major allergen in patients suffering from extrinsic bronchial asthma. Binds to IgE.
Alkaline protease that allows assimilation of proteinaceous substrates. Acts as a significant virulence factor in invasive aspergillosis. Required for regular sporulation.
Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. Is also involved in ribosome biogenesis. Associates with pre-60S subunits in the nucleus and is involved in its nuclear export.
Monomer. Associates with the 60S ribosomal subunit.
Phosphorylation at Ser-174 and Ser-175 promotes nuclear export.
Homodimer (By similarity). Part of the atg5-atg12/atg16 complex. Several units of each may be present in this complex (By similarity).
Stabilizes the atg5-atg12 conjugate which is necessary for autophagy. The atg5-atg12/atg16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS). Recruits also atg3 to the PAS. Involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress (By similarity).
Abolishes the production of pseurotin but leads to the accumulation of deepoxy-synerazol (PubMed:24082142, PubMed:24939566).
Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of pseurotin A, a competitive inhibitor of chitin synthase and an inducer of nerve-cell proliferation (PubMed:24082142, PubMed:24939566). The PKS-NRPS hybrid synthetase psoA is responsible for the biosynthesis of azaspirene, one of the first intermediates having the 1-oxa-7-azaspiro[4,4]-non-2-ene-4,6-dione core of pseurotin, via condensation of one acetyl-CoA, 4 malonyl-CoA, and a L-phenylalanine molecule (PubMed:24082142, PubMed:24939566). The dual-functional monooxygenase/methyltransferase psoF seems to be involved in the addition of the C3 methyl group onto the pseurotin scaffold (PubMed:24939566). Azaspirene is then converted to synerazol through 4 steps including oxidation of C17 by the cytochrome P450 monooxygenase psoD, O-methylation of the hydroxy group of C8 by the methyltransferase psoC, and the trans-to-cis isomerization of the C13 olefin by the glutathione S-transferase psoE (PubMed:24939566, PubMed:27072782). The fourth step of synerazol production is performed by the dual-functional monooxygenase/methyltransferase psoF which seems to catalyze the epoxidation of the intermediate deepoxy-synerazol (PubMed:24939566). Synerazol can be attacked by a water molecule nonenzymatically at two different positions to yield two diol products, pseurotin A and pseurotin D (PubMed:24939566).
Catalytic subunit in the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance.
Belongs to the glucose-6-phosphate dehydrogenase family.
Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis.
Belongs to the short-chain dehydrogenases/reductases (SDR) family. ERG27 subfamily.
Sterol-C4-methyl oxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (By similarity). Erg27 is a catalytic component of the C-4 demethylation complex that catalyzes the conversion of 4,4-dimethylfecosterol into fecosterol via 4-methylfecosterol (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (PubMed:18191972) (Probable).
Belongs to the small GTPase superfamily. Ran family.
Belongs to the V-ATPase proteolipid subunit family.
Proton-conducting pore forming of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments.
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and VOA1). The decameric c-ring forms the proton-conducting pore, and is composed of eight proteolipid subunits c, one subunit c' and one subunit c''.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily.
Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
Belongs to the dihydrofolate reductase family.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
Belongs to the alternative oxidase family.
Catalyzes cyanide-resistant oxygen consumption. May increase respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures.
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
Belongs to the glycosyl hydrolase 20 family.
Belongs to the SOS response-associated peptidase family.
Belongs to the DEAD box helicase family. DEAH subfamily. DDX15/PRP43 sub-subfamily.
Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Belongs to the proteasome subunit S2 family.
Belongs to the cysteine synthase/cystathionine beta-synthase family.
Mediates inactivation of the TORC1 complex in response to amino acid starvation. Required for meiotic nuclear division (By similarity).
Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint (By similarity).
Plays a role in maintenance of chromatin structure during RNA polymerase II transcription elongation thereby repressing transcription initiation from cryptic promoters. Mediates the reassembly of nucleosomes onto the promoters of at least a selected set of genes during repression; the nucleosome reassembly is essential for transcriptional repression (By similarity).
Belongs to the Mediator complex subunit 10 family.
O-methyltransferase; part of the gene cluster that mediates the biosynthesis of trypacidin, a mycotoxin with antiprotozoal activity and that plays a role in the infection process (PubMed:26278536, PubMed:26242966). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) tpcC (PubMed:26242966). The atrochrysone carboxyl ACP thioesterase tpcB then breaks the thioester bond and releases the atrochrysone carboxylic acid from tpcC (PubMed:26242966). The decarboxylase tpcK converts atrochrysone carboxylic acid to atrochrysone which is further reduced into emodin anthrone (PubMed:26242966). The next step is performed by the emodin anthrone oxygenase tpcL that catalyzes the oxidation of emodinanthrone to emodin (PubMed:26242966). Emodin O-methyltransferase encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin to form questin (PubMed:26242966). Ring cleavage of questin by questin oxidase tpcI leads to desmethylsulochrin via several intermediates including questin epoxide (By similarity). Another methylation step catalyzed by tpcM leads to the formation of sulochrin which is further converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes the conversion of monomethylsulfochrin to trypacidin (PubMed:26242966). Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)), thus triggering host necrotic cell death (PubMed:22319557). The trypacidin pathway is also able to produce endocrocin via a distinct route from the endocrocin Enc pathway (PubMed:26242966).
Resulted in loss of trypacidin production (PubMed:26242966).
Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3. Interacts with snoRNA U3. Interacts with MPP10, KRI1 and with ribosomal proteins RPS1A, RPS4A, RPS4B, RPS8A, RPS8B, RPS11A, RPS11B, RPS13, RPS24, RPS25, RPL4A, RPL7B, RPL8, RPL23, RPL25 and RPL28.
Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. Essential for vegetative growth.
Belongs to the GHMP kinase family. Mevalonate kinase subfamily.
Expression is down-regulated during iron starvation.
Mevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). Erg12 converts mevalonate into 5-phosphomevalonate (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase erg12 (AFUA_4G07780) first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase erg8 (AFUA_5G10680). The diphosphomevalonate decarboxylase mvd1 (AFUA_4G07130) then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase idi1 (AFUA_6G11160) then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase erg20 (AFUA_5G02450) catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (PubMed:16110826, PubMed:22106303) (Probable).
Belongs to the dihydroxyacetone kinase (DAK) family.
Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde.
Belongs to the SurE nucleotidase family.
Dodecapentaenoate synthase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) (PubMed:23488861, PubMed:24568283). Within the pathway, the polyketide synthase af370 produces the dodecapentaenoyl group of fumagillin via the condensation of one acetyl-CoA starter unit and 5 malonyl-CoA elongation units (PubMed:23488861). The pathway begins with the conversion of farnesyl pyrophosphate (FPP) to beta-trans-bergamotene by the membrane-bound beta-trans-bergamotene synthase af520. The multifunctional cytochrome P450 monooxygenase af510 then converts beta-trans-bergamotene into 5-keto-demethoxyfumagillol via several oxydation steps 5-keto-demethoxyfumagillol is then subjected to successive C-6 hydroxylation and O-methylation by the dioxygenase af480 and O-methyltransferase af390-400, respectively, to yield 5-keto-fumagillol, which is then stereoselectively reduced by the keto-reductase af490 to 5R-hydroxy-seco-sesquiterpene. The next step is the polyketide transferase af380-catalyzed transfer of a dodecapentaenoyl group synthesized by the polyketide synthase af370 onto 5R-hydroxy-seco-sesquiterpene which leads to the production of prefumagillin. Finally, oxidative cleavage by the monooxygenase af470 converts prefumagillin to fumagillin (PubMed:24568283) (Probable).
The release of the polyketide chain from the non-reducing polyketide synthase is mediated by the thioesterase (TE) domain localized at the C-ter of the protein (By similarity).
Belongs to the mitochondrial pyruvate carrier (MPC) (TC 2.A.105) family.
Mediates the uptake of pyruvate into mitochondria.
Belongs to the Clp1 family. NOL9/GRC3 subfamily.
Polynucleotide 5'-kinase involved in rRNA processing.
Belongs to the iron-containing alcohol dehydrogenase family. Hydroxyacid-oxoacid transhydrogenase subfamily.
Belongs to the dynactin subunits 5/6 family. Dynactin subunit 6 subfamily.
Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules.
Golgi membrane protein involved in vesicular trafficking and spindle migration.
The VTT domain was previously called the SNARE-assoc domain. As there is no evidence that this domain associates with SNARE proteins, it was renamed as VMP1, TMEM41, and TVP38 (VTT) domain.
Activates the atg1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Finally, atg13 is also required for glycogen storage during stationary phase (By similarity).
Belongs to the ATG13 family. Fungi subfamily.
Interacts with atg1 to form the atg1-atg13 kinase complex.
Required for nuclear migration within hyphae during vegetative growth.
Self-associates. Interacts with nudF (By similarity).
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Belongs to the methyltransferase superfamily. NTM1 family.
Adaptor protein complex 3 (AP-3) is a heterotetramer.
Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane.
ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping. Is involved in G1/S DNA-damage checkpoint recovery, probably through the regulation of the translational status of a subset of mRNAs. May also have a role in translation and mRNA nuclear export (By similarity).
Belongs to the DEAD box helicase family. DDX6/DHH1 subfamily.
Displays specific fusarinine C (FsC) esterase activity but does not hydrolyze triacetylfusarinine C (TAFC), which has the same core structure as fusarinine C (PubMed:24038704). Both extra- and intracellular siderophores have been shown to be crucial for the virulence (PubMed:24038704). Subsequent to chelation of iron and uptake, FsC and TAFC are hydrolyzed and the iron is transferred to the metabolism or to the intracellular siderophore ferricrocin (FC) for transport and storage of iron (PubMed:24038704).
Leads to decreased growth and increased intracellular accumulation of hydrolysis products of the siderophore fusarinine C (PubMed:24038704).
Fumigaclavine B O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:26972831). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:15870460). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482, PubMed:21409592). EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482). EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482). Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831). Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909).
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II.
Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner, facilitating the efficient association of RNA processing factors with their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is thought to be involved in mRNA degradation by activating the decapping step in the 5'-to-3' mRNA decay pathway. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 di-snRNP, spliceosomal U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds directly to the 3'-terminal U-tract of U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. LSM2-LSM8 probably also is involved degradation of nuclear pre-mRNA by targeting them for decapping, and in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA (By similarity).
Component of the heptameric LSM1-LSM7 complex, which consists of lsm1, lsm2, lsm3, lsm4, lsm5, lsm6 and lsm7. Component of the heptameric LSM2-LSM8 complex, which consists of lsm2, lsm3, lsm4, lsm5, lsm6, lsm7 and lsm8. The LSm subunits form a seven-membered ring structure with a doughnut shape (By similarity).
Belongs to the bacterial ribosomal protein bS21 family.
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
Belongs to the class VI-like SAM-binding methyltransferase superfamily. CHO2 family.
Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily.
In the C-terminal section; belongs to the histidinol dehydrogenase family.
ATP-grasp enzyme; part of the gene cluster that mediates the biosynthesis of the isoquinoline alkaloids fumisoquin A, fumisoquin B and fumisoquin C; as well as small amounts of fumipyrrole as a shunt metabolite (PubMed:25582336, PubMed:27065235). The products of the cluster lead to a brown coloration and are important for growth and conidiation (PubMed:25582336). The nonribosomal peptide synthetase-like protein fsqF, which lacks a canonical condensation domain, is required for addition of a serine-derived dehydroalanine moiety to activated tyrosine but is not essential for the subsequent steps leading to isoquinoline formation (PubMed:27065235). A different enzyme, most likely the ATP-grasp enzyme fsqD, is responsible for activation of tyrosine (Probable). Three additional enzymes encoded by the fsq cluster, the N-methyltransferase fsqC, the phenol 2-monooxygenase fsqG and the FAD-dependent oxidase fsqB, catalyze the formation of the isoquinoline ring system in the fumisoquins (PubMed:27065235, PubMed:30194285). FsqB converts the fspF thiolation domain-bound (2S,4S,5S)-2-amino-6-(3,4-dihydroxyphenyl)-4-hydroxy-5-(methylamino)hexanoyl into isoquinoline (PubMed:27065235, PubMed:30194285). The cyclization most likely proceeds via a two-step mechanism, beginning with FAD-dependent oxidation of the methyl group to an iminium species followed by electrophilic attack on the deprotonated phenol (Probable).
Binds 2 magnesium or manganese ions per subunit.
Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1 subfamily.
Belongs to the mitochondrion-specific ribosomal protein mL41 family.
Belongs to the peroxisomal targeting signal receptor family.
Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
Component of the HAT-B complex composed of at least hat1 and hat2. The HAT-B complex binds to histone H4 tail.
Regulatory subunit of the histone acetylase B (HAT-B) complex. The complex acetylates 'Lys-12' of histone H4 which is required for telomeric silencing.
Probable GPI-anchored aspartic-type endopeptidase which contributes to virulence.
Belongs to the mitochondrion-specific ribosomal protein mS33 family.
Guanine nucleotide-exchange factor (GEF) required for the formation or budding of transport vesicles from the ER.
Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).
Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Plays a pivotal role as a pathogenicity determinant during infections and contributes to the ability of the pathogen to persist within the mammalian host (By similarity).
Acetylxylan esterase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone (By similarity).
Has a modular structure: a carbohydrate esterase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix. Necessary for type 2 peroxisome targeting signal (PTS2)-containing protein processing and facilitates peroxisome matrix protein import.
Belongs to the scytalone dehydratase family.
Fenoxanil inhibits arp1 scytalone dehydratase activity (PubMed:19703288).
Homotrimer (By similarity). Each subunit contains an active site, located in the central part of the hydrophobic core of the monomer, which functions independently (By similarity).
Impairs the production of dihydroxynaphthalene (DHN)-melanin and results in reddish-pink conidial phenotype (PubMed:9383199, PubMed:26972005). Up-regulates complement component C3 deposition on conidial surfaces (PubMed:9383199). Causes enhanced insect mortality compared to the parent strain in a wax moth Galleria mellonella infection model, probably through exacerbated immune response of the wax moth (PubMed:19156203).
Scytalone dehydratase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment and a structural component of the conidial wall (PubMed:10515939, PubMed:19156203). The first step of the pathway is the production of the heptaketide naphtopyrone YWA1 by the polyketide synthase alb1 though condensation of acetyl-CoA with malonyl-CoA (PubMed:10515939). The naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase ayg1 though chain-length shortening (PubMed:10515939). 1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to yield scytalone (PubMed:10515939). The scytalone dehydratase arp1 then reduces scytalone to 1,3,8-THN (PubMed:10515939). 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to yield vermelone (PubMed:10515939). Vermelone is further converted by the multicopper oxidase abr1 to 1,8-DHN (PubMed:10515939). Finally the laccase abr2 transforms 1,8-DHN to DHN-melanin (PubMed:10515939). DHN-melanin biosynthesis appears to be initiated in endosomes where early enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to melanin deposition on the cell surface where late enzymes (abr1 and abr2) localize (PubMed:26972005). DHN-melanin is an important structural component of the outer cell wall and is required for the presence of conidial surface hydrophobins (PubMed:19703288). DHN-melanin also plays a crucial role in fungal virulence, including a protective role against the host's immune defenses (PubMed:19156203, PubMed:20145078, PubMed:21747802, PubMed:21573171, PubMed:24818666). DHN-melanin protects also conidia against amoeba predation (PubMed:25684622).
Belongs to the heat shock protein 90 family.
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.
BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (By similarity). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (By similarity). Binds to the sequence 5'-CATTCY-3', where Y is a pyrimidine, making both major- and minor-groove contacts (By similarity). Essential for differentiation and functionality of phialides as conidiogenous cells (PubMed:20966095). Regulates autolysis and cell death (PubMed:20966095). Positively regulates expression of the gliotoxin biosynthetic gene cluster in actively growing vegetative cells, and likely bridges morphological and chemical development during the life-cycle (PubMed:26032501). Negatively regulates expression of the melanin biosynthetic gene cluster (PubMed:24123270).
Highly expressed during conidiation (PubMed:20966095). Expression is positively regulated by hsp90 (PubMed:22822234). Expression is decreased by 2',4'-Dihydroxychalcone (2',4'-DHC) (PubMed:26190922).
Results in the formation of aberrant conidiophores exhibiting reiterated cylinder-like terminal cells lacking spores and causes delayed autolysis and cell death (PubMed:20966095). Reduces significantly expression of the gliotoxin biosynthetic gene cluster including gliM, gliP, gliT, and gliZ (PubMed:26032501).
Essential for the assembly of ubiquinol-cytochrome c reductase. It has a direct effect on the correct occurrence of the Rieske protein, core 4, core 5 and apocytochrome b.
Belongs to the complex I NDUFA5 subunit family.
Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family. Adenine deaminase type 2 subfamily.
Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism.
Belongs to the DHHC palmitoyltransferase family. PFA5 subfamily.
Belongs to the dynactin subunit 4 family.
In the C-terminal section; belongs to the TrpB family.
In the N-terminal section; belongs to the TrpA family.
Farnesyl pyrophosphate synthase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). Erg20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase erg12 (AFUA_4G07780) first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase erg8 (AFUA_5G10680). The diphosphomevalonate decarboxylase mvd1 (AFUA_4G07130) then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase idi1 (AFUA_6G11160) then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase erg20 (AFUA_5G02450) catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (PubMed:16110826, PubMed:22106303) (Probable).
Belongs to the homogentisate dioxygenase family.
Catalyzes the prenylation of L-tryptophan at the C-7 position of the indole moiety. The enzyme is specific for dimethylallyl diphosphate (DMAPP) as prenyl donor. Accepts also D-tryptophan, typtophan-derivatives with modifications at the side chain or the indole ring, and linear and cyclic dipeptides such as H-L-Trp-L-Gly-OH or cyclo-L-Trp-L-Gly as substrates, however with lower efficiency. Also has tryptophan aminopeptidase activity towards linear peptides with a tryptophanyl moiety at the N-terminus. Dipeptides are better substrates than peptides with 3 or more amino acids. Enzymatic rate constants however are much higher for the prenyltransferase activity than for the aminopeptidase activity.
Belongs to the ETF beta-subunit/FixA family.
Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids (By similarity).
Component of the signal peptidase complex (SPC) composed of a catalytic subunit SEC11 and three accessory subunits SPC1, SPC2 and SPC3 (By similarity). The complex induces a local thinning of the ER membrane which is used to measure the length of the signal peptide (SP) h-region of protein substrates. This ensures the selectivity of the complex towards h-regions shorter than 18-20 amino acids (By similarity). SPC associates with the translocon complex (By similarity).
The C-terminal short (CTS) helix is essential for catalytic activity. It may be accommodated as a transmembrane helix in the thinned membrane environment of the complex, similarly to the signal peptide in the complex substrates.
Belongs to the serine/threonine dehydratase family.
Belongs to the methyltransferase superfamily. L-isoaspartyl/D-aspartyl protein methyltransferase family.
Belongs to the replication factor A protein 2 family.
Heterohexamer; composed of 3 copies of TIM9 and 3 copies of TIM10, named soluble 70 kDa complex. Associates directly with the TIM22 complex, whose core is composed of TIM22 and TIM54. Interacts with the transmembrane regions of multi-pass transmembrane proteins in transit (By similarity).
The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIM10 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity).
Belongs to the glucose-6-phosphate 1-epimerase family.
Catalyzes the interconversion between the alpha and beta anomers from at least three hexose 6-phosphate sugars (Glc6P, Gal6P, and Man6P).
Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
Belongs to the eukaryotic ribosomal protein eS17 family.
Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins.
Belongs to the TFIIF beta subunit family.
Involved in conidial and mycelial cell wall biogenesis.
Belongs to the fatty acyl-CoA reductase family.
Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
Fumigaclavine A dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:22453123). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:15870460). EasL shows also tryptophan aminopeptidase activity with preference for linear peptides containing a tryptophanyl moiety at the N-terminus (PubMed:18635009). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482, PubMed:21409592). EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482). EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482). Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831). Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909).
Belongs to the WD repeat peroxin-7 family.
Belongs to the eukaryotic ribosomal protein eS30 family.
Growth under standard conditions leads to moderate phosphorylation of mpkA and hppD and hmgA activities are balanced leading further to degradation of HGA and formation of 4-maleylacetoacetate (PubMed:19715768). Cell wall stress, resulting in disturbance of balanced hppD and hmgA enzyme activity, (with reduced hmgA activity), leads to HGA accumulation that polymerizes to pyomelanin (PubMed:19715768).
Homogentisate 1,2-dioxygenase; part of the L-tyrosine degradation gene cluster that mediates the biosynthesis of the brownish pigment pyomelanin as an alternative melanin (PubMed:19028908, PubMed:19715768, PubMed:22046314). The 4-hydroxyphenylpyruvate dioxygenase hppD catalyzes the conversion of 4-hydroxyphenylpyruvate to homogentisic acid (HGA) (PubMed:19028908, PubMed:22046314). The protein hmgX is crucial for this conversion and thus, probably functions as an accessory factor to mediate specific activity of hppD (PubMed:22046314). The homogentisate 1,2-dioxygenase hmgA is then involved in the cleavage of the aromatic ring of HGA and its conversion to 4-maleylacetoacetate (PubMed:19028908, PubMed:19715768). When hmgA activity is lowered by the cell wall integrity (CWI) signaling pathway, HGA accumulates and leads to the production of pyomelanin through benzoquinone acetic acid after oxidation and polymerization (PubMed:19715768). On the opposite, in non-stress conditions, both hppD and hmgA activities are balanced and HGA is degraded into 4-maleylacetoacetate (PubMed:19715768). 4-maleylacetoacetate is further converted to 4-fumarylacetoacetate by the maleylacetoacetate isomerase maiA, which is degraded into fumarate and acetoacetate by the fumarylacetoacetase fahA (Probable).
Impairs growth on L-tyrosine as the sole carbon (PubMed:19028908). Leads to the accumulation of homogentisic acid (HGA) and its subsequent polymerization to pyomelanin (PubMed:19028908).
Expressed constitutively with similar lebels in swollen conidia, germlings and hyphae (PubMed:21062375).
Leads to attenuated virulence in mouse models of haematogenously disseminated and invasive pulmonary aspergillosis (PubMed:21062375). Results in increased expression of sreA and reduced expression of hapX iron acquisition transcription factors (PubMed:21062375). Impairs also gluconeogenesis (PubMed:21062375).
Transcription factor that governs genes involved in reductive and siderophore-mediated iron acquisition, and carbon metabolism (PubMed:21062375). Suppresses the expression of sreA and induces hapX to stimulate expression of genes involved in both reductive iron assimilation and siderophore-mediated iron uptake which is essential for the maximal virulence (PubMed:21062375). Regulates also genes involved in gluconeogenesis (PubMed:21062375).
Pectinolytic enzyme involved in the degradation of xylogalacturonan (xga), a galacturonan backbone heavily substituted with xylose, and which is one important component of the hairy regions of pectin. Activity requires a galacturonic acid backbone substituted with xylose (By similarity).
Forms a stable heterodimer with spt16. The spt16-pob3 dimer weakly associates with multiple molecules of nhp6 to form the FACT complex (By similarity).
In contrast to the orthologous protein in animals and plants, this protein does not contain a HMG box DNA-binding domain. This function may instead be provided by the HMG box of the associated nhp6 protein in the FACT complex of fungi.
Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit apl3 and beta-type subunit apl1), a medium chain (mu-type subunit apm4) and a small adaptin (sigma-type subunit aps2).
Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration (By similarity).
Induced by thermal stress (PubMed:20439478). Repressed by oxidative stress (PubMed:20439478).
Simultaneous disruption of tpsA abolishes trehalose biosynthesis during hyphal and conidia formation, and delays germination (PubMed:20439478). Simultaneous disruption of tpsA results in abnormal cell wall formation, sensitivity to caspofungin, calcofluor white, thermal stress and oxidative stress, and hypervirulence in a mouse model of aspergillosis (PubMed:20439478).
Belongs to the universal ribosomal protein uS13 family.
Essential for vacuolar protein sorting. Required for vacuole biogenesis, stability and to maintain vacuole morphology.
Belongs to the phosphatase 2A regulatory subunit.
The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.
Belongs to the eukaryotic ribosomal protein eL6 family.
FsqF lacks the condensation domain that is essential for canonical peptide bond formation, and bioinformatic analysis of the vicinity of fsqF did not reveal any genes that could code for a second NRPS or free-standing condensation domain.
Nonribosomal peptide synthetase-like enzyme; part of the gene cluster that mediates the biosynthesis of the isoquinoline alkaloids fumisoquin A, fumisoquin B and fumisoquin C; as well as small amounts of fumipyrrole as a shunt metabolite (PubMed:25582336, PubMed:27065235). The products of the cluster lead to a brown coloration and are important for growth and conidiation (PubMed:25582336). The nonribosomal peptide synthetase-like protein fsqF, which lacks a canonical condensation domain, is required for addition of a serine-derived dehydroalanine moiety to activated tyrosine but is not essential for the subsequent steps leading to isoquinoline formation (PubMed:27065235). A different enzyme, most likely the ATP-grasp enzyme fsqD, is responsible for activation of tyrosine (Probable). Three additional enzymes encoded by the fsq cluster, the N-methyltransferase fsqC, the phenol 2-monooxygenase fsqG and the FAD-dependent oxidase fsqB, catalyze the formation of the isoquinoline ring system in the fumisoquins (PubMed:27065235, PubMed:30194285). FsqB converts the fspF thiolation domain-bound (2S,4S,5S)-2-amino-6-(3,4-dihydroxyphenyl)-4-hydroxy-5-(methylamino)hexanoyl into isoquinoline (PubMed:27065235, PubMed:30194285). The cyclization most likely proceeds via a two-step mechanism, beginning with FAD-dependent oxidation of the methyl group to an iminium species followed by electrophilic attack on the deprotonated phenol (Probable).
Prevents the production of fumipyrrole and leads to reduced growth and sporulation, but does not affect virulence in infected mice (PubMed:25582336). Abolishes completely the production of isoquinolines as well as of pyrroles and leads to the production of a single brightly red shunt metabolite, the anthranilic acid-substituted isoquinoline (PubMed:27065235).
Belongs to the tRNA-intron endonuclease family.
Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body.
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. NIM1 subfamily.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM5/TYW2 family.
S-adenosyl-L-methionine-dependent transferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-adenosyl-L-methionine to the C-7 position of 4-demethylwyosine (imG-14) to produce wybutosine-86.
Abolishes the production of fumiquinazoline A and C but does not accumulate fumiquinazoline F (PubMed:24612080).
Expression is positively regulated by brlA, a conidiation-specific transcription factor involved in the early stage of asexual development and necessary for conidiophore formation (PubMed:24612080). Expression is also induced by the cell wall integrity (CWI) signaling pathway that includes the mitogen-activated protein kinase mpkA and the transcription factor rlmA (PubMed:33705521). Expression is negatively regulated by the transcription factor sebA (PubMed:33705521).
Interacts with the mitogen-activated protein kinase mpkA.
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module (PubMed:17464044). Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product (PubMed:17464044). Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme (PubMed:17464044). Occasionally, epimerase (E) domains (responsible for L- to D- amino acid conversion) are present within the NRP synthetase (PubMed:17464044). NRPS11 has the following architecture: A-T-C (PubMed:17464044, PubMed:20804163).
Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the antitumor fumiquinazolines that confer a dual-usage capability to defend against phagocytes in the environment and animal hosts (PubMed:20225828, PubMed:20804163, PubMed:21899262, PubMed:24612080, PubMed:33705521). The simplest member is fumiquinazoline F (FQF) with a 6-6-6 tricyclic core derived from anthranilic acid (Ant), tryptophan (Trp), and alanine (Ala) (PubMed:20225828). The trimodular NRPS fmqA is responsible for FQF formation (PubMed:20225828). Modules 1, 2 and 3 of fmqA are predicted to activate and load Ant, Trp and Ala, respectively, providing for the assembly of an Ant-Trp-Ala-S-enzyme intermediate that would undergo double cyclization for chain release and generation of the tricyclic 6-6-6 product fumiquinazoline F (PubMed:20225828). The presence of an E domain predicted for module 2 of fmqA is consistent with epimerization of L-Trp to D-Trp during assembly to generate the R-stereocenter at C14 of FQF (PubMed:20225828). The FAD-dependent monooxygenase fmqB and the monomodular NRPS fmqC then maturate FQF to FQA (PubMed:20804163). FmqB oxidizes the 2',3'-double bond of the indole side chain of FQF, and fmqC activates L-Ala as the adenylate, installs it as the pantetheinyl thioester on its carrier protein domain, and acylates the oxidized indole for subsequent intramolecular cyclization to create the 6-5-5-imidazolindolone of FQA (PubMed:20804163). The FAD-linked oxidoreductase fmqD introduces a third layer of scaffold complexity by converting FQA to the spirohemiaminal FQC, presumably by catalyzing the formation of a transient imine within the pyrazinone ring (PubMed:21899262). FQC subsequently converts nonenzymatically to the known cyclic aminal FQD (PubMed:21899262).
Phosphorylated by mpkA during conidiogenesis.
Abrogates gliotoxin biosynthesis and leads to the accumulation of the shunt metabolite 6-benzyl-6-hydroxy-1-methoxy-3-methylene-piperazine-2,5-dione (PubMed:21513890).
Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). Gliotoxin contributes to pathogenesis during invasive aspergillosis (PubMed:17601876, PubMed:18199036). In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species (PubMed:17601876).
Belongs to the C/M/P thioester hydrolase family.
Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS beta, which binds to DNA mismatches thereby initiating DNA repair. MSH3 provides substrate-binding and substrate specificity to the complex. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. Acts mainly to repair insertion-deletion loops (IDLs) from 2 to 13 nucleotides in size, but can also repair base-base and single insertion-deletion mismatches that occur during replication. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions.
Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a ternary complex with MutL alpha (MLH1-PMS1).
May function both as a monomer and a homodimer.
Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family.
MFS-type transporter; part of the gene cluster that mediates the biosynthesis of fumigermin that inhibits germination of spores of the inducing S.rapamycinicus, and thus helps the fungus to defend resources in the shared habitat against a bacterial competitor (PubMed:32083553). May be involved in the secretion of fumigermin (Probable).
Belongs to the eukaryotic ribosomal protein eS19 family.
Belongs to the NFYB/HAP3 subunit family.
Involved in deacetylation of histones, chromatin assembly and chromosome segregation. May act as a transcriptional oscillator, directing histone deacetylases to specific chromosomal domains. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair (By similarity).
Belongs to the Cu-Zn superoxide dismutase family.
Belongs to the myo-inositol oxygenase family.
Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.
The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Required for 60S pre-ribosomal subunits export to the cytoplasm.
Abolishes the production of all fumiquinazolines (PubMed:24612080).
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module (PubMed:17464044). Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product (PubMed:17464044). Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme (PubMed:17464044). Occasionally, epimerase (E) domains (responsible for L- to D- amino acid conversion) are present within the NRP synthetase (PubMed:17464044). NRPS12 has the following architecture: A-T-C-A-T-E-C-A-T-C (PubMed:17464044, PubMed:20225828).
Belongs to the WD repeat coronin family.
Belongs to the NADPH--cytochrome P450 reductase family.
This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis.
Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.
Belongs to the AB hydrolase superfamily. AB hydrolase 2 family.
Hydrolyzes fatty acids from S-acylated cysteine residues in proteins with a strong preference for palmitoylated G-alpha proteins over other acyl substrates. Mediates the deacylation of G-alpha proteins such as GPA1 in vivo, but has weak or no activity toward palmitoylated Ras proteins. Has weak lysophospholipase activity in vitro; however such activity may not exist in vivo.
Belongs to the amidase family. GatA subfamily.
Belongs to the V-ATPase D subunit family.
Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole.
Has a role in transport between endoplasmic reticulum and Golgi.
Belongs to the cyclophilin-type PPIase family. PPIL1 subfamily.
Probably involved in transcription regulation via its interaction with the INO80 complex, a chromatin remodeling complex.
Belongs to the methylenetetrahydrofolate reductase family.
Belongs to the fatty acid desaturase type 1 family.
Expected to bind 2 Fe(2+) ions per subunit.
Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates.
Belongs to the mitochondrion-specific ribosomal protein mL50 family.
E3 RING-finger protein, member of the UBC2/RAD6 epistasis group. Associates to the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA.
Interacts with E2 UBC2, forming a complex with ubiquitin ligase activity.
Causes an allergic reaction in human. Associated with allergic bronchopulmonary aspergillosis.
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:22453123). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:15870460). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482, PubMed:21409592). EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482). EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482). Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831). Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909). The role of the cytochrome P450 monooxygenase easK within the cluster has not been identified yet (PubMed:26972831).
Component of the endosomal sorting complex required for transport II (ESCRT-II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs.
Belongs to the TAF9 family. CENP-S/MHF1 subfamily.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM61 family.
Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA.
Abolishes the production of fumiquinazoline A and C and shows a 19-fold accumulation in fumiquinazoline F production (PubMed:24612080).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the antitumor fumiquinazolines that confer a dual-usage capability to defend against phagocytes in the environment and animal hosts (PubMed:20225828, PubMed:20804163, PubMed:21899262, PubMed:24612080, PubMed:33705521). The simplest member is fumiquinazoline F (FQF) with a 6-6-6 tricyclic core derived from anthranilic acid (Ant), tryptophan (Trp), and alanine (Ala) (PubMed:20225828). The trimodular NRPS fmqA is responsible for FQF formation (PubMed:20225828). Modules 1, 2 and 3 of fmqA are predicted to activate and load Ant, Trp and Ala, respectively, providing for the assembly of an Ant-Trp-Ala-S-enzyme intermediate that would undergo double cyclization for chain release and generation of the tricyclic 6-6-6 product fumiquinazoline F (PubMed:20225828). The presence of an E domain predicted for module 2 of fmqA is consistent with epimerization of L-Trp to D-Trp during assembly to generate the R-stereocenter at C14 of FQF (PubMed:20225828). The FAD-dependent monooxygenase fmqB and the monomodular NRPS fmqC then maturate FQF to FQA (PubMed:20804163). FmqB oxidizes the 2',3'-double bond of the indole side chain of FQF, and fmqC activates L-Ala as the adenylate, installs it as the pantetheinyl thioester on its carrier protein domain, and acylates the oxidized indole for subsequent intramolecular cyclization to create the 6-5-5-imidazolindolone of FQA (PubMed:20804163). The FAD-linked oxidoreductase fmqD introduces a third layer of scaffold complexity by converting FQA to the spirohemiaminal FQC, presumably by catalyzing the formation of a transient imine within the pyrazinone ring (PubMed:21899262). FQC subsequently converts nonenzymatically to the known cyclic aminal FQD (PubMed:21899262).
Belongs to the 2-oxoadipate dioxygenase/decarboxylase family.
Belongs to the type-II 3-dehydroquinase family.
Homododecamer. Adopts a ring-like structure, composed of an arrangement of two hexameric rings stacked on top of one another.
Is involved in the catabolism of quinate. Allows the utilization of quinate as carbon source via the beta-ketoadipate pathway.
Small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import.
Acyltransferase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid (PubMed:19415934, PubMed:19216560, PubMed:29158519). Protostadienol synthase helA cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol)(PubMed:19415934, PubMed:19216560, PubMed:29158519). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid (PubMed:19216560). Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton (PubMed:29158519). This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid (PubMed:19415934, PubMed:19216560, PubMed:29158519). Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order (PubMed:29158519). The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21 (PubMed:29158519). C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation (PubMed:19415934, PubMed:29158519). The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC (PubMed:19415934, PubMed:29158519).
Belongs to the plant acyltransferase family.
Glucosidase involved in the degradation of cellulosic biomass. Active on lichenan (By similarity).
Belongs to the eukaryotic ribosomal protein eS24 family.
ATP-dependent DNA helicase involved in DNA damage repair by homologous recombination and in genome maintenance. Capable of unwinding D-loops. Plays a role in limiting crossover recombinants during mitotic DNA double-strand break (DSB) repair. Component of a FANCM-MHF complex which promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork.
Belongs to the DEAD box helicase family. DEAH subfamily. FANCM sub-subfamily.
Interacts with the MHF histone-fold complex to form the FANCM-MHF complex.
Belongs to the Mediator complex subunit 9 family.
Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding.
Belongs to the iron-containing alcohol dehydrogenase family.
Phosphorylation of the TEDS site (Ser-372) is required for the polarization of the actin cytoskeleton. Phosphorylation probably activates the myosin-I ATPase activity (By similarity).
The myosin motor domain displays actin-stimulated ATPase activity and generates a mechanochemical force.
The tail domain participates in molecular interactions that specify the role of the motor domain (By similarity). It is composed of several tail homology (TH) domains, namely a putative phospholipid-binding myosin tail domain (also named TH1), an Ala- and Pro-rich domain (TH2), followed by an SH3 domain and a C-terminal acidic domain (TH3).
Type-I myosin implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Plays an important role in polarized growth, spore germination, hyphal morphogenesis, and septal wall formation (By similarity).
Acetylated by gcn5 to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by esa1. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription (By similarity).
Monoubiquitinated by the ubc2-bre1 complex to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and H3K79me formation. H2BK123ub1 also modulates the formation of double-strand breaks during meiosis and is a prerequisite for DNA-damage checkpoint activation (By similarity).
Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su or H2BK17su, occurs preferentially near the telomeres and represses gene transcription.
To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H2BK6ac = acetylated Lys-8; H2BK6su = sumoylated Lys-8; H2BK7ac = acetylated Lys-9; H2BK7su = sumoylated Lys-9; H2BK11ac = acetylated Lys-15; H2BK16ac = acetylated Lys-25; H2BK16su = sumoylated Lys-25; H2BK17su = sumoylated Lys-26; H2BK123ub1 = monoubiquitinated Lys-134.
Component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. Involved in resistance to acriflavine, and required for normal growth on a range of sole carbon sources, including fructose, cellobiose, raffinose, and starch, and reduced utilization of amino acids, including GABA and beta-alanine, as sole carbon and nitrogen sources (By similarity).
Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family.
Belongs to the protein kinase superfamily. ADCK protein kinase family.
Belongs to the tRNA(His) guanylyltransferase family.
Expression is positively regulated by brlA, a conidiation-specific transcription factor involved in the early stage of asexual development and necessary for conidiophore formation (PubMed:24612080).
MFS transporter; part of the gene cluster that mediates the biosynthesis of the antitumor cytotoxic peptidyl alkaloids fumiquinazolines that confer a dual-usage capability to defend against phagocytes in the environment and animal hosts (PubMed:20804163, PubMed:24612080, PubMed:33705521). Probably involved in fumiquinazolines metabolism and transport (PubMed:24612080).
Seems not to affect fumiquinazolines production (PubMed:24612080).
Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP2/CFD1 subfamily.
Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of nbp35 and two labile, bridging clusters between subunits of the nbp35-cfd1 heterotetramer.
Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The nbp35-cfd1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins.
Heterotetramer of 2 nbp35 and 2 cfd1 chains.
Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. YchF/OLA1 subfamily.
Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP.
Xylan 1,4-beta-xylosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Involved in the partitioning of the mitochondrial organelle and mitochondrial DNA (mtDNA) inheritance.
DHAD activity is inhibited in dose-dependent manner by 2-hydroxy-3-methylbutyric acid with an IC(50) of about 8 mM.
Dihydroxyacid dehydratase that catalyzes the third step in the common pathway leading to biosynthesis of branched-chain amino acids (PubMed:23028460). Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively (By similarity). IlvC and the branched-chain amino acid biosynthesis are crucial for virulence and may be a potential target to develop antifungal agents (PubMed:23028460).
Requires supplementation with isoleucine and valine for growth (PubMed:23028460). Results in considerably lower kidney tissue burden in murine infection models (PubMed:23028460).
Transcription factor required for normal voriconazole resistance (PubMed:36374043). Contributes to the function of atrR and regulates the expression of the atrR target gene abcG1 (PubMed:36374043).
Belongs to the 5'-AMP-activated protein kinase beta subunit family.
Serine hydrolase involved in the detoxification of formaldehyde.
Ubiquitin thioesterase component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. Deubiquitinates the creA catabolic repressor and the quinate permease qutD. Also plays a role in response to carbon starvation and the control of extracellular proteases activity (By similarity).
Belongs to the helicase family. SKI2 subfamily.
Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotriene B(4) as the product compared to the homologous mammalian enzyme (in vitro).
Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.
Heterohexamer of two PFD-alpha type and four PFD-beta type subunits.
Elastase inhibitor. Non-competitive inhibitor of A.fumigatus elastase with a Ki of 1.6 nM. Inhibits the fibrinogenase and collagenase activities of A.fumigatus elastase. Inhibitor of A.flavus elastase and human leukocyte elastase, and weakly inhibits porcine pancreatic elastase. Does not inhibit elastase from P.aeruginosa or C.atrox venom.
DNA-binding protein that induces severe bending of DNA. Required for DNA-binding by the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. Also augments the fidelity of transcription by RNA polymerase III independently of any role in the FACT complex (By similarity).
Weakly associates with the stable spt16-pob3 heterodimer to form the FACT complex.
3-ketosteroid 1-dehydrogenase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid (PubMed:19415934, PubMed:19216560, PubMed:29158519). Protostadienol synthase helA cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol)(PubMed:19415934, PubMed:19216560, PubMed:29158519). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid (PubMed:19216560). Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton (PubMed:29158519). This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid (PubMed:19415934, PubMed:19216560, PubMed:29158519). Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order (PubMed:29158519). The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21 (PubMed:29158519). C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation (PubMed:19415934, PubMed:29158519). The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC (PubMed:19415934, PubMed:29158519).
Belongs to the FAD-dependent oxidoreductase 2 family. 3-oxosteroid dehydrogenase subfamily.
Involved in nucleolar processing of pre-18S ribosomal RNA. Involved in ribosome biosynthesis (By similarity).
Decarboxylase; part of the gene cluster that mediates the biosynthesis of trypacidin, a mycotoxin with antiprotozoal activity and that plays a role in the infection process (PubMed:26278536, PubMed:26242966). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) tpcC (PubMed:26242966). The atrochrysone carboxyl ACP thioesterase tpcB then breaks the thioester bond and releases the atrochrysone carboxylic acid from tpcC (PubMed:26242966). The decarboxylase tpcK converts atrochrysone carboxylic acid to atrochrysone which is further reduced into emodin anthrone (PubMed:26242966). The next step is performed by the emodin anthrone oxygenase tpcL that catalyzes the oxidation of emodin anthrone to emodin (PubMed:26242966). Emodin O-methyltransferase encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin to form questin (PubMed:26242966). Ring cleavage of questin by questin oxidase tpcI leads to desmethylsulochrin via several intermediates including questin epoxide (By similarity). Another methylation step catalyzed by tpcM leads to the formation of sulochrin which is further converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes the conversion of monomethylsulfochrin to trypacidin (PubMed:26242966). Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)), thus triggering host necrotic cell death (PubMed:22319557). The trypacidin pathway is also able to produce endocrocin via a distinct route from the endocrocin Enc pathway (PubMed:26242966).
Belongs to the aromatic-ring hydroxylase family. KMO subfamily.
Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid.
FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of fumigermin that inhibits germination of spores of the inducing S.rapamycinicus, and thus helps the fungus to defend resources in the shared habitat against a bacterial competitor (PubMed:32083553). The partially reducing polyketide synthase fngA alone is sufficient for the production of fumigermin (PubMed:32083553). FgnA catalyzes the condensation of 3 malonyl-CoA units to an acetyl-CoA starter, and 3 methylations to yield fumigermin (PubMed:32083553). It is remarkable that the five cluster genes including fgnA are conserved in distantly related fungi, supporting the assumption of a fumigermin cluster; it is thus possible that originally all five genes were functional, but that the genes encoding tailoring enzymes became inactive from mutations, similar to the case of the fgnA gene in strains A1163 and Af293 (Probable).
Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.
Non-catalytic component of the proteasome.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Erg6/SMT family.
Expression is significantly suppressed in the presence of alpha-bisabolol.
In Aspergillus, the biosynthesis pathway of the sterol precursors leading to the prevalent sterol ergosterol differs from yeast. The ringsystem of lanosterol in S.cerevisiae is firstly demethylised in three enzymatic steps leading to the intermediate zymosterol and secondly a methyl group is added to zymosterol by the sterol 24-C-methyltransferase to form fecosterol. In Aspergillus, lanosterol is firstly transmethylated by the sterol 24-C-methyltransferase leading to the intermediate eburicol and secondly demethylated in three steps to form fecosterol.
Specific and total activity is decreased in presence of alpha-bisabolol.
Sterol 24-C-methyltransferase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:18191972, PubMed:28224386). Methylates lanosterol at C-24 to produce eburicol (PubMed:18191972, PubMed:28224386). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (PubMed:16110826, PubMed:18191972) (Probable).
Belongs to the tyrosyl-DNA phosphodiesterase family.
Essential protein which may be involved in threonine biosynthesis.
Belongs to the glutaminase PdxT/SNO family.
E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Probably involved in the regulatory network controlling carbon source utilization.
Causes an allergic reaction in human. Binds to IgE via three immunodominant epitopes localized at the C-terminal part.
Expression is controlled by the prtT transcription factor.
Secreted alkaline protease that allows assimilation of proteinaceous substrates. Acts as a significant virulence factor in invasive aspergillosis. Involved in immune evasion from the human and mice complement systems during infection. Efficiently cleaves important components of the complement cascade such as such as C3, C4, C5, and C1q, as well as IgG, which leads to down-regulation of complement activation at the hyphal surface.
Belongs to the F-actin-capping protein alpha subunit family.
Catalyzes the second and fifth step in the 'de novo' purine biosynthesis pathway; contains phosphoribosylamine--glycine ligase (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS) activities.
In the C-terminal section; belongs to the AIR synthase family.
In the N-terminal section; belongs to the GARS family.
Component of the SMC5-SMC6 complex, that promotes sister chromatid alignment after DNA damage and facilitates double-stranded DNA breaks (DSBs) repair via homologous recombination between sister chromatids.
Belongs to the complex I NDUFA8 subunit family.
Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val) (By similarity). Part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) (PubMed:23488861, PubMed:24082142, PubMed:24568283). Since fumagillin is known to inhibit eukaryotic type 2 methionine aminopeptidase, af410 encodes a self-resistant enzyme for A.fumigatus toward fumagillin (PubMed:23488861).
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.
Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.
Belongs to the JHDM3 histone demethylase family.
Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Also plays a role in the assembly of the exocyst (By similarity).
Forms a one-to-one complex with cytochrome c.
Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs and play a central role in ribosomal RNA processing. The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs. Catalyzes pseudouridylation at position 93 in U2 snRNA. Also catalyzes pseudouridylation of mRNAs; H/ACA-type snoRNAs probably guide pseudouridylation of mRNAs.
Belongs to the universal ribosomal protein uL15 family.
Delta(7)-sterol 5(6)-desaturase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:16436696, PubMed:18191972). Erg3B catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol (PubMed:16436696, PubMed:18191972). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (PubMed:16110826, PubMed:18191972) (Probable).
Does not affect the susceptibility to amphotericin B, itraconazole, fluconazole, voriconazole, and ketoconazole (PubMed:16436696). Leads to the accumulation of the non-C-5 desaturated sterols 24-methylcholesta-7,22-dien-3beta-ol, 24-methylcholesta-7,22,24(28)-trien-3beta-ol, and 24-methylcholesta-7,24(28)-dien-3beta-ol (PubMed:16436696, PubMed:18191972).
Belongs to the TFIIE beta subunit family.
Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase.
Tetramer of two alpha and two beta chains.
Belongs to the very long-chain fatty acids dehydratase HACD family.
Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Belongs to the Mediator complex subunit 20 family.
Belongs to the acetyltransferase family. GCN5 subfamily.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. KIN-5/BimC subfamily.
The C-terminal 2 residues are removed by ATG4 to expose Gly-116 at the C-terminus. The C-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin.
Ubiquitin-like modifier involved in autophagosomes formation. With atg4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy.
Belongs to the PpiC/parvulin rotamase family. PIN4 subfamily.
Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.
Sterol O-acyltransferase that catalyzes the formation of stery esters.
Required for the synthesis of 40S ribosome subunits. Has a role in processing 20S pre-rRNA into the mature 18S rRNA, where it is required for cleavage at the 3' end of the mature 18S rRNA (D-site). Accompanies the 20S pre-rRNA from the nucleus to the cytoplasm.
Heterohexamer; composed of 3 copies of TIM8 and 3 copies of TIM13, named soluble 70 kDa complex. Associates with the TIM22 complex, whose core is composed of TIM22 and TIM54. Interacts with the transmembrane regions of multi-pass transmembrane proteins in transit (By similarity).
Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIM8-TIM13 complex is non essential and only mediates the import of few proteins, while the predominant TIM9-TIM10 70 kDa complex is crucial and mediates the import of much more proteins (By similarity).
The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIM13 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity).
Transporter that is probably involved in the transport of copper, even if it does not act as a major copper transporter.
Belongs to the 5'-3' exonuclease family.
Multifunctional protein that exhibits several independent functions at different levels of the cellular processes. 5'-3' exonuclease component of the nonsense-mediated mRNA decay (NMD) which is a highly conserved mRNA degradation pathway, an RNA surveillance system whose role is to identify and rid cells of mRNA with premature termination codons and thus prevents accumulation of potentially harmful truncated proteins.
Belongs to the thiolase-like superfamily. HMG-CoA synthase family.
Hydroxymethylglutaryl-CoA synthase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity). Erg13A and erg13B condense acetyl-CoA with acetoacetyl-CoA to form hydroxymethylglutaryl-CoA (HMG-CoA) (By similarity). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase erg10B that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases erg13A and erg13B then condense acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases hmg1 and hmg2. Mevalonate is also a precursor for the extracellular siderophore triacetylfusarinine C (TAFC) (PubMed:16110826, PubMed:22106303) (Probable).
Belongs to the CTL (choline transporter-like) family.
Probably involved in transport through the plasma membrane.
Belongs to the eukaryotic-type N-acetylglucosamine kinase family.
Belongs to the eukaryotic ribosomal protein eS4 family.
Belongs to the ERCC1/RAD10/SWI10 family.
Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP1/NBP35 subfamily.
Belongs to the CND1 (condensin subunit 1) family.
Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.
After transfer of sugars to endogenous macromolecular acceptors, the enzyme converts nucleoside diphosphates to nucleoside monophosphates which in turn exit the Golgi lumen in a coupled antiporter reaction, allowing entry of additional nucleotide sugar from the cytosol.
Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Leads to high sensitivity to allyl alcohol, a compound indicative for potential defects in carbon catabolite repression (CCR), but does not affect growth in non-stress conditions, nor in the presence of 2-deoxyglucose (2DG), an additional indicator for defects in CCR (PubMed:32667960). Leads also to sensitivity to acrolein, menadione and t-butyl hydroperoxide (PubMed:32667960). Abolishes the production of gliotoxin (GT) and accumulates bisdethiobis(methylthio)-gliotoxin (BmGT) (PubMed:32667960). Leads to reduced expression of gliZ, gliT, gliF and gtmA in GT-inducing conditions (PubMed:32667960). Loses all ability to protect itself against exogenously added GT as well and reduces virulence (PubMed:32667960).
Transcription factor that is involved in protection against oxidative stress (PubMed:32667960). Binds to promoter regions of the gliotoxin (GT) biosynthetic genes gliZ, gliF, gliT, gliM, gliA and gtmA (PubMed:32667960). Two related but different DNA motifs (5'-TCGG-3' and 5'-CGGNCGG-3') are specifically enriched among rglT binding sites in GT-inducing conditions (PubMed:32667960). Also indirectly regulates the expression of gliP, gliG, gliH and gliN (PubMed:32667960). Plays a key role in resistance against exogenously-added GT and GT biosynthesis, mainly through the direct regulation of gliT (PubMed:32667960). Furthermore, rglT is important for virulence in chemotherapeutic mice with invasive pulmonary aspergillosis (IPA) (PubMed:32667960).
In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.
In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.
Belongs to the ketol-acid reductoisomerase family.
Component of the ER-mitochondria encounter structure (ERMES) or MDM complex, composed of mmm1, mdm10, mdm12 and mdm34. A mmm1 homodimer associates with one molecule of mdm12 on each side in a pairwise head-to-tail manner, and the SMP-LTD domains of mmm1 and mdm12 generate a continuous hydrophobic tunnel for phospholipid trafficking.
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. Mdm12 is required for the interaction of the ER-resident membrane protein mmm1 and the outer mitochondrial membrane-resident beta-barrel protein mdm10. The mdm12-mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The mdm10-mdm12-mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the mdm12-mmm1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily.
Catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Phosphorylated in response to DNA damage.
Regulatory subunit of the slx1-slx4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Component of the small ribosomal subunit, ribosomal RNA processing complex (SSU RRP complex).
Required for small ribosomal subunit (SSU) synthesis. Has a role in the processing of early nucleolar and late cytoplasmic pre-RNA species (By similarity).
The COPII coat is composed of at least 5 proteins: the sec23/24 complex, the sec13/31 complex, and the protein sar1. sec13 and sec31 make a 2:2 tetramer that forms the edge element of the COPII outer coat. The tetramer self-assembles in multiple copies to form the complete polyhedral cage. Interacts (via WD 8) with sec13 (By similarity).
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. NOG subfamily.
Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
Belongs to the glycosyltransferase 4 family.
Methyltransferase; part of the gene cluster that mediates the biosynthesis of pseurotin A, a competitive inhibitor of chitin synthase and an inducer of nerve-cell proliferation (PubMed:24082142, PubMed:24939566). The PKS-NRPS hybrid synthetase psoA is responsible for the biosynthesis of azaspirene, one of the first intermediates having the 1-oxa-7-azaspiro[4,4]-non-2-ene-4,6-dione core of pseurotin, via condensation of one acetyl-CoA, 4 malonyl-CoA, and a L-phenylalanine molecule (PubMed:24082142, PubMed:24939566). The dual-functional monooxygenase/methyltransferase psoF seems to be involved in the addition of the C3 methyl group onto the pseurotin scaffold (PubMed:24939566). Azaspirene is then converted to synerazol through 4 steps including oxidation of C17 by the cytochrome P450 monooxygenase psoD, O-methylation of the hydroxy group of C8 by the methyltransferase psoC, and the trans-to-cis isomerization of the C13 olefin by the glutathione S-transferase psoE (PubMed:24939566). The fourth step of synerazol production is performed by the dual-functional monooxygenase/methyltransferase psoF which seems to catalyze the epoxidation of the intermediate deepoxy-synerazol (PubMed:24939566). Synerazol can be attacked by a water molecule nonenzymatically at two different positions to yield two diol products, pseurotin A and pseurotin D (PubMed:24939566).
Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit family.
Belongs to the bacterial ribosomal protein bS16 family.
Belongs to the 5'-3' exonuclease family. XRN2/RAT1 subfamily.
Possesses 5'->3' exoribonuclease activity. Required for the processing of nuclear mRNA and rRNA precursors. May promote termination of transcription by RNA polymerase II (By similarity).
Belongs to the protein kinase superfamily. BUD32 family.
This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event (By similarity). BUD32 has protein kinase activity in vitro, but in the context of the EKC/KEOPS complex, the catalytic subunit KAE1 switches the activity of BUD32 from kinase into ATPase (By similarity).
Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation. Active on laminarin and lichenan (By similarity).
Intracellular phospholipase B that catalyzes the double deacylation of phosphatidylcholine (PC) to glycerophosphocholine (GroPCho). Plays an important role in membrane lipid homeostasis. Responsible for the rapid PC turnover in response to inositol, elevated temperatures, or when choline is present in the growth medium (By similarity).
Abolishes the production of xanthocillin derivatives including a dimethoxyl formyl xanthocillin derivative, the sulfated formyl xanthocillin derivative fumiformamide, a 1,2-diformylamido derivative named melanocin E, and the imidazole-containing melanocin F.
Expressed during copper starvation via the regulation of both aceA and macA transcription factors.
Isocyanide synthase; part of the gene cluster that mediates the biosynthesis of the isocyanide xanthocillin and its derivatives (PubMed:29844112). The first step of the pathway consists in the conversion of tyrosine into a vinyl-isonitrile intermediate by the isocyanide synthase xanB (PubMed:29844112). Subsequent oxidative dimerization of this intermediate to form xanthocillin may involve the cytochrome P450 monooxygenase xanG, whose expression is coregulated with that of XanB (PubMed:29844112). Xanthocillin can be further modified by the isonitrile hydratase-like protein xanA which introduces N-formyl groups and the methyltransferase xanE which introduces methyl groups, leading to the production of several derivatives including fumiformamide (PubMed:29844112). Finally, fumiformamide can be subject to both oxidative and reductive cyclization to yield melanocins E and F, respectively (PubMed:29844112).
Activity is inhibited bythe antifunfal copmpounds PD 404,182, 6-nitroso-1,2-benzopyrone, and calmidazolium chloride with IC(50) values of 3.9 uM, 35.2 uM, and 19.2 uM, respectively (PubMed:28720735).
Acyl-carrier-protein synthase that transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier-protein (PubMed:12664133, PubMed:21195204, PubMed:28720735). The 4'-phosphopantetheine (4'-PPT) portion of CoA provides the essential prosthetic group for a number of carrier proteins and multi-domain enzymes, priming them for the acceptance of acyl building blocks in fatty acid synthesis and many aspects of secondary metabolism mediated by polyketide synthases (PKSs) and non-ribosomal peptide synthetases (NRPSs) (PubMed:21195204, PubMed:28720735). PptA is able to transfer the cofactor to a broad range of enzymes with acyl- or peptidyl-carrier protein domains and activates target enzymes involved in the synthesis of lysine, but also secondary metabolites including gliotoxin, fumigaclavine C, fumiquinazole A, fumiquinazoline C, pyripyroprene A, fumagillin, the siderophores triacetylfusarinine C (TAFC) and ferricrocin (FC), and dihydroxy naphthalene (DHN)-melanin (PubMed:21195204, PubMed:28720735). Plays an essential role in virulence (PubMed:28720735).
Belongs to the P-Pant transferase superfamily.
Leads to the loss of the green conidial pigment and decreased viability of conidia (PubMed:21195204). Impairs virulence in both insect and murine infection models (PubMed:28720735).
PptA is a druggable target in Aspergillus species that can be targeted in a selective way (PubMed:28720735). Its combined role in both primary and secondary metabolism, encompassing multiple virulence determinants, makes it a very promising antifungal drug target candidate (PubMed:28720735).
Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding.
Functions in the early steps of protein synthesis of a small number of specific mRNAs. Acts by directing the binding of methionyl-tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it binds methionyl-tRNAi to 40S subunits in a codon-dependent manner, whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a GTP-dependent manner.
Belongs to the glycosyl hydrolases 36 family.
3' to 5' exoribonuclease required for proper 3' end maturation of MRP RNA and of the U5L snRNA.
Belongs to the eukaryotic ATPase B chain family.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. In yeast, the dimeric form of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta, epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j and k.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
ABC transporter that seems not to be involved in the efflux of toxic substances, at least not the classical compounds such as itraconazole, amphotericin B, voriconazole, posaconazole, ravuconazole, or echinocandins.
Does not lead to growth defects or changes in developmental patterns and does not affect sensitivity to itraconazole, amphotericin B, voriconazole, posaconazole, ravuconazole, or echinocandins.
Leads to severe polarity defect, hypersensitivity to ER stress, and attenuated virulence; when prmA is also deleted.
Magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the endoplasmic reticulum lumen (Probable). Its activity is coupled to the unfolded protein response (UPR) and Ca(2+) import into the endoplasmioc reticulum is important for redox homeostasis, virulence, cell wall biosynthesis, and resistance to antifungal compounds that inhibit Ca2+ signaling (PubMed:32487759, PubMed:34663092). With pmrA, promotes radial growth and conidiation (PubMed:32487759).
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. SPB1 subfamily.
Component of the nucleolar and nucleoplasmic pre-60S ribosomal particle.
Required for proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit.
Has a role in nuclear-cytoplasmic transport of proteins and mRNAs.
The complex LTO1:YAE1 may function as a target specific adapter that probably recruits apo-RPLI1 to the cytosolic iron-sulfur protein assembly (CIA) complex machinery. May be required for biogenesis of the large ribosomal subunit and initiation of translation.
Part of the multisubunit TRAPP (transport protein particle) complex.
Plays a key role in the late stages of endoplasmic reticulum to Golgi traffic.
Impairs gliotoxin production (PubMed:16757745, PubMed:16956378, PubMed:17601876). In vitro, the culture supernatant of the gliP-deficient strains show a reduced cytotoxic effect on both macrophage-like cells and T-cell lines. Shows attenuated virulence in nonneutropenic mice immunosuppressed with corticosteroids, but normal virulence in neutropenic mice (PubMed:18199036). It also has reduced virulence in a Drosophila melanogaster model (PubMed:18199036).
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module (PubMed:17464044). Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product (PubMed:17464044). Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme (PubMed:17464044). Occasionally, epimerase (E) domains (responsible for L- to D-amino acid conversion) are present within the NRP synthetase (PubMed:17464044). GliP has the following architecture: A-T-C-A-T-C-T (PubMed:17154540, PubMed:17464044).
Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide-bridged cyclic dipeptide (PubMed:15979823, PubMed:16757745, PubMed:16956378, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). Gliotoxin contributes to pathogenesis during invasive aspergillosis (PubMed:17601876, PubMed:18199036). In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species (PubMed:17601876).
Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.
Belongs to the chorismate synthase family.
Belongs to the DHHC palmitoyltransferase family. PFA4 subfamily.
Mediates the reversible addition of palmitate to target proteins, thereby regulating their membrane association and biological function.
Belongs to the actin family. ARP6 subfamily.
Belongs to the class I-like SAM-binding methyltransferase superfamily. MenG/UbiE family.
Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Belongs to the type IA topoisomerase family.
Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand.
Belongs to the ferredoxin--NADP reductase type 1 family.
Belongs to the velvet family. VeA subfamily.
Component of the velvet transcription factor complex that controls sexual/asexual developmental ratio in response to light, promoting sexual development in the darkness while stimulating asexual sporulation under illumination (By similarity). The velvet complex hat acts as a global regulator for secondary metabolite gene expression (By similarity). Controls the expression of hundreds of genes, including those comprising more than a dozen known secondary metabolite gene clusters (PubMed:24116213). Controls the expression of the gliotoxin gene cluster (PubMed:23087369). Controls the expression of the fumagillin, fumitremorgin G, fumigaclavine C and glionitrin gene clusters (PubMed:24116213). The regulation of the fumagillin gene cluster and fumagillin production is performed through direct control of the expression of fumR (PubMed:24116213). Negatively regulates conidiation (PubMed:22970834, PubMed:23087369). Required for normal protease activity (PubMed:23087369).
Reduces sporulation capacities on nitrate-containing medium (PubMed:16002655). Results in the abundant formation of conidiophores (PubMed:22970834). Leads to a reduction of gliotoxin production (PubMed:23087369). Decreases the production of fumagillin, fumitremorgin G, fumigaclavine C and Glionitrin A (PubMed:24116213). Reduces also protease activity (PubMed:23087369).
The C-terminal PEST domain is a region rich in proline, glutamic acid, serine and threonine residues that is required for the light-dependent regulation of development and secondary metabolism (By similarity).
Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament.
Belongs to the eukaryotic ribosomal protein eS21 family.
Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Has a physiological role leading to 18S rRNA stability (By similarity).
Belongs to the phytoene/squalene synthase family.
Squalene synthase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:16110826) (Probable). Erg9 produces squalene from 2 farnesyl pyrophosphate moieties (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (PubMed:16110826, PubMed:18191972) (Probable).
Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Component of the PAM complex, at least composed of mtHsp70, MGE1/mgeA, tim44, PAM16/pamP, PAM17/pamQ and PAM18/pamR.
Belongs to the universal ribosomal protein uL13 family.
Belongs to the acetyltransferase family. ARD1 subfamily.
ABC-type transporter; part of the gene cluster that mediates the biosynthesis of the isoquinoline alkaloids fumisoquin A, fumisoquin B and fumisoquin C; as well as small amounts of fumipyrrole as a shunt metabolite (PubMed:25582336, PubMed:27065235). The products of the cluster lead to a brown coloration and are important for growth and conidiation (PubMed:25582336). FsqE possibly plays a role of self-protection (Probable).
Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Involved in pre-mRNA splicing and cell cycle progression. Required for the spliceosome assembly and initiation of the DNA replication (By similarity).
Constitutively expressed on glucose medium and on ethanol.
Has no detectable activity towards cis-acontiate or cis-homoaconitate.
O-methyltransferase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) (PubMed:24568283, PubMed:23488861). Within the pathway, the O-methyltransferase af390-400 acts as a 5-dehydro-6-demethoxy-6-hydroxyfumagillol O-methyltransferase that methyltes the hydroxylated position C-6 of 5-dehydro-6-demethoxy-6-hydroxyfumagillol to yield 5-keto-fumagillol (PubMed:24568283). The pathway begins with the conversion of farnesyl pyrophosphate (FPP) to beta-trans-bergamotene by the membrane-bound beta-trans-bergamotene synthase af520. The multifunctional cytochrome P450 monooxygenase af510 then converts beta-trans-bergamotene into 5-keto-demethoxyfumagillol via several oxydation steps. 5-keto-demethoxyfumagillol is then subjected to successive C-6 hydroxylation and O-methylation by the dioxygenase af480 and O-methyltransferase af390-400, respectively, to yield 5-keto-fumagillol, which is then stereoselectively reduced by the keto-reductase af490 to 5R-hydroxy-seco-sesquiterpene. The next step is the polyketide transferase af380-catalyzed transfer of a dodecapentaenoyl group synthesized by the polyketide synthase af370 onto 5R-hydroxy-seco-sesquiterpene which leads to the production of prefumagillin. Finally, oxidative cleavage by the monooxygenase af470 converts prefumagillin to fumagillin (PubMed:24568283) (Probable).
Isonitrile hydratase-like protein; part of the gene cluster that mediates the biosynthesis of the isocyanide xanthocillin and its derivatives (PubMed:29844112). The first step of the pathway consists in the conversion of tyrosine into a vinyl-isonitrile intermediate by the isocyanide synthase xanB (PubMed:29844112). Subsequent oxidative dimerization of this intermediate to form xanthocillin may involve the cytochrome P450 monooxygenase xanG, whose expression is coregulated with that of XanB (PubMed:29844112). Xanthocillin can be further modified by the isonitrile hydratase-like protein xanA which introduces N-formyl groups and the methyltransferase xanE which introduces methyl groups, leading to the production of several derivatives including fumiformamide (PubMed:29844112). Finally, fumiformamide can be subject to both oxidative and reductive cyclization to yield melanocins E and F, respectively (PubMed:29844112).
Major facilitator transporter involved in fusarinine C (FsC) uptake (PubMed:36125294). In contrast to TAFC-mediated iron uptake, FsC-mediated iron uptake via mirD does not play a significant role during infection (PubMed:36125294).
Abolishes the production of pseurotin but leads to the accumulation of demethyl-deepoxy-synerazol (PubMed:24082142, PubMed:24939566).
Dual-functional monooxygenase/methyltransferase; part of the gene cluster that mediates the biosynthesis of pseurotin A, a competitive inhibitor of chitin synthase and an inducer of nerve-cell proliferation (PubMed:24082142, PubMed:24939566). The PKS-NRPS hybrid synthetase psoA is responsible for the biosynthesis of azaspirene, one of the first intermediates having the 1-oxa-7-azaspiro[4,4]-non-2-ene-4,6-dione core of pseurotin, via condensation of one acetyl-CoA, 4 malonyl-CoA, and a L-phenylalanine molecule (PubMed:24082142, PubMed:24939566). The dual-functional monooxygenase/methyltransferase psoF seems to be involved in the addition of the C3 methyl group onto the pseurotin scaffold (PubMed:24939566). Azaspirene is then converted to synerazol through 4 steps including oxidation of C17 by the cytochrome P450 monooxygenase psoD, O-methylation of the hydroxy group of C8 by the methyltransferase psoC, and the trans-to-cis isomerization of the C13 olefin by the glutathione S-transferase psoE (PubMed:24939566). The fourth step of synerazol production is performed by the dual-functional monooxygenase/methyltransferase psoF which seems to catalyze the epoxidation of the intermediate deepoxy-synerazol (PubMed:24939566). Synerazol can be attacked by a water molecule nonenzymatically at two different positions to yield two diol products, pseurotin A and pseurotin D (PubMed:24939566).
In the C-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily.
In the N-terminal section; belongs to the FAD-binding monooxygenase family.
PsoF is a unique bifunctional enzyme catalyzing two different types of reactions at completely separate steps of the pseurotin biosynthetic pathway and comprised an unusual combination of two domains, one homologous to a methyltransferase (MT) and another to an FAD-containing monooxygenase (FMO) (PubMed:24939566).
Mitochondrial transporter that mediates uptake of thiamine pyrophosphate (ThPP) into mitochondria.
Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (By similarity). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (By similarity).
Amino acid oxidase; part of the gene cluster that mediates the biosynthesis of the isoquinoline alkaloids fumisoquin A, fumisoquin B and fumisoquin C; as well as small amounts of fumipyrrole as a shunt metabolite (PubMed:25582336, PubMed:27065235, PubMed:30194285). The products of the cluster lead to a brown coloration and are important for growth and conidiation (PubMed:25582336). The nonribosomal peptide synthetase-like protein fsqF, which lacks a canonical condensation domain, is required for addition of a serine-derived dehydroalanine moiety to activated tyrosine but is not essential for the subsequent steps leading to isoquinoline formation (PubMed:27065235). A different enzyme, most likely the ATP-grasp enzyme fsqD, is responsible for activation of tyrosine (Probable). Three additional enzymes encoded by the fsq cluster, the N-methyltransferase fsqC, the phenol 2-monooxygenase fsqG and the FAD-dependent oxidase fsqB, catalyze the formation of the isoquinoline ring system in the fumisoquins (PubMed:27065235, PubMed:30194285). FsqB converts the fspF thiolation domain-bound (2S,4S,5S)-2-amino-6-(3,4-dihydroxyphenyl)-4-hydroxy-5-(methylamino)hexanoyl into isoquinoline (PubMed:27065235, PubMed:30194285). The cyclization most likely proceeds via a two-step mechanism, beginning with FAD-dependent oxidation of the methyl group to an iminium species followed by electrophilic attack on the deprotonated phenol (Probable).
Is able to convert N-methyl-3,4-dihydroxy-DL-phenylalanine (N-methyl-DOPA) directly into cyclic isoquinoline, in vitro (PubMed:27065235, PubMed:30194285). The absence of the meta-hydroxyl group, as in L-N-methyl-tyrosine, leads to a 25-fold lower rate of reduction and the formation of the demethylated product L-tyrosine, instead of a cyclic product (PubMed:30194285). Does not accept the D-stereoisomer of N-methyltyrosine, in contrast to N-methyl-DOPA, for which both stereoisomers are oxidized with similar rates (PubMed:30194285).
Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis.
Belongs to the Mediator complex subunit 7 family.
Belongs to the mitochondrion-specific ribosomal protein mS23 family.
Transcription factor that specifically regulates the neosartoricin biosynthesis gene cluster (PubMed:23758576, PubMed:23368997).
Belongs to the eukaryotic ribosomal protein eS27 family.
Catalyzes the NAD(H)-dependent interconversion of D-fructose and D-mannitol in the mannitol metabolic pathway. Has a preference for NADH over NADPH.
BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (By similarity). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (By similarity). Plays an essential role in the completion of conidial maturation and is essential for trehalose biogenesis in conidia (PubMed:20966095). Negatively regulates expression of the melanin biosynthetic gene cluster (PubMed:24123270). Also plays an a role in the early phase of fungal growth including proper hyphal branching (PubMed:20966095).
Causes the formation of defective spore walls and a lack of trehalose biogenesis, leading to a rapid loss of spore viability and reduced tolerance to various stresses (PubMed:20966095). Leads also to delayed germtube formation and reduced hyphal branching (PubMed:20966095).
Highly expressed during conidiation (PubMed:18298443, PubMed:20966095). Expression is positively regulated by hsp90 (PubMed:22822234). Expression is also controlled by upstream regulators calA and crzA (PubMed:18298443). Expression is decreased by 2',4'-Dihydroxychalcone (2',4'-DHC) (PubMed:26190922).
Phosphomevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). Erg8 converts 5-phosphomevalonate to 5-diphosphomevalonate (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase erg12 (AFUA_4G07780) first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase erg8 (AFUA_5G10680). The diphosphomevalonate decarboxylase mvd1 (AFUA_4G07130) then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase idi1 (AFUA_6G11160) then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase erg20 (AFUA_5G02450) catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (PubMed:16110826, PubMed:22106303) (Probable).
Belongs to the PEP-utilizing enzyme family.
Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q). Is required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly.
Belongs to the dynactin subunits 5/6 family. Dynactin subunit 5 subfamily.
Oxidoreductase; part of the gene cluster that mediates the biosynthesis of trypacidin, a mycotoxin with antiprotozoal activity and that plays a role in the infection process (PubMed:26278536, PubMed:26242966). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) tpcC (PubMed:26242966). The atrochrysone carboxyl ACP thioesterase tpcB then breaks the thioester bond and releases the atrochrysone carboxylic acid from tpcC (PubMed:26242966). The decarboxylase tpcK converts atrochrysone carboxylic acid to atrochrysone which is further reduced into emodin anthrone (PubMed:26242966). The next step is performed by the emodin anthrone oxygenase tpcL that catalyzes the oxidation of emodinanthrone to emodin (PubMed:26242966). Emodin O-methyltransferase encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin to form questin (PubMed:26242966). Ring cleavage of questin by questin oxidase tpcI leads to desmethylsulochrin via several intermediates including questin epoxide (By similarity). Another methylation step catalyzed by tpcM leads to the formation of sulochrin which is further converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes the conversion of monomethylsulfochrin to trypacidin (PubMed:26242966). Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)), thus triggering host necrotic cell death (PubMed:22319557). The trypacidin pathway is also able to produce endocrocin via a distinct route from the endocrocin Enc pathway (PubMed:26242966).
Involved in cytoplasm to vacuole transport (Cvt), pexophagy, mitophagy and nucleophagy. Recruits mitochondria for their selective degradation via autophagy (mitophagy) during starvation. Works as scaffold proteins that recruit ATG proteins to the pre-autophagosome (PAS), the site of vesicle/autophagosome formation. Required for the Cvt vesicles completion (By similarity).
Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class II DHOase subfamily.
Bifunctional heme-containing enzyme that oxidizes linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (within the N-terminal heme peroxidase domain), which is subsequently isomerized to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (within the C-terminal P450 heme thiolate domain). Oxidized unsaturated fatty acids, so-called oxylipins, derived from endogenous fatty acids, influence the development of the asexual conidiophores and sexual cleistothecia and regulate the secondary metabolism. These substances were collectively named psi factors and are primarily a mixture of hydroxylated oleic, linoleic and alpha-linolenic acids. They are termed psi-beta, psi-alpha, and psi-gamma, respectively. Oxylipins may also serve as activators of mammalian immune responses contributing to enhanced resistance to opportunistic fungi and as factors that modulate fungal development contributing to resistance to host defenses.
Belongs to the VAMP-associated protein (VAP) (TC 9.B.17) family.
In the C-terminal section; belongs to the NAGSA dehydrogenase family.
In the N-terminal section; belongs to the acetylglutamate kinase family.
Belongs to the OMP decarboxylase family.
Belongs to the eukaryotic-type primase small subunit family.
Belongs to the creA/MIG C2H2-type zinc-finger protein family.
Transcription regulator component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. Represses the transcription of the alcR, alcA and aldA genes by binding to a GC-rich region in their promoter. Also plays a role in response to carbon starvation and the control of extracellular proteases activity (By similarity).
Ubiquitinated. Deubiquitinated by creB, probably to control its activity or amount (By similarity).
Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family.
Belongs to the neutral ceramidase family.
Belongs to the diacylglycerol acyltransferase family.
Belongs to the mannose-6-phosphate isomerase type 1 family.
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.
Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
Expression is induced under iron limitation (PubMed:28367141).
Major facilitator transporter that contributes to the maintenance of intracellular siderophore ferricrocin (FC) levels (PubMed:28367141). Plays a role in conidiation and confers protection against oxidative stress (PubMed:28367141). Contributes also to fungal virulence in the Galleria mellonella animal model system (PubMed:28367141). Does not appear to play a role in either siderophore export or uptake (PubMed:28367141).
Reduces growth under iron limitation and increases sensitivity to hydrogen peroxide (PubMed:28367141). Decreases intracellular ferricrocin level under iron limitation (PubMed:28367141). Leads to increased abundance of siderophore biosynthetic enzymes and of hapX (PubMed:28367141). Finally, decreases the virulence in the Galleria mellonella animal model system (PubMed:28367141).
Belongs to the TRAFAC class YlqF/YawG GTPase family. NOG2 subfamily.
GTPase that associates with pre-60S ribosomal subunits in the nucleolus and is required for their nuclear export and maturation.
Negative regulator of transcription elongation.
Belongs to the peptidase C19 family. PAN2 subfamily.
Binds 2 metal cations per subunit in the catalytic exonuclease domain.
Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein pab1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by xrn1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails.
Contains a pseudo-UCH domain. This ubiquitin C-terminal hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain is predicted to be catalytically inactive because it lacks the active site catalytic triad characteristic of thiol proteases, with residues at the equivalent structural positions that are incompatible with catalysis, and it cannot bind ubiquitin. It functions as a structural scaffold for intra- and intermolecular interactions in the complex.
Forms a heterotrimer with an asymmetric homodimer of the regulatory subunit pan3 to form the poly(A)-nuclease (PAN) deadenylation complex.
Positively regulated by the regulatory subunit pan3.
The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with pan3.
Component of ORC, a complex composed of at least 6 subunits: ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle dependent manner. It is sequentially assembled at the exit from anaphase of mitosis and disassembled as cells enter S phase.
Inactive carboxypeptidase that may play a role in cell wall organization and biogenesis.
Lacks the conserved Glu residue in position 490 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates.
Involved in maceration and soft-rotting of plant tissue.
Causes decreased production of triacetylfusarinine C (TAFC) but not fusarinine C (FsC) (PubMed:21062375). Attenuates virulence in a murine model of invasive aspergillosis (PubMed:21062375). Also increases zinc sensitivity (PubMed:21062375).
Expression is repressed by iron (PubMed:21062375). Expression is induced by the zinc cluster transcription factor acuM to stimulate expression of genes involved in both reductive iron assimilation and siderophore-mediated iron uptake (PubMed:20941352).
Transcription factor required for repression of genes during iron starvation (PubMed:21062375). Represses iron-dependent and mitochondrial-localized activities including respiration, TCA cycle, amino acid metabolism, iron-sulfur-cluster and heme biosynthesis (PubMed:21062375). Iron starvation causes a massive remodeling of the amino acid pool and hapX is essential for the coordination of the production of siderophores and their precursor ornithine (PubMed:21062375).
Belongs to the steroid 5-alpha reductase family. Polyprenol reductase subfamily.
Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism.
Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1/sscA) (By similarity).
Heterodimer with PAM18/pamR. Component of the PAM complex, at least composed of mtHsp70, MGE1/mgeA, tim44, PAM16/pamP, PAM17/pamQ and PAM18/pamR (By similarity).
The J domain is essential for co-chaperone activity and mediates the heterodimerization with the J-like domain of PAM16.
Inclusion body (IB) resident protein that interacts strongly with lipid droplet (LD) proteins. Involved in LD-mediated IB clearing after protein folding stress, probably by enabling access to the IBs of an LD-stored soluble sterol derivative that acts as chaperone in inclusion clearing.
Belongs to the DEAD box helicase family. DDX56/DBP9 subfamily.
Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily.
PPIase that acts as a histone chaperone. Histone proline isomerase that increases the rate of cis-trans isomerization at prolines on the histone H3 N-terminal tail. Proline isomerization influences H3 methylation thereby regulating gene expression.
Belongs to the thiamine pyrophosphokinase family.
Expression is under the control of the secondary metabolism regulator laeA (PubMed:17432932). Expression is completely abrogated when gliT is deleted in cells exposed to exogenous gliotoxin (PubMed:25311525).
Belongs to the non-repetitive/WGA-negative nucleoporin family.
Component of the TIM23 complex, at least composed of TIM23/timX, TIM17/timQ, tim50 and TIM21/timU. Interacts with preproteins in transit (By similarity).
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Required to direct preproteins in transit and direct them to the channel protein TIM23, and possibly facilitates transfer of the translocating proteins from the TOM complex to the TIM23 complex (By similarity).
Belongs to the peptidase M28 family. M28B subfamily.
Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. May methylate the carboxyl group of leucine residues to form alpha-leucine ester residues (By similarity).
Conjugated to atg12; which is essential for autophagy.
Involved in cytoplasm to vacuole transport (Cvt) and autophagic vesicle formation. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy). Also required for mitophagy, which eliminates defective or superfluous mitochondria in order to fulfill cellular energy requirements and prevent excess ROS production. Conjugation with atg12, through a ubiquitin-like conjugating system involving atg7 as an E1-like activating enzyme and atg10 as an E2-like conjugating enzyme, is essential for its function. The atg12-atg5 conjugate acts as an E3-like enzyme which is required for lipidation of atg8 and atg8 association to the vesicle membranes (By similarity).
In the N-terminal section; belongs to the MoaB/Mog family.
Belongs to the DNA polymerase type-A family.
Belongs to the metallo-dependent hydrolases superfamily. ATZ/TRZ family.
Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Lipid transfer protein required for autophagosome completion and peroxisome degradation. Tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum (ER) and mediates direct lipid transfer from ER to IM for IM expansion. Atg2 binds to the ER exit site (ERES), which is the membrane source for autophagosome formation, using basic residues in its N-terminal region (NR) and to the expanding edge of the IM through its C-terminal region. The latter binding is assisted by an atg18-PtdIns3P interaction. Atg2 then extracts phospholipids from the membrane source using its NR and transfers them to atg9 to the IM through its predicted beta-sheet-rich structure for membrane expansion.
Probable lysosomal cobalamin transporter. Required to export cobalamin from lysosomes allowing its conversion to cofactors.
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. GON7 likely plays a supporting role to the catalytic subunit KAE1 in the complex. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Belongs to the eukaryotic ribosomal protein eL30 family.
Required for respiratory activity and maintenance and expression of the mitochondrial genome.
Belongs to the helicase family. PIF1 subfamily.
DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability.
Displays specific TAFC esterase activity but does not hydrolyze fusarinine C, which has the same core structure as TAFC (PubMed:17586718). Hydrolysis optimizes but is not essential for TAFC-mediated iron uptake (PubMed:17586718).Both extra- and intracellular siderophores have been shown to be crucial for the virulence (PubMed:17586718). Subsequent to chelation of iron and uptake, FsC and TAFC are hydrolyzed and the iron is transferred to the metabolism or to the intracellular siderophore ferricrocin (FC) for transport and storage of iron (PubMed:17586718). Hydrolyzes both TAFC and DF-TAFC with equal efficiencies, suggesting that its function might not be restricted to the release of iron from the siderophore but might also include the degradation of the iron-free chelator to protect cells (PubMed:17586718).
Eliminates TAFC esterase activity and causes increased intracellular accumulation of TAFC and TAFC hydrolysis products (PubMed:17586718). Reduces the intracellular transfer rate of iron from TAFC to DF-FC and delays iron sensing (PubMed:17586718). Causes a decreased radial growth rate under iron-depleted but not iron-replete conditions (PubMed:17586718).
Expression is induced during iron deprivation (PubMed:17586718).
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Belongs to the MoaE family. MOCS2B subfamily.
Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group.
Abolishes the production of endocrocin (PubMed:22492455).
Atrochrysone carboxyl ACP thioesterase; part of the gene cluster that mediates the biosynthesis of endocrocin, a simple anthraquinone interesting for many biotechnological applications (PubMed:22492455, PubMed:23592999). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) encA (PubMed:22492455). The atrochrysone carboxyl ACP thioesterase encB then breaks the thioester bond and releases the atrochrysone carboxylic acid from encA (PubMed:22492455). The atrochrysone carboxylic acid is then converted to endocrocin anthrone which is further oxidized into endocrocin by the anthrone oxygenase encC (PubMed:22492455). The exact function of encD has not been identified yet, but it negatively regulates endocrocin production, likely through the modification of endocrocin itself (PubMed:22492455).
Belongs to the adenosylhomocysteinase family.
Belongs to the ubiquitin-activating E1 family. UBA3 subfamily.
Catalytic subunit of the dimeric E1 enzyme, which activates NEDD8.
Has a modular structure: a carbohydrate-binding module (CBM) at the N-terminus, a linker rich in serines, and a C-terminal endo-1,4-mannanase catalytic module. The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Belongs to the oxidase-dependent Fe transporter (OFeT) (TC 9.A.10.1) family.
Does not affect the virulence in a murine model of invasive aspergillosis (PubMed:15504822). Displays an 8-fold increase in external siderophore triacetylfusarinine C (TAFC) production after 12h of growth in iron-depleted conditions (PubMed:15504822).
Expression is up-regulated during iron starvation and is controlled by the GATA-type transcription factor sreA and the Zinc cluster transcription factor acuM (PubMed:15504822, PubMed:18721228, PubMed:21062375).
High affinity iron permease; part of the reductive iron assimilatory system (RIA), a siderophore-independent high affinity iron uptake mechanism (PubMed:15504822).
This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Belongs to the bacterial ribosomal protein bL27 family.
Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells. Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy, mitophagy, and pexophagy.
The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctate structures.
Transcription factor required for protein utilization and degradation. Regulates transcription of major secreted proteases including a serine alkaline protease (alk1), a metalloprotease (mep), an aspergillopepsin (pep1), a sedolisin (sed2) and two dipeptidyl-peptidases (dppIV and dppV). However, it is not a virulence determinant in leukopenic mice.
Belongs to the mitochondrion-specific ribosomal protein mL53 family.
Expression is induced upon voriconazole treatment (PubMed:12135575, PubMed:15504870). Expression is increased in clinical azole-resistant isolates (PubMed:26933209, PubMed:28080217, PubMed:29124846). Expression is down-regulated by tetrandrine and posaconazole in a synergistic manner (PubMed:28080217).
Pleiotropic ABC efflux transporter involved in the basal level of azole susceptibility (PubMed:26933209, PubMed:28080217). Confers resistance to fluconazole and voriconazole (PubMed:26933209).
Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate.
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. FDH subfamily.
Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms.
Belongs to the glycosyl hydrolase 63 family.
Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor.
Belongs to the ubiquitin-conjugating enzyme family. UEV subfamily.
Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
Belongs to the pterin-4-alpha-carbinolamine dehydratase family.
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
Mixed-linked glucanase involved in the degradation of complex natural cellulosic substrates.
Essential factor for the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB).
Belongs to the complex I 49 kDa subunit family.
Belongs to the ubiquitin conjugation factor E4 family.
Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin. Active against paranitrophenyl-acetate, methyl ferulate and wheat arabinoxylan (By similarity).
Forms the NCT transcriptional regulatory complex with nctB and mot1.
Results in a reduction in growth rate (PubMed:31969561). Leads to a multidrug-resistance phenotype, including the azoles (itraconazole, voriconazole and posaconazole), as well as the salvage therapeutic amphotericin B and terbinafine, an agent used in the treatment of chronic and allergic disease (PubMed:31969561). Leads also to transcriptional derepression of cdr1B and its over-production (PubMed:31969561). Results also in a notable increase in the immunogenic properties of Aspergillus fumigatus, but does not result in loss of virulence (PubMed:31969561).
Belongs to the U1 small nuclear ribonucleoprotein C family.
Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region.
U1 snRNP is composed of the 7 core Sm proteins B/B', D1, D2, D3, E, F and G that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP, and at least 3 U1 snRNP-specific proteins U1-70K, U1-A and U1-C. U1-C interacts with U1 snRNA and the 5' splice-site region of the pre-mRNA.
ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.
Belongs to the SEC23/SEC24 family. SEC24 subfamily.
The COPII coat is composed of at least 5 proteins: the sec23/24 complex, the sec13/31 complex, and the protein sar1. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
Involved in nucleolar integrity and required for processing of the pre-rRNA for the 60S ribosome subunit.
Questin oxidase; part of the gene cluster that mediates the biosynthesis of trypacidin, a mycotoxin with antiprotozoal activity and that plays a role in the infection process (PubMed:26278536, PubMed:26242966). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) tpcC (PubMed:26242966). The atrochrysone carboxyl ACP thioesterase tpcB then breaks the thioester bond and releases the atrochrysone carboxylic acid from tpcC (PubMed:26242966). The decarboxylase tpcK converts atrochrysone carboxylic acid to atrochrysone which is further reduced into emodin anthrone (PubMed:26242966). The next step is performed by the emodin anthrone oxygenase tpcL that catalyzes the oxidation of emodinanthrone to emodin (PubMed:26242966). Emodin O-methyltransferase encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin to form questin (PubMed:26242966). Ring cleavage of questin by questin oxidase tpcI leads to desmethylsulochrin via several intermediates including questin epoxide (By similarity). Another methylation step catalyzed by tpcM leads to the formation of sulochrin which is further converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes the conversion of monomethylsulfochrin to trypacidin (PubMed:26242966). Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)), thus triggering host necrotic cell death (PubMed:22319557). The trypacidin pathway is also able to produce endocrocin via a distinct route from the endocrocin Enc pathway (PubMed:26242966).
Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U47 in cytoplasmic tRNAs (By similarity). Catalyzes the synthesis of dihydrouridine in some mRNAs, thereby affecting their translation (By similarity).
Belongs to the peptidase M67A family. CSN5 subfamily.
Catalytic component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes.
Component of the COP9 signalosome (CSN) complex.
The JAMM motif is essential for the protease activity of the CSN complex resulting in deneddylation of cullins. It constitutes the catalytic center of the complex (By similarity).
Belongs to the poly(A) polymerase family.
Binds 2 magnesium ions. Also active with manganese.
Polymerase that creates the 3'-poly(A) tail of mRNA's.
Belongs to the 2H phosphoesterase superfamily. USB1 family.
Phosphodiesterase responsible for the U6 snRNA 3' end processing. Acts as an exoribonuclease (RNase) responsible for trimming the poly(U) tract of the last nucleotides in the pre-U6 snRNA molecule, leading to the formation of mature U6 snRNA.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RMT2 methyltransferase family.
S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that methylates the delta-nitrogen atom of arginine residues to form N5-methylarginine (type IV) in target proteins. Monomethylates ribosomal protein L12.
Belongs to the chaperonin (HSP60) family.
Belongs to the FNT transporter (TC 2.A.44) family.
ATP-dependent RNA helicase required for 60S ribosomal subunit synthesis. Involved in efficient pre-rRNA processing, predominantly at site A3, which is necessary for the normal formation of 25S and 5.8S rRNAs (By similarity).
Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production.
Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Accumulates the intermediate 4-dimethylallyl-L-abrine (PubMed:21409592).
Catalase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid (PubMed:15933009, PubMed:23435153, PubMed:26972831). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:15870460). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20039019, PubMed:20526482, PubMed:21409592, PubMed:23435153). EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline (PubMed:20526482). EasG then catalyzes the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:20526482). Hydrolysis of festuclavine by easM then leads to the formation of fumigaclavine B which is in turn acetylated by easN to fumigaclavine A (PubMed:26972831). Finally, easL catalyzes the conversion of fumigaclavine A into fumigaclavine C by attaching a dimethylallyl moiety to C-2 of the indole nucleus (PubMed:19672909).
In the C-terminal section; belongs to the anthranilate synthase component I family.
Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes (By similarity).
Belongs to the Mediator complex subunit 16 family.
Belongs to the lipoxygenase family. Manganese lipoxygenase subfamily.
Lipoxygenase that metabolizes linoleic acid to 9- and 13-hydroperoxy fatty acids. Specific towards 13-HPODE yielding 89% of the total HPODE.
Three His residues, the carboxyl oxygen of the C-terminal Ile or Val residue, and a fifth residue, usually Asn, ligate the metal, which binds water to form a catalytic base Mn(2+)OH(2) for hydrogen abstraction.
Belongs to the globin family. Two-domain flavohemoproteins subfamily.
Brevianamide F prenyltransferase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities (PubMed:16000710, PubMed:23649274). The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA (PubMed:16755625). Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B (PubMed:16000710, PubMed:19113967, PubMed:21105662, PubMed:23090579). FtmPT1/ftmB shows also tryptophan aminopeptidase activity with preference for linear peptides containing a tryptophanyl moiety at the N-terminus (PubMed:18635009). The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively (PubMed:19226505). The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B (PubMed:18683158). Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties (PubMed:19763315). In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Belongs to the cytochrome c oxidase subunit 6A family.
Belongs to the class VI-like SAM-binding methyltransferase superfamily. Isoprenylcysteine carboxyl methyltransferase family.
Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase complex; essential for the ER localization.
Component of the 1.8 MDa SAGA transcription coactivator-HAT complex. SAGA is built of 5 distinct domains with specialized functions. Within the SAGA complex, SUS1, SGF11, SGF73 and UBP8 form an additional subcomplex of SAGA called the DUB module (deubiquitination module). Interacts directly with SGF73, SUS1 and UBP8.
Functions as component of the transcription regulatory histone acetylation (HAT) complex SAGA. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation and deubiquitination. SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). Involved in transcriptional regulation of a subset of SAGA-regulated genes. Within the SAGA complex, participates in a subcomplex, that specifically deubiquitinates histones H2B.
Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1 subfamily.
Mitochondrial GTPase involved in assembly of the large ribosomal subunit. Plays a role in expression of the mitochondrial translational machinery.
Belongs to the SMC family. SMC3 subfamily.
Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.
Catalyzes the dephosphorylation of the nucleoside 5'-monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and deoxythymidine monophosphate (dTMP).
Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. 6-phosphogluconolactonase subfamily.
Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Belongs to the SMC family. SMC1 subfamily.
Component of the nascent polypeptide-associated complex (NAC), a dynamic component of the ribosomal exit tunnel, protecting the emerging polypeptides from interaction with other cytoplasmic proteins to ensure appropriate nascent protein targeting. The NAC complex also promotes mitochondrial protein import by enhancing productive ribosome interactions with the outer mitochondrial membrane and blocks the inappropriate interaction of ribosomes translating non-secretory nascent polypeptides with translocation sites in the membrane of the endoplasmic reticulum. EGD1 may act as a transcription factor that exert a negative effect on the expression of several genes that are transcribed by RNA polymerase II.
Belongs to the complex I NDUFS5 subunit family.
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2 homeostasis at the plasma membrane. Heme-binding protein that may play a role in organic oxidant-induced stress responses.
Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 2 subfamily.
Belongs to the squalene monooxygenase family.
Squalene epoxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:16110826) (Probable). Erg1 catalyzes the epoxidation of squalene into 2,3-epoxysqualene (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (PubMed:16110826, PubMed:18191972) (Probable).
Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of trypacidin, a mycotoxin with antiprotozoal activity and that plays a role in the infection process (PubMed:26278536, PubMed:26242966). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) tpcC (PubMed:26242966). The atrochrysone carboxyl ACP thioesterase tpcB then breaks the thioester bond and releases the atrochrysone carboxylic acid from tpcC (PubMed:26242966). The decarboxylase tpcK converts atrochrysone carboxylic acid to atrochrysone which is further reduced into emodin anthrone (PubMed:26242966). The next step is performed by the emodin anthrone oxygenase tpcL that catalyzes the oxidation of emodinanthrone to emodin (PubMed:26242966). Emodin O-methyltransferase encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin to form questin (PubMed:26242966). Ring cleavage of questin by questin oxidase tpcI leads to desmethylsulochrin via several intermediates including questin epoxide (By similarity). Another methylation step catalyzed by tpcM leads to the formation of sulochrin which is further converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes the conversion of monomethylsulfochrin to trypacidin (PubMed:26242966). Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)), thus triggering host necrotic cell death (PubMed:22319557). The trypacidin pathway is also able to produce endocrocin via a distinct route from the endocrocin Enc pathway (PubMed:26242966).
Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Component of the HAT-B complex composed of at least hat1 and hat2. The HAT-B complex binds to histone H4 tail (By similarity).
Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Belongs to the universal ribosomal protein uS19 family.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily.
Ca(2+). Can also use Mg(2+), but with lower efficiency.
Involved in the maturation of Asn-linked oligosaccharides. Progressively trims alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2) (By similarity).
Leads to the accumulation of 4-methyl fecosterol and 4,4-dimethyl fecosterol (PubMed:25107308). Displays a dmoderate susceptibility to hypoxia and the endoplasmic reticulum stress-inducing agent DTT, but does not affect virulence in murine or insect models of invasive aspergillosis (PubMed:25107308).
Sterol-C4-methyl oxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:25107308). Erg25A is a catalytic component of the C-4 demethylation complex that catalyzes the conversion of 4,4-dimethylfecosterol into fecosterol via 4-methylfecosterol (PubMed:25107308). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (PubMed:16110826, PubMed:18191972) (Probable).
N-methyltransferase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). Gliotoxin contributes to pathogenesis during invasive aspergillosis (PubMed:17601876, PubMed:18199036). In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species (PubMed:17601876).
Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Pectinolytic enzymes consist of four classes of enzymes: pectine lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Hydrolyzes alpha-D-galacturonopyranosyl-(1,2)-alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions of pectins (By similarity).
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Belongs to the activator 1 large subunit family.
Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2 (By similarity).
The DPH-type metal-binding (MB) domain can bind either zinc or iron ions.
2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of endocrocin, a simple anthraquinone interesting for many biotechnological applications (PubMed:22492455). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) encA (PubMed:22492455). The atrochrysone carboxyl ACP thioesterase encB then breaks the thioester bond and releases the atrochrysone carboxylic acid from encA (PubMed:22492455). The atrochrysone carboxylic acid is then converted to endocrocin anthrone which is further oxidized into endocrocin by encC (PubMed:22492455). The exact function of encD has not been identified yet, but it negatively regulates endocrocin production, likely through the modification of endocrocin itself (PubMed:22492455).
Results in increased endocrocin production (PubMed:22492455).
FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of the antitumor fumiquinazolines that confer a dual-usage capability to defend against phagocytes in the environment and animal hosts (PubMed:20225828, PubMed:20804163, PubMed:21899262, PubMed:24612080, PubMed:33705521). The simplest member is fumiquinazoline F (FQF) with a 6-6-6 tricyclic core derived from anthranilic acid (Ant), tryptophan (Trp), and alanine (Ala) (PubMed:20225828). The trimodular NRPS fmqA is responsible for FQF formation (PubMed:20225828). Modules 1, 2 and 3 of fmqA are predicted to activate and load Ant, Trp and Ala, respectively, providing for the assembly of an Ant-Trp-Ala-S-enzyme intermediate that would undergo double cyclization for chain release and generation of the tricyclic 6-6-6 product fumiquinazoline F (PubMed:20225828). The presence of an E domain predicted for module 2 of fmqA is consistent with epimerization of L-Trp to D-Trp during assembly to generate the R-stereocenter at C14 of FQF (PubMed:20225828). The FAD-dependent monooxygenase fmqB and the monomodular NRPS fmqC then maturate FQF to FQA (PubMed:20804163). FmqB oxidizes the 2',3'-double bond of the indole side chain of FQF, and fmqC activates L-Ala as the adenylate, installs it as the pantetheinyl thioester on its carrier protein domain, and acylates the oxidized indole for subsequent intramolecular cyclization to create the 6-5-5-imidazolindolone of FQA (PubMed:20804163). The FAD-linked oxidoreductase fmqD introduces a third layer of scaffold complexity by converting FQA to the spirohemiaminal FQC, presumably by catalyzing the formation of a transient imine within the pyrazinone ring (PubMed:21899262). FQC subsequently converts nonenzymatically to the known cyclic aminal FQD (PubMed:21899262).
Leads to a significant decrease but not complete loss of fumiquinazoline C production and accumulates fumiquinazoline A (PubMed:24612080).
Belongs to the V-ATPase H subunit family.
Involved in pre-mRNA splicing. Binds and is required for the stability of snRNA U1, U2, U4 and U5 which contain a highly conserved structural motif called the Sm binding site. Involved in cap modification.
Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pyripyropene A, a specific human acyl-coenzyme A:cholesterol acyltransferase 2 inhibitor (PubMed:20861902). The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase pyr1 (PubMed:20861902). Nicotinyl-CoA is then a substrate of polyketide synthase pyr2 to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase pyr6 to yield farnesyl-HPPO (PubMed:20861902). The next steps consist of an epoxidation of farnesyl-HPPO to epoxyfarnesyl-HPPO by FAD-dependent monooxygenase pyr5 and a cyclization of the terpenoid portion by the terpene cyclase pyr4 to yield deacetyl-pyripyropene E (PubMed:20861902). The 2 cytochrome P450 monooxygenases pyr3 and pyr9, and the 2 acetyltransferases pyr7 and pyr8 are involved in the conversion of deacetyl-pyripyropene E into pyripyropene A through several cycles of oxidation and acetylation steps (PubMed:20861902). Pyr7 acetylates deacetyl-pyripyropene E to pyripyropene E which is oxidized to 11-deacetyl-pyripyropene O by pyr3, which is in turn acetylated into pyripyropene O by pyr8 (PubMed:21224862, PubMed:26019565). Pyripyropene O is then oxidized to deacetyl-pyripyropene A by pyr9 (PubMed:21224862). Deacetyl-pyripyropene A is finally acetylated to pyripyropene A by pyr8 (PubMed:26019565).
ATP-binding RNA helicase involved in transcription elongation and required for the export of mRNA out of the nucleus. SUB2 also plays a role in pre-mRNA splicing and spliceosome assembly. May be involved in rDNA and telomeric silencing, and maintenance of genome integrity (By similarity).
Belongs to the DEAD box helicase family. DECD subfamily.
Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
Belongs to the eukaryotic ribosomal protein eL13 family.
Resulted in loss of trypacidin and questin production (PubMed:26242966).
Transcription factor that regulates the expression of the gene clusters that mediate the biosynthesis of trypacidin, a metabolite with antiprotozoal activity and a possible role in the infection process (PubMed:26278536, PubMed:26242966). Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)), thus triggering host necrotic cell death (PubMed:22319557).
Belongs to the alcohol acetyltransferase FCK4 family.
Probable alcohol acetyltransferase; part of the crm gene cluster that mediates the biosynthesis of a yet unidentified copper-responsive metabolite.
Involved in the early part of the secretory pathway.
Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.
DEAD-box RNA helicase-like protein required for pre-18S rRNA processing, specifically at sites A0, A1, and A2.
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
NAD(+)-dependent glutamate dehydrogenase which degrades glutamate to ammonia and alpha-ketoglutarate.
Belongs to the mitochondrial Rho GTPase family.
Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution.
Belongs to the prephenate/arogenate dehydrogenase family.
Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
Belongs to the glycogen phosphorylase family.
Expression is under the control of the secondary metabolism regulator laeA (PubMed:17432932). Expression up-regulated upon exposure to exogenous gliotoxin (PubMed:25311525).
Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid (PubMed:19415934, PubMed:19216560, PubMed:29158519). Protostadienol synthase helA cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol)(PubMed:19415934, PubMed:19216560, PubMed:29158519). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid (PubMed:19216560). Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton (PubMed:29158519). This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid (PubMed:19415934, PubMed:19216560, PubMed:29158519). Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order (PubMed:29158519). The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21 (PubMed:29158519). C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation (PubMed:19415934, PubMed:29158519). The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC (PubMed:19415934, PubMed:29158519).
In the N-terminal section; belongs to the FGAMS family.
Belongs to the eukaryotic RPB8 RNA polymerase subunit family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.
Belongs to the glycosyltransferase 3 family.
Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.
GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle.
Belongs to the acyl carrier protein (ACP) family.
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.
Required for N-linked oligosaccharide assembly. Has a role in the last step of the synthesis of the Man(5)GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum.
Probable rhomboid-type serine protease that catalyzes intramembrane proteolysis.
Belongs to the eukaryotic release factor 1 family. Pelota subfamily.
Component of the Dom34-Hbs1 complex, a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway (PubMed:20890290). In the Dom34-Hbs1 complex, dom34 recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel. Following ribosome-binding, the Dom34-Hbs1 complex promotes the disassembly of stalled ribosomes, followed by degradation of damaged mRNAs as part of the NGD pathway.
Belongs to the four-carbon acid sugar kinase family.
Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA.
ATP-dependent RNA helicase required for ribosome biogenesis. Involved in the release of U14 snoRNA in pre-ribosomal complexes. Required for pre-rRNA cleavage at site A2 (By similarity).
Belongs to the DEAD box helicase family. DDX10/DBP4 subfamily.
Interacts with the U3 and U14 snoRNAs. Associates with pre-ribosomal complexes (By similarity).
Belongs to the STE12 transcription factor family.
Belongs to the eukaryotic RPC34/RPC39 RNA polymerase subunit family.
Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity. Regulates radial hyphal growth and germination. Involved in virulence and mediates resistance to oxidative stress.
Belongs to the type II topoisomerase family.
Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.
Transcription regulator that specifically up-regulates the gene cluster that mediates the biosynthesis of the isocyanide xanthocillin and its derivatives.
Virtually eliminates the production of all pathway metabolites, including fumiformamide, melanocin E, melanocin F, but also the sulfated xanthocillin derivative BU-4704 and xanthocillin X monomethyl ether.
Belongs to the Rieske iron-sulfur protein family.
Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family.
Belongs to the Nudix hydrolase family. DCP2 subfamily.
Heptaketide hydrolyase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment and a structural component of the conidial wall (PubMed:10515939, PubMed:11350964, PubMed:15310761, PubMed:19156203). The first step of the pathway is the production of the heptaketide naphtopyrone YWA1 by the polyketide synthase alb1 though condensation of acetyl-CoA with malonyl-CoA (PubMed:10515939). The naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase ayp1 though chain-length shortening (PubMed:10515939, PubMed:11350964). 1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to yield scytalone (PubMed:10515939, PubMed:11350964, PubMed:15310761). The scytalone dehydratase arp1 then reduces scytalone to 1,3,8-THN (PubMed:10515939). 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to yield vermelone (PubMed:10515939). Vermelone is further converted by the multicopper oxidase abr1 to 1,8-DHN (PubMed:10515939). Finally the laccase abr2 transforms 1,8-DHN to DHN-melanin (PubMed:10515939). DHN-melanin biosynthesis appears to be initiated in endosomes where early enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to melanin deposition on the cell surface where late enzymes (abr1 and abr2) localize (PubMed:26972005). DHN-melanin is an important structural component of the outer cell wall and is required for the presence of conidial surface hydrophobins (PubMed:19703288). DHN-melanin also plays a crucial role in fungal virulence, including a protective role against the host's immune defenses (PubMed:19156203, PubMed:20145078, PubMed:21501368, PubMed:21747802, PubMed:21573171, PubMed:24818666). DHN-melanin protects also conidia against amoeba predation (PubMed:25684622).
Leads to a yellow-green color of conidia (PubMed:11350964, PubMed:26972005). Impairs the accumulation of 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) (PubMed:11350964). Results in an altered conidial surface with masked surface rodlet layer, leaky cell wall allowing the deposition of proteins on the cell surface and exposing the otherwise-masked cell wall polysaccharides at the surface (PubMed:24818666). Decreases the protection against the host's immune defenses (PubMed:21501368). Causes enhanced insect mortality compared to the parent strain in a wax moth Galleria mellonella infection model, probably through exacerbated immune response of the wax moth (PubMed:19156203).
Serine protease inhibitors strongly inhibit activity (PubMed:15310761). Moreover, 3,4-dichloroisocoumarinshows and 2-acetyl-1,3,6,8-tetrahydroxynaphthalene act also as a strong inhibitor (PubMed:15310761).
Belongs to the Mediator complex subunit 4 family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM4 family.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono- and dimethylates elongation factor 1-alpha at 'Lys-316'. May play a role in intracellular transport.
Interacts with the flavoprotein subunit within the SDH catalytic dimer.
Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit of the SDH catalytic dimer.
ATP-binding RNA helicase involved in ribosome assembly.
Associates with pre-ribosomal particles.
Belongs to the DEAD box helicase family. DDX27/DRS1 subfamily.
Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair.
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.
Belongs to the replication factor A protein 3 family.
Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has also a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides.
May be involved in metabolism of dipeptides or may affect host defense mechanisms. Has a substrate specificity limited to the hydrolysis of X-Ala, His-Ser, and Ser-Tyr dipeptides at a neutral pH optimum (By similarity).
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for l- to d- amino acid conversion) are present within the NRP synthetase. NRPS4 has the following architecture: A-T-C-A-C.
Nonribosomal peptide synthase; part of the siderophore biosynthetic pathway (PubMed:15953695, PubMed:17845073, PubMed:17464044). Aspergillus fumigatus produces four types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake; and intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial iron distribution and storage. TAFC consists of three N(2)-acetyl-N(5)-anhydromevalonyl-N(5)-hydroxyornithine residues cyclically linked by ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-(N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of all four siderophores depends on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA (PubMed:15504822, PubMed:16113265). Subsequently, the pathways for biosynthesis of extra- and intracellular siderophores split (PubMed:17845073). For biosynthesis of extracellular siderophores, the transacylase sidF transfers anhydromevalonyl to N(5)-hydroxyornithine (PubMed:17845073). The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by sidI and sidH respectively (PubMed:22106303). The acetylation of N(5)-hydroxyornithine for FC biosynthesis involves the constitutively expressed sidL (PubMed:21622789). FC is hydroxylated to HFC by an as yet uncharacterized enzyme during conidiation (PubMed:17845073). Assembly of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal peptide synthetases (NRPS), sidD and sidC respectively (PubMed:15953695, PubMed:17845073, PubMed:17464044). Subsequently, sidG catalyzes N2-acetylation of FsC for forming TAFC (PubMed:17845073). Both extra- and intracellular siderophores are crucial for growth during iron limitation and virulence (PubMed:16113265).
Efflux pump that provides the dual role of gliotoxin export and self-protection by allowing the fungus to evade the harmful effect of its own gliotoxin production (PubMed:15979823, PubMed:15707846, PubMed:24847038, PubMed:26150413). Moreover, it contributes also to the virulence through gliotoxin secretion (PubMed:24847038).
Expression is also under the control of the gipA transcription factor (PubMed:24784729).
Increases the susceptibility to gliotoxin (PubMed:24847038). Leads to complete deficient gliotoxin secretion but still retains the ability to efflux bisdethiobis(methylthio)gliotoxin (BmGT) (PubMed:26150413). Leads to increased survival of infected mice (PubMed:24847038).
12-alpha,13-alpha-dihydroxyfumitremorgin C prenyltransferase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities (PubMed:18683158, PubMed:23649274). The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA (PubMed:16755625). Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B (PubMed:16000710, PubMed:21105662, PubMed:23090579). The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively (PubMed:19226505). The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B (PubMed:18683158). Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties (PubMed:19763315). In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Does not affect whole genome H3K4 methylation.
H3K4 demethylase-like protein (PubMed:23638376). Might not act as a H3K4 demethylase or is not the major H3K4 demethylase since its deletion does not affect whole genome H3K4 methylation (PubMed:23638376).
Belongs to the Mediator complex subunit 12 family.
Component of the srb8-11 complex. The srb8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The srb8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex (By similarity).
Expression is up-regulated during co-cultivation of A.fumigatus with Streptomyces rapamycinicus that triggers the production of the polyketide fumigermin during the bacterial-fungal interaction.
Impairs the production of fumigermin triggered by Streptomyces rapamycinicus during the bacterial-fungal interaction.
Multidomain protein; including a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a dehydratase (DH) domain that reduces hydroxyl groups to enoyl groups; a methyltransferase (CMeT) domain responsible for the incorporation of methyl groups; a ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm.
Partially reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumigermin that inhibits germination of spores of the inducing S.rapamycinicus, and thus helps the fungus to defend resources in the shared habitat against a bacterial competitor (PubMed:32083553). The partially reducing polyketide synthase fngA alone is sufficient for the production of fumigermin (PubMed:32083553). FgnA catalyzes the condensation of 3 malonyl-CoA units to an acetyl-CoA starter, and 3 methylations to yield fumigermin (PubMed:32083553). It is remarkable that the five cluster genes including fgnA are conserved in distantly related fungi, supporting the assumption of a fumigermin cluster; it is thus possible that originally all five genes were functional, but that the genes encoding tailoring enzymes became inactive from mutations, similar to the case of the fgnA gene in strains A1163 and Af293 (Probable).
Belongs to the mitochondrion-specific ribosomal protein mS29 family.
Belongs to the acetyltransferase family.
N-acetylglutamate synthase involved in arginine biosynthesis.
Belongs to the deoxyhypusine hydroxylase family.
Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.
Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily.
Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation), facilitation of DNA opening and initiation of transcription. SAGA is required for recruitment of the basal transcription machinery. SLIK is proposed to have partly overlapping functions with SAGA.
Belongs to the methylaspartate ammonia-lyase family.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase NEP1 family.
Required for pre-18S rRNA processing. May bind microtubules.
In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
Plays a role in nonsense-mediated mRNA decay.
Heterodimer with alg13 to form a functional enzyme.
Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit alg13 to the ER (By similarity).
Belongs to the DNA polymerase type-Y family.
Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase (By similarity).
The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By similarity).
Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit.
Serine/threonine-protein kinase involved in transcription regulation. Phosphorylates the UBC2/RAD6 ubiquitin-conjugating enzyme (E2), leading to monoubiquitination of histone H2B and the silencing of telomeric-associated genes. Also required for histone H3 methylation. Necessary for the recovery from pheromone-induced growth arrest in the cell cycle G1 phase (By similarity).
Type IV dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
ABC efflux transporter that confers resistance to fluconazole (FLC) but shows no resistance to other azoles (PubMed:32209680). Is also able to transport rhodamine 6G (R-6G), a known substrate for many ABC transporters (PubMed:32209680).
Expression is highly induced in a single triazole-resistant isolate (DI16-8).
The efflux inhibitor FK506 does not impair the transport activity.
Belongs to the WD repeat IPI3/WDR18 family.
Belongs to the nucleoporin interacting component (NIC) family.
Belongs to the ribose 5-phosphate isomerase family.
Belongs to the WD repeat PROPPIN family.
Component of the PI(3,5)P2 regulatory complex.
The L/FRRG motif is essential for the cytoplasm to vacuole transport (Cvt) pathway, for the recruitment of atg8 and atg16 to the PAS in nutrient-rich medium, and for its recruitment to and dissociation from the PAS under starvation conditions.
The N-terminus might form a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2), leading to the association of the protein to the membrane.
The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Necessary for proper vacuole morphology. Plays an important role in osmotically-induced vacuole fragmentation. Required for cytoplasm to vacuole transport (Cvt) vesicle formation, pexophagy and starvation-induced autophagy. Involved in correct atg9 trafficking to the pre-autophagosomal structure. Might also be involved in premeiotic DNA replication (By similarity).
RNA-binding protein involved in post-transcriptional regulation through transcript degradation.
Exhibits a reduced copper content and leads to cell decolorization due to lower laccase activity, when ctrC is also deleted.
Expression is up-regulated by copper deficiency and decreased dramatically when the copper concentration increases (PubMed:25281782). Expression is up-regulated by the deletion of ctrC (PubMed:25281782).
Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol.
Acyl-carrier-protein synthase transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier-protein (PubMed:21195204). The 4'-phosphopantetheine (4'-PPT) portion of CoA provides the essential prosthetic group for a number of carrier proteins and multi-domain enzymes, priming them for the acceptance of acyl building blocks in fatty acid synthesis and many aspects of secondary metabolism mediated by polyketide synthases (PKSs) and non-ribosomal peptide synthetases (NRPSs) (PubMed:21195204). PptB is specific for the mitochondrial acyl carrier protein acpA (PubMed:21195204).
Essential for viability (PubMed:21195204). Leads to swollen spores in heterokaryons with a low germination rate and arrest at this stage (PubMed:21195204).
Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and ADA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation.