The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family.
Acyl-CoA dehydrogenase; part of the gene cluster that mediates the biosynthesis of aspyridones (PubMed:17369821, Ref.5). The polyketide-amino acid backbone preaspyridone A is first assembled by the PKS-NRPS hybrid apdA (PubMed:17369821, PubMed:20828130). The assembly of preaspyridone A is initiated by loading of malonyl-CoA onto apdA, followed by decarboxylation to yield the acetyl starter unit (PubMed:20828130). The growing polyketide chain then elongates into a tetraketide (PubMed:20828130). The adpA PKS module catalyzes three Claisen condensations, as well as beta-keto processing and methylation (PubMed:17369821, PubMed:20828130). Alpha-methylation step during polyketide synthesis is a prerequisite and a key checkpoint for chain transfer between PKS and NRPS modules (PubMed:25494235). The downstream NRPS module contains the condensation (C), adenylation (A), and thiolation (T) domains and catalyzes the incorporation of tyrosine via the formation of the L-tyrosinyl-thioester and the amide linkage between L-tyrosinyl-thioester and the tetraketide (PubMed:20828130). The bimodular assembly line is terminated with a reductase (R) domain that facilitates formation and release of the tetramic acid product (PubMed:20828130). Because apdA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase apdC (PubMed:17369821, PubMed:20828130, Ref.5). ApdC appears to operate with different stereoselectivity in different PKS cycle (Ref.5). Combined with apdC, apdA is proposed to synthesize preaspyridone A via about 20 enzymatic steps (PubMed:20828130). A number of oxidative steps performed successively by the cytochrome P450 monooxygenases apdE and apdB are required for the conversion of preaspyridone A to aspyridone A (PubMed:17369821). The cytochrome P450 monooxygenase apdE is responsible for the oxidative dephenylation of preaspyridone A (Ref.5). Finally, the predicted FAD-dependent monooxygenase apdD and the acyl-CoA dehydrogenase apdG may be involved in the transformation of aspyridone A into aspyridone B (PubMed:17369821) (Probable).
Belongs to the acyl-CoA dehydrogenase family.
Expression is positively regulated by the aspyridones cluster specific transcription regulator apdR (PubMed:17369821).
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.
Belongs to the eukaryotic ribosomal protein eS7 family.
Belongs to the ThrE exporter (TC 2.A.79) family.
Belongs to the UTP23/FCF1 family. FCF1 subfamily.
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).
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.
Belongs to the DNA polymerase type-X family.
DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities. Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
Belongs to the SMC family. SMC2 subfamily.
Belongs to the oligopeptide OPT transporter family.
Belongs to the quinolone epoxide rearrangement protein penF family.
Quinolone epoxide rearrangement protein; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins (PubMed:25251934, PubMed:28114276). The first stage is catalyzed by the nonribosomal pepdide synthetase asqK that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (PubMed:25251934). AsqK is also able to use anthranilic acid and L-phenylalanine as substrates to produce cyclopeptin, but at a tenfold lower rate (PubMed:25251934). 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase asqJ through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (PubMed:25251934, PubMed:26553478). AsqJ also converts its first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin (PubMed:25251934). AsqJ is a very unique dioxygenase which is capable of catalyzing radical-mediated dehydrogenation and epoxidation reactions sequentially on a 6,7-benzo-diazepinedione substrate in the 4'-methoxyviridicatin biosynthetic pathway (PubMed:25251934). AsqJ is also capable of converting cyclopeptin into dehydrocyclopeptin (PubMed:25251934). The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI (PubMed:30026518). Cyclopenin can also be converted into viridicatin by asqI (PubMed:30026518). 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase asqH1 then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase asqF to yield conjugated aryl diene (By similarity). The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase asqH2 to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain (By similarity). The FAD-dependent monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin (PubMed:30026518). Finally, after dehydratation of the epoxide at C3 by asqC, the quinolone epoxide rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring system in aspoquinolone (PubMed:30026518).
Belongs to the GMC oxidoreductase family.
Heterodimer with ALG13 to form a functional enzyme.
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.
Belongs to the class-II aminoacyl-tRNA synthetase family.
Belongs to the oxygen-dependent FAD-linked oxidoreductase family.
Belongs to the glycosyl hydrolase 3 family.
Belongs to the DNA polymerase type-Y family.
Belongs to the acetyl-CoA hydrolase/transferase family.
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 glycosyl hydrolase 16 family.
Belongs to the snRNP Sm proteins family.
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.
Belongs to the zinc-containing alcohol dehydrogenase family.
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 DNA repair enzymes AP/ExoA family.
Belongs to the isocitrate and isopropylmalate dehydrogenases 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.
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex.
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aspyridones (PubMed:17369821, Ref.5). The polyketide-amino acid backbone preaspyridone A is first assembled by the PKS-NRPS hybrid apdA (PubMed:17369821, PubMed:20828130). The assembly of preaspyridone A is initiated by loading of malonyl-CoA onto apdA, followed by decarboxylation to yield the acetyl starter unit (PubMed:20828130). The growing polyketide chain then elongates into a tetraketide (PubMed:20828130). The adpA PKS module catalyzes three Claisen condensations, as well as beta-keto processing and methylation (PubMed:17369821, PubMed:20828130). Alpha-methylation step during polyketide synthesis is a prerequisite and a key checkpoint for chain transfer between PKS and NRPS modules (PubMed:25494235). The downstream NRPS module contains the condensation (C), adenylation (A), and thiolation (T) domains and catalyzes the incorporation of tyrosine via the formation of the L-tyrosinyl-thioester and the amide linkage between L-tyrosinyl-thioester and the tetraketide (PubMed:20828130). The bimodular assembly line is terminated with a reductase (R) domain that facilitates formation and release of the tetramic acid product (PubMed:20828130). Because apdA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase apdC (PubMed:17369821, PubMed:20828130, Ref.5). ApdC appears to operate with different stereoselectivity in different PKS cycle (Ref.5). Combined with apdC, apdA is proposed to synthesize preaspyridone A via about 20 enzymatic steps (PubMed:20828130). A number of oxidative steps performed successively by the cytochrome P450 monooxygenases apdE and apdB are required for the conversion of preaspyridone A to aspyridone A (PubMed:17369821). The cytochrome P450 monooxygenase apdE is responsible for the oxidative dephenylation of preaspyridone A (Ref.5). Finally, the predicted FAD-dependent monooxygenase apdD and the acyl-CoA dehydrogenase apdG may be involved in the transformation of aspyridone A into aspyridone B (PubMed:17369821) (Probable).
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 alpha-IPM synthase/homocitrate synthase family. Homocitrate synthase LYS20/LYS21 subfamily.
Catalyzes the aldol-type condensation of 2-oxoglutarate with acetyl-CoA to yield homocitrate. Carries out the first step of the alpha-aminoadipate (AAA) lysine biosynthesis pathway.
Belongs to the eukaryotic ribosomal protein eL8 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.
Belongs to the PA-phosphatase related phosphoesterase family.
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Maintains high levels of reduced glutathione in the cytosol.
Belongs to the metallo-dependent hydrolases superfamily.
Lacks conserved residue(s) required for the propagation of feature annotation.
Belongs to the NtaA/SnaA/DszA monooxygenase 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.
Up-regulated when grown with elevated levels of potassium chloride.
May be required for cytoplasm to vacuole transport (Cvt) and pexophagy.
The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctate structures.
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 glycosyl hydrolase 5 (cellulase A) family.
Belongs to the carbon-nitrogen hydrolase superfamily. Nitrilase family.
Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
This protein has four functional calcium-binding sites.
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 lysine N-acyltransferase MbtK family.
Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
Belongs to the ABC transporter superfamily. ABCG family. PDR (TC 3.A.1.205) subfamily.
Belongs to the fungal hydrophobin family.
Impairs the synthesis of austinol and dehydroaustinol (PubMed:21658102, PubMed:22329759).
In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes (Probable). Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives (Probable).
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 (PubMed:22329759).
Non-reducing polyketide synthase; part of the gene cluster A that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725).
The release of the polyketide chain from the non-reducing polyketide synthase is mediated by the thioesterase (TE) domain localized at the C-terminus of the protein (PubMed:23368695).
Belongs to the aldehyde dehydrogenase family.
Belongs to the eukaryotic release factor 1 family.
Expression is induced by an intimate physical interaction of the fungal mycelia with the bacterium Streptomyces hygroscopicus (PubMed:19666480). Expression is repressed by VeA and MvlA via histone 3 acetylation by the SAGA/ADA complex (PubMed:23892751, PubMed:23841751).
Fails to produce F9775 A and B, but accumulates diorcinol and continues to yield orsellinic acid (PubMed:20174687).
Tyrosinase-like protein; part of the gene cluster that mediates the biosynthesis of orsellinic acid, as well as of the cathepsin K inhibitors F9775 A and F9775 B (PubMed:19666480, PubMed:20174687). The non-reducing polyketide synthase orsA produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:19666480, PubMed:20174687). Further modifications by the decarboxylase orsB and the tyrosinase-like protein orsC lead to the production of F9775 A and F9775 B (PubMed:20174687). The functions of orsD and orsE remain unclear since only orsB and orsC are required to convert orsellinic acid into F9775 A and F9775 B (PubMed:20174687).
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.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. Dihydroflavonol-4-reductase subfamily.
Belongs to the ATPase alpha/beta chains family.
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Involved in the assembly of the cytochrome c oxidase complex.
Activated by threonine and tyrosine phosphorylation.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily.
Belongs to the polysaccharide lyase 1 family.
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).
Belongs to the copper transporter (Ctr) (TC 1.A.56) family. SLC31A subfamily.
Belongs to the NmrA-type oxidoreductase family.
Belongs to the AB hydrolase superfamily. Lipase family.
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).
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.
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.
The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits.
Belongs to the acetyltransferase family. MAK3 subfamily.
Belongs to the nucleoporin Nup84/Nup107 family.
Functions as a component of the nuclear pore complex (NPC).
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
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 monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family.
Up-regulated during co-cultivation with L.plantarum.
Belongs to the metallo-beta-lactamase superfamily.
Thioesterase; part of the pkg gene cluster that mediates the biosynthesis of dihydrocitreoisocoumarin and 6,8-dihydroxy-3-(2-oxopropyl)-isocoumarin (PubMed:22510154). The non-reducing polyketide synthase pkgA performs the condensation of one acetyl-CoA starter unit with 6 and 5 malonyl-CoA units, respectively (PubMed:22510154). As pkgA lacks a releasing domain, the thioesterase pkgB is necessary to break the thioester bond and release dihydrocitreoisocoumarin and 6,8-dihydroxy-3-(2-oxopropyl)-isocoumarin from pkgA (PubMed:22510154).
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).
Asperfuranone provides anti-proliferative activity in human non-small cell lung cancer cells (PubMed:20148857).
Completely abolishes the production of asperfuranone (PubMed:19199437).
Expression is regulated by the asperfuranone cluster transcription factor afoA (PubMed:19199437).
Polyketide synthase; part of the gene cluster that mediates the biosynthesis of asperfuranone, a probable antitumor agent (PubMed:19199437). The polyketide synthase afoG is responsible for producing the 3,5-dimethyloctadienone moiety from acetyl-CoA, three malonyl-CoA, and two S-adenosyl methionines (SAM) (PubMed:19199437). The 3,5-dimethyloctadienone moiety is then loaded onto the SAT domain of afoE and extended with four malonyl-CoA and one SAM, which leads to the formation of 2,4-dihydroxy-6-(5,7-dimethyl-2-oxo-trans-3-trans-5-nonadienyl)-3-methylbenzaldehyde (compound 2) after reductive release and aldol condensation (PubMed:19199437). AfoD is the next enzyme in the biosynthesis sequence and hydroxylates the side chain at the benzylic position of compound 2 (PubMed:19199437). After benzylic hydroxylation, a furan ring is formed after five-member ring hemiacetal formation and water elimination (PubMed:19199437). AfoF and afoC are proposed to oxidize the R-diketone proton and to reduce the unconjugated carbonyl group, respectively, to generate asperfuranone (PubMed:19199437). Since no intermediates could be isolated from afoF and afoC deletants, the sequence of these two enzymes is not fully understood (PubMed:19199437). Moreover, since afoC deletant still produces a small amount of asperfuranone, other endogenous oxidoreductases might catalyze the same reaction with much less efficiency (PubMed:19199437).
Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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.
E.nidulans has two beta-tubulin genes: benA and tubC; benA is expressed during vegetative growth.
Rhizoxin, an antibiotic that exhibits potent anti-mitotic activity against most eukaryotic cells except for yeasts, binds to beta tubulin.
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.
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 SOS response-associated peptidase family.
Belongs to the bacterial ribosomal protein bL28 family.
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.
Belongs to the inositol monophosphatase superfamily.
Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Regulates the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS (By similarity). Involved in osmoadaptation.
Down-regulated when grown with elevated levels of potassium chloride.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family.
Belongs to the thiolase-like superfamily. Thiolase family.
GTPase-activating protein for the ADP ribosylation factor family.
Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.
Delta(8)-fatty-acid desaturase which introduces a double bond at the 8-position in the long-chain base (LCB) of ceramides. Required for the formation of the di-unsaturated sphingoid base (E,E)-sphinga-4,8-dienine during glucosylceramide (GluCer) biosynthesis.
Belongs to the universal ribosomal protein uS12 family.
Belongs to the CTL (choline transporter-like) family.
Probably involved in transport through the plasma membrane.
Belongs to the eIF-2B alpha/beta/delta subunits family.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
Belongs to the indoleamine 2,3-dioxygenase family.
Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.
Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein.
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 universal ribosomal protein uL13 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.
Belongs to the kinesin light chain family.
Belongs to the acetate uptake transporter (AceTr) (TC 2.A.96) family.
Exoribonuclease involved in ribosome biosynthesis. Involved in the processing of ITS1, the internal transcribed spacer localized between the 18S and 5.8S rRNAs.
Transcription factor involved in RNA polymerase II transcription regulation. May function in both SPT15/TBP post-recruitment and recruitment steps of transcription (By similarity).
Belongs to the small GTPase superfamily. Ran family.
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.
Part of the gene cluster that mediates the biosynthesis of orsellinic acid, as well as of the cathepsin K inhibitors F9775 A and F9775 B (PubMed:19666480, PubMed:20174687). The non-reducing polyketide synthase orsA produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:19666480, PubMed:20174687). Further modifications by the decarboxylase orsB and the tyrosinase-like protein orsC lead to the production of F9775 A and F9775 B (PubMed:20174687). The functions of orsD and orsE remain unclear since only orsB and orsC are required to convert orsellinic acid into F9775 A and F9775 B (PubMed:20174687).
Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
3' to 5' exoribonuclease required for proper 3' end maturation of MRP RNA and of the U5L snRNA.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
Both zinc fingers are required to induce development (PubMed:2108321).
BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (PubMed:8508769, PubMed:5366214, PubMed:2823119, PubMed:2655931, PubMed:2196567,PubMed:7704830). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (PubMed:2823119, PubMed:2655931, PubMed:2108321). Binds promoters of target genes at brlA response elements (BREs) containing the conserved sequence 5'-(C/A)(A/G)AGGG(G/A)-3' (PubMed:8417986). Controls the expression of the conidiophore-specific phenol oxidase ivoB (PubMed:1901560). Controls the expression of the hydrophobin rodA (PubMed:2065971). Mediates the developmental switch from the indeterminate, apical growth pattern of vegetative cells to the budding growth pattern of conidiophores (PubMed:3293800). Expression of brlA leads to activation of abaA, wetA and stuA, cessation of vegetative growth, cellular vacuolization and spore formation.
Expression is induced during conidiation, after conidiophore stalks had formed and had begun to vesiculate (PubMed:2823119). Positively regulated by abaA (PubMed:2655931). Negatively regulated by velC (PubMed:24587098). Expression is also controlled by acoD (PubMed:1508186).
Prevents the formation of normal conidiophores (PubMed:2823119).
Belongs to the glycosyl hydrolase 43 family.
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.
Atrochrysone carboxylic acid synthase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative (PubMed:20139316, PubMed:21351751). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG (PubMed:20139316). The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG (PubMed:20139316). The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone (PubMed:20139316). The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emodinanthrone to emodin (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751, PubMed:22909031). The short chain dehydrogenase mdpC converts the tautomers of emodin hydroquinone into the 3-hydroxy-3,4-dihydroan-thracen-1(2H)-one derivative (PubMed:22909031, PubMed:26266881). These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin (PubMed:22730213). Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps (PubMed:22730213).
Impairs the production of monodictyphenone and any of the intermediates of the pathway (PubMed:20139316, PubMed:21351751).
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).
Belongs to the acetyltransferase family. NAA40 subfamily.
Belongs to the universal ribosomal protein uL14 family.
Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
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 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.
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).
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.
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.
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.
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.
Averufin oxidase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:8643646). The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK (PubMed:8962148). The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (PubMed:8643646) (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF (PubMed:10618248). 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG (PubMed:24957370). The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme (PubMed:24957370). The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone (PubMed:10618248). The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone (PubMed:24957370). The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) (PubMed:24957370). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) (PubMed:8999832). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin (PubMed:7486998). The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin (PubMed:24957370). The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP (PubMed:8900026).
The genes forming the sterigmatocystin biosynthesis cluster are co-regulated and induced on oatmeal porridge or the fungal isolates were grown either on oatmeal porridge or in YEC medium (0.2% yeast extract, 5.0% corn steep liquor) (PubMed:8643646, PubMed:8017929). Expression is positively regulated by the cluster-specific transcription factor aflR that binds the palindromic sequence 5'-TCG(N5)CGA-3'found in the promoter (PubMed:9680223).
By ethanol and ethylacetate. Basal level and ethanol-induced expression repressed by acetate when grown on lactose. By ethyl methyl ketone (EMK). Transcriptionally regulated by transcriptional activator alcR and carbon catabolite repressor creA.
No visible phenotype. Does not affect growth on ethanol, glycerol or acetate as a sole carbon source. Does not result in phenotypes related to possible secretion of ammonia. Grows normally on media with low concentrations of ethanol. No effect when screening for allylalcohol and n-propanol toxicity. AlcA and alcS double mutant has no difference in phenotype from alcA single mutant. FacA and alcS double mutant does not differ from a single facA mutant in its ability to grow on a medium with glycerol as a carbon source either alone or in presence of ethanol.
Belongs to the protein kinase superfamily. RIO-type Ser/Thr kinase 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).
Belongs to the selenium-binding protein family.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.
Belongs to the universal ribosomal protein uL2 family.
Belongs to the xanthine dehydrogenase family.
Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
By 2-thiouric acid. Repressed by ammonium.
Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid (By similarity).
Belongs to the glycosyl hydrolase 1 family.
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.
Belongs to the universal ribosomal protein uS4 family.
Belongs to the activator 1 small subunits family.
Belongs to the type-B carboxylesterase/lipase family.
Belongs to the snRNP core protein family.
Expression is induced during co-cultivation with Streptomyces rapamycinicus.
Results in a significantly reduced expression of orsA and orsD, and in complete loss of orsellinic acid production, during response to Streptomyces rapamycinicus.
Transcription regulator that acts as a central regulatory node for the integration of external bacterial signals leading to the regulation of secondary metabolite gene clusters such as orsellinic, lecanoric acid, cichorine, 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (dba), emericellamide or microperfuranone clusters.
Belongs to the ribose 5-phosphate isomerase family.
Belongs to the CoA-transferase III family.
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CHEK2 subfamily.
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.
Deletion of the conserved eukaryotic csnE deneddylase subunit of the COP9 signalosome leading to defect in protein degradation results in the activation of the silenced dba gene cluster (PubMed:23001671). Expression is controlled by the transcription factor flbB (PubMed:25701285).
Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of the antibiotic 2,4- dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives (PubMed:23001671). Probably binds the conserved motif 5'-CT/CCG/AGA/CG/CT/A/CA/TT/A/GC-3' found in all dba cluster promoters and that shows significant similarities to the binding sites of other fungal C6 finger domain transcription factors (Probable).
Belongs to the eukaryotic ribosomal protein eL34 family.
Accumulates at about the time sterigmata appear and remains at high levels throughout the final stages of conidiophore formation and during spore differentiation and maturation.
Contributes to surface hydrophobicity, which is important for processes such as association of hyphae in reproductive structures, dispersal of aerial spores and adhesion of pathogens to host structures. Important for the formation of hydrophobic rodlet layers of asexually-produced spores.
Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family.
Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family.
Expression is strongly increased by imazalil (PubMed:9180695). Expression is also strongly increased in the presence of hygromycin and 4-nitroquinoline oxide (4-NQO) (PubMed:11872487). Curiously, expression is repressed in the presence of camptothecin, imazalil and itraconazole (PubMed:11872487).
Pleiotropic ABC efflux transporter involved in the basal level of drugs susceptibility, including antibiotics, azole fungicides and plant defense toxins.
Belongs to the chaperonin (HSP60) family.
May participate in assembly and/or disassembly of proteins imported into the mitochondrion. HSP60 are ATPases and have affinity for unfolded proteins (By similarity). Involved in osmoadaptation.
Belongs to the gamma-glutamylcyclotransferase family.
Genetic studies provided compelling evidence implicating ivoA in the biosynthesis of N-acetyl-hydroxytryptophan (Ref.3, PubMed:28108400). The proposed acetyltransferase activity of ivoA is however an unlikely fit for a single-module NRPS and further studies showed that ivoA actually catalyzes ATP-dependent unidirectional stereo-inversion of L-tryptophan to D-tryptophan (PubMed:31573806).
Impairs the production of the gray-brown conidiophore pigment and leads to 'ivory' (colorless) conidiophores (PubMed:2126551).
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. IvoA has the following mono-modular architecture: A-T-E-C.
Nonribosomal peptide synthetase; part of the pathway that mediates the biosynthesis of the gray-brown conidiophore pigment (PubMed:23617571, PubMed:28108400). The first step of the pathway is performed by the nonribosomal peptide synthetase ivoA that catalyzes ATP-dependent unidirectional stereoinversion of L-tryptophan to D-tryptophan with complete conversion (PubMed:31573806). While the stereoinversion is catalyzed by the epimerization (E) domain of ivoA, the terminal condensation (C) domain stereoselectively hydrolyzes D-tryptophanyl-S-phosphopantetheine thioester and thus represents a non-canonical C domain function (PubMed:31573806). D-tryptophan is acetylated, probably by an endogenous acetyltransferase (Probable). N-acetyltryptophan is further 6-hydroxylated into N-acetyl-6-hydroxytryptophan (AHT) by the cytochrome P450 monooxygenase ivoC (PubMed:28108400). N-acetyl-6-hydroxytryptophan is substrate of the N-acetyl-6-hydroxytryptophan oxidase ivoB to produce the gray-brown conidiophore pigment (PubMed:2126551, PubMed:28108400, Ref.3).
Belongs to the glycosyltransferase 39 family.
Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Involved in determination of the onset of polarized growth and morphogenesis. Plays a role in the regulation of branching in hyphae and spore formation.
Although strongly related to the peptide:N-glycanase enzyme, it lacks the conserved active site Cys in position 246, which is replaced by a Val residue suggesting that it has no activity.
Belongs to the transglutaminase-like superfamily. PNGase family.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
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).
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 cytochrome c oxidase VIIc family.
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.
Probably involved in transcription regulation via its interaction with the INO80 complex, a chromatin remodeling complex.
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 (By similarity). Phosphorylated by pbsB in response to osmotic and oxidative stresses.
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.
The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Belongs to the phospholipid scramblase family.
Belongs to the ribose-phosphate pyrophosphokinase family.
Belongs to the glycosyltransferase 32 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.
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
[Alpha(6)beta(6)] hexamers of two multifunctional subunits (alpha and beta).
Belongs to the protein-tyrosine phosphatase family. Non-receptor class CDC14 subfamily.
Protein phosphatase which antagonizes mitotic cyclin-dependent kinase nimX, the inactivation of which is essential for exit from mitosis. To access its substrates, is released from nucleolar sequestration during mitosis. Plays an essential in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint. Involved in chromosome segregation, where it is required for meiosis I spindle dissambly as well as for establishing two consecutive chromosome segregation phases (By similarity). Required for the transcription of the two major endoglucanase genes eglA and eglB and growth on synthetic cellulose as the sole carbon source.
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 ammonia transporter channel (TC 1.A.11.2) family.
Belongs to the glycosyl hydrolase 28 family.
Belongs to the tRNA pseudouridine synthase TruA family.
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.
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.
Transcription factor that regulates specifically the 4'-methoxyviridicatin/aspoquinolone biosynthesis cluster (PubMed:25251934).
Belongs to the multicopper oxidase family.
Required for the conversion of the yellow polyketide pigment synthesized by wA to the conidial green pigment.
Specifically expressed late during asexual development.
Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
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.
Induced by transcription factor stuA upon carbon starvation and during early sexual development.
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.
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 chloride channel (TC 2.A.49) family.
Belongs to the CND3 (condensin subunit 3) 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 AB hydrolase superfamily. LDAH family.
Belongs to the carotenoid oxygenase family.
Belongs to the GHMP kinase family. Mevalonate kinase subfamily.
Negative regulator of mitosis in E.nidulans. This protein is part of a regulatory pathway that includes the nimA protein kinase. It is required to prevent premature entry into mitosis. Mutations to this protein both cause cells to enter mitosis and prevent them from leaving mitosis.
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.
In the N-terminal section; belongs to the MoaB/Mog family.
Belongs to the sirtuin family. Class I subfamily.
NAD-dependent histone deacetylase, which could function in telomeric silencing, cell cycle progression and chromosome stability.
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.
Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a ternary complex with MutL alpha (MLH1-PMS1).
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. Active against linseed rhamnogalacturonan.
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Belongs to the SNF2/RAD54 helicase family.
Component of the NuA4 histone acetyltransferase complex.
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 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 concentrative nucleoside transporter (CNT) (TC 2.A.41) family.
Belongs to the universal ribosomal protein uS3 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.
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.
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).
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.
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.
Belongs to the glycosyl hydrolase 18 family. Chitinase class V subfamily.
Essential protein which may be involved in threonine biosynthesis.
Required for pre-18S rRNA processing. May bind microtubules.
The GINS complex plays an essential role in the initiation of DNA replication.
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 class-I pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the trans-sulfuration enzymes family.
Belongs to the ubiquitin-activating E1 family. ULA1 subfamily.
Regulatory subunit of the dimeric UBA3-ULA1 E1 enzyme.
Belongs to the arylamine N-acetyltransferase 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 sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:8643646, PubMed:10618248). The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK (PubMed:8962148). The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (PubMed:8643646) (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF (PubMed:10618248). 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG (PubMed:24957370). The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme (PubMed:24957370). The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone (PubMed:10618248). The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone (PubMed:24957370). The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) (PubMed:24957370). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) (PubMed:8999832). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin (PubMed:7486998). The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin (PubMed:24957370). The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP (PubMed:8900026).
Impairs the production of sterigmatocystin and leads to the accumulation of averantin.
Involved in regulation of nuclear migration. May be involved in regulating nuclear positioning.
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
Belongs to the nucleoporin interacting component (NIC) family.
Belongs to the peptidase C2 family. PalB/RIM13 subfamily.
Required for the proteolytic cleavage of the transcription factor pacC in response to alkaline ambient pH. Probably is the signaling protease that mediates the first proteolytic cleavage within the signaling protease box of pacC, yielding the 53 kDa 'open' conformation intermediate protein, which is committed to further processing. Required for virulence in invasive pulmonary aspergillosis (IPA).
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.
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).
Involved in ribosomal large subunit assembly.
Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 2 subfamily.
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 purine-cytosine permease (2.A.39) family.
Belongs to the glycosyl hydrolase 76 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 acyl carrier protein (ACP) family.
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
ABC transporter; part of the gene cluster that mediates the biosynthesis of aspercryptins, linear lipopeptides built from six amino acids including 2 highly unusual and nonproteogenic amino acids, 2-amino-octanoic acid (2aoa) and 2-amino-dodecanol (2adol) (PubMed:23248299, PubMed:27310134, PubMed:26563584).
Belongs to the ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily.
Does not alter the yield of aspercryptin significantly (PubMed:26563584).
Expression is positively regulated by the aspercryptin cluser-specific transcription factor atnN (PubMed:27310134).
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.
Belongs to the 2-oxoacid dehydrogenase family.
Belongs to the prefoldin subunit alpha family.
Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. UbiG/COQ3 family.
Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9.
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Belongs to the inositol phosphokinase (IPK) family.
Belongs to the pseudouridine synthase TruB family.
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.
Component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs).
Required for proper 27S pre-rRNA processing and 60S ribosome subunit assembly.
Belongs to the aconitase/IPM isomerase family.
May act as a negative regulator of salt tolerance.
Belongs to the glycosyl hydrolase 10 (cellulase F) family.
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. Involved in the degradation of complex natural cellulosic substrates.
Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:8643646). The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK (PubMed:8962148). The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (PubMed:8643646) (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF (PubMed:10618248). 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG (PubMed:24957370). The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme (PubMed:24957370). The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone (PubMed:10618248). The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone (PubMed:24957370). The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) (PubMed:24957370). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) (PubMed:8999832). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin (PubMed:7486998). The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin (PubMed:24957370). The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP (PubMed:8900026).
Highly reducing polyketide synthase; part of the pkh gene cluster that mediates the biosynthesis of 2,4-dihydroxy-6-[(3E,5E,7E)-2-oxonona-3,5,7-trienyl]benzaldehyde (PubMed:22510154). The highly reducing polyketide synthase pkhB first produces the (2E,4E,6E)-octa-2,4,6-trienyl strater unit for the non-reducing polyketide synthase pkhA (PubMed:22510154). This octatrienoyl starter is then loaded onto the SAT domain of the NR-PKS pkhA to be condensed with 4 malonyl-CoA units to yield 2,4-dihydroxy-6-[(3E,5E,7E)-2-oxonona-3,5,7-trienyl]benzaldehyde (PubMed:22510154).
Multidomain protein; including an N-terminal starter unit:ACP transacylase (SAT) domain, a beta-ketoacyl synthase (KS) domain, a malonyl-CoA:ACP transacylase (MAT) domain, a product template (PT) domain that controls the immediate cyclization regioselectivity of the reactive polyketide backbone, an acyl carrier protein (ACP) domain, and a reductive NADPH-binding domain that is required for NADPH-dependent product release.
In the C-terminal section; belongs to the anthranilate synthase component I 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).
Octamer of two non-identical subunits IDH1 and IDH2.
Belongs to the mitochondrial carrier (TC 2.A.29) family.
Belongs to the iron/ascorbate-dependent oxidoreductase family.
Catalyzes the ferrous insertion into protoporphyrin IX.
Belongs to the serine/threonine dehydratase family.
Dually phosphorylated on Thr-171 and Tyr-173, which activates the enzyme.
Mitogen-activated protein kinase required for growth on media where sorbitol or mannitol is the sole carbon source.
Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
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.
By phenylacetate (PhoAc), 2OH-PhoAc, 3OH-PhoAc, 4OH-PhoAc, phenylalanine, and tyrosine. Not induced by acetate or glutamate. Expression is partially repressed by glucose.
Disruption of the fahA gene results in phenylalanine toxicity, secretion of succinylacetone and the absence of growth. This is analogous to the genetic disease, type I hereditary tyrosinemia in humans.
Use of phenylalanine and phenylacetate as a carbon source.
Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.
Expression is induced by nicotinate and 6-OH nicotinate, subject to nitrogen metabolite repression mediated by the GATA factor areA, and strictly regulated by the cluster-specific transcription regulator hnxR (PubMed:29212709).
Flavin oxidoreductase, part of the hnx cluster involved in the purine degradation (PubMed:29212709). The nicotinate hydroxylase hnxS accepts nicotinate as a substrate and catalyzes the first step of nicotinate catabolism (PubMed:29212709). The major facilitator-type transporters hxnP and hxnZ are probably involved in the uptake of nicotinate-derived metabolites, and the oxidoreductases hxnT and hxnY in the further metabolism of 6-OH nicotinic acid (PubMed:29212709).
Belongs to the complex I 30 kDa subunit family.
Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of emericellamides, secondary metabolites acting as antibiotics (PubMed:18559263). The biosynthesis of emericellamides initiates from the highly reducing polyketide synthase easB which catalyzes the formation of the linear polyketide chain (PubMed:18559263). EasB produces several polyketides that can be further processed by the downstream enzymes (PubMed:18559263). The polyketides are released from easB as linear polyketide carboxylic acids, which are converted to CoA thioesters by the acyl-CoA ligase easD (PubMed:18559263). The substrates are then loaded onto the acyltransferase easC, which shuttles them to the first thiolation (T) domain of the nonribosomal peptide synthetase easA (PubMed:18559263). EasA then performs condensation of the polyketides with one glycine, two alanine, one valine and one leucine residues (PubMed:18559263). A last step of cyclization leads to the production of emericellamides (PubMed:18559263).
Belongs to the ATP-dependent AMP-binding enzyme family.
Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity.
Impairs the production of emerecellamide A, C, D, E and F (PubMed:18559263).
Belongs to the peptidase M67A family. CSN6 subfamily.
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 (By similarity). The CSN complex seems to link protein degradation to sexual development.
Component of the COP9 signalosome (CSN) complex.
Belongs to the tryptophan dimethylallyltransferase family.
Prenyltransferase; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins (PubMed:25251934). The first stage is catalyzed by the nonribosomal pepdide synthetase asqK that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (PubMed:25251934). AsqK is also able to use anthranilic acid and L-phenylalanine as substrates to produce cyclopeptin, but at a tenfold lower rate (PubMed:25251934). 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase asqJ through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (PubMed:25251934, PubMed:26553478). AsqJ also converts its first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin (PubMed:25251934). AsqJ is a very unique dioxygenase which is capable of catalyzing radical-mediated dehydrogenation and epoxidation reactions sequentially on a 6,7-benzo-diazepinedione substrate in the 4'-methoxyviridicatin biosynthetic pathway (PubMed:25251934). AsqJ is also capable of converting cyclopeptin into dehydrocyclopeptin (PubMed:25251934). The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI (PubMed:30026518). Cyclopenin can also be converted into viridicatin by asqI (PubMed:30026518). 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase asqH1 then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase asqF to yield conjugated aryl diene (By similarity). The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase asqH2 to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain (By similarity). The FAD-dependent monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin (PubMed:30026518). Finally, after dehydratation of the epoxide at C3 by asqC, the quinolone epoxide rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring system in aspoquinolone (PubMed:30026518).
Belongs to the PDK/BCKDK protein kinase 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. In the complex, it is required to stimulate activity of mtHSP70 (SSC1/sscA) (By similarity).
Heterodimer with PAM16/pamP. 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.
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. Active on laminarin and lichenan.
Most highly regulated expression during conidiation.
Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes.
Regulates also the sphingolipid metabolism.
Belongs to the NUP186/NUP192/NUP205 family.
Belongs to the EF-1-beta/EF-1-delta family.
Belongs to the transferase hexapeptide repeat family.
Belongs to the prefoldin subunit beta 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).
Belongs to the glycosyltransferase 4 family.
Required for asexual sporulation and normal colony development. May be involved in brlA activation. Could play a regulatory role in controlling the flug-initiated signal transduction pathway that triggers the asexual reproduction.
The fungal-differentiation regulator (Fungal-DR) domain is only found in fungal regulator of G-protein signaling (RGS) proteins that regulate differentiation pathways. It is required for function (By similarity).
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 peptidase M28 family. M28B subfamily.
Belongs to the cyclin family. Cyclin C 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 phosphoenolpyruvate carboxykinase (ATP) family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
Belongs to the radical SAM superfamily. Biotin synthase family.
Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.
Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Biotin synthase; part of the cluster involved in the biosynthesis of biotin (also known as vitamin B8 or vitamin H), a water-soluble vitamin that functions as a prosthetic group of many carboxylases, such as acetyl-CoA carboxylase and pyruvate carboxylase (PubMed:20713166). Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism (By similarity).
Expression is increased when transferring biotin auxotrophic mutant mycelia from biotin-supplemented medium to biotin-deficient medium.
Belongs to the dihydroxyacetone kinase (DAK) family.
Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde.
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 polysaccharide monooxygenase AA13 family.
Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation.
Probable adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
Required for the assembly of cytochrome c oxidase.
Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
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 (By similarity). The CSN complex seems to link protein degradation to sexual development. Required for fruit body formation.
Highly expressed on medium lacking a nitrogen, carbon or sulfur source.
Secreted alkaline protease that allows assimilation of proteinaceous substrates.
Belongs to the class-I aminoacyl-tRNA synthetase family.
Belongs to the TPT transporter family. SLC35D subfamily.
Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen.
Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family. Azg-like subfamily.
Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
Belongs to the class I-like SAM-binding methyltransferase superfamily.
Impairs the synthesis of austinol and dehydroaustinol (PubMed:22329759).
In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives.
Methyltransferase; part of the gene cluster A that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725).
Belongs to the iron-containing alcohol dehydrogenase family. Hydroxyacid-oxoacid transhydrogenase subfamily.
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.
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).
Belongs to the eukaryotic/archaeal RNase P protein component 3 family.
Belongs to the cyclophilin-type PPIase family. PPIL3 subfamily.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit.
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.
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 major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family.
Deletion of the conserved eukaryotic csnE deneddylase subunit of the COP9 signalosome leading to defect in protein degradation results in the activation of the silenced dba gene cluster (PubMed:23001671). Expression is positively regulated by the dba cluster specific transcription factor dbaA (PubMed:23001671). Expression is also controlled by the transcription factor flbB (PubMed:25701285).
MFS-type transporter; part of the gene cluster that mediates the biosynthesis of the antibiotic 2,4- dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives (PubMed:23001671). Is probably involved in the transport of the metabolites to the environment (Probable).
Strongly reduces the production of yellow pigmentation.
Belongs to the diacylglycerol acyltransferase family.
Belongs to the triosephosphate isomerase family.
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 intradiol ring-cleavage dioxygenase family.
Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine.
Belongs to the DASH complex DAD3 family.
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.
Belongs to the eukaryotic ribosomal protein eL21 family.
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).
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.
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).
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 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 (By similarity).
Belongs to the DNA polymerase alpha subunit B family.
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).
Belongs to the DNA polymerase epsilon subunit B family.
Belongs to the DNA photolyase class-1 family.
Forms a one-to-one complex with ATPase to inhibit the enzyme activity completely.
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.
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 class-II aminoacyl-tRNA synthetase family. Alax-L subfamily.
Required for respiratory activity and maintenance and expression of the mitochondrial genome.
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.
Activated by C-terminal proteolytic cleavage. At neutral to alkaline ambient pH, the signaling protease (probably palB) cleaves pacC within the conserved 24-residue signaling protease box, removing the C-terminal interacting region C and producing a 53 kDa 'open' conformation intermediate protein, which is committed to further processing. In an ambient pH-independent reaction, the processing protease (probably the proteasome) removes additional C-terminal residues to yield the 27 kDa functional form.
Binds to DNA. Interacts with palA, which binds to the two YPX[LI] motifs and is required for proteolytic processing.
Interacting regions A, B and C form intramolecular interactions in the full-length translation product at acidic ambient pH, keeping the protein in a 'closed' conformation preventing proteolytic cleavage by the processing protease.
Met-5 is the major initiator, but Met-1 may also be used.
Only zinc fingers 2 and 3 contact DNA. Zinc finger 1 interacts with zinc finger 2.
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. Specifically recognizes and binds the consensus sequence 5'-GCCARG-3'. Required for virulence in invasive pulmonary aspergillosis (IPA).
Belongs to the Mediator complex subunit 19 family.
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 FPP/GGPP synthase family.
Expression is positively regulated by the cluster-specific transcription factor pbcR.
Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) (PubMed:22506079, PubMed:27098256). Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors (PubMed:22506079, PubMed:27098256). The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes (PubMed:22506079, PubMed:27098256). Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene (PubMed:22506079, PubMed:27098256). The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable).
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.
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. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.
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.
Belongs to the DNA polymerase type-B family.
Belongs to the DNA mismatch repair MutL/HexB family.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.
Impairs the production of terrequinone A (PubMed:18029206).
Indole prenyltransferase; part of the gene cluster that mediates the biosynthesis of terrequinone A, an antitumor agent (PubMed:17704773, PubMed:16426969, PubMed:17291795, PubMed:22083274). The first step in the biosynthetic pathway for terrequinone A is formation of indole pyruvic acid (IPA) from L-tryptophan by the aminotransferase tdiD (PubMed:17704773). The nonribosomal peptide synthase tdiA then immediately converts unstable IPA to didemethylasterriquinone D (DDAQ D), via condensation of 2 IPA molecules (PubMed:17704773). The symmetric connectivity of the 2 IPA molecules is thought to arise by head-to-tail dual Claisen condensations facilitated by the TE domain (PubMed:17704773). TdiB then catalyzes reverse prenylation by transferring dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to yield asterriquinone C-1 (PubMed:18029206). Finally, tdiC and tdiE enzymes robustly convert asterriquinone C-1 to terrequinone A via a transformation involving regular prenylation at carbon atom 5, which requires elimination of the hydroxy group on C-5 (PubMed:17704773, PubMed:18029206).
Specifically expressed at both asexual stages (PubMed:26773375). Expression is positively regulated by the secondary metabolism regulator laeA (PubMed:16426969, PubMed:17291795). Expression is also positively regulated by mpkB (PubMed:18378656). Expression is also positively regulated by mtfA (PubMed:24066102).
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 ndc80, nuf2, spc24 and spc25.
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.
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PDPK1 subfamily.
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.
Acetate induction mediated by facB regulatory gene and probably by amdA regulatory gene. Omega amino acid induction is dependent on amdR regulatory gene.
Allows acetamide to be used as a sole carbon or nitrogen source.
Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine (By similarity).
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 glycosyl hydrolase 13 family.
Associates with DNA double-strand breaks.
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.
Mitochondrial transporter that mediates uptake of thiamine pyrophosphate (ThPP) into mitochondria.
Belongs to the GTP cyclohydrolase I type 2/NIF3 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 (By similarity).
TFIIA is a heterodimer composed of the large toa1 and the small toa2 subunits.
Belongs to the PIGG/PIGN/PIGO family. PIGO subfamily.
Abolishes the production of ent-pimara-8(14),15-diene (PD).
Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) (PubMed:22506079, PubMed:27098256). Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors (PubMed:22506079, PubMed:27098256). The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes (PubMed:22506079, PubMed:27098256). Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene (PubMed:22506079, PubMed:27098256). The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable).
The DEXXE A-type cyclization motif at positions 664-668 is responsible for the formation of ent-kaurene.
The DXDD B-type cyclization motif at positions 328-331 is responsible for the formation of ent-CDP.
The VYDTAW motif is widely conserved among diterpene cyclases in plants and fungi.
Belongs to the ATP-dependent DNA ligase family.
Allopurinol inhibits catalytic activity in a linear fashion (PubMed:363427).
Expression is induced by nicotinate and 6-OH nicotinate, subject to nitrogen metabolite repression mediated by the GATA factor areA, and strictly regulated by the cluster-specific transcription regulator hnxR (PubMed:4581274, PubMed:29212709).
Nicotinate hydroxylase, part of the hnx cluster involved in the purine degradation (PubMed:4581274). The nicotinate hydroxylase hnxS accepts nicotinate as a substrate and catalyzes the first step of nicotinate catabolism (PubMed:4581274). HnxS accepts also hypoxanthine, but not xanthine, as a substrate (PubMed:4581274, PubMed:363427, PubMed:29212709). The major facilitator-type transporters hxnP and hxnZ are probably involved in the uptake of nicotinate-derived metabolites, and the oxidoreductases hxnT and hxnY in the further metabolism of 6-OH nicotinic acid (PubMed:4581274).
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.
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 amino acid/polyamine transporter 2 family.
Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
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 (By similarity).
Component of the HAT-B complex composed of at least hat1 and hat2. The HAT-B complex binds to histone H4 tail.
Belongs to the glucose-6-phosphate 1-epimerase family.
Belongs to the paxM FAD-dependent monooxygenase family.
Completely abolishes the production of asperfuranone (PubMed:19199437). Produces a large amount of intermediates including 2,4-dihydroxy-6-(5,7-dimethyl-2-oxo-trans-3-trans-5-nonadienyl)-3-methylbenzaldehyde (PubMed:19199437).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of asperfuranone, a probable antitumor agent (PubMed:19199437). The polyketide synthase afoG is responsible for producing the 3,5-dimethyloctadienone moiety from acetyl-CoA, three malonyl-CoA, and two S-adenosyl methionines (SAM) (PubMed:19199437). The 3,5-dimethyloctadienone moiety is then loaded onto the SAT domain of afoE and extended with four malonyl-CoA and one SAM, which leads to the formation of 2,4-dihydroxy-6-(5,7-dimethyl-2-oxo-trans-3-trans-5-nonadienyl)-3-methylbenzaldehyde (compound 2) after reductive release and aldol condensation (PubMed:19199437). AfoD is the next enzyme in the biosynthesis sequence and hydroxylates the side chain at the benzylic position of compound 2 (PubMed:19199437). After benzylic hydroxylation, a furan ring is formed after five-member ring hemiacetal formation and water elimination (PubMed:19199437). AfoF and afoC are proposed to oxidize the R-diketone proton and to reduce the unconjugated carbonyl group, respectively, to generate asperfuranone (PubMed:19199437). Since no intermediates could be isolated from afoF and afoC deletants, the sequence of these two enzymes is not fully understood (PubMed:19199437). Moreover, since afoC deletant still produces a small amount of asperfuranone, other endogenous oxidoreductases might catalyze the same reaction with much less efficiency (PubMed:19199437).
Belongs to the Mediator complex subunit 6 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).
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 polysaccharide lyase 3 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).
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 FAD-dependent glycerol-3-phosphate dehydrogenase family.
Belongs to the group II decarboxylase 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.
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.
Transcription activation of genes for enzymes and proteins of quinate metabolism by binding to a 16 base-pair sequence (consensus 5'-GGATAANNNNTTATCC-3') in front of each qut gene.
Belongs to the DDOST 48 kDa subunit family.
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).
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 AB hydrolase superfamily. MetX family.
Transfers a succinyl group from succinyl-CoA to L-serine, forming succinyl-L-serine. Has also weak serine acetyl transferase activity and homoserine succinyl transferase activity.
Belongs to the cyclophilin-type PPIase family. PPIase B subfamily.
Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment.
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).
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.
In the C-terminal section; belongs to the AIR carboxylase family. Class I subfamily.
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.
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.
Belongs to the lcsJ thioesterase family.
Part of the gene cluster that mediates the biosynthesis of aspercryptins, linear lipopeptides built from six amino acids including 2 highly unusual and nonproteogenic amino acids, 2-amino-octanoic acid (2aoa) and 2-amino-dodecanol (2adol) (PubMed:23248299, PubMed:27310134, PubMed:26563584). The core structure of aspercryptins is as follows: Ser/Ala-Thr-Ile/Val-2aoa-Asn-2adol (PubMed:27310134). The first step of aspercryptin biosynthesis is the generation of the fatty acid precursors, octanoic and dodecanoic acids, by the FAS subunits atnF and atnM (PubMed:27310134, PubMed:26563584). The fatty acid precursors are likely transformed into the corresponding alpha-amino fatty acids in three steps (PubMed:27310134, PubMed:26563584). First, they are hydroxylated by the cytochrome P450 monooxygenase atnE, then oxidized to the corresponding alpha-keto acids by the NAD(P)-dependent oxidoreductase atnD, and finally converted to the alpha-amino fatty acids by the PLP-dependent aminotransferases atnH or atnJ (PubMed:27310134, PubMed:26563584). the alpha-amino fatty acids, 2-amino-octanoic and 2-amino-dodecanoic acids, are recognized, activated, and covalently tethered to the NRPS atnA by its fourth and sixth adenylation domains (PubMed:27310134). The second module of atnA is the Thr module and contains an epimerase (E) domain responsible for the epimerization of Thr to D-allo-Thr (PubMed:26563584). Additionally, despite atnA having only one epimerase domain, the first amino acid of aspercryptin A1 is D-Ser, suggesting that serine is either loaded directly as D-Ser on the first module or that the epimerase domain in the threonine module epimerizes both L-Ser and L-Thr (PubMed:27310134). After condensation of the hexapeptide of aspercryptin, the C-terminal reductase (TE) domain might be involved in the reductive release and production of the aldehyde hexapeptide (PubMed:26563584). Further reduction would generate aspercryptins (PubMed:27310134, PubMed:26563584). The variety of aspercryptins produced reflects the flexibiliy of the atnA NRPS, allowing incorporation of alanine instead of serine, valine for isoleucine, and a C10 fatty amino alcohol instead of the C12 version (PubMed:27310134). AtnB seems to be involved in the selectivity for Ile versus Val by the third module (PubMed:26563584). Moreover, type B, C and D aspercryptins have an additional N-terminal cichorine, acetyl and propionyl group respectively (PubMed:27310134).
Didemethylasterriquinone D synthetase; part of the gene cluster that mediates the biosynthesis of terrequinone A, an antitumor agent (PubMed:17704773, PubMed:16426969, PubMed:17291795, PubMed:22083274). The first step in the biosynthetic pathway for terrequinone A is formation of indole pyruvic acid (IPA) from L-tryptophan by the aminotransferase tdiD (PubMed:17704773). The nonribosomal peptide synthase tdiA then immediately converts unstable IPA to didemethylasterriquinone D (DDAQ D), via condensation of 2 IPA molecules (PubMed:17704773). The symmetric connectivity of the 2 IPA molecules is thought to arise by head-to-tail dual Claisen condensations facilitated by the TE domain (PubMed:17704773). TdiB then catalyzes reverse prenylation by transferring dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to yield asterriquinone C-1 (PubMed:18029206). Finally, tdiC and tdiE enzymes robustly convert asterriquinone C-1 to terrequinone A via a transformation involving regular prenylation at carbon atom 5, which requires elimination of the hydroxy group on C-5 (PubMed:17704773, PubMed:18029206).
Belongs to the glycosyl hydrolase 26 family.
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Belongs to the spermidine/spermine synthase family.
Catalyzes the intermembrane transfer of phosphatidylglycerol and phosphatidylinositol.
May be involved in vacuolar sorting and osmoregulation.
Belongs to the FAD-binding monooxygenase family.
FAD-binding monooxygenase; part of the gene cluster A that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725).
Impairs the synthesis of austinol and dehydroaustinol and accumulates the intermediate compound protoaustinoid A (PubMed:22329759).
Belongs to the phosphoglycerate kinase family.
An increase in fruity aroma was organoleptically detected in the wine produced by the recombinant wine yeast strain T73 expressing xnlA.
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.
Expressed in the presence of D-xylose under conditions of alkaline ambient pH, probably under the regulation of the pacC transcription factor. Repressed in presence of glucose through the action of the creA transcription repressor.
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 regulate activity of mtHSP70 (SSC1/sscA) via its interaction with PAM18/TIM14. May act by positioning PAM18/pamR in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation (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-like region, although related to the J domain does not stimulate ATPase activity of mtHSP70. It nevertheless mediates the heterodimerization with the J domain of PAM18 and is therefore essential for PAM complex function (By similarity).
Belongs to the chitin synthase family. Class II subfamily.
Belongs to the glycosyl hydrolase 25 family.
Belongs to the terpene cyclase/mutase family.
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.
Belongs to the homogentisate dioxygenase family.
During growth with phenylacetate and phenylalanine.
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).
Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:16844780, PubMed:22238011, PubMed:28124733). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:22238011, PubMed:28124733). Also degrades suberin, a specialized macromolecule found in the cell wall of various plant tissues (By similarity).
Induced during growth on cutin, in a manner dependent on transcription factors FarA and FARB (PubMed:30863878). Induced during growth on olive oil (PubMed:30863878, PubMed:22238011). Not induced during growth on the lipidic carbon sources 16-hydroxyhexadecanoic acid and propyl ricinoleate (synthetic cutin monomers), or triacetin and triesterate (triglycerides) (PubMed:30863878). Repressed during growth on glucose and on starch (PubMed:30863878, PubMed:22238011).
May be exploited in the production of biodiesel.
Partially inhibited by the serine protease inhibitor phenylmethanesulfonyl fluoride (PubMed:28124733). Inhibited by various ions, including copper, iron, sodium, potassium, magnesium and calcium (PubMed:28124733). Inhibited by the chelating agent EDTA (ethylenediaminetetraacetic acid) (PubMed:28124733). Inhibited by the surfactants sodium dodecyl sulfate and polysorbate 80 (PubMed:28124733).
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 ALG6/ALG8 glucosyltransferase family.
Belongs to the Mediator complex subunit 12 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 (By similarity).
Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan.
Cell wall protein involved in development of asexual structures such as phialide and conidium development, and thus required for spore formation (PubMed:14599891). Plays a role as a general stress protectant produced by the fungus in competition with antagonistic bacteria (By similarity).
Expression is highly induced by the V-ATPase inhibitor bafilomycin B1 and by oncanamycin A (PubMed:10376827, PubMed:12207217). The promoter contains two abaA ATTS DNA binding motifs (PubMed:14599891).
Leads to reduced sporulation and division of phialides instead of forming a single flask-shaped cell.
Mainly present in phialides and conidia.
RNA-binding nucleolar protein required for pre-rRNA processing. Involved in production of 18S rRNA and assembly of small ribosomal subunit.
Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.
Probable sequencing error places a 'ESWIKTV' sequence at a wrong position.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.
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).
Belongs to the adaptor complexes small subunit family.
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).
Belongs to the ubiquitin-conjugating enzyme family.
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.
E.nidulans has two beta-tubulin genes: benA and tubC; tubC is expressed exclusively during the events of asexual sporulation (conidiation).
Belongs to the protein-tyrosine phosphatase family.
Belongs to the palmitoyl-protein thioesterase family.
Belongs to the band 7/mec-2 family. Flotillin subfamily.
Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus.
Abolishes the production of aspernidine A, but accumulates the intermediate aspernidine E.
Dehydrogenase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone (PubMed:23706169). The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non-reducing polyketide synthase pkfA (PubMed:22510154). Hydroxylation, methylation of one of the phenol groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E (PubMed:23706169). The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable).
Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini.
Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits.
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.
Required for the proteolytic cleavage of the transcription factor pacC in response to alkaline ambient pH. Might be a pH sensor.
Belongs to the replication factor A protein 2 family.
Belongs to the eukaryotic ribosomal protein eL33 family.
Involved in nucleolar processing of pre-18S ribosomal RNA.
Belongs to the eukaryotic ribosomal protein eS17 family.
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.
Migration on a 2D-gel is shifted by co-cultivation with L.plantarum.
Belongs to the cysteine synthase/cystathionine beta-synthase family.
Putative cysteine synthase that catalyzes the conversion of O-acetyl-L-serine (OAS) into cysteine, the last step in the cysteine biosynthesis pathway. However, in contrast to cysteine synthase cysB, this CS-like protein seems not to function in cysteine biosynthesis.
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.
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 AB hydrolase superfamily.
Demethylates proteins that have been reversibly carboxymethylated. Demethylates the phosphatase PP2A catalytic subunit (By similarity).
Belongs to the C/M/P thioester hydrolase family.
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Esterase; part of the inp gene cluster that mediates the biosynthesis of fellutamide B, a mycotoxin that acts as a proteasome inhibitor (PubMed:20952652, PubMed:27294372). In the first step of fellutabmide B biosynthesis inpC activates 3-hydroxydodecanoic acid to generate 3-hydroxydodecanoyl-AMP that is then loaded onto the T0 domain of inpB (PubMed:27294372). The 3-hydroxydodecanoyl-S-phosphopantetheinyl-T0 is sequentially extended with L-Asn and L-Gln by the two CAT modules of inpB (PubMed:27294372). The linear lipodipeptide from inpB is then transferred onto inpA for the addition of the third amino acid, L-Leu (PubMed:27294372). Reductive releasing of the lipotripeptide by the TE domain of inpA produces (2S)-fellutamide B (PubMed:27294372). InpF might be involved in the release and transfer of the lipodipeptide from inpB to inpA (PubMed:27294372). The inp cluster-encoded proteasome subunit inpE confers resistance to internally produced fellutamides (PubMed:27294372). The MFS efflux transporter inpD may contribute to fellutamide resistance as well (PubMed:27294372).
Greatly diminishes the production of fellutamides (PubMed:27294372).
Belongs to the glycosyltransferase 48 family.
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 trichodiene synthase family.
Belongs to the histone deacetylase family. HD type 2 subfamily.
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events.
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 sphingosine N-acyltransferase family.
In the C-terminal section; belongs to the MoaC family.
In the N-terminal section; belongs to the radical SAM superfamily. MoaA family.
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.
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 transient receptor potential (TRP) ion channel 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.
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.
Belongs to the actin-binding proteins ADF family. GMF subfamily.
Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
Expression is inhibited by PKA activity but is not subject to glucose repression (PubMed:16376592). Not expressed in dormant conidia but only during germination (PubMed:16376592, PubMed:17703972).
No visible phenotype. The double deletion of cetA and calA results in cell wall defects and lyse during germination, leading to the inhibition of germination (PubMed:17703972).
Secreted thaumatin-like protein that, with cetA, plays an essential role in early conidial germination with a possible role in cell wall remodeling (PubMed:17703972).
Belongs to the peroxisomal membrane protein PXMP2/4 family.
Belongs to the copper/topaquinone oxidase family.
Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
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.
Belongs to the PPP phosphatase family. PP-1 subfamily.
Plays an important role in the control of mitosis by reversing the action of the nimA kinase.
Belongs to the major facilitator superfamily. Proton-dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
Belongs to the DASH complex DAD2 family.
Alpha-ketoglutarate-dependent xanthine dioxygenase is a non-heme mononuclear Fe(2+) enzyme that decarboxylates alpha-ketoglutarate to succinate and CO(2) while hydroxylating xanthine to generate uric acid (PubMed:15948966, PubMed:17429948, PubMed:18036331). Allows xanthine utilization as a nitrogen source (PubMed:15948966). Whereas xanA is highly specific for xanthine, alpha-ketoadipic acid can replace alpha-ketoglutarate as a cosubstrate (PubMed:17429948). Exhibits ferroxidase activity in the absence of substrates (PubMed:18036331).
Cu(2+) and Zn(2+) completely inhibit the xanthine dioxygenase activity, whereas Co(2+), Mn(2+), and Ni(2+) partially inhibit the activity. The inactive metal ions are presumed to compete for the Fe(2+)-binding site (PubMed:17429948). N-oxalylglycine (NOG), a known inhibitor of several Fe(2+)/alpha-ketoglutarate-dependent dioxygenase family members, competes with alpha-ketoglutarate and provides a Ki of 0.12 uM for inhibition (PubMed:17429948). 6,8-dihydroxypurine acts as a slow-binding competitive inhibitor (PubMed:18036331). The thiol-specific inhibitors 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) and iodoacetamide, inhibit also the catalytic activity (PubMed:18036331).
Expression is induced by uric acid which is mediated by the transcription factor UaY, together with the AreA GATA factor (PubMed:17367381). The promoter contains 4 A/CGATAR areA-binding sites (PubMed:17367381).
Glycosylated (PubMed:17429948). Is subject to both N- and O-linked glycosylation (PubMed:17429948).
Blocks propionyl-CoA utilization, as well as growth on propionate. Impairs production of several polyketides such as sterigmatocystin.
Catalyzes the synthesis of (2S,3S)-2-methylcitrate from propionyl-CoA and oxaloacetate and also from acetyl-CoA and oxaloacetate with a greater efficiency. Also has citrate synthase activity and can substitute for the loss of citA activity.
Expression is highly induced by propionate. Also induced by ethanol. Transcription is subject to CreA-mediated carbon repression.
Belongs to the xlnR/xlr1 family. araR subfamily.
Impairs growth on L-arabinose, but only a small growth reduction on L-arabitol.
Transcriptional activator of the arabinanolytic system. Involved in the regulation of extracellular arabinanolytic genes and in the regulation of the intracellular activities of L-arabinose catabolic genes in the pentose catabolic pathway (PCP) in response to the presence of L-arabinose.
Component of the GINS complex which is a heterotetramer of sld5, psf1, psf2 and psf3.
Belongs to the DHHC palmitoyltransferase family. ERF2/ZDHHC9 subfamily.
Palmitoyltransferase specific for Ras proteins.
The DHHC domain is required for palmitoyltransferase activity.
Belongs to the glycosyl hydrolase 38 family.
Belongs to the phage and mitochondrial RNA polymerase family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Belongs to the TFIIF beta 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 cysteine dioxygenase family.
Belongs to the glycosyltransferase 15 family.
Belongs to the glycosyltransferase 8 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.
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 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 (By similarity). The CSN complex seems to link protein degradation to sexual development. Required for fruit body formation.
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 class-II fumarase/aspartase family. Fumarase subfamily.
Component of the ribosomal small subunit (SSU) processome.
Involved in nucleolar processing of pre-18S ribosomal RNA. Involved in ribosome biosynthesis (By similarity).
4'-phosphopantetheine is transferred from CoA to a specific serine of the acyl carrier domain by the C-terminal PPT domain. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Belongs to the thiolase-like superfamily. Fungal fatty acid synthetase subunit alpha family.
Eliminates more than 99.5% of aspercryptin production (PubMed:26563584).
Fatty acid synthase subunit alpha; part of the gene cluster that mediates the biosynthesis of aspercryptins, linear lipopeptides built from six amino acids including 2 highly unusual and nonproteogenic amino acids, 2-amino-octanoic acid (2aoa) and 2-amino-dodecanol (2adol) (PubMed:23248299, PubMed:27310134, PubMed:26563584). The core structure of aspercryptins is as follows: Ser/Ala-Thr-Ile/Val-2aoa-Asn-2adol (PubMed:27310134). The first step of aspercryptin biosynthesis is the generation of the fatty acid precursors, octanoic and dodecanoic acids, by the FAS subunits atnF and atnM (PubMed:27310134, PubMed:26563584). The fatty acid precursors are likely transformed into the corresponding alpha-amino fatty acids in three steps (PubMed:27310134, PubMed:26563584). First, they are hydroxylated by the cytochrome P450 monooxygenase atnE, then oxidized to the corresponding alpha-keto acids by the NAD(P)-dependent oxidoreductase atnD, and finally converted to the alpha-amino fatty acids by the PLP-dependent aminotransferases atnH or atnJ (PubMed:27310134, PubMed:26563584). the alpha-amino fatty acids, 2-amino-octanoic and 2-amino-dodecanoic acids, are recognized, activated, and covalently tethered to the NRPS atnA by its fourth and sixth adenylation domains (PubMed:27310134). The second module of atnA is the Thr module and contains an epimerase (E) domain responsible for the epimerization of Thr to D-allo-Thr (PubMed:26563584). Additionally, despite atnA having only one epimerase domain, the first amino acid of aspercryptin A1 is D-Ser, suggesting that serine is either loaded directly as D-Ser on the first module or that the epimerase domain in the threonine module epimerizes both L-Ser and L-Thr (PubMed:27310134). After condensation of the hexapeptide of aspercryptin, the C-terminal reductase (TE) domain might be involved in the reductive release and production of the aldehyde hexapeptide (PubMed:26563584). Further reduction would generate aspercryptins (PubMed:27310134, PubMed:26563584). The variety of aspercryptins produced reflects the flexibiliy of the atnA NRPS, allowing incorporation of alanine instead of serine, valine for isoleucine, and a C10 fatty amino alcohol instead of the C12 version (PubMed:27310134). AtnB seems to be involved in the selectivity for Ile versus Val by the third module (PubMed:26563584). Moreover, type B, C and D aspercryptins have an additional N-terminal cichorine, acetyl and propionyl group respectively (PubMed:27310134).
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.
Belongs to the mannose-6-phosphate isomerase type 1 family.
Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Belongs to the eukaryotic ribosomal protein eL31 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 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.
Belongs to the chromate ion transporter (CHR) (TC 2.A.51) family.
Belongs to the Nudix hydrolase family. DCP2 subfamily.
Belongs to the heat shock protein 70 family.
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.
Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily.
Belongs to the shaker potassium channel beta subunit family.
Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of emericellamides, secondary metabolites acting as antibiotics (PubMed:18559263). The biosynthesis of emericellamides initiates from the highly reducing polyketide synthase easB which catalyzes the formation of the linear polyketide chain (PubMed:18559263). EasB produces several polyketides that can be further processed by the downstream enzymes (PubMed:18559263). The polyketides are released from easB as linear polyketide carboxylic acids, which are converted to CoA thioesters by the acyl-CoA ligase easD (PubMed:18559263). The substrates are then loaded onto the acyltransferase easC, which shuttles them to the first thiolation (T) domain of the nonribosomal peptide synthetase easA (PubMed:18559263). EasA then performs condensation of the polyketides with one glycine, two alanine, one valine and one leucine residues (PubMed:18559263). A last step of cyclization leads to the production of emericellamides (PubMed:18559263).
The NRPS easA is a multimodular enzymatic assembly that contains 18 domains grouped into five modules corresponding to each of the five amino acid monomers incorporated (PubMed:18559263). The second to the fifth modules contain the three core domains, the condensation (C) domain responsible for catalyzing peptide bond formation, adenylation (A) domain responsible for selecting the amino acid monomer substrate, and the thiolation (T) domain (PubMed:18559263). The first module in the NRPS contains a unique T-E-C-A-T-E structure where (E) domains are epimerization domains (PubMed:18559263). The NRPS does not contain a TE domain at the end of module 5, presumably suggesting that TE is not necessary for the cyclization of the emericellamides (PubMed:18559263).
Belongs to the Mediator complex subunit 16 family.
Belongs to the glycosyl hydrolase 2 family.
Belongs to the acetyltransferase family. GNA1 subfamily.
Expressed during both sexual and asexual development (PubMed:26773375). Expression is positively regulated by the secondary metabolism regulator laeA (PubMed:16426969, PubMed:17291795).
Probable NADPH-dependent quinone reductase; part of the gene cluster that mediates the biosynthesis of terrequinone A, an antitumor agent (PubMed:17704773, PubMed:16426969, PubMed:17291795, PubMed:22083274). The first step in the biosynthetic pathway for terrequinone A is formation of indole pyruvic acid (IPA) from L-tryptophan by the aminotransferase tdiD (PubMed:17704773). The nonribosomal peptide synthase tdiA then immediately converts unstable IPA to didemethylasterriquinone D (DDAQ D), via condensation of 2 IPA molecules (PubMed:17704773). The symmetric connectivity of the 2 IPA molecules is thought to arise by head-to-tail dual Claisen condensations facilitated by the TE domain (PubMed:17704773). TdiB then catalyzes reverse prenylation by transferring dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to yield asterriquinone C-1 (PubMed:18029206). Finally, tdiC and tdiE enzymes robustly convert asterriquinone C-1 to terrequinone A via a transformation involving regular prenylation at carbon atom 5, which requires elimination of the hydroxy group on C-5 (PubMed:17704773, PubMed:18029206).
Belongs to the glycosyl hydrolase 31 family.
Belongs to the pyrroline-5-carboxylate reductase family.
Component of the chromatin-remodeling INO80 complex.
Probably involved in transcription regulation via its interaction with the INO80 complex, a chromatin-remodeling complex.
Belongs to the nucleoporin Nup133 family.
Carbamylation 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 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'.
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.
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.
Abolishes the production of orsellinic acid, lecanoric acid and F-9775A/B (PubMed:19666480, PubMed:20174687).
Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of orsellinic acid, as well as of the cathepsin K inhibitors F9775 A and F9775 B (PubMed:19666480, PubMed:20174687). The non-reducing polyketide synthase orsA produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:19666480, PubMed:20174687). Further modifications by the decarboxylase orsB and the tyrosinase-like protein orsC lead to the production of F9775 A and F9775 B (PubMed:20174687). The functions of orsD and orsE remain unclear since only orsB and orsC are required to convert orsellinic acid into F9775 A and F9775 B (PubMed:20174687).
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 'GDSL' lipolytic enzyme family.
Plays a key role in the degradation of rhamnogalacturonan in the cell wall. Involved in degradation of pectin.
Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the nitrate reductase family.
Binds 1 heme group. The heme group is called cytochrome b-557.
Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Nonessential protein required for the fusion of transport vesicles derived from the endocytic pathway with the Golgi complex.
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.
Belongs to the protein prenyltransferase subunit beta family.
ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair.
Component of the INO80 chromatin-remodeling complex.
The DBINO region is involved in binding to DNA.
Belongs to the eukaryotic ribosomal protein eL28 family.
Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint.
Belongs to the universal ribosomal protein uS5 family.
Involved in the utilization of lactams. Required for the conversion of exogenous 2-pyrrolidinone (gamma-butyrolactam) to endogenous gamma-amino-n-butyrate (GABA).
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.
Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.
Divalent metal cations. Prefers magnesium or manganese.
Belongs to the DNA polymerase type-B-like family.
Belongs to the phosphosulfolactate synthase family.
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the polyenes aspernidgulenes (PubMed:30302871). The carbon backbone of aspernidgulenes is synthesized by the HR-PKS sdgA, which accepts acetyl-CoA as the starter unit and performs malonyl-CoA extensions as well as regioselective methylation and reduction (PubMed:30302871). The resulting nonaketide offloads the HR-PKS by intramolecular lactonization to yield the 5,6-dihydro-alpha-pyrone-containing hexaenoic acids preaspernidgulene A1 and A2 (PubMed:30302871). The FAD-dependent monooxygenase sdgC then installs the first epoxide on the penultimate double bond (PubMed:30302871). Subsequently, the FAD-dependent monooxygenase sdgF presumably generates a ketone intermediate through Meinwald rearrangement involving a hydride shift (PubMed:30302871). Next, sdgC introduces another epoxide on the last olefin of the ketone intermediate after E/Z isomerization (PubMed:30302871). The epoxide hydrolase sdgD then catalyzes stereospecific cyclization of the 5,6-dihydro-alpha-pyrone and opening of the epoxide ring to form an oxygenated trimethylcyclopentanone and an oxabicyclo[2.2.1]heptane unit (PubMed:30302871). Finally, the bicyclic unit undergoes hydrolytic cleavage, either spontaneously or catalyzed by sdgD, to assemble the dimethyl-gamma-lactone moiety in aspernidgulene A1 (PubMed:30302871).
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 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.
Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Binds 1 thiamine pyrophosphate per subunit.
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.
Expression is under the control of the nsdD transcription factor required for sexual development. Transcript level is the highest at the beginning of asexual development and decreases thereafter to increase again at the late stage.
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.
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).
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 (By similarity).
Belongs to the actin family. ARP6 subfamily.
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).
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 AAA ATPase family. BCS1 subfamily.
Belongs to the eukaryotic ribosomal protein eS21 family.
Component of the small 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. Has a physiological role leading to 18S rRNA stability.
Belongs to the DASH complex ASK1 family.
Belongs to the universal ribosomal protein uS9 family.
Belongs to the glutamine synthetase family.
Belongs to the protein kinase superfamily. ADCK protein kinase family.
Belongs to the DEAD box helicase family. DEAH subfamily. DDX15/PRP43 sub-subfamily.
Belongs to the acetyltransferase family.
N-acetylglutamate synthase involved in arginine biosynthesis.
Belongs to the CDP-alcohol phosphatidyltransferase class-II family.
Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
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.
Catalyzes the reversible hydration of cis-homoaconitate to (2R,3S)-homoisocitrate, a step in the alpha-aminoadipate pathway for lysine biosynthesis.
Belongs to the chorismate synthase family.
Belongs to the adaptor complexes medium subunit family.
Belongs to the glycosyltransferase 34 family.
Multidomain protein; including an N-terminal starter unit:ACP transacylase (SAT) domain, a beta-ketoacyl synthase (KS) domain, a malonyl-CoA:ACP transacylase (MAT) domain, a product template (PT) domain that controls the immediate cyclization regioselectivity of the reactive polyketide backbone, an acyl carrier protein (ACP) domain, a methyltransferase (CMeT) domain responsible for the incorporation of methyl groups, and a reductive NADPH-binding domain that is required for NADPH-dependent product release.
Non-reducing polyketide synthase that synthesizes 6-ethyl-2,4-dihydroxy-3,5-dimethylbenzaldehyde via condensation of one propanoyl-CoA starter unit with 3 malonyl-CoA units, as well as 2 methylation steps.
Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX.
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.
Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand.
Displays partial derepression of activities subject to nitrogen metabolic repression.
Lacks the conserved Tyr residue in position 127 in the active site triad of Ser-Tyr-Lys that is necessary for dehydrogenase activity, suggesting that it has no oxidoreductase activity.
May be a redox sensor protein. Has much higher affinity for NAD(P) than for NAD(P)H. Has similar affinity for NAD and NADP. Negative transcriptional regulator involved in the post-transcriptional modulation of the GATA-type transcription factor areA, forming part of a system controlling nitrogen metabolite repression (By similarity). Interferes with the interaction between areA and target DNA. Overexpression leads to areA inhibition.
Up-regulated in nitrogen-sufficient conditions and down-regulated in nitrogen-limiting conditions.
MAP4K component of the MAPK pathway required for the mating pheromone response and the regulation of cell polarity and cell cycle.
In the C-terminal section; belongs to the Cu-Zn superoxide dismutase 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.
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 mitochondrial pyruvate carrier (MPC) (TC 2.A.105) family.
Mediates the uptake of pyruvate into mitochondria.
Belongs to the glutamate--cysteine ligase type 3 family.
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins.
Belongs to the histidinol dehydrogenase family.
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Belongs to the proteasome subunit S5A family.
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 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).
Belongs to the eukaryotic ribosomal protein eL22 family.
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 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.
Component of the dolichol-phosphate mannose (DPM) synthase complex.
Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit to the ER.
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).
Dehydrogenase involved in the conversion of monodictyphenone to the prenyl xanthones such as emericellin, shamixanthone and epishamixanthone (PubMed:21351751, PubMed:22730213). Monodictyphenone is first converted to variecoxanthone A via a paeciloxanthone intermediate by the consecutive actions of the FAD-dependent monooxygenase mdpD and the xanthone prenyltransferase xptB (PubMed:21351751). XptB catalyzes regular O-prenylation at the hydroxy group of C-7 of the xanthone ring (PubMed:23150454). Variecoxanthone A is further prenylated to emericellin by xptA before being reduced to shamixanthone and epishamixanthone by the dehydrogenase xptC (PubMed:21351751).
Impairs the production of the xanthones shamixanthone and epishamixanthone; and accumulates variecoxanthone A and emericellin (PubMed:21351751).
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family.
Catalyzes the hydrolysis of ATP coupled with the transport of calcium.
Abolishes the production of Aspernidine A.
Multidomain protein; including an N-terminal starter unit:ACP transacylase (SAT) domain, a beta-ketoacyl synthase (KS) domain, a malonyl-CoA:ACP transacylase (MAT) domain, a product template domain, a acyl carrier protein (ACP) domain, a methyltransferase domain and a reductive NADPH-binding domain that is required for NADPH-dependent product release.
Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone (PubMed:23706169). The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non-reducing polyketide synthase pkfA, via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units (PubMed:22510154). Hydroxylation, methylation of one of the phenol groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E (PubMed:23706169). The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of aspyridones (PubMed:17369821, Ref.5). The polyketide-amino acid backbone preaspyridone A is first assembled by the PKS-NRPS hybrid apdA (PubMed:17369821, PubMed:20828130). The assembly of preaspyridone A is initiated by loading of malonyl-CoA onto apdA, followed by decarboxylation to yield the acetyl starter unit (PubMed:20828130). The growing polyketide chain then elongates into a tetraketide (PubMed:20828130). The adpA PKS module catalyzes three Claisen condensations, as well as beta-keto processing and methylation (PubMed:17369821, PubMed:20828130). Alpha-methylation step during polyketide synthesis is a prerequisite and a key checkpoint for chain transfer between PKS and NRPS modules (PubMed:25494235). The downstream NRPS module contains the condensation (C), adenylation (A), and thiolation (T) domains and catalyzes the incorporation of tyrosine via the formation of the L-tyrosinyl-thioester and the amide linkage between L-tyrosinyl-thioester and the tetraketide (PubMed:20828130). The bimodular assembly line is terminated with a reductase (R) domain that facilitates formation and release of the tetramic acid product (PubMed:20828130). Because apdA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase apdC (PubMed:17369821, PubMed:20828130, Ref.5). ApdC appears to operate with different stereoselectivity in different PKS cycle (Ref.5). Combined with apdC, apdA is proposed to synthesize preaspyridone A via about 20 enzymatic steps (PubMed:20828130). A number of oxidative steps performed successively by the cytochrome P450 monooxygenases apdE and apdB are required for the conversion of preaspyridone A to aspyridone A (PubMed:17369821). The cytochrome P450 monooxygenase apdE is responsible for the oxidative dephenylation of preaspyridone A (Ref.5). Finally, the predicted FAD-dependent monooxygenase apdD and the acyl-CoA dehydrogenase apdG may be involved in the transformation of aspyridone A into aspyridone B (PubMed:17369821) (Probable).
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
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.
Belongs to the RNA polymerase beta chain family.
Plays a role in vesicular protein sorting.
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 Mediator complex subunit 22 family.
Belongs to the SAICAR synthetase family.
Involved in DNA double-strand break (DSB) repair and recombination. Promotes the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase (By similarity).
Part of a complex that includes RAD51, RAD52 and RAD59.
Involved in pre-mRNA splicing and cell cycle progression.
Glucosidase involved in the degradation of cellulosic biomass. Has both alpha- and beta-glucosidase activity.
Belongs to the pseudouridine synthase TruD family.
N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.
Does not lead to any phenotypic changes.
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the antibiotic 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives (PubMed:22510154, PubMed:23001671). The direct non-reducing polyketide synthase dbaI product is 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA), produced by condensation of one acetyl-CoA starter unit with 4 malonyl-CoA units and one methylation step (PubMed:22510154). The FAD-dependent monooxygenase dbaH is responsible for the synthesis of yellow pigments derived from the oxidation of DHMBA (PubMed:23001671). The roles of dbaB, C, E and F have still to be determined (Probable).
Negative regulator of transcription elongation.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily.
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).
Induced by the antibiotic concanamycin A. Down-regulated when grown with elevated levels of potassium chloride.
Belongs to the protein kinase superfamily.
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 peptidase M28 family. M28E subfamily.
Extracellular aminopeptidase that allows assimilation of proteinaceous substrates.
Belongs to the enoyl-CoA hydratase/isomerase family.
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.
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 putative lipase ROG1 family.
Expression is up-regulated in the presence of benzoate.
Intradiol ring-cleavage dioxygenase; part of the benzoic acid degradation pathway also known as the protocatechuic acid pathway (PubMed:25479309). Benzoic acid debradation begins with the conversion of benzoic acid into 4-hydroxybenzoic acid through hydroxylation by the benzoate-4-monooxygenase bphA, and its partner NADPH-cytochrome P450 reductase cprA which act as a mediator in electron donation from NADPH (By similarity). 4-Hydroxybenzoic acid is then converted into 3,4-dihydroxybenzoic acid (also called protocatechuic acid) by the p-hydroxybenzoate-m-hydroxylase phhA (Probable). Protocatechuic acid is converted into 3-carboxy-cis,cis-muconic acid by the intradiol ring-cleavage dioxygenase prcA, which is further metabolized through the 3-oxoadipate pathway to finally enter the tricarboxylic acid cycle (TCA) (Probable).
Expression is positively regulated by the secondary metabolism cross-pathway regulator scpR (PubMed:20952652).
Leads to decreased production of asperfuranone (PubMed:19199437).
Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of asperfuranone, a probable antitumor agent (PubMed:19199437).
Catalytic subunit in the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.
Belongs to the glycosyltransferase 20 family.
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.
Belongs to the GHMP kinase family. Homoserine kinase subfamily.
Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle pole or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly. Interacts physically with beta-tubulin and is involved in microtubule function.
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.
Belongs to the Mediator complex subunit 13 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.
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 major facilitator superfamily.
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.
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.
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 TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.
Non-reducing polyketide synthase; part of the pki gene cluster that mediates the biosynthesis of 2,4-dihydroxy-3-methyl-6-(2-oxoundecyl)benzaldehyde (PubMed:22510154). The first step in the pathway is the generation of the decanoyl starter unit by the FAS composed of subunits pkiB and pkiC, which is then transferred directly from the FAS to the SAT domain of the non-reducing polyketide synthase pkiA (PubMed:22510154). PkiA condenses the decanoyyl starter unit with 4 malonyl-CoA units and performs one methylation step to yield 2,4-dihydroxy-3-methyl-6-(2-oxoundecyl)benzaldehyde (PubMed:22510154).
Belongs to the tellurite-resistance/dicarboxylate transporter (TDT) family.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
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. Active against rye arabinoxylan and xylohexaose, but not paranitrophenyl-beta-xyloside.
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).
Belongs to the glycosyltransferase 2 family.
Belongs to the universal ribosomal protein uS10 family.
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Belongs to the mitochondrion-specific ribosomal protein mL50 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.
Abolishes the production of cichorine and accumulates nidulol.
Cichorine and its derivatives are promising in the course of developing novel herbicides.
Oxidoreductase; part of the gene cluster that mediates the biosynthesis of cichorine, a phytotoxin active against knapweed, corn, and soybeans (PubMed:24244835). The first step in the pathway is performed by the non-reducing polyketide synthase pkbA that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units (PubMed:22510154). PkbA also catalyzes one methylation step to produce 3-methylorsellinate (PubMed:22510154). The nonribosomal peptide synthase-like protein cicB, the cytochrome P450 monooxygenase cicH and the O-methyltransferase cicE are involved in the conversion of 3-methylorsellinate into nidulol (PubMed:24244835). CicB converts 3-methylorsellinate to a yet unidentified intermediate, cicH may play a ring-closing role for cichorine and cicE is plausibly responsible for the methylation of one of the phenol groups (Probable). The oxidoreductase cicC acts downstream with still unidentified enzymes to further convert nidulol into cichorine (PubMed:24244835).
Belongs to the polysaccharide deacetylase family.
Evidence supports a metal cofactor but evidence for cobalt is inconsistent.
Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine polymers in chitin to form chitosan and acetate.
Inhibited by metal chelator ethylenediaminetetraacetic acid (EDTA).
Belongs to the protein prenyltransferase subunit alpha family.
Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to cysteines occuring in specific C-terminal amino acid sequences.
Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.
Belongs to the glycosyl hydrolase 36 family.
Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides (By similarity). Not active on paranitrophenyl-alpha-galactoside and raffinose.
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).
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 polyketide transferase af380 family.
Belongs to the helicase family. RAD25/XPB subfamily.
Belongs to the velvet family. VosA subfamily.
Component of the velB-VosA heterodimeric complex that plays a dual role in activating genes associated with spore maturation and repressing certain development-associated genes (PubMed:17912349, PubMed:21152013, PubMed:23049895, PubMed:24391470). Controls primarily the late process of sporulation including trehalose biogenesis (PubMed:17912349). The complex binds DNA through the DNA-binding domain of vosA that recognizes an 11-nucleotide consensus sequence 5'-CTGGCCGCGGC-3' consisting of two motifs in the promoters of key developmental regulatory genes (PubMed:24391470). The vosA-velB complex binds to the beta-glucan synthase fksA gene promoter in asexual spores for repression (PubMed:25960370).
Expression is induced in conidia, ascospores and during the late phase of conidiation when conidia differentiate and become mature (PubMed:17912349). During vegetative growth, expression quickly drops and continues to be undetectable (or low) until 24 hours post induction of conidiation (PubMed:17912349). Expression is positively regulated by abaA (PubMed:23049895). Expression is under the regulation of the flbE transcription factor (PubMed:20817115). Expression is also under the regulation of the flbC transcription factor (PubMed:20624219).
Forms a heterodimeric complex with VelB; the formation of the velB-vosA complex is light-dependent (PubMed:21152013, PubMed:23049895). Interacts also with velC (PubMed:24587098).
Results in the lack of trehalose in spores, a rapid loss of the cytoplasm, organelles and viability of spores, and a dramatic reduction in tolerance of conidia to heat and oxidative stress (PubMed:17912349). Down-regulates genes associated with spore maturation and up-regulates certain development-associated genes (PubMed:24391470). Results in elevated accumulation of beta-glucan in asexual spores (PubMed:25960370).
The N-terminal velvet domain contains a NF-kappa-B-like fold and is involved in DNA-binding (PubMed:24391470).
Belongs to the glycosyl hydrolase 15 family.
Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
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.
Inactive carboxypeptidase that may play a role in cell wall organization and biogenesis.
Lacks the conserved Glu residue in position 477 essential for carbopeptidase activity. The mature form lacks catalytic activity towards synthetic peptide substrates.
A pair of annexin repeats may form one binding site for calcium and phospholipid.
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).
Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins (PubMed:25251934). The first stage is catalyzed by the nonribosomal pepdide synthetase asqK that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (PubMed:25251934). AsqK is also able to use anthranilic acid and L-phenylalanine as substrates to produce cyclopeptin, but at a tenfold lower rate (PubMed:25251934). 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase asqJ through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (PubMed:25251934, PubMed:26553478). AsqJ also converts its first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin (PubMed:25251934). AsqJ is a very unique dioxygenase which is capable of catalyzing radical-mediated dehydrogenation and epoxidation reactions sequentially on a 6,7-benzo-diazepinedione substrate in the 4'-methoxyviridicatin biosynthetic pathway (PubMed:25251934). AsqJ is also capable of converting cyclopeptin into dehydrocyclopeptin (PubMed:25251934). The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI (PubMed:30026518). Cyclopenin can also be converted into viridicatin by asqI (PubMed:30026518). 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase asqH1 then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase asqF to yield conjugated aryl diene (By similarity). The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase asqH2 to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain (By similarity). The FAD-dependent monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin (PubMed:30026518). Finally, after dehydratation of the epoxide at C3 by asqC, the quinolone epoxide rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring system in aspoquinolone (PubMed:30026518).
Endoplasmic reticulum-Golgi intermediate compartment membrane
Plays a role in transport between endoplasmic reticulum and Golgi.
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.
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.
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.
Component of the 2-(3-amino-3-carboxypropyl)histidine synthase complex composed of dph1, dph2, dph3 and a NADH-dependent reductase, predominantly cbr1.
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. Releases the terminal mannose residue from mannobiose, mannotriose and galactosyl-mannotriose (GM3), but not from galactosyl-mannobiose (GM2) or di-galactosyl-mannopentaose (G2M5).
In contrast to clade A beta-mannosidases, which are likely secreted, clade B proteins appear to be intracellular.
Impairs the production of monodictyphenone, but still enables the synthesis of intermediates until emodin.
Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative (PubMed:20139316, PubMed:21351751, PubMed:22730213, PubMed:22909031, PubMed:26266881). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG (PubMed:20139316). The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG (PubMed:20139316). The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone (PubMed:20139316). The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emodinanthrone to emodin (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751, PubMed:22909031). The short chain dehydrogenase mdpC converts the tautomers of emodin hydroquinone into the 3-hydroxy-3,4-dihydroan-thracen-1(2H)-one derivative (PubMed:22909031, PubMed:26266881). These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin (PubMed:22730213). Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps (PubMed:22730213).
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.
Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily.
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 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 RecA family. RAD51 subfamily.
Required both for recombination and for the repair of DNA damage caused by X-rays.
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).
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.
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.
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.
Abolishes the production of aspercryptin (PubMed:26563584).
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aspercryptins, linear lipopeptides built from six amino acids including 2 highly unusual and nonproteogenic amino acids, 2-amino-octanoic acid (2aoa) and 2-amino-dodecanol (2adol) (PubMed:23248299, PubMed:27310134, PubMed:26563584). The core structure of aspercryptins is as follows: Ser/Ala-Thr-Ile/Val-2aoa-Asn-2adol (PubMed:27310134). The first step of aspercryptin biosynthesis is the generation of the fatty acid precursors, octanoic and dodecanoic acids, by the FAS subunits atnF and atnM (PubMed:27310134, PubMed:26563584). The fatty acid precursors are likely transformed into the corresponding alpha-amino fatty acids in three steps (PubMed:27310134, PubMed:26563584). First, they are hydroxylated by the cytochrome P450 monooxygenase atnE, then oxidized to the corresponding alpha-keto acids by the NAD(P)-dependent oxidoreductase atnD, and finally converted to the alpha-amino fatty acids by the PLP-dependent aminotransferases atnH or atnJ (PubMed:27310134, PubMed:26563584). the alpha-amino fatty acids, 2-amino-octanoic and 2-amino-dodecanoic acids, are recognized, activated, and covalently tethered to the NRPS atnA by its fourth and sixth adenylation domains (PubMed:27310134). The second module of atnA is the Thr module and contains an epimerase (E) domain responsible for the epimerization of Thr to D-allo-Thr (PubMed:26563584). Additionally, despite atnA having only one epimerase domain, the first amino acid of aspercryptin A1 is D-Ser, suggesting that serine is either loaded directly as D-Ser on the first module or that the epimerase domain in the threonine module epimerizes both L-Ser and L-Thr (PubMed:27310134). After condensation of the hexapeptide of aspercryptin, the C-terminal reductase (TE) domain might be involved in the reductive release and production of the aldehyde hexapeptide (PubMed:26563584). Further reduction would generate aspercryptins (PubMed:27310134, PubMed:26563584). The variety of aspercryptins produced reflects the flexibiliy of the atnA NRPS, allowing incorporation of alanine instead of serine, valine for isoleucine, and a C10 fatty amino alcohol instead of the C12 version (PubMed:27310134). AtnB seems to be involved in the selectivity for Ile versus Val by the third module (PubMed:26563584). Moreover, type B, C and D aspercryptins have an additional N-terminal cichorine, acetyl and propionyl group respectively (PubMed:27310134).
Belongs to the eukaryotic ribosomal protein eL14 family.
Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA polymerase subunit family.
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.
Does not affect production of fellutamides (PubMed:27294372).
MFS efflux transporter; part of the inp gene cluster that mediates the biosynthesis of fellutamide B, a mycotoxin that acts as a proteasome inhibitor (PubMed:20952652, PubMed:27294372). In the first step of fellutabmide B biosynthesis inpC activates 3-hydroxydodecanoic acid to generate 3-hydroxydodecanoyl-AMP that is then loaded onto the T0 domain of inpB (PubMed:27294372). The 3-hydroxydodecanoyl-S-phosphopantetheinyl-T0 is sequentially extended with L-Asn and L-Gln by the two CAT modules of inpB (PubMed:27294372). The linear lipodipeptide from inpB is then transferred onto inpA for the addition of the third amino acid, L-Leu (PubMed:27294372). Reductive releasing of the lipotripeptide by the TE domain of inpA produces (2S)-fellutamide B (PubMed:27294372). InpF might be involved in the release and transfer of the lipodipeptide from inpB to inpA (PubMed:27294372). The inp cluster-encoded proteasome subunit inpE confers resistance to internally produced fellutamides (PubMed:27294372). The MFS efflux transporter inpD may contribute to fellutamide resistance as well (PubMed:27294372).
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.
Component of the endosomal sorting complex required for transport II (ESCRT-II).
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.
Acetyltransferase; part of the gene cluster that mediates the biosynthesis of asperlin, a polyketide showing anti-inflammatory, antitumor and antibiotic activities (PubMed:30339758). The first step of the asperlin biosynthesis is the production of the intermediate 2,4,6-octatrienoic acid by the highly redusing polyketide synthase alnA with cleavage of the PKS product by the esterase alnB (PubMed:30339758). 2,4,6-octatrienoic acid is further converted to asperlin via several steps involving the remaining enzymes from the cluster (PubMed:30339758).
Expression is controlled by the asperlin biosynthesis cluster-specific transcription factor alnR.
Fully eliminates the production of asperlin.
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.
Belongs to the choline monooxygenase family.
Catalyzes the first step of the osmoprotectant glycine betaine synthesis.
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).
Fatty acid synthase alpha subunit; part of the pki gene cluster that mediates the biosynthesis of 2,4-dihydroxy-3-methyl-6-(2-oxoundecyl)benzaldehyde (PubMed:22510154). The first step in the pathway is the generation of the decanoyl starter unit by the FAS composed of subunits pkiB and pkiC, which is then transferred directly from the FAS to the SAT domain of the non-reducing polyketide synthase pkiA (PubMed:22510154). PkiA condenses the decanoyyl starter unit with 4 malonyl-CoA units and performs one methylation step to yield 2,4-dihydroxy-3-methyl-6-(2-oxoundecyl)benzaldehyde (PubMed:22510154).
Induced by oleic acid and stearic acid, but not by linoleic acid.
Belongs to the cyclophilin-type PPIase family. PPIL4 subfamily.
Belongs to the aromatic-ring hydroxylase family.
Monooxygenase; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins (PubMed:25251934). The first stage is catalyzed by the nonribosomal pepdide synthetase asqK that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (PubMed:25251934). AsqK is also able to use anthranilic acid and L-phenylalanine as substrates to produce cyclopeptin, but at a tenfold lower rate (PubMed:25251934). 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase asqJ through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (PubMed:25251934, PubMed:26553478). AsqJ also converts its first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin (PubMed:25251934). AsqJ is a very unique dioxygenase which is capable of catalyzing radical-mediated dehydrogenation and epoxidation reactions sequentially on a 6,7-benzo-diazepinedione substrate in the 4'-methoxyviridicatin biosynthetic pathway (PubMed:25251934). AsqJ is also capable of converting cyclopeptin into dehydrocyclopeptin (PubMed:25251934). The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI (PubMed:30026518). Cyclopenin can also be converted into viridicatin by asqI (PubMed:30026518). 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase asqH1 then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase asqF to yield conjugated aryl diene (By similarity). The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase asqH2 to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain (By similarity). The FAD-dependent monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin (PubMed:30026518). Finally, after dehydratation of the epoxide at C3 by asqC, the quinolone epoxide rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring system in aspoquinolone (PubMed:30026518).
Belongs to the bacterial ribosomal protein bL32 family.
Belongs to the nucleoporin NSP1/NUP62 family.
Expression is induced during late sexual development in the dark (PubMed:26773375).
Fails to produce asperthecin (PubMed:18978088).
Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment (PubMed:18978088, PubMed:21866960). Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules (PubMed:18978088). Polyketide is subsequently hydrolyzed by the action of aptB into endocrocin-9-anthrone (PubMed:18978088). Endocrocin-9-anthrone is then oxidized into endocrocin by aptC (PubMed:18978088). Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis cluster (PubMed:18978088). Finally, aptC or another endogenous oxygenase catalyzes additional oxidation steps to form asperthecin.
Belongs to the universal ribosomal protein uS11 family.
BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (PubMed:2655931, PubMed:2196567). They act individually and together to regulate their own expression and that of numerous other sporulation-specific gene (PubMed:2655931, PubMed:2823119). Controls temporal and spatial specificity in Aspergillus development (PubMed:2655931, PubMed:7704830). Directs the differentiation of phialides and is continuously required for maintenance of their function (PubMed:2152124). Expression of abaA leads to activation of brlA and wetA, cessation of vegetative growth, and accentuated cellular vacuolization (PubMed:2655931). Binds to the sequence 5'-CATTCY-3', where Y is a pyrimidine, making both major- and minor-groove contacts (PubMed:8139553). Multiple abaA binding sites are present in the cis-acting regulatory regions of several developmentally controlled structural genes as well as those of the upstream regulatory gene brlA, the downstream regulatory gene wetA, and abaA itself (PubMed:8139553).
Expression is induced during conidiation, after conidiophore vesicles, metullae, and phialides had formed (PubMed:2823119). Negatively regulated by velC (PubMed:24587098). In the promoter, a 45-base-pair region encompassing the major and minor abaA transcription initiation sites contains directly repeated sequences related to the mammalian initiator (Inr) element and is sufficient for correct transcription initiation and for developmental induction (PubMed:2117702).
Prevents the formation of normal conidiophores (PubMed:2823119, PubMed:2152124). Fails to form any viable conidia, even though it does produce morphologically normal phialides(PubMed:2655931).
Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans.
Belongs to the class-A beta-lactamase family.
Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Involved in nucleotide excision repair.
Belongs to the alpha-ketoglutarate dehydrogenase family.
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 (By similarity).
Belongs to the glycosyl hydrolase 62 family.
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 glycosyl hydrolase 7 (cellulase C) family.
Belongs to the MIP/aquaporin (TC 1.A.8) family.
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.
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.
Impairs the synthesis of austinol and dehydroaustinol and accumulates (5'R)-isoaustinone (PubMed:22329759).
Part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725).
Belongs to the universal ribosomal protein uL4 family.
Efflux pump; part of the gene cluster that mediates the biosynthesis of asperfuranone, a probable antitumor agent (PubMed:19199437).
Strongly diminishes production of asperfuranone (PubMed:19199437).
Required for the maintenance of the structure of the mitochondrial inner membrane. Involved in mitochondrial morphology. Causes growth arrest when highly overexpressed (By similarity).
Belongs to the acetyltransferase family. ARD1 subfamily.
Belongs to the eukaryotic/archaeal RNase P protein component 2 family.
Belongs to the ATPase gamma chain family.
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.
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.
Belongs to the universal ribosomal protein uL18 family.
Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
In the C-terminal section; belongs to the eukaryotic ribosomal protein eL40 family.
In the N-terminal section; belongs to the ubiquitin family.
In the N-terminal section; belongs to the FGAMS family.
Required for synthesis of 60S ribosomal subunits and the transport of pre-ribosomes from the nucleoplasm to the cytoplasm.
Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
Belongs to the WD repeat peroxin-7 family.
Has a role in the initiation of DNA replication. Required at S-phase checkpoint (By similarity).
Belongs to the DASH complex SPC34 family.
Belongs to the small GTPase superfamily. Arf family.
GTP-binding protein involved in protein trafficking; modulates vesicle budding and uncoating within the Golgi apparatus.
Belongs to the PheA/TfdB FAD monooxygenase family.
Citrate synthase is found in nearly all cells capable of oxidative metabolism.
Belongs to the SMC family. RAD50 subfamily.
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.
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.
Alpha-fucosidase involved in degradation of fucosylated xyloglucans. Hydrolyzes alpha-1,2-linked fucose. Active on cotton xyloglucan oligomers but not active on paranitrophenyl-fucoside.
Belongs to the glycosyl hydrolase 95 family.
This enzyme is required for electron transfer from NADP to cytochrome P450.
Belongs to the peptidase S26 family. IMP2 subfamily.
Belongs to the Mediator complex subunit 5 family.
Acyl-CoA ligase; part of the inp gene cluster that mediates the biosynthesis of fellutamide B, a mycotoxin that acts as a proteasome inhibitor (PubMed:20952652, PubMed:27294372). In the first step of fellutabmide B biosynthesis inpC activates 3-hydroxydodecanoic acid to generate 3-hydroxydodecanoyl-AMP that is then loaded onto the T0 domain of inpB (PubMed:27294372). The 3-hydroxydodecanoyl-S-phosphopantetheinyl-T0 is sequentially extended with L-Asn and L-Gln by the two CAT modules of inpB (PubMed:27294372). The linear lipodipeptide from inpB is then transferred onto inpA for the addition of the third amino acid, L-Leu (PubMed:27294372). Reductive releasing of the lipotripeptide by the TE domain of inpA produces (2S)-fellutamide B (PubMed:27294372). InpF might be involved in the release and transfer of the lipodipeptide from inpB to inpA (PubMed:27294372). The inp cluster-encoded proteasome subunit inpE confers resistance to internally produced fellutamides (PubMed:27294372). The MFS efflux transporter inpD may contribute to fellutamide resistance as well (PubMed:27294372).
Eliminates the production of fellutamides (PubMed:27294372).
Belongs to the universal ribosomal protein uS7 family.
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.
Oxidoreductase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) (PubMed:22506079, PubMed:27098256). Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors (PubMed:22506079, PubMed:27098256). The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes (PubMed:22506079, PubMed:27098256). Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene (PubMed:22506079, PubMed:27098256). The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable).
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.
In the C-terminal section; belongs to the peptidase M41 family.
In the N-terminal section; belongs to the AAA ATPase family.
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.
May negatively regulate the snf1 kinase.
The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER).
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.
Belongs to the iron/manganese superoxide dismutase family.
Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. 6-phosphogluconolactonase subfamily.
Belongs to the lysophospholipase family.
Catalyzes the release of fatty acids from lysophospholipids.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis.
Belongs to the chitin synthase family. Class I subfamily.
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).
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 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 SMC family. SMC4 subfamily.
Positively regulates the expression of 5 genes involved in the catabolism of certain amides (amdS), omega amino acids (gatA and gabA), and lactams (lamA and lamB) in the presence of omega amino acid inducers.
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.
Belongs to the PEP-utilizing enzyme family.
Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
Assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. Acts as a F-box protein exchange factor when interacting with candA-C (By similarity).
Cells show a dark red color when grown on an air-medium interface that induces development. Cells are able to initiate the cycle but are blocked in the initial stage of early nest formation. Cells exhibit reduction in asexual development and block in sexual development.
In E.nidulans, CAND1 is separated into 2 distinct proteins: candA-N and candA-C (AC Q5BAH2), corresponding to the N- and C-termini respectively of the protein in other species.
Interacts with candA-C. Interacts with unneddylated cullins culA and culD; interaction occurs only when complexed with candA-C.
Belongs to the lipid-translocating exporter (LTE) (TC 9.A.26.1) family.
Eliminates more than 70% of aspercryptin production (PubMed:26563584).
Probable lipid transporter; part of the gene cluster that mediates the biosynthesis of aspercryptins, linear lipopeptides built from six amino acids including 2 highly unusual and nonproteogenic amino acids, 2-amino-octanoic acid (2aoa) and 2-amino-dodecanol (2adol) (PubMed:23248299, PubMed:27310134, PubMed:26563584). The core structure of aspercryptins is as follows: Ser/Ala-Thr-Ile/Val-2aoa-Asn-2adol (PubMed:27310134). The first step of aspercryptin biosynthesis is the generation of the fatty acid precursors, octanoic and dodecanoic acids, by the FAS subunits atnF and atnM (PubMed:27310134, PubMed:26563584). The fatty acid precursors are likely transformed into the corresponding alpha-amino fatty acids in three steps (PubMed:27310134, PubMed:26563584). First, they are hydroxylated by the cytochrome P450 monooxygenase atnE, then oxidized to the corresponding alpha-keto acids by the NAD(P)-dependent oxidoreductase atnD, and finally converted to the alpha-amino fatty acids by the PLP-dependent aminotransferases atnH or atnJ (PubMed:27310134, PubMed:26563584). the alpha-amino fatty acids, 2-amino-octanoic and 2-amino-dodecanoic acids, are recognized, activated, and covalently tethered to the NRPS atnA by its fourth and sixth adenylation domains (PubMed:27310134). The second module of atnA is the Thr module and contains an epimerase (E) domain responsible for the epimerization of Thr to D-allo-Thr (PubMed:26563584). Additionally, despite atnA having only one epimerase domain, the first amino acid of aspercryptin A1 is D-Ser, suggesting that serine is either loaded directly as D-Ser on the first module or that the epimerase domain in the threonine module epimerizes both L-Ser and L-Thr (PubMed:27310134). After condensation of the hexapeptide of aspercryptin, the C-terminal reductase (TE) domain might be involved in the reductive release and production of the aldehyde hexapeptide (PubMed:26563584). Further reduction would generate aspercryptins (PubMed:27310134, PubMed:26563584). The variety of aspercryptins produced reflects the flexibiliy of the atnA NRPS, allowing incorporation of alanine instead of serine, valine for isoleucine, and a C10 fatty amino alcohol instead of the C12 version (PubMed:27310134). AtnB seems to be involved in the selectivity for Ile versus Val by the third module (PubMed:26563584). Moreover, type B, C and D aspercryptins have an additional N-terminal cichorine, acetyl and propionyl group respectively (PubMed:27310134).
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 WD repeat G protein beta family.
Belongs to the TRAPP small subunits family. BET3 subfamily.
Belongs to the UbiA prenyltransferase family.
Prenyltransferase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone (PubMed:23706169). The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non-reducing polyketide synthase pkfA (PubMed:22510154). Hydroxylation, methylation of one of the phenol groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E (PubMed:23706169). The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable).
Belongs to the Necrosis inducing protein (NPP1) family.
In the C-terminal section; belongs to the eukaryotic ribosomal protein eS31 family.
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.
Required for growth under high-pressure and low-temperature conditions.
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.
Histone methyltransferase that trimethylates histone H3 'Lys-36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression.
Isochorismatase-like protein; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins (PubMed:25251934). The first stage is catalyzed by the nonribosomal pepdide synthetase asqK that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (PubMed:25251934). AsqK is also able to use anthranilic acid and L-phenylalanine as substrates to produce cyclopeptin, but at a tenfold lower rate (PubMed:25251934). 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase asqJ through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (PubMed:25251934, PubMed:26553478). AsqJ also converts its first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin (PubMed:25251934). AsqJ is a very unique dioxygenase which is capable of catalyzing radical-mediated dehydrogenation and epoxidation reactions sequentially on a 6,7-benzo-diazepinedione substrate in the 4'-methoxyviridicatin biosynthetic pathway (PubMed:25251934). AsqJ is also capable of converting cyclopeptin into dehydrocyclopeptin (PubMed:25251934). The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI (PubMed:30026518). Cyclopenin can also be converted into viridicatin by asqI (PubMed:30026518). 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase asqH1 then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase asqF to yield conjugated aryl diene (By similarity). The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase asqH2 to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain (By similarity). The FAD-dependent monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin (PubMed:30026518). Finally, after dehydratation of the epoxide at C3 by asqC, the quinolone epoxide rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring system in aspoquinolone (PubMed:30026518).
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.
Belongs to the actin-binding proteins ADF family. Twinfilin subfamily.
Expression is inhibited by PKA activity and is subject to glucose repression (PubMed:17703972). Expressed primarily in conidia (PubMed:12409104). Expressed and secreted during germination and early growth (PubMed:16376592, PubMed:17703972).
Secreted thaumatin-like protein that, with calA, plays an essential role in early conidial germination with a possible role in cell wall remodeling (PubMed:16376592, PubMed:17703972).
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).
Belongs to the methyltransferase superfamily. LCMT family.
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).
Belongs to the mandelate racemase/muconate lactonizing enzyme family. GlucD subfamily.
Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP1/NBP35 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.
Belongs to the eukaryotic ribosomal protein eS27 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. Has no activity with adenosine as a substrate.
Belongs to the WD repeat NOL10/ENP2 family.
Highly expressed in presence of carboxymethylcellulose (CMC).
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 flavin oxidoreductase frp 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.
Belongs to the ubiquitin-activating E1 family.
Belongs to the STE12 transcription factor family.
Expression is low in vegetative hyphae and increases during conidiophore development.
Transcription factor involved in sexual reproduction. Required for cleistothecial development and ascosporogenesis. Not required for asexual reproduction (conidiation). May act to repress medA expression.
Down-regulated in nitrogen-sufficient conditions and up-regulated in nitrogen-limiting conditions.
Transcription activator that binds the consensus DNA element 5'-CGATAG-3' and mediates nitrogen metabolite repression. Activates the transcription of uapA.
Belongs to the ubiquitin-activating E1 family. UBA3 subfamily.
Catalytic subunit of the dimeric E1 enzyme, which activates NEDD8.
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 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.
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.
Has a role in transport between endoplasmic reticulum and Golgi.
Belongs to the four-carbon acid sugar kinase family.
Belongs to the glycosyl hydrolase 32 family.
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).
Belongs to the proteasome subunit S9 family.
Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes.
Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint (By similarity).
Belongs to the universal ribosomal protein uL6 family.
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).
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 universal ribosomal protein uS15 family.
Belongs to the fungal fatty acid synthetase subunit beta family.
Belongs to the eukaryotic ribosomal protein eL32 family.
The GINS complex plays an essential role in the initiation of DNA replication. Has a role in chromosome segregation (By similarity).
Glucosidase involved in the degradation of cellulosic biomass. Active on lichenan.
May be involved in a process influencing telomere capping.
Belongs to the DHHC palmitoyltransferase family. AKR/ZDHHC17 subfamily.
Palmitoyltransferase specific for casein kinase 1.
Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
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 protein disulfide isomerase family.
Belongs to the Mediator complex subunit 31 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 anthrone oxygenase family.
Efflux pump that may be involved in the secretion of aspyridones (PubMed:17369821).
Belongs to the LIMR family. LMBRD1 subfamily.
Probable lysosomal cobalamin transporter. Required to export cobalamin from lysosomes allowing its conversion to cofactors (By similarity).
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.
Belongs to the glycosyl hydrolase 20 family.
Belongs to the BPG-independent phosphoglycerate mutase family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family.
O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins (PubMed:25251934). The first stage is catalyzed by the nonribosomal pepdide synthetase asqK that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (PubMed:25251934). AsqK is also able to use anthranilic acid and L-phenylalanine as substrates to produce cyclopeptin, but at a tenfold lower rate (PubMed:25251934). 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase asqJ through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (PubMed:25251934, PubMed:26553478). AsqJ also converts its first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin (PubMed:25251934). AsqJ is a very unique dioxygenase which is capable of catalyzing radical-mediated dehydrogenation and epoxidation reactions sequentially on a 6,7-benzo-diazepinedione substrate in the 4'-methoxyviridicatin biosynthetic pathway (PubMed:25251934). AsqJ is also capable of converting cyclopeptin into dehydrocyclopeptin (PubMed:25251934). The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI (PubMed:30026518). Cyclopenin can also be converted into viridicatin by asqI (PubMed:30026518). 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase asqH1 then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase asqF to yield conjugated aryl diene (By similarity). The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase asqH2 to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain (By similarity). The FAD-dependent monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin (PubMed:30026518). Finally, after dehydratation of the epoxide at C3 by asqC, the quinolone epoxide rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring system in aspoquinolone (PubMed:30026518).
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.
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 (PubMed:18556559). VeA acts as a bridging protein between laeA and velB (PubMed:18556559).
Expression is negatively regulated by the transcription factor AflR, as well as by two signal transduction elements, protein kinase A and rasA. Expression is up-regulated in D.melanogaster-challenged colonies in a Drosophila-Aspergillus insect-fungus model system (PubMed:24023705). Expression is also controled by mpkB (PubMed:18378656).
Methyltransferase that performs automethylation at Met-207 (PubMed:23532849). No other methyl-accepting substrate has been identified yet (PubMed:23532849). Component of the velvet transcription factor complex that acts as a global regulator for secondary metabolite gene expression (PubMed:15075281, PubMed:20132440). Controls the expression of the sterigmatocystin, penicillin, and lovastatin gene clusters (PubMed:15075281, PubMed:16968230). Controls light-dependent formation of the velB-vosA complex, veA protein modification, and is required for light-mediated inhibition of sexual development (PubMed:21152013). Within the velvet complex, controls light-dependent secondary metabolism (PubMed:18556559). Involved in the defense response against Drosophila melanogaster larval grazing (PubMed:24023705).
Reduces secondary metabolite production, including sterigmatocystin, a carcinogen biochemically related to the agricultural contaminant aflatoxin. Results in constitutive sexual differentiation (PubMed:21152013). Impairs defense response against D.melanogaster larval grazing (PubMed:24023705).
Catalyzes the exchange of ADP and ATP across the membrane.
Belongs to the universal ribosomal protein uS17 family.
Belongs to the mitochondrion-specific ribosomal protein mS23 family.
Component of the mitochondrial small ribosomal subunit.
Belongs to the PI3/PI4-kinase family. Type III PI4K subfamily.
Belongs to the GST superfamily. Kappa 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 membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.
Sterol O-acyltransferase that catalyzes the formation of stery esters.
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).
Belongs to the DEAD box helicase family. DDX5/DBP2 subfamily.
Belongs to the glycosyltransferase 22 family.
Belongs to the Mediator complex subunit 14 family.
Belongs to the metallo-dependent hydrolases superfamily. ACMSD family.
Decarboxylase; part of the gene cluster that mediates the biosynthesis of orsellinic acid, as well as of the cathepsin K inhibitors F9775 A and F9775 B (PubMed:19666480, PubMed:20174687). The non-reducing polyketide synthase orsA produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:19666480, PubMed:20174687). Further modifications by the decarboxylase orsB and the tyrosinase-like protein orsC lead to the production of F9775 A and F9775 B (PubMed:20174687). The functions of orsD and orsE remain unclear since only orsB and orsC are required to convert orsellinic acid into F9775 A and F9775 B (PubMed:20174687).
Fails to produce F9775 A and B, but accumulates gerfelin and continues to yield orsellinic acid (PubMed:20174687).
Belongs to the bacterial ribosomal protein bL12 family.
Positive regulator of phosphatidylinositol 4,5-bisphosphate turnover and negatively regulates signaling through the cell integrity pathway. Involved in rDNA silencing (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.
Belongs to the AB hydrolase superfamily. AB hydrolase 4 family.
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. Plays a role in the regulation of filamentous growth and chronological longevity (By similarity).
The GxGxxG motif is important for the function, possibly through binding with ATP.
Acyltransferase; part of the gene cluster that mediates the biosynthesis of emericellamides, secondary metabolites acting as antibiotics (PubMed:18559263). The biosynthesis of emericellamides initiates from the highly reducing polyketide synthase easB which catalyzes the formation of the linear polyketide chain (PubMed:18559263). EasB produces several polyketides that can be further processed by the downstream enzymes (PubMed:18559263). The polyketides are released from easB as linear polyketide carboxylic acids, which are converted to CoA thioesters by the acyl-CoA ligase easD (PubMed:18559263). The substrates are then loaded onto the acyltransferase easC, which shuttles them to the first thiolation (T) domain of the nonribosomal peptide synthetase easA (PubMed:18559263). EasA then performs condensation of the polyketides with one glycine, two alanine, one valine and one leucine residues (PubMed:18559263). A last step of cyclization leads to the production of emericellamides (PubMed:18559263).
Belongs to the plant acyltransferase family.
Belongs to the DODA-type extradiol aromatic ring-opening dioxygenase family.
Belongs to the dermatan-sulfate isomerase family.
RNA-binding protein involved in post-transcriptional regulation through transcript degradation.
Belongs to the universal ribosomal protein uL15 family.
Cytochrome P450 monooxygenase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725).
Belongs to the metallo-dependent hydrolases superfamily. NagA family.
Binds 1 divalent metal cation per subunit.
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.
Belongs to the glycosyl hydrolase 54 family.
Expressed in presence of L-arabinol and repressed in presence of glucose and glycerol. Expression is also pH regulated probably through the action of the pacC transcription factor and is higher at acidic pHs.
Organized into two domains: an N-terminal catalytic domain and a C-terminal arabinose-binding domain (ABD).
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.
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).
Belongs to the glycosyltransferase 3 family.
Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.
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.
Belongs to the Mediator complex subunit 18 family.
Belongs to the eukaryotic ribosomal protein eS28 family.
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.
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.
Involved in nuclear export, actin cytoskeleton organization and vesicular transport.
Strongly diminishes the production of asperlin.
Transcriptional regulator involved in the positive regulation of the expression of the gene cluster that mediates the biosynthesis of asperlin, a polyketide showing anti-inflammatory, antitumor and antibiotic activities.
Specific in hydrolyzing the terminal glycosidic bond of polygalacturonic acid and oligogalacturonates.
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 ZIP transporter (TC 2.A.5) family.
Dehydrogenase; part of the gene cluster that mediates the biosynthesis of orsellinic acid, as well as of the cathepsin K inhibitors F9775 A and F9775 B (PubMed:19666480, PubMed:20174687). The non-reducing polyketide synthase orsA produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:19666480, PubMed:20174687). Further modifications by the decarboxylase orsB and the tyrosinase-like protein orsC lead to the production of F9775 A and F9775 B (PubMed:20174687). The functions of orsD and orsE remain unclear since only orsB and orsC are required to convert orsellinic acid into F9775 A and F9775 B (PubMed:20174687).
Transcription factor that acts as a positive regulator of nonrepressible acid phosphatase activity. Is a major regulator of responses to nitrogen and carbon starvation and is essential for the expression of genes involved in vegetative incompatibility (like pin-c, het-6, and tol). Vegetative incompatibility is a non-self-recognition system ubiquitous in filamentous fungi which results in programmed cell death (By similarity).
Was originally thought to be a phosphatase.
Activated by Ca(2+)/calmodulin (PubMed:8898358). Binding of calmodulin may relieve intrasteric autoinhibition (Probable).
Autophosphorylated in a calcium/calmodulin-dependent manner.
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.
Calcium/calmodulin-dependent protein kinase (PubMed:2835766). Required in nuclear division cycle for progression from G2 to mitosis. Required for hyphal growth (PubMed:8898358).
Spores arrest with a single nucleus and fail to extend a germ tube.
The autoinhibitory domain overlaps with the calmodulin binding region and interacts in the inactive folded state with the catalytic domain as a pseudosubstrate.
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.
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins (PubMed:25251934, PubMed:28114276). The first stage is catalyzed by the nonribosomal pepdide synthetase asqK that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (PubMed:25251934, PubMed:28114276). AsqK is also able to use anthranilic acid and L-phenylalanine as substrates to produce cyclopeptin, but at a tenfold lower rate (PubMed:25251934). 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase asqJ through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (PubMed:25251934, PubMed:26553478). AsqJ also converts its first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin (PubMed:25251934). AsqJ is a very unique dioxygenase which is capable of catalyzing radical-mediated dehydrogenation and epoxidation reactions sequentially on a 6,7-benzo-diazepinedione substrate in the 4'-methoxyviridicatin biosynthetic pathway (PubMed:25251934). AsqJ is also capable of converting cyclopeptin into dehydrocyclopeptin (PubMed:25251934). The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI (PubMed:30026518). Cyclopenin can also be converted into viridicatin by asqI (PubMed:30026518). 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase asqH1 then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase asqF to yield conjugated aryl diene (By similarity). The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase asqH2 to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain (By similarity). The FAD-dependent monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin (PubMed:30026518). Finally, after dehydratation of the epoxide at C3 by asqC, the quinolone epoxide rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring system in aspoquinolone (PubMed:30026518).
Belongs to the carnitine/choline acetyltransferase family.
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.
Belongs to the imidazoleglycerol-phosphate dehydratase family.
Catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols.
Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family.
Inducible by 2-thiouric acid, and highly repressible by ammonium.
Not detected in resting conidiospores. Transcription is activated during the isotropic growth phase of conidiospores.
Ubiquitinated by hulA. Ubiquitination leads to internalization, sorting into the endosomal pathway to the vacuolar lumen where uapA is eventually degraded.
Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) (PubMed:22506079, PubMed:27098256). Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors (PubMed:22506079, PubMed:27098256). The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes (PubMed:22506079, PubMed:27098256). Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene (PubMed:22506079, PubMed:27098256). The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable).
Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
Belongs to the eukaryotic RPA49/POLR1E RNA polymerase subunit family.
Belongs to the bacterial ribosomal protein bL27 family.
Belongs to the V-ATPase D subunit family.
Required for the formation of actin cables at hyphal tips. Involved in establishment and maintenance of hyphal polarity axes. Stabilizes the localization of the formin sepA at sites of polarized growth.
Involved in the transport of siderophore triacestylfusarinine C and so has a role in iron homeostasis.
Expressed in presence of xylan and repressed by glucose.
Multifunctional dioxygenase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725).
Residues at positions 150 and 232 are important for the type of reaction catalyzed, using identical substrate (PubMed:29317628). Both ausE and prhA accept preaustinoid A1 as a substrate to form divergent products through dynamic skeletal rearrangement (PubMed:29317628). AusE (containing 'Leu-150' and 'Ser-232') first desaturates at C1-C2 to form preaustinoid A2, followed by rearrangement leading to the formation of the spiro-lactone in preaustinoid A3 (PubMed:29317628). In contrast, prhA (containing 'Val-150' and 'Ala-232') first desaturates at C5-C6 to form berkeleyone B, followed by rearrangement of the A/B-ring to form the cycloheptadiene moiety in berkeleydione (PubMed:22234162).
Belongs to the bacterial ribosomal protein bS21 family.
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.
In the C-terminal section; belongs to the TrpB family.
In the N-terminal section; belongs to the TrpA family.
Impairs the production of monodictyphenone and of any of the intermediates of the pathway (PubMed:20139316, PubMed:21351751).
Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative (PubMed:20139316, PubMed:21351751).
Belongs to the G-alpha family. G(q) subfamily.
A component of the endosomal sorting required for transport complex III (ESCRT-III) (By similarity). Interacts with palA.
Required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB).
Belongs to the SMC family. SMC3 subfamily.
Involved in chromosome segregation in mitosis.
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 class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
The AWS and SET domains are necessary for transcription repression.
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 anthranilate synthase component I family.
Converts proline to delta-1-pyrroline-5-carboxylate.
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 eukaryotic release factor 1 family. Pelota subfamily.
May function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs.
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 deadenlyation-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.
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 Mediator complex subunit 4 family.
Belongs to the universal ribosomal protein uS19 family.
Belongs to the fluoride exporter Fluc/FEX family.
Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
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.
Belongs to the methylenetetrahydrofolate reductase family.
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.
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.
Norsolorinic acid reductase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:8643646). The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK (PubMed:8962148). The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (PubMed:8643646) (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF (PubMed:10618248). 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG (PubMed:24957370). The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme (PubMed:24957370). The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone (PubMed:10618248). The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone (PubMed:24957370). The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) (PubMed:24957370). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) (PubMed:8999832). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin (PubMed:7486998). The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin (PubMed:24957370). The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP (PubMed:8900026).
The genes forming the sterigmatocystin biosynthesis cluster are co-regulated and induced on oatmeal porridge or the fungal isolates were grown either on oatmeal porridge or in YEC medium (0.2% yeast extract, 5.0% corn steep liquor).
Belongs to the DEAD box helicase family.
Belongs to the eukaryotic ribosomal protein eL6 family.
Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by a guanine nucleotide-exchange factor (GEF) and inactivated by a GTPase-activating protein (GAP).
Belongs to the small GTPase superfamily. Ras family.
Belongs to the peptidase M28 family. M28A subfamily.
Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
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.
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.
Cyclin-dependent kinase that acts as a master regulator of the mitotic and meiotic cell cycles.
Forms a stable but non-covalent complex with a regulatory subunit (SUC1) and with a cyclin.
Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-180 activates it.
Fatty acid synthase beta subunit; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:8643646). The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK (PubMed:8962148). The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (PubMed:8643646) (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF (PubMed:10618248). 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG (PubMed:24957370). The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme (PubMed:24957370). The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone (PubMed:10618248). The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone (PubMed:24957370). The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) (PubMed:24957370). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) (PubMed:8999832). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin (PubMed:7486998). The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin (PubMed:24957370). The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP (PubMed:8900026).
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).
Involved in the second step of GPI biosynthesis. De-N-acetylation of N-acetylglucosaminyl-phosphatidylinositol.
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.
This protein functions as a dosage-dependent inducer in mitotic control. It is a tyrosine protein phosphatase required for progression of the cell cycle. It may directly dephosphorylate p34(cdc2) and activate the p34(cdc2) kinase activity.
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.
Essential component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. Required for the maturation of extramitochondrial Fe/S proteins.
It is uncertain whether Met-1 or Met-2 is the initiator.
Highly specific phosphatase involved in the metabolism of ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of tRNA splicing.
Belongs to the Mediator complex subunit 8 family.
Belongs to the heat shock protein 90 family.
Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone (PubMed:23706169). The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non-reducing polyketide synthase pkfA (PubMed:22510154). Hydroxylation, methylation of one of the phenol groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E (PubMed:23706169). The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable).
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 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).
Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Active against locust bean gum and gum guar (PubMed:16844780). Also has transglycosylation activity (PubMed:21867780, PubMed:24950755).
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; an enoylreductase (ER) domain that reduces enoyl groups to alkyl group; 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.
Belongs to the 'GDXG' lipolytic enzyme family.
Esterase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:8643646). The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK (PubMed:8962148). The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (PubMed:8643646) (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF (PubMed:10618248). 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG (PubMed:24957370). The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme (PubMed:24957370). The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone (PubMed:10618248). The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone (PubMed:24957370). The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) (PubMed:24957370). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) (PubMed:8999832). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin (PubMed:7486998). The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin (PubMed:24957370). The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP (PubMed:8900026).
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 NDUFA12 subunit family.
Belongs to the RNA polymerase beta' chain family.
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).
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.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC7 subfamily.
Required for early events during cytokinesis including localization of cytoskeletal components to the cytokinetic ring.
Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly.
Interacts with histone H3 and histone H4.
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 peroxiredoxin family. Prx6 subfamily.
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.
Belongs to the neutral sphingomyelinase family.
Peroxidase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:8643646). The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK (PubMed:8962148). The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (PubMed:8643646) (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF (PubMed:10618248). 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG (PubMed:24957370). The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme (PubMed:24957370). The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone (PubMed:10618248). The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone (PubMed:24957370). The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) (PubMed:24957370). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) (PubMed:8999832). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin (PubMed:7486998). The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin (PubMed:24957370). The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP (PubMed:8900026).
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Type IV dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
In the N-terminal section; belongs to the dsDNA virus mRNA guanylyltransferase family.
Responsible for methylating the 5'-cap structure of mRNAs.
Belongs to the universal ribosomal protein uL3 family.
Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol.
Belongs to the PI3/PI4-kinase family. ATM subfamily.
Belongs to the mannitol dehydrogenase family.
Catalyzes the NAD(H)-dependent interconversion of D-fructose and D-mannitol in the mannitol metabolic pathway.
Belongs to the prokaryotic/mitochondrial release factor family.
Belongs to the scytalone dehydratase family.
Scytalone dehydratase-like protein; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative (PubMed:20139316, PubMed:21351751, PubMed:22730213). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG (PubMed:20139316). The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG (PubMed:20139316). The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone (PubMed:20139316). The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emodinanthrone to emodin (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751). These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin (PubMed:22730213). Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps (PubMed:22730213).
Component of the cleavage factor I (CF I) involved in pre-mRNA 3'-end processing.
Belongs to the bacterial ribosomal protein bS16 family.
Belongs to the helicase family. SKI2 subfamily.
Proteasome subunit beta type-6; part of the inp gene cluster that mediates the biosynthesis of fellutamide B, a mycotoxin that acts as a proteasome inhibitor (PubMed:20952652, PubMed:27294372). In the first step of fellutabmide B biosynthesis inpC activates 3-hydroxydodecanoic acid to generate 3-hydroxydodecanoyl-AMP that is then loaded onto the T0 domain of inpB (PubMed:27294372). The 3-hydroxydodecanoyl-S-phosphopantetheinyl-T0 is sequentially extended with L-Asn and L-Gln by the two CAT modules of inpB (PubMed:27294372). The linear lipodipeptide from inpB is then transferred onto inpA for the addition of the third amino acid, L-Leu (PubMed:27294372). Reductive releasing of the lipotripeptide by the TE domain of inpA produces (2S)-fellutamide B (PubMed:27294372). InpF might be involved in the release and transfer of the lipodipeptide from inpB to inpA (PubMed:27294372). The inp cluster-encoded proteasome subunit inpE confers resistance to internally produced fellutamides (PubMed:27294372). The MFS efflux transporter inpD may contribute to fellutamide resistance as well (PubMed:27294372).
Strongly inhibits growth in fellutamide B-producing conditions (PubMed:27294372).
Belongs to the RecA family. DMC1 subfamily.
Belongs to the pyridoxine kinase family.
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.
Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function.
Belongs to the metallo-dependent hydrolases superfamily. ATZ/TRZ family.
Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Belongs to the V-ATPase H 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 made up of two complexes: the ATP-hydrolytic V1 complex and the proton translocation V0 complex.
Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling. The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane. PEX12 also regulates PEX5 recycling by activating the E3 ubiquitin-protein ligase activity of PEX10. When PEX5 recycling is compromised, PEX12 stimulates PEX10-mediated polyubiquitination of PEX5, leading to its subsequent degradation.
Component of the PEX2-PEX10-PEX12 retrotranslocation channel, composed of PEX2, PEX10 and PEX12.
The RING-type zinc-finger is degenerated and only coordinates one zinc ions, preventing E3 ubiquitin-protein ligase activity.
The three subunits of the retrotranslocation channel (PEX2, PEX10 and PEX12) coassemble in the membrane into a channel with an open 10 Angstrom pore. The RING-type zinc-fingers that catalyze PEX5 receptor ubiquitination are positioned above the pore on the cytosolic side of the complex.
Belongs to the OMP decarboxylase family.
Interacts with pacC by binding to its two YPX[LI] motifs.
Required for the proteolytic cleavage of the transcription factor pacC in response to alkaline ambient pH. May act as a scaffold protein that recruits the calpain-like protease palB via vps32 to its substrate pacC (By similarity).
Long-chain fatty alcohol oxidase involved in the omega-oxidation pathway of lipid degradation.
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 U2 small nuclear ribonucleoprotein A family.
Belongs to the oligoribonuclease family.
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.
Belongs to the helicase family. RecQ subfamily.
Baeyer-Villiger oxidase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative (PubMed:20139316, PubMed:21351751, PubMed:22730213). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG (PubMed:20139316). The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG (PubMed:20139316). The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone (PubMed:20139316). The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emodinanthrone to emodin (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751). These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin (PubMed:22730213). Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps (PubMed:22730213).
Belongs to the AflY oxidoreductase family.
Impairs the production of monodictyphenone, but still enables the synthesis of intermediates until emodin (PubMed:20139316, PubMed:21351751). Results in major accumulation of chrysophanol and its 6-hydroxymethyl shunt product aloe-emodin (PubMed:22730213).
Belongs to the dTDP-4-dehydrorhamnose reductase family. MAT2B subfamily.
Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration.
Impairs the biosynthesis of nidulanin A and related compounds (PubMed:23248299).
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 (By similarity). Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product (By similarity). 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 (By similarity). Occasionally, methyltransferase domains (responsible for amino acid methylation) are present within the NRP synthetase (By similarity).
Nonribosomal peptide synthase involved in the synthesis of nidulanin A and derived compounds (PubMed:23248299). Nidulanin A is a tetracyclopeptide with the sequence L-Phe-L-Kyn-L-Val-D-Val and an isoprene unit N-linked to the amino group of L-kynurenine (PubMed:23248299). The NRPS nlsA is responsible of the synthesis of the cyclopeptide and the prenyltransferase nptA adds the isoprene unit on the L-kynurenine residue of nidulanin A (PubMed:23248299). Further modifications lead to additional oxygenated related compounds (PubMed:23248299).
Belongs to the aldo/keto reductase family. Glutamate--cysteine ligase light chain subfamily.
Heterodimer of a catalytic heavy chain and a regulatory light chain.
Belongs to the asaB hydroxylase/desaturase family.
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 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.
Component of the peroxisomal translocation machinery.
Belongs to the glycosyltransferase group 1 family.
Involved in mitochondrial genome encoded proteins translation. Involved in the binding of tRNA to the ribosomes (By similarity).
Part of the mitochondrial small ribosomal subunit.
ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives.
Belongs to the carbohydrate kinase PfkB family.
Belongs to the histone deacetylase family. HD type 1 subfamily.
Ribosomal protein P0 is the functional equivalent of E.coli protein L10.
Belongs to the universal ribosomal protein uL16 family.
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative (PubMed:20139316, PubMed:21351751, PubMed:22730213). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG (PubMed:20139316). The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG (PubMed:20139316). The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone (PubMed:20139316). The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emodinanthrone to emodin (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751). These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin (PubMed:22730213). Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps (PubMed:22730213).
Nuclear chaperone required for maturation and nuclear export of pre-60S ribosome subunits.
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.
Belongs to the small GTPase superfamily. Rho family.
Has a role in cell polarity, primary and secondary germ tube emergence and cell wall deposition.
Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2)) required for protein glycosylation.
Belongs to the chitin synthase family. Class V subfamily.
Results in a hypersensitivity to miconazole.
Transcription factor that regulates expression of the genes related to resistance to azole compounds, including clotrimazole and miconazole.
Belongs to the universal ribosomal protein uL5 family.
Belongs to the STXBP/unc-18/SEC1 family.
Component of the pre-66S ribosomal particle.
Involved in the biogenesis of the 60S ribosomal subunit.
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.
Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
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.
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.
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.
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 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. Active against tamarind xyloglucan.
Impairs the production of sterigmatocystin and leads to the accumulation of versicolorin A.
Versicolorin reductase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:8017929, PubMed:8643646). The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK (PubMed:8962148). The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (PubMed:8643646) (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF (PubMed:10618248). 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG (PubMed:24957370). The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme (PubMed:24957370). The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone (PubMed:10618248). The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone (PubMed:24957370). The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) (PubMed:24957370). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) (PubMed:8999832). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin (PubMed:7486998). The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin (PubMed:24957370). The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP (PubMed:8900026).
May form heterododecamers with RVB2. Component of the SWR1 chromatin remodeling complex, the INO80 chromatin remodeling complex, and of the R2TP complex (By similarity).
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1), a complex that is involved in endosomal cargo sorting.
Belongs to the DASH complex DAD1 family.
Involved in spliceosome maturation and the first step of pre-mRNA splicing.
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.
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.
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).
Belongs to the thioesterase PaaI family.
Abolishes the production of cichorine and leads to the accumulation of 3-methylorsellinic acid.
Belongs to the adenylate-forming reductase family.
Contains three distinct domains: an adenylation (A) domain that activates the substrate amino acid which is subsequently covalently linked as a thioester (aminoacyl-S-PCP) to the 4'-phosphopantetheine prosthetic group of the second domain, the peptidyl carrier protein (PCP) domain, as well as a reductase (R) release domain.
Nonribosomal peptide synthase-like protein; part of the gene cluster that mediates the biosynthesis of cichorine, a phytotoxin active against knapweed, corn, and soybeans (PubMed:24244835). The first step in the pathway is performed by the non-reducing polyketide synthase pkbA that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units (PubMed:22510154). PkbA also catalyzes one methylation step to produce 3-methylorsellinate (PubMed:22510154). The nonribosomal peptide synthase-like protein cicB, the cytochrome P450 monooxygenase cicH and the O-methyltransferase cicE are involved in the conversion of 3-methylorsellinate into nidulol (PubMed:24244835). CicB converts 3-methylorsellinate to a yet unidentified intermediate, cicH may play a ring-closing role for cichorine and cicE is plausibly responsible for the methylation of one of the phenol groups (Probable). The oxidoreductase cicC acts downstream with still unidentified enzymes to further convert nidulol into cichorine (PubMed:24244835).
Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family.
Required for gamma-tubulin complex recruitment to the microtubule organizing center (MTOC).
Belongs to the beta-class carbonic anhydrase family.
Belongs to the fumigaclavine B O-acetyltransferase family.
O-acyltransferase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725).
Belongs to the universal ribosomal protein uL22 family.
Belongs to the nucleosome assembly protein (NAP) 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.
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.
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).
Belongs to the threonine aldolase family.
Aminotransferase; part of the gene cluster that mediates the biosynthesis of terrequinone A, an antitumor agent (PubMed:17704773, PubMed:16426969, PubMed:17291795, PubMed:22083274). The first step in the biosynthetic pathway for terrequinone A is formation of indole pyruvic acid (IPA) from L-tryptophan by the aminotransferase tdiD (PubMed:17704773). The nonribosomal peptide synthase tdiA then immediately converts unstable IPA to didemethylasterriquinone D (DDAQ D), via condensation of 2 IPA molecules (PubMed:17704773). The symmetric connectivity of the 2 IPA molecules is thought to arise by head-to-tail dual Claisen condensations facilitated by the TE domain (PubMed:17704773). TdiB then catalyzes reverse prenylation by transferring dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to yield asterriquinone C-1 (PubMed:18029206). Finally, tdiC and tdiE enzymes robustly convert asterriquinone C-1 to terrequinone A via a transformation involving regular prenylation at carbon atom 5, which requires elimination of the hydroxy group on C-5 (PubMed:17704773, PubMed:18029206).
Expression is positively regulated by the secondary metabolism regulator laeA (PubMed:16426969, PubMed:17291795).
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.
Belongs to the eukaryotic RPC34/RPC39 RNA polymerase subunit family.
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.
In the C-terminal section; belongs to the DHPS 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.
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.
Belongs to the complex I 23 kDa subunit family.
Belongs to the eukaryotic ribosomal protein eL42 family.
Belongs to the glycosyl hydrolases 36 family.
Essential role in pre-mRNA splicing. Also essential for entry into mitosis (G2/M progression) as well as for chromosome segregation during mitosis.
Belongs to the bZIP family. YAP subfamily.
Decreases the level of cutinase cut4 during oxidative stress.
NapA contains a C-terminal cysteine rich domain (c-CRD), but lacks the N-terminal CRD (n-CRD) found in the yeast homolog YAP1. It probably also contains embedded in the c-CRD a nuclear export signal, with which the nuclear export protein CRM1 may interact in the absence of inter- or intramolecular disulfide bonds (or otherwise oxidized/modified cysteines) within the c-CRD.
Oxidative stress induces conformational changes through oxidation of cysteine residues, masking the nuclear export signal, thus abolishing nuclear export by CRM1/exportin 1.
Transcription activator involved in oxidative stress response, specifically during hyphal growth. Regulates the transcription of genes encoding antioxidant enzymes and components of the cellular thiol-reducing pathways including the mycelium-specific catalase catB (but not the conidia-specific catalase catA), thioredoxin reductase trxB and thioredoxin thiO (PubMed:17617701). Preferentially binds to promoters with the core binding site 5'-TTA[CG]TAA-3'. Activity of the transcription factor is controlled through oxidation of specific cysteine residues resulting in the alteration of its subcellular location. Activation by hydroperoxides induces nuclear accumulation and as a result NapA transcriptional activity (By similarity).
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. MOCOS subfamily.
By the nicotinate utilization transcriptional activating systems.
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.
Belongs to the eukaryotic ribosomal protein eL13 family.
Belongs to the dynein heavy chain family.
Consists of at least two heavy chains and a number of intermediate and light chains.
Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required to maintain uniform nuclear distribution in hyphae.
Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function.
Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Active against locust bean gum and gum guar (PubMed:16844780). Also has efficient transglycosylation activity. Produces mainly mannopentaose and mannoheptaose out of mannotetraose. May even prefer sugars as acceptors instead of water (PubMed:24950755).
Required for proper homologous chromosome pairing and efficient cross-over and intragenic recombination during meiosis.
Involved in CDC48-dependent protein degradation through the ubiquitin/proteasome pathway.
Autoacetylation at Lys-320 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.
Required for the completion of mitosis in Aspergillus nidulans.
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 (By similarity).
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.
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 phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type II 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. 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.
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.
The C2 domains have an essential, but non-catalytic function. They may facilitate interactions with other proteins and are required for lipid transport function.
May be involved in the response to oxidative stress.
By the unfolded protein response pathway. Accumulation of unfolded proteins in the ER leads to splicing of the hacA precursor mRNA to produce the mature form.
Transcriptional activator involved in the unfolded protein response (UPR) pathway. Recognizes and binds to the UPR element (UPRE) in the promoter of UPR-regulated genes. Increases the synthesis of endoplasmic reticulum-resident proteins required for protein folding as well as components of the secretory pathway (By similarity).
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.
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).
Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway.
Belongs to the alkaline ceramidase family.
Belongs to the JHDM3 histone demethylase family.
Belongs to the complex I 49 kDa subunit 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.
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.
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.
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.
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 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).
Belongs to the eukaryotic ribosomal protein eS25 family.
Belongs to the glycosyl hydrolase 18 family. Chitinase class III subfamily.
Expressed specifically highly during conidia germination and in the marginal growth regions of colonies.
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.
NRPS-like enzyme with an unusual domain architecture that converts back glycine betaine to choline via a 2-step reduction mechanism, and thereby can be an alternative source of choline (PubMed:31061132). Permits direct reutilization of endogenously stored glycine betaine for on-demand biosynthesis of choline and choline derivatives, including phospholipid phosphatidylcholine (PC) which has an essential role in maintaining membrane integrity and functionality, or choline-O-sulfate, a mean for intracellular sulfate storage (PubMed:31061132). Glycine betaine is activated by the adenylation (A) domain, and transferred to the thiolation (T) domain (PubMed:31061132). Movement of the phosphopantetheine arm to the thioester reductase domain R1 then allows thioester reduction by NADPH of glycine betainoyl thioester to glycine betaine aldehyde, which is in turn reduced to choline by the aldehyde reductase domain R2 (PubMed:31061132).
Severely impairs the hyphae growth and conidiation at high level glycine betaine (PubMed:31061132). Exhibits a choline-auxotroph character, when the phosphatidylethanolamine N-methyltransferase choA is also deleted (PubMed:31061132).
The NRPS-like protein ATRR has an unusual domain arcitecture (A-T-R1-R2), with the adenylation domain A activating and thioesterifying glycine betaine which is then channeled through the phosphopantetheine arm of the T domain, the thioester reductase domain R1 reducing glycine betainoyl thioester to glycine betaine aldehyde, and the aldehyde reductase domain R2 converting glycine betaine aldehyde into choline.
The tetramethylammonium ion, which mimics the head group of glycine betaine, acts as a competitive inhibitor of ATRR A domain, whereas the potency decreased by three orders of magnitude with dimethylammonium (PubMed:31061132). Choline is a mixed inhibitor for both glycine betaine reductase and aldehyde reductase activity but more potent in competition against glycine betaine in the first reduction step (PubMed:31061132). Therefore, choline could act as a feedback inhibitor to regulate ATRR enzymatic activity (PubMed:31061132). The lowered binding affinity of choline to R2 favors the release of choline after glycine betaine aldehyde reduction to avoid direct product inhibition (PubMed:31061132).
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.
Belongs to the glucosamine/galactosamine-6-phosphate isomerase family.
Common component of the spliceosome and rRNA processing machinery.
Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit family.
GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) form together the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5).
In eukaryotes EC 6.3.5.5 is synthesized by two pathway-specific (arginine and pyrimidine) genes under separate control.
In the central section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.
This protein is a 'fusion' protein encoding three enzymatic activities of the pyrimidine pathway (GATase, CPSase, and ATCase).
Associates in the nucleolus with the 60S and pre-60S ribosomal subunits.
Belongs to the DEAD box helicase family. DDX18/HAS1 subfamily.
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.
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.
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.
Iterative polyketide synthase; part of the gene cluster that mediates the biosynthesis of asperfuranone, a probable antitumor agent (PubMed:19199437). The polyketide synthase afoG is responsible for producing the 3,5-dimethyloctadienone moiety from acetyl-CoA, three malonyl-CoA, and two S-adenosyl methionines (SAM) (PubMed:19199437). The 3,5-dimethyloctadienone moiety is then loaded onto the SAT domain of afoE and extended with four malonyl-CoA and one SAM, which leads to the formation of 2,4-dihydroxy-6-(5,7-dimethyl-2-oxo-trans-3-trans-5-nonadienyl)-3-methylbenzaldehyde (compound 2) after reductive release and aldol condensation (PubMed:19199437, PubMed:22510154). AfoD is the next enzyme in the biosynthesis sequence and hydroxylates the side chain at the benzylic position of compound 2 (PubMed:19199437). After benzylic hydroxylation, a furan ring is formed after five-member ring hemiacetal formation and water elimination (PubMed:19199437). AfoF and afoC are proposed to oxidize the R-diketone proton and to reduce the unconjugated carbonyl group, respectively, to generate asperfuranone (PubMed:19199437). Since no intermediates could be isolated from afoF and afoC deletants, the sequence of these two enzymes is not fully understood (PubMed:19199437). Moreover, since afoC deletant still produces a small amount of asperfuranone, other endogenous oxidoreductases might catalyze the same reaction with much less efficiency (PubMed:19199437).
Activity is inhibited by 2,3-dihydroxynaphthalene, phenylhydrazine, diethyl dithiocarbamate and 8-hydroxyquinolene (PubMed:2126551).
Impairs the production of the gray-brown conidiophore pigment and leads to 'ivory' (colorless) conidiophores and accumulation of N-acetyl-6-hydroxytryptophan (AHT) (PubMed:2126551).
Nonribosomal peptide synthetase; part of the pathway that mediates the biosynthesis of the gray-brown conidiophore pigment (PubMed:23617571, PubMed:28108400). The first step of the pathway is performed by the nonribosomal peptide synthetase ivoA that catalyzes ATP-dependent unidirectional stereoinversion of L-tryptophan to D-tryptophan with complete conversion (PubMed:31573806). While the stereoinversion is catalyzed by the epimerization (E) domain of ivoA, the terminal condensation (C) domain stereoselectively hydrolyzes D-tryptophanyl-S-phosphopantetheine thioester and thus represents a non-canonical C domain function (PubMed:31573806). D-tryptophan is acetylated, probably by an endogenous acetyltransferase (Probable). N-acetyltryptophan is further 6-hydroxylated into N-acetyl-6-hydroxytryptophan (AHT) by the cytochrome P450 monooxygenase ivoC (PubMed:28108400). N-acetyl-6-hydroxytryptophan is substrate of the N-acetyl-6-hydroxytryptophan oxidase ivoB to produce the gray-brown conidiophore pigment (PubMed:2126551, PubMed:28108400, Ref.4).
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 HMG-CoA reductase family.
Belongs to the SLC35F solute transporter family.
Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity.
Homohexamer. Binds to nucleic acids. Binds single-stranded DNA and RNA with higher affinity than double-stranded DNA.
The normal physiological role of the enzyme is unknown, but it is not essential for the viability of yeast cells. Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity. Acts as a repressor in the GAL4 regulatory system, but this does not require either the peptidase or nucleic acid-binding activities.
Belongs to the WD repeat coronin family.
Terpene cyclase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725).
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.
Heterodimer of an alpha and a beta subunit.
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.
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.
Belongs to the universal ribosomal protein uS8 family.
Belongs to the LDH/MDH superfamily. MDH type 1 family.
Belongs to the eukaryotic ribosomal protein eL20 family.
Belongs to the bacterial ribosomal protein bL17 family.
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).
Phosphorylation of the TEDS site (Ser-371) 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 (By similarity). Plays an important role in polarized growth, spore germination, hyphal morphogenesis, and septal wall formation.
Belongs to the dynactin 150 kDa subunit 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.
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.
Belongs to the ACC deaminase/D-cysteine desulfhydrase family.
Belongs to the AP endonuclease 2 family.
Belongs to the cytidylyltransferase family.
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of asperlin, a polyketide showing anti-inflammatory, antitumor and antibiotic activities (PubMed:30339758). The first step of the asperlin biosynthesis is the production of the intermediate 2,4,6-octatrienoic acid by the highly redusing polyketide synthase alnA with cleavage of the PKS product by the esterase alnB (PubMed:30339758). 2,4,6-octatrienoic acid is further converted to asperlin via several steps involving the remaining enzymes from the cluster (PubMed:30339758).
Bifunctional enzyme; part of the cluster involved in the biosynthesis of biotin (also known as vitamin B8 or vitamin H), a water-soluble vitamin that functions as a prosthetic group of many carboxylases, such as acetyl-CoA carboxylase and pyruvate carboxylase (PubMed:20713166). Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA) to form an ureido ring (PubMed:20713166). Catalyzes also the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA) (PubMed:20713166). It is the only animotransferase known to utilize SAM as an amino donor (By similarity).
In the C-terminal section; belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.
In the N-terminal section; belongs to the dethiobiotin synthetase family.
Recovery of biotin-prototrophic clones from transformation of biotin-auxotrophic mutants suggests that bioDA could be usedas a new and convenient genetic marker for transformation.
Belongs to the Mediator complex subunit 7 family.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily.
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.
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).
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 SMC family. SMC1 subfamily.
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 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.
Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins.
Belongs to the PpiC/parvulin rotamase family. PIN4 subfamily.
Belongs to the small heat shock protein (HSP20) family.
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.
Converts protoheme IX and farnesyl diphosphate to heme O.
Belongs to the arrestin family. PalF/RIM8 subfamily.
Required for the proteolytic cleavage of the transcription factor pacC in response to alkaline ambient pH.
Belongs to the proteasome subunit S2 family.
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 glycosyl hydrolase 35 family.
Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
Belongs to the universal ribosomal protein uS13 family.
Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family.
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.
Down-regulated under iron limitation conditions.
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.
Expression is increased 50-fold during the establishment of developmental competence (PubMed:1516832, PubMed:2062309, PubMed:17630328). Expression is positively controlled by brlA (PubMed:1516832). Expression is also regulated by the LAMMER kinase lkhA (PubMed:23516554).
Leads to defective conidiophore morphology and impairs conidia production (PubMed:25550299). Affects cell wall beta-1,3-glucan biosynthesis (PubMed:25359270).
Transcription factor that regulates asexual reproduction (PubMed:1516832, PubMed:8722771, PubMed:9312029, PubMed:25550299). 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 (PubMed:9312029, PubMed:25359270). Required from the very earliest events of asexual reproduction until completion of conidiophore development, but is not specifically required for differentiation of conidia (PubMed:1516832). Represses transcription of the abaA developmental regulatory gene and of the developmentally regulated awh11 gene (PubMed:9312029). Controls the expression of the catalase-peroxidase gene cpeA (PubMed:12455692). Plays an important role in cell wall biogenesis during the development by controlling the transcription level of fksA (PubMed:25359270).
Involved in protein synthesis. Involved in microtubule stabilization (By similarity). Involved in osmoadaptation.
Belongs to the TRAPP small subunits family.
Part of the multisubunit transport protein particle (TRAPP) complex.
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.
Belongs to the class VI-like SAM-binding methyltransferase superfamily. Isoprenylcysteine carboxyl methyltransferase family.
Belongs to the gluconokinase GntK/GntV family.
Belongs to the DEAD box helicase family. DDX24/MAK5 subfamily.
Belongs to the amidase family. GatA subfamily.
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).
Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:8643646, PubMed:7486998). The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK (PubMed:8962148). The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (PubMed:8643646) (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF (PubMed:10618248). 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG (PubMed:24957370). The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme (PubMed:24957370). The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone (PubMed:10618248). The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone (PubMed:24957370). The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) (PubMed:24957370). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) (PubMed:8999832). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin (PubMed:7486998). The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin (PubMed:24957370). The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP (PubMed:8900026).
Belongs to the eukaryotic NMN adenylyltransferase family.
Belongs to the class-I DAHP synthase family.
Involved in amino sugar synthesis (formation of chitin, supplies the amino sugars of asparagine-linked oligosaccharides of glycoproteins).
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).
Belongs to the class I-like SAM-binding methyltransferase superfamily. Erg6/SMT family.
Catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of lanosterol to form eburicol.
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).
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 transcriptional coactivator PC4 family.
Deaminates gamma-aminobutyric acid (GABA) to succinate-semialdehyde, which in turn is converted to succinate by the succinate semialdehyde dehydrogenase (By similarity). Required for the degradation of GABA, which is important for utilization of GABA as nitrogen source.
Belongs to the WD repeat PROPPIN family.
Involved in mitochondrial or peroxisomal functions and amino acid signaling pathways.
May contain a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2), leading to the association of the protein to the membrane.
Belongs to the ferredoxin--NADP reductase type 1 family.
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 (By similarity).
Belongs to the Mediator complex subunit 17 family.
Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:8643646). The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK (PubMed:8962148). The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (PubMed:8643646) (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF (PubMed:10618248). 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG (PubMed:24957370). The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme (PubMed:24957370). The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone (PubMed:10618248). The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone (PubMed:24957370). The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) (PubMed:24957370). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) (PubMed:8999832). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin (PubMed:7486998). The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin (PubMed:24957370). The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP (PubMed:8900026).
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 2 acyl-carrier proteins (ACPs) that serve as the tether of the growing and completed polyketide via its phosphopantetheinyl arm.
Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of cichorine, a phytotoxin active against knapweed, corn, and soybeans (PubMed:22510154, PubMed:24244835, PubMed:30708999). The first step in the pathway is performed by the non-reducing polyketide synthase pkbA that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units (PubMed:22510154). PkbA also catalyzes one methylation step to produce 3-methylorsellinate (PubMed:22510154). The nonribosomal peptide synthase-like protein cicB, the cytochrome P450 monooxygenase cicH and the O-methyltransferase cicE are involved in the conversion of 3-methylorsellinate into nidulol (PubMed:24244835). CicB converts 3-methylorsellinate to a yet unidentified intermediate, cicH may play a ring-closing role for cichorine and cicE is plausibly responsible for the methylation of one of the phenol groups (Probable). The oxidoreductase cicC acts downstream with still unidentified enzymes to further convert nidulol into cichorin (PubMed:24244835).
Belongs to the WD repeat CDC20/Fizzy family.
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 diphosphomevalonate decarboxylase family.
Belongs to the PPP phosphatase family. PP-Z subfamily.
Belongs to the invertebrate defensin family.
Belongs to the beta-cyclopiazonate dehydrogenase family.
Deletion of the conserved eukaryotic csnE deneddylase subunit of the COP9 signalosome leading to defect in protein degradation results in the activation of the silenced dba gene cluster (PubMed:23001671). Expression is positively regulated by the dba cluster specific transcription factors dbaA and dbaG (PubMed:23001671). Expression is also controlled by the transcription factor flbB (PubMed:25701285).
FAD-dependent oxidoreductase; part of the gene cluster that mediates the biosynthesis of the antibiotic 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives (PubMed:22510154, PubMed:23001671). The direct non-reducing polyketide synthase dbaI product is 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA), produced by condensation of one acetyl-CoA starter unit with 4 malonyl-CoA units and one methylation step (PubMed:22510154). The FAD-dependent monooxygenase dbaH is responsible for the synthesis of yellow pigments derived from the oxidation of DHMBA (PubMed:23001671). The roles of dbaB, C, E and F have still to be determined (Probable).
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).
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.
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 cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.
FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:8643646, PubMed:10618248). The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK (PubMed:8962148). The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (PubMed:8643646) (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF (PubMed:10618248). 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG (PubMed:24957370). The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme (PubMed:24957370). The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone (PubMed:10618248). The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone (PubMed:24957370). The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) (PubMed:24957370). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) (PubMed:8999832). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin (PubMed:7486998). The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin (PubMed:24957370). The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP (PubMed:8900026).
Impairs the production of sterigmatocystin and leads to the accumulation of averufin.
In the C-terminal section; belongs to the histidinol dehydrogenase 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.
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.
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.
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 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 adenosylhomocysteinase family.
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.
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.
Belongs to the iron-containing alcohol dehydrogenase family.
Belongs to the velvet family. VelC subfamily.
Leads to increased number of conidia and reduced production of cleistothecia (PubMed:24587098). Increases expression of brlA, abaA, wetA and vosA genes that control sequential activation of asexual sporulation (PubMed:24587098).
Specifically accumulates during the early phase of sexual development (PubMed:24587098).
Velvet-domain-containing protein that acts as a positive regulator of sexual development (PubMed:24587098). Positively regulates the production of the sexual fruiting bodies called cleistothecia (PubMed:24587098).
Facilitates protein transport into the nucleus. Could be part of a multicomponent system of cytosolic factors that assemble at the pore complex during nuclear import (By similarity).
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.
Has no detectable activity towards cis-acontiate or cis-homoaconitate.
G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site.
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Belongs to the ubiquitin conjugation factor E4 family.
Belongs to the P-Pant transferase superfamily.
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier-protein. The enzyme is able to transfer the cofactor to a broad range of enzymes with acyl- or peptidyl-carrier protein domains. Required for primary biological processes such as growth and asexual/sexual development, and activates target enzymes involved in the synthesis of metabolites such as fatty acids, polyketides and nonribosomal peptides, lysine, siderophore, penicillin, sterigmatocystin, shamixantone, dehydroaustinol, and pigments.
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.
Catalyzes the final step in the metabolic pathway of hydroxyproline (By similarity). Involved in osmoadaptation.
Belongs to the 5'-AMP-activated protein kinase beta subunit family.
Belongs to the PNP/MTAP phosphorylase family.
Belongs to the mitochondrion-specific ribosomal protein mS41 family.
Belongs to the ketopantoate reductase family.
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.
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.
Cysteine protease that plays a key role in cytoplasm to vacuole transport (Cvt) and autophagy by mediating both proteolytic activation and delipidation of ATG8. 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. The protease activity is required for proteolytic activation of ATG8: cleaves the C-terminal amino acid of ATG8 to reveal a C-terminal glycine. ATG8 ubiquitin-like activity requires the exposure of the glycine at the C-terminus for its conjugation to phosphatidylethanolamine (PE) and its insertion to membranes, which is necessary for autophagy. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. In addition to the protease activity, also catalyzes deconjugation of PE-conjugated forms of ATG8 during macroautophagy: ATG8 delipidation is required to release the protein from membranes, which facilitates multiple events during macroautophagy, and especially for efficient autophagosome biogenesis, the assembly of ATG9-containing tubulovesicular clusters into phagophores/autophagosomes, and for the disassembly of PAS-associated ATG components. ATG8 delipidation by ATG4 also recycles ATG8-PE generated on inappropriate membranes to maintain a reservoir of unlipidated ATG8 that is required for autophagosome formation at the PAS.
Belongs to the phosphohexose mutase family.
Catalyzes the reversible interconversion of glucose 1-phosphate and glucose 6-phosphate (PubMed:10660061). 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 (By similarity).
Microperfuranone synthase is the only protein required for the biosynthesis of the secondary metabolite microperfuranone from phenylpyruvic acid (PPA) (PubMed:22627757). Several steps for the microperfuranione biosynthesis have been proposed (PubMed:22627757). These steps include the activation of PPA, by the micA adenylation (A) domain to AMP-phenylpyruvic acid followed by loading of the PPA unit to the thiolation and peptide carrier (T) domain and eventually transferring to the thioesterase (TE) domain (PubMed:22627757). After loading another PPA unit onto the T domain, aldol condensation establishes the carbon-carbon bond between the alpha- and beta-carbon of the two PPA units (PubMed:22627757). Sulfur-assisted furan ring formation, TE domain mediated hydrolysis, decarboxylation, and keto-enol tautomerization would generate microperfuranone attached to the T domain (PubMed:22627757). Finally, microperfuranone is released by the TE domain (PubMed:22627757).
Mediates the induction of a number of unlinked genes involved in purine utilization. Binds to the consensus sequence 5'-TCGGNNNNNNCCGA-3'.
Assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. Acts as a F-box protein exchange factor when interacting with candA-N (By similarity).
In E.nidulans, CAND1 is separated into 2 distinct proteins: candA-N (AC C8VP82) and candA-C, corresponding to the N- and C-termini respectively of the protein in other species.
Interacts with candA-N. Interacts with unneddylated cullins culA and culD.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.
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).
Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1 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 NADH dehydrogenase family.
Expressed in the presence of D-xylose under conditions of acidic ambient pH, probably under the regulation of the pacC transcription factor. Repressed in presence of glucose through the action of the creA transcription repressor.
Belongs to the archaeal/bacterial/fungal opsin family.
In the C-terminal section; belongs to the NAD synthetase family.
Aminotransferase; part of the gene cluster that mediates the biosynthesis of aspercryptins, linear lipopeptides built from six amino acids including 2 highly unusual and nonproteogenic amino acids, 2-amino-octanoic acid (2aoa) and 2-amino-dodecanol (2adol) (PubMed:23248299, PubMed:27310134, PubMed:26563584). The core structure of aspercryptins is as follows: Ser/Ala-Thr-Ile/Val-2aoa-Asn-2adol (PubMed:27310134). The first step of aspercryptin biosynthesis is the generation of the fatty acid precursors, octanoic and dodecanoic acids, by the FAS subunits atnF and atnM (PubMed:27310134, PubMed:26563584). The fatty acid precursors are likely transformed into the corresponding alpha-amino fatty acids in three steps (PubMed:27310134, PubMed:26563584). First, they are hydroxylated by the cytochrome P450 monooxygenase atnE, then oxidized to the corresponding alpha-keto acids by the NAD(P)-dependent oxidoreductase atnD, and finally converted to the alpha-amino fatty acids by the PLP-dependent aminotransferases atnH or atnJ (PubMed:27310134, PubMed:26563584). the alpha-amino fatty acids, 2-amino-octanoic and 2-amino-dodecanoic acids, are recognized, activated, and covalently tethered to the NRPS atnA by its fourth and sixth adenylation domains (PubMed:27310134). The second module of atnA is the Thr module and contains an epimerase (E) domain responsible for the epimerization of Thr to D-allo-Thr (PubMed:26563584). Additionally, despite atnA having only one epimerase domain, the first amino acid of aspercryptin A1 is D-Ser, suggesting that serine is either loaded directly as D-Ser on the first module or that the epimerase domain in the threonine module epimerizes both L-Ser and L-Thr (PubMed:27310134). After condensation of the hexapeptide of aspercryptin, the C-terminal reductase (TE) domain might be involved in the reductive release and production of the aldehyde hexapeptide (PubMed:26563584). Further reduction would generate aspercryptins (PubMed:27310134, PubMed:26563584). The variety of aspercryptins produced reflects the flexibiliy of the atnA NRPS, allowing incorporation of alanine instead of serine, valine for isoleucine, and a C10 fatty amino alcohol instead of the C12 version (PubMed:27310134). AtnB seems to be involved in the selectivity for Ile versus Val by the third module (PubMed:26563584). Moreover, type B, C and D aspercryptins have an additional N-terminal cichorine, acetyl and propionyl group respectively (PubMed:27310134).
Eliminates approximately 70% of aspercryptin production (PubMed:26563584).
Belongs to the ATP phosphoribosyltransferase family.
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 TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.
Catalyzes the synthesis of activated sulfate.
Belongs to the membrane magnesium transporter (TC 1.A.67) family.
Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family.
Belongs to the SIMIBI class G3E GTPase family. UreG subfamily.
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.
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 FNT transporter (TC 2.A.44) family.
Belongs to the complex I NDUFA8 subunit 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 (By similarity).
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.
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 Cu-Zn superoxide dismutase family.
Abolishes trehalose degradation during conidial germination and delays germ tube formation (PubMed:10320571). Resistance to thermal stress (PubMed:10320571).
Belongs to the glycosyl hydrolase 37 family.
Expressed during spore germination and growth.
Hydrolyzes intracellular trehalose to glucose (Probable). The disaccharide trehalose serves as a storage carbohydrate that is mobilized during conidial germination (PubMed:10320571). Regulates the level of trehalose as a protectant for cell integrity during heat stress (PubMed:10320571).
Induced during recovery from thermal stress.
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.
Belongs to the eukaryotic ribosomal protein eS19 family.
Belongs to the eukaryotic ribosomal protein eS12 family.
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.
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 zinc-containing alcohol dehydrogenase family. Class-III subfamily.
Belongs to the myo-inositol oxygenase family.
Blocks production of sterigmatocystin and all sterigmatocystin intermediate substrates but does not affect transcription of the pathway genes.
Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:7642507, PubMed:8643646). The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK (PubMed:8962148). The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (PubMed:8643646) (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF (PubMed:10618248). 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG (PubMed:24957370). The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme (PubMed:24957370). The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone (PubMed:10618248). The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone (PubMed:24957370). The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) (PubMed:24957370). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) (PubMed:8999832). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin (PubMed:7486998). The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin (PubMed:24957370). The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP (PubMed:8900026).
The domain architecture includes a starter unit:ACP transacylase (SAT) domain, a beta-ketoacyl synthase (KS) domain, a malonyl-CoA:ACP transacylase (MAT) domain, a product template (PT) domain, 2 acyl-carrier (ACP) domains, and a thioesterase/Claisen cyclase (TE/CLC) domain (By similarity). The SAT domain receives a C6-fatty acid starter unit and transfers it onto the ACP for chain elongation. The KS accepts the hexanoyl-ACP unit and subsequent malonate extender units are loaded onto the ACP from the MAT domain for chain extension to generate the linear poly-beta-keto ACP-bound intermediate. The linear intermediate is then cyclized and aromatized in the PT domain. The resulting bicyclic intermediate is ultimately transferred from the ACP to the TE/CLC domain and undergoes Claisen-type C-C bond cyclization to release the product norsolorinic acid anthrone (noranthrone), which spontaneously oxidizes in vitro to norsolorinic acid (By similarity).
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.
Belongs to the eukaryotic ribosomal protein eS24 family.
Atrochrysone carboxyl ACP thioesterase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative (PubMed:20139316, PubMed:21351751). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG (PubMed:20139316). The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG (PubMed:20139316). The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone (PubMed:20139316). The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emodinanthrone to emodin (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751, PubMed:22909031). The short chain dehydrogenase mdpC converts the tautomers of emodin hydroquinone into the 3-hydroxy-3,4-dihydroan-thracen-1(2H)-one derivative (PubMed:22909031, PubMed:26266881). These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin (PubMed:22730213). Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps (PubMed:22730213).
Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family.
Carbamylation allows a single lysine to coordinate two divalent metal cations.
Binds 1 heme c group covalently per subunit.
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.
Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the antibiotic 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives (PubMed:22510154, PubMed:23001671). The direct non-reducing polyketide synthase dbaI product is 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA), produced by condensation of one acetyl-CoA starter unit with 4 malonyl-CoA units and one methylation step (PubMed:22510154). The FAD-dependent monooxygenase dbaH is responsible for the synthesis of yellow pigments derived from the oxidation of DHMBA (PubMed:23001671). The roles of dbaB, C, E and F have still to be determined (Probable).
Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase subunit family.
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).
Belongs to the TrkH potassium transport family.
Required for nuclear migration within hyphae during vegetative growth.
Self-associates (By similarity). Interacts with nudF.
Belongs to the WD repeat LIS1/nudF family.
Dimerization mediated by the LisH domain may be required to activate dynein.
Interacts with dynein (By similarity). Self-associates. Interacts with bnfA, nudC and nudE.
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.
Accumulates preferentially during asexual sporulation.
Impairs the production of terrequinone A (PubMed:17291795).
Probable methyltransferase; part of the gene cluster that mediates the biosynthesis of terrequinone A, an antitumor agent (PubMed:17704773, PubMed:16426969, PubMed:17291795, PubMed:22083274). The first step in the biosynthetic pathway for terrequinone A is formation of indole pyruvic acid (IPA) from L-tryptophan by the aminotransferase tdiD (PubMed:17704773). The nonribosomal peptide synthase tdiA then immediately converts unstable IPA to didemethylasterriquinone D (DDAQ D), via condensation of 2 IPA molecules (PubMed:17704773). The symmetric connectivity of the 2 IPA molecules is thought to arise by head-to-tail dual Claisen condensations facilitated by the TE domain (PubMed:17704773). TdiB then catalyzes reverse prenylation by transferring dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to yield asterriquinone C-1 (PubMed:18029206). Finally, tdiC and tdiE enzymes robustly convert asterriquinone C-1 to terrequinone A via a transformation involving regular prenylation at carbon atom 5, which requires elimination of the hydroxy group on C-5 (PubMed:17704773, PubMed:18029206).
Mixed-linked glucanase involved in the degradation of complex natural cellulosic substrates. Active on laminarin. lichenan, soluble carboxymethyl cellulose but not on pustulan.
Belongs to the ribulose-phosphate 3-epimerase family.
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.
Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family.
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.
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.
Belongs to the prenylcysteine oxidase family.
Belongs to the methyltransferase superfamily. L-isoaspartyl/D-aspartyl protein methyltransferase family.
Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins.
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.
Impairs the synthesis of austinol and dehydroaustinol and accumulates the intermediate compound isoaustinone (PubMed:22329759).
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.
Belongs to the glycosyl hydrolase 67 family.
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.
Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily.
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.
Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway (PubMed:6381643, Ref.5). Has also cysteine synthase (O-acetylserine sulfhydrylase) activity in vitro, but seems only be involved in the alternative pathway of methionine biosynthesis in E.nidulans (PubMed:17482430, PubMed:6381643, PubMed:8249501).
E.nidulans has another enzyme having cysteine synthase (O-acetylserine sulfhydrylase) activity (cysB) that has been shown to be the enzyme of physiological importance in cysteine biosynthesis.
Up-regulated under sulfur limitation and down-regulated by high methionine concentrations.
Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.
By ethanol, threonine and acetaldehyde. Expression is autoregulated and subject to carbon catabolite repression.
Positive regulatory protein for the ethanol regulon, alcA and aldA. It control positively its own expression and possibly in a negative fashion the expression of the gene coding for ADH-II.
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).
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 dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family.
Required for nuclear movement. May interact between microtubules and nuclei and/or may be involved in the generation of force used to move nuclei during interphase.
Belongs to the eukaryotic AdoMetDC family.
Belongs to the GTP cyclohydrolase II family.
Belongs to the universal ribosomal protein uL23 family.
Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family.
Belongs to the membrane-bound ascI terpene cyclase family.
Epoxide hydrolase; part of the gene cluster that mediates the biosynthesis of the polyenes aspernidgulenes (PubMed:30302871). The carbon backbone of aspernidgulenes is synthesized by the HR-PKS sdgA, which accepts acetyl-CoA as the starter unit and performs malonyl-CoA extensions as well as regioselective methylation and reduction (PubMed:30302871). The resulting nonaketide offloads the HR-PKS by intramolecular lactonization to yield the 5,6-dihydro-alpha-pyrone-containing hexaenoic acids preaspernidgulene A1 and A2 (PubMed:30302871). The FAD-dependent monooxygenase sdgC then installs the first epoxide on the penultimate double bond (PubMed:30302871). Subsequently, the FAD-dependent monooxygenase sdgF presumably generates a ketone intermediate through Meinwald rearrangement involving a hydride shift (PubMed:30302871). Next, sdgC introduces another epoxide on the last olefin of the ketone intermediate after E/Z isomerization (PubMed:30302871). The epoxide hydrolase sdgD then catalyzes stereospecific cyclization of the 5,6-dihydro-alpha-pyrone and opening of the epoxide ring to form an oxygenated trimethylcyclopentanone and an oxabicyclo[2.2.1]heptane unit (PubMed:30302871). Finally, the bicyclic unit undergoes hydrolytic cleavage, either spontaneously or catalyzed by sdgD, to assemble the dimethyl-gamma-lactone moiety in aspernidgulene A1 (PubMed:30302871).
NAD(+)-dependent glutamate dehydrogenase which degrades glutamate to ammonia and alpha-ketoglutarate.
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex cfd1-nbp35. Electrons are transferred to dre2 from NADPH via the FAD- and FMN-containing protein tah18. Tah18-dre2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit rnr2.
Monomer. Interacts with tah18. Interacts with mia40.
The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine. It is required for correct assembly of the 2 Fe-S clusters.
The twin Cx2C motifs are involved in the recognition by the mitochondrial mia40-erv1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space.
Belongs to the V-ATPase F subunit family.
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).
Belongs to the succinate/malate CoA ligase beta 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 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.
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase NEP1 family.
Belongs to the peptidase S8 family. Furin subfamily.
Belongs to the ABC transporter superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201) subfamily.
Expression is strongly increased in the presence of cycloheximide, camptothecin, imazalil, itraconazole, hygromycin and 4-nitroquinoline oxide (4-NQO).
Fenamirol efflux transporter activity is inhibited by the cyclosporin derivative PSC 833, nigericin, reserpine and valinomycin (PubMed:10954082). The effect of reserpine is transiant, while that of the cyclosporin derivative PSC 833, nigericin and valinomycin is proportional to the time of exposure (PubMed:10954082). Cyclohexinmide has inhibitory effect only when applied prior to addition of the fungicide (PubMed:10954082).
Leads to the cellular accumulation of fenarimol (PubMed:10954082). Leads to increased susceptibility to cycloheximide, the cyclosporin derivative PSC 833, nigericin and valinomycin (PubMed:10954082).
Pleiotropic ABC efflux transporter involved in the protection of the cells against a wide range of toxic compounds (PubMed:10954082). Confers resistance to the azole fenarimol via efflux transport (PubMed:10954082). May also be involved in the secretion of penicillin (PubMed:10954082).
Belongs to the glycosyl hydrolase 65 family.
Part of the multisubunit TRAPP (transport protein particle) complex.
Plays a key role in the late stages of endoplasmic reticulum to Golgi traffic.
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.
Belongs to the histidine acid phosphatase family.
Belongs to the WD repeat BOP1/ERB1 family.
In the C-terminal section; belongs to the trehalose phosphatase family.
In the N-terminal section; belongs to the glycosyltransferase 20 family.
Eliminates the production of aspercryptin (PubMed:27310134, PubMed:26563584).
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 (By similarity). Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product (By similarity). 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 (By similarity). Occasionally, methyltransferase domains (responsible for amino acid methylation) are present within the NRP synthetase (By similarity). InpA has the following architecture: A-T-C-A-T-E-C-A-T-C-A-T-C-A-T-C-A-T-TE (PubMed:27310134).
Nonribosomal peptide synthase; part of the gene cluster that mediates the biosynthesis of aspercryptins, linear lipopeptides built from six amino acids including 2 highly unusual and nonproteogenic amino acids, 2-amino-octanoic acid (2aoa) and 2-amino-dodecanol (2adol) (PubMed:23248299, PubMed:27310134, PubMed:26563584). The core structure of aspercryptins is as follows: Ser/Ala-Thr-Ile/Val-2aoa-Asn-2adol (PubMed:27310134). The first step of aspercryptin biosynthesis is the generation of the fatty acid precursors, octanoic and dodecanoic acids, by the FAS subunits atnF and atnM (PubMed:27310134, PubMed:26563584). The fatty acid precursors are likely transformed into the corresponding alpha-amino fatty acids in three steps (PubMed:27310134, PubMed:26563584). First, they are hydroxylated by the cytochrome P450 monooxygenase atnE, then oxidized to the corresponding alpha-keto acids by the NAD(P)-dependent oxidoreductase atnD, and finally converted to the alpha-amino fatty acids by the PLP-dependent aminotransferases atnH or atnJ (PubMed:27310134, PubMed:26563584). the alpha-amino fatty acids, 2-amino-octanoic and 2-amino-dodecanoic acids, are recognized, activated, and covalently tethered to the NRPS atnA by its fourth and sixth adenylation domains (PubMed:27310134). The second module of atnA is the Thr module and contains an epimerase (E) domain responsible for the epimerization of Thr to D-allo-Thr (PubMed:26563584). Additionally, despite atnA having only one epimerase domain, the first amino acid of aspercryptin A1 is D-Ser, suggesting that serine is either loaded directly as D-Ser on the first module or that the epimerase domain in the threonine module epimerizes both L-Ser and L-Thr (PubMed:27310134). After condensation of the hexapeptide of aspercryptin, the C-terminal reductase (TE) domain might be involved in the reductive release and production of the aldehyde hexapeptide (PubMed:26563584). Further reduction would generate aspercryptins (PubMed:27310134, PubMed:26563584). The variety of aspercryptins produced reflects the flexibiliy of the atnA NRPS, allowing incorporation of alanine instead of serine, valine for isoleucine, and a C10 fatty amino alcohol instead of the C12 version (PubMed:27310134). AtnB seems to be involved in the selectivity for Ile versus Val by the third module (PubMed:26563584). Moreover, type B, C and D aspercryptins have an additional N-terminal cichorine, acetyl and propionyl group respectively (PubMed:27310134).
Belongs to the alkaline phosphatase family.
Belongs to the DEAD box helicase family. DDX54/DBP10 subfamily.
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 proteasome subunit S14 family.
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.
Golgi membrane protein involved in vesicular trafficking.
Belongs to the GTP-binding SRP family. SRP54 subfamily.
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). Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes.
Has a two domain structure: the G-domain binds GTP; the M-domain binds the 7S RNA in presence of SRP19 and also binds the signal sequence.
Signal recognition particle consists of a 7S RNA molecule and at least six protein subunits.
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 TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.
Involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs.
May be involved in protection from oxidative damage.
Belongs to the eukaryotic ribosomal protein eS6 family.
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of cichorine, a phytotoxin active against knapweed, corn, and soybeans (PubMed:24244835). The first step in the pathway is performed by the non-reducing polyketide synthase pkbA that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units (PubMed:22510154). PkbA also catalyzes one methylation step to produce 3-methylorsellinate (PubMed:22510154). The nonribosomal peptide synthase-like protein cicB, the cytochrome P450 monooxygenase cicH and the O-methyltransferase cicE are involved in the conversion of 3-methylorsellinate into nidulol (PubMed:24244835). CicB converts 3-methylorsellinate to a yet unidentified intermediate, cicH may play a ring-closing role for cichorine and cicE is plausibly responsible for the methylation of one of the phenol groups (Probable). The oxidoreductase cicC acts downstream with still unidentified enzymes to further convert nidulol into cichorine (PubMed:24244835).
Belongs to the SurE nucleotidase family.
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.
Regulates the cell cycle in a nutrient dependent manner.
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 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 (By similarity).
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 folylpolyglutamate synthase family.
May mediate the reduction of outer membrane cytochrome b5.
Belongs to the eukaryotic/archaeal RNase P protein component 1 family.
Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family.
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
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.
Abolishes the production of aspernidine A, but accumulates the intermediate aspernidine D.
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone (PubMed:23706169). The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non-reducing polyketide synthase pkfA (PubMed:22510154). Hydroxylation, methylation of one of the phenol groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E (PubMed:23706169). The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable).
Imeairs expression of the sterigmatocystin cluster genes.
Transcription factor; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:8643646, PubMed:8662194). Binds to the palindromic sequence 5'-TCG(N5)CGA-3'found in the promoter regions of several sterigmatocystin cluster genes to induce their expression (PubMed:9680223).
Belongs to the glutamate synthase family.
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.
Belongs to the WD repeat G protein beta family. Ribosomal protein RACK1 subfamily.
Belongs to the G-protein coupled receptor 4 family.
Belongs to the glycosyl hydrolase family 6.
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.
Able to transport with low efficiency all natural purines as well as purine analogs.
Belongs to the steroid 5-alpha reductase family.
Belongs to the eukaryotic ribosomal protein eL27 family.
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:8643646, PubMed:8999832). The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK (PubMed:8962148). The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (PubMed:8643646) (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF (PubMed:10618248). 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG (PubMed:24957370). The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme (PubMed:24957370). The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone (PubMed:10618248). The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone (PubMed:24957370). The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) (PubMed:24957370). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) (PubMed:8999832). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin (PubMed:7486998). The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin (PubMed:24957370). The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP (PubMed:8900026).
Impairs the production of sterigmatocystin and leads to the accumulation of dihydrosterigmatocystin.
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.
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.
Required for replication-independent chromatin assembly and for the periodic repression of histone gene transcription during the cell cycle.
O-methyltransferase; part of the gene cluster that mediates the biosynthesis of cichorine, a phytotoxin active against knapweed, corn, and soybeans (PubMed:24244835). The first step in the pathway is performed by the non-reducing polyketide synthase pkbA that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units (PubMed:22510154). PkbA also catalyzes one methylation step to produce 3-methylorsellinate (PubMed:22510154). The nonribosomal peptide synthase-like protein cicB, the cytochrome P450 monooxygenase cicH and the O-methyltransferase cicE are involved in the conversion of 3-methylorsellinate into nidulol (PubMed:24244835). CicB converts 3-methylorsellinate to a yet unidentified intermediate, cicH may play a ring-closing role for cichorine and cicE is plausibly responsible for the methylation of one of the phenol groups (Probable). The oxidoreductase cicC acts downstream with still unidentified enzymes to further convert nidulol into cichorine (PubMed:24244835).
Iron/alpha-ketoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins (PubMed:25251934, PubMed:26553478). The first stage is catalyzed by the nonribosomal pepdide synthetase asqK that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (PubMed:25251934). AsqK is also able to use anthranilic acid and L-phenylalanine as substrates to produce cyclopeptin, but at a tenfold lower rate (PubMed:25251934). 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase asqJ through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (PubMed:25251934, PubMed:26553478). AsqJ also converts its first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin (PubMed:25251934). AsqJ is a very unique dioxygenase which is capable of catalyzing radical-mediated dehydrogenation and epoxidation reactions sequentially on a 6,7-benzo-diazepinedione substrate in the 4'-methoxyviridicatin biosynthetic pathway (PubMed:25251934). AsqJ is also capable of converting cyclopeptin into dehydrocyclopeptin (PubMed:25251934). The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI (PubMed:30026518). Cyclopenin can also be converted into viridicatin by asqI (PubMed:30026518). 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase asqH1 then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase asqF to yield conjugated aryl diene (By similarity). The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase asqH2 to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain (By similarity). The FAD-dependent monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin (PubMed:30026518). Finally, after dehydratation of the epoxide at C3 by asqC, the quinolone epoxide rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring system in aspoquinolone (PubMed:30026518).
Catalyzes the conversion of O-succinyl-L-serine into cysteine, the last step in the cysteine biosynthesis pathway (By similarity). Can also use O-acetyl-L-serine (PubMed:17482430).
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
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.
Belongs to the DASH complex DUO1 family.
Belongs to the glycosyl hydrolase 81 family.
Ca(2+). Can also use Mg(2+), but with lower efficiency.
Belongs to the galactose-1-phosphate uridylyltransferase type 1 family.
Belongs to the universal ribosomal protein uL11 family.
Belongs to the Clp1 family. NOL9/GRC3 subfamily.
Polynucleotide 5'-kinase involved in rRNA processing.
Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
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).
ABC-type transporter; part of the gene cluster that mediates the biosynthesis of cichorine, a phytotoxin active against knapweed, corn, and soybeans (PubMed:24244835). CicA is probably involved in the secretion of cichorine (Probable).
In the N-terminal section; belongs to the cytochrome P450 family.
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.
Belongs to the HAD-like hydrolase superfamily. S-2-haloalkanoic acid dehalogenase family.
Required for nuclear division. Could function in the mitotic spindle.
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of an adenine present in helix 65 in 25S rRNA.
Isopenicillin N synthase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic (PubMed:3319778, PubMed:11755401). IpnA catalyzes the cyclization of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) to form isopenicillin N (IPN) that contains the beta-lactam nucleus (PubMed:3319778, PubMed:11755401, PubMed:28703303). The penicillin biosynthesis occurs via 3 enzymatic steps, the first corresponding to the production of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) by the NRPS acvA. The tripeptide ACV is then cyclized to isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase penDE to yield penicillin in the peroxisomal matrix (By similarity).
Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.
Belongs to the glutaminase PdxT/SNO family.
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.
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 PHP hydrolase family. HisK subfamily.
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.
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 MsrB Met sulfoxide reductase family.
Belongs to the IPP isomerase type 1 family.
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. Active against linseed rhamnogalacturonan.
Belongs to the glycosyltransferase 28 family.
Probable sterol 3-beta-glucosyltransferase that mediates autophagic degradation of peroxisomes (pexophagy) (By similarity). Also required for cytoplasm to vacuole transport (Cvt) and autophagic degradation of mitochondria (mitophagy) and nuclei (nucleophagy) (By similarity).
The GRAM and PH domains are required for the localization of ATG26 to the preautophagosomal structure (PAS) and are involved in autophagy (By similarity).
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.
Component of the ER membrane protein complex (EMC).
Belongs to the sterol desaturase family. SCS7 subfamily.
Binds 2 Zn(2+) ions per subunit that likely form a catalytic dimetal center.
Ceramide hydroxylase involved in the hydroxylation of sphingolipid-associated very long chain fatty acids. Postulated to hydroxylate the very long chain fatty acid of dihydroceramides and phytoceramides at C-2.
Esterase; part of the gene cluster that mediates the biosynthesis of the antibiotic 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives (PubMed:22510154, PubMed:23001671). The direct non-reducing polyketide synthase dbaI product is 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA), produced by condensation of one acetyl-CoA starter unit with 4 malonyl-CoA units and one methylation step (PubMed:22510154). The FAD-dependent monooxygenase dbaH is responsible for the synthesis of yellow pigments derived from the oxidation of DHMBA (PubMed:23001671). The roles of dbaB, C, E and F have still to be determined (Probable).
Activation probably requires a transfer of a phosphate group between a His in the histidine kinase domain and an Asp of the response regulatory domain.
May be part of a two-component regulatory system required for formation of conidia on certain growth media.
Belongs to the complex I NDUFS4 subunit family.
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.
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. Ubiquitinates 'Lys-528' of the uric acid/xanthine transporter uapA at the cell membrane, leading to its internalization, sorting into the endosomal pathway to the vacuolar lumen where it is eventually degraded.
5'-hydroxyaverantin dehydrogenase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:8643646). The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK (PubMed:8962148). The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (PubMed:8643646) (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF (PubMed:10618248). 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG (PubMed:24957370). The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme (PubMed:24957370). The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone (PubMed:10618248). The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone (PubMed:24957370). The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) (PubMed:24957370). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) (PubMed:8999832). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin (PubMed:7486998). The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin (PubMed:24957370). The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP (PubMed:8900026).
Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan (By similarity).
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 (By similarity).
Belongs to the clathrin heavy chain family.
Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
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 deoxyhypusine synthase family.
Beta-glucosidases are one of a number of cellulolytic enzymes, and catalyze the last step releasing glucose from the inhibitory cellobiose.
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation.
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.
Forms a stable heterodimer with pob3. The spt16-pob3 dimer weakly associates with multiple molecules of nhp6 to form the FACT complex (By similarity).
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.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family.
Belongs to the glycerate kinase type-1 family.
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in endosomal cargo sorting.
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.
Involved in the proteasome-dependent degradation of fructose-1,6-bisphosphatase.
Belongs to the eukaryotic ribosomal protein eS4 family.
Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily.
Belongs to the mitochondrion-specific ribosomal protein mL46 family.
Expression is strongly increased in the presence of cycloheximide, imazalil, fenarimol, pisatin, itraconazole and 4-nitroquinoline oxide (4-NQO).
Leads to increased sensitivity to different classes of agricultural fungicides: cyprodinil (anilinopyrimidine), ketoconazole, prochloraz and propiconazole (azoles), carbendazim (a benzimidazole), fenpiclonil and fludioxonil (phenylpyrroles), fluazinam (a phenylpyridianine), azoxystrobin, kresoxim-methyl and trifloxystrobin (strobirulins), 4-nitroquinoline oxide (a mutagenic agent), camptothecin (a plant alkaloid) and the phytoalexin resveratrol (a stilbene).
Pleiotropic ABC efflux transporter involved in the basal level of drugs susceptibility, including antibiotics, azole fungicides and plant defense toxins (PubMed:9180695). Confers resistance to cycloheximide, chloramphenicol, imazalil, sulfomethuron methyl, pyrimethanil, quintozene, acriflavine, rhodamine 6G, the azoles fenarimol and miconazole, and to the dicarboximides iprodione and vinchlozolin (PubMed:9180695, PubMed:10931903).
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 uS2 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).
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.
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 cyclophilin-type PPIase family. PPIase D subfamily.
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.
Belongs to the complex I NDUFB11 subunit 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).
Both IUM domains are necessary for efficient binding to ubiquitin.
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.
Expression is induced by ethanol and ethyl acetate and is mediated by the specific transcriptional activator of genes of the acetate utilization pathway facB. Expression is also induced by low concentrations of acetate or propionate and under the controle of the facB transcription activator.
High affinity monocarboxylate transporter (MCT) involved in acetate uptake. Unlike other activities involved in acetate utilization, acpA is dispensable for growth on the acetate precursor ethanol.
Leads to reduced growth when acetate is used as sole carbon source at low concentration and in a high pH medium.
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).
Expression is increased at the beginning of the stationary phase of growth and reaches maximum in the early autolytic phase of growth.
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. Has also significant antifungal activity against various fungal species.
Belongs to the WD repeat DCAF13/WDSOF1 family.
Belongs to the V-ATPase G 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.
Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic (PubMed:2120195, PubMed:2110531). AatA catalyzes the exchange of the alpha-aminoadipyl side chain of isopenicillin N for phenylacetic acid to yield penicillin (PubMed:2120195, PubMed:2110531). This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively (By similarity). The penicillin biosynthesis occurs via 3 enzymatic steps, the first corresponding to the production of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) by the NRPS acvA. The tripeptide ACV is then cyclized to isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase penDE to yield penicillin in the peroxisomal matrix (By similarity).
The active form of the enzyme results from processing of the 40-kDa monomeric precursor to a heterodimer containing subunits of 11 and 29 kDa.
The pre-AAT protein is synthesized as 40 kDa precursor which is then self-processed into an 11 kDa (protein A) and a 29 kDa (protein B). The B protein carries AAT activity.
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 deadenlyation-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 FKBP-type PPIase family. FKBP2 subfamily.
Belongs to the eukaryotic ribosomal protein eL24 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 1 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 (By similarity). Also a component of the nuclear pore complex (By similarity).
Belongs to the dynein light chain family.
Homodimer. 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). Component of the nuclear pore complex (NPC). The nuclear pore complex 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.
Belongs to the archaeal rpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family.
Involved in cellular morphogenesis. Required for traffic between late Golgi and early endosomes, and for the normal structure and organization of the endoplasmic reticulum (By similarity). During the vegetative phase, contributes to the highly polarized hyphal growth. Required for the reproductive cycle. Involved in conidiophore initiation and differentiation. May have a role in controlling the balance between vegetative proliferation and developmental morphogenesis.
Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Catalyzes the conversion of L-ornithine to N(5)-hydroxyornithine, the first step in the biosynthesis of all hydroxamate-containing siderophores, such as the secreted triacetylfusarinine C (TAFC) involved in iron uptake and the intracellular iron storage compound desferriferricrocin (DFFC).
Essential for viabiliy. Grows only on siderophore-supplemented growth-medium, but shows decreased conidiation.
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 class-II DAHP synthase family.
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 tyrosyl-DNA phosphodiesterase family.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. BimC subfamily.
Important role in mitotic dividing cells. Microtubule motor required for spindle body separation.
ApdA has the following domain architecture: KS-MAT-DH-MT-KR-ACP-C-A-T-R (Probable). The apdA PKS module (domains KS to ACP) is responsible for the biosynthesis of the polyketide chain and catalyzes three Claisen condensations, as well as beta-keto processing and methylation (PubMed:20828130, PubMed:25494235). The downstream NRPS module contains the condensation (C), adenylation (A), and thiolation (T) domains and catalyzes the formation of the L-tyrosinyl-thioester and the amide linkage between L-tyrosinyl-thioester and the tetraketide (PubMed:20828130, PubMed:25494235). The bimodular assembly line is terminated with a putative reductase (R) domain that facilitates formation and release of the tetramic acid product (PubMed:20828130, PubMed:25494235).
Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of aspyridones (PubMed:17369821, PubMed:20828130, Ref.5). The polyketide-amino acid backbone preaspyridone A is first assembled by the PKS-NRPS hybrid apdA (PubMed:17369821, PubMed:20828130). The assembly of preaspyridone A is initiated by loading of malonyl-CoA onto apdA, followed by decarboxylation to yield the acetyl starter unit (PubMed:20828130). The growing polyketide chain then elongates into a tetraketide (PubMed:20828130). The adpA PKS module catalyzes three Claisen condensations, as well as beta-keto processing and methylation (PubMed:17369821, PubMed:20828130). Alpha-methylation step during polyketide synthesis is a prerequisite and a key checkpoint for chain transfer between PKS and NRPS modules (PubMed:25494235). The downstream NRPS module contains the condensation (C), adenylation (A), and thiolation (T) domains and catalyzes the incorporation of tyrosine via the formation of the L-tyrosinyl-thioester and the amide linkage between L-tyrosinyl-thioester and the tetraketide (PubMed:20828130). The bimodular assembly line is terminated with a reductase (R) domain that facilitates formation and release of the tetramic acid product (PubMed:20828130). Because apdA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase apdC (PubMed:17369821, PubMed:20828130, Ref.5). ApdC appears to operate with different stereoselectivity in different PKS cycle (Ref.5). Combined with apdC, apdA is proposed to synthesize preaspyridone A via about 20 enzymatic steps (PubMed:20828130). A number of oxidative steps performed successively by the cytochrome P450 monooxygenases apdE and apdB are required for the conversion of preaspyridone A to aspyridone A (PubMed:17369821). The cytochrome P450 monooxygenase apdE is responsible for the oxidative dephenylation of preaspyridone A (Ref.5). Finally, the predicted FAD-dependent monooxygenase apdD and the acyl-CoA dehydrogenase apdG may be involved in the transformation of aspyridone A into aspyridone B (PubMed:17369821) (Probable).
In the C-terminal section; belongs to the NRP synthetase family.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family.
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.
Mediator of diverse signals that repress RNA polymerase III transcription. Inhibits the de novo assembly of TFIIIB onto DNA.
Decreases the production of aspercryptin by more than 80% but increases the titer of aspercryptin with Ile replaced by Val more than six-fold (PubMed:26563584).
Part of the gene cluster that mediates the biosynthesis of aspercryptins, linear lipopeptides built from six amino acids including 2 highly unusual and nonproteogenic amino acids, 2-amino-octanoic acid (2aoa) and 2-amino-dodecanol (2adol) (PubMed:23248299, PubMed:27310134, PubMed:26563584). The core structure of aspercryptins is as follows: Ser/Ala-Thr-Ile/Val-2aoa-Aasn-2adol (PubMed:27310134). The first step of aspercryptin biosynthesis is the generation of the fatty acid precursors, octanoic and dodecanoic acids, by the FAS subunits atnF and atnM (PubMed:27310134, PubMed:26563584). The fatty acid precursors are likely transformed into the corresponding alpha-amino fatty acids in three steps (PubMed:27310134, PubMed:26563584). First, they are hydroxylated by the cytochrome P450 monooxygenase atnE, then oxidized to the corresponding alpha-keto acids by the NAD(P)-dependent oxidoreductase atnD, and finally converted to the alpha-amino fatty acids by the PLP-dependent aminotransferases atnH or atnJ (PubMed:27310134, PubMed:26563584). the alpha-amino fatty acids, 2-amino-octanoic and 2-amino-dodecanoic acids, are recognized, activated, and covalently tethered to the NRPS atnA by its fourth and sixth adenylation domains (PubMed:27310134). The second module of atnA is the Thr module and contains an epimerase (E) domain responsible for the epimerization of Thr to D-allo-Thr (PubMed:26563584). Additionally, despite atnA having only one epimerase domain, the first amino acid of aspercryptin A1 is D-Ser, suggesting that serine is either loaded directly as D-Ser on the first module or that the epimerase domain in the threonine module epimerizes both L-Ser and L-Thr (PubMed:27310134). After condensation of the hexapeptide of aspercryptin, the C-terminal reductase (TE) domain might be involved in the reductive release and production of the aldehyde hexapeptide (PubMed:26563584). Further reduction would generate aspercryptins (PubMed:27310134, PubMed:26563584). The variety of aspercryptins produced reflects the flexibiliy of the atnA NRPS, allowing incorporation of alanine instead of serine, valine for isoleucine, and a C10 fatty amino alcohol instead of the C12 version (PubMed:27310134). AtnB seems to be involved in the selectivity for Ile versus Val by the third module (PubMed:26563584). Moreover, type B, C and D aspercryptins have an additional N-terminal cichorine, acetyl and propionyl group respectively (PubMed:27310134).
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. NOG subfamily.
Belongs to the SMC family. SMC6 subfamily.
Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.
Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of aspercryptins, linear lipopeptides built from six amino acids including 2 highly unusual and nonproteogenic amino acids, 2-amino-octanoic acid (2aoa) and 2-amino-dodecanol (2adol) (PubMed:23248299, PubMed:27310134, PubMed:26563584). The core structure of aspercryptins is as follows: Ser/Ala-Thr-Ile/Val-2aoa-Asn-2adol (PubMed:27310134). The first step of aspercryptin biosynthesis is the generation of the fatty acid precursors, octanoic and dodecanoic acids, by the FAS subunits atnF and atnM (PubMed:27310134, PubMed:26563584). The fatty acid precursors are likely transformed into the corresponding alpha-amino fatty acids in three steps (PubMed:27310134, PubMed:26563584). First, they are hydroxylated by the cytochrome P450 monooxygenase atnE, then oxidized to the corresponding alpha-keto acids by the NAD(P)-dependent oxidoreductase atnD, and finally converted to the alpha-amino fatty acids by the PLP-dependent aminotransferases atnH or atnJ (PubMed:27310134, PubMed:26563584). the alpha-amino fatty acids, 2-amino-octanoic and 2-amino-dodecanoic acids, are recognized, activated, and covalently tethered to the NRPS atnA by its fourth and sixth adenylation domains (PubMed:27310134). The second module of atnA is the Thr module and contains an epimerase (E) domain responsible for the epimerization of Thr to D-allo-Thr (PubMed:26563584). Additionally, despite atnA having only one epimerase domain, the first amino acid of aspercryptin A1 is D-Ser, suggesting that serine is either loaded directly as D-Ser on the first module or that the epimerase domain in the threonine module epimerizes both L-Ser and L-Thr (PubMed:27310134). After condensation of the hexapeptide of aspercryptin, the C-terminal reductase (TE) domain might be involved in the reductive release and production of the aldehyde hexapeptide (PubMed:26563584). Further reduction would generate aspercryptins (PubMed:27310134, PubMed:26563584). The variety of aspercryptins produced reflects the flexibiliy of the atnA NRPS, allowing incorporation of alanine instead of serine, valine for isoleucine, and a C10 fatty amino alcohol instead of the C12 version (PubMed:27310134). AtnB seems to be involved in the selectivity for Ile versus Val by the third module (PubMed:26563584). Moreover, type B, C and D aspercryptins have an additional N-terminal cichorine, acetyl and propionyl group respectively (PubMed:27310134).
Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes like acuF, acuG and acuN.
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.
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 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.
Belongs to the eukaryotic RPA43 RNA polymerase subunit family.
Belongs to the proteasome subunit S3 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 eukaryotic ribosomal protein eS26 family.
Accepts electrons from ETF and reduces ubiquinone.
Belongs to the glycosyl hydrolase 27 family.
Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides.
Plays a central role in chromosome cohesion during cell division by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms.
Belongs to the major facilitator superfamily. Nitrate/nitrite porter (TC 2.A.1.8) family.
Belongs to the fatty acyl-CoA reductase family.
Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.
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.
Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP.
Decreases strongly intracellular carboxypeptidase activity.
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).
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.
Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative (PubMed:20139316, PubMed:21351751, PubMed:22730213). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG (PubMed:20139316). The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG (PubMed:20139316). The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone by mdpH-1 and mdpH-2 (PubMed:20139316). Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751). These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin (PubMed:22730213). Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps (PubMed:22730213).
Impairs the production of monodictyphenone, but leads to the accumulation of endocrocin (PubMed:20139316, PubMed:21351751).
Reduces the amounts of DHMBA produced and strongly reduces the production of yellow pigmentation.
Transcription factor that coregulates the expression of the gene cluster that mediates the biosynthesis of the antibiotic 2,4- dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives (PubMed:23001671). Specifically positively regulates the expression of the FAD-dependent oxidoreductase dbaF (PubMed:23001671).
Belongs to the DNA polymerase delta/II small subunit 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.
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.
Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the polyenes aspernidgulenes (PubMed:30302871). The carbon backbone of aspernidgulenes is synthesized by the HR-PKS sdgA, which accepts acetyl-CoA as the starter unit and performs malonyl-CoA extensions as well as regioselective methylation and reduction (PubMed:30302871). The resulting nonaketide offloads the HR-PKS by intramolecular lactonization to yield the 5,6-dihydro-alpha-pyrone-containing hexaenoic acids preaspernidgulene A1 and A2 (PubMed:30302871). The FAD-dependent monooxygenase sdgC then installs the first epoxide on the penultimate double bond (PubMed:30302871). Subsequently, the FAD-dependent monooxygenase sdgF presumably generates a ketone intermediate through Meinwald rearrangement involving a hydride shift (PubMed:30302871). Next, sdgC introduces another epoxide on the last olefin of the ketone intermediate after E/Z isomerization (PubMed:30302871). The epoxide hydrolase sdgD then catalyzes stereospecific cyclization of the 5,6-dihydro-alpha-pyrone and opening of the epoxide ring to form an oxygenated trimethylcyclopentanone and an oxabicyclo[2.2.1]heptane unit (PubMed:30302871). Finally, the bicyclic unit undergoes hydrolytic cleavage, either spontaneously or catalyzed by sdgD, to assemble the dimethyl-gamma-lactone moiety in aspernidgulene A1 (PubMed:30302871).
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.
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).
In the 2nd section; belongs to the type-I 3-dehydroquinase family.
In the N-terminal section; belongs to the shikimate kinase family.
Interacts with qutA; transcriptional activator of the quinate utilization pathway genes.
Is homologous throughout its length with the C-terminal 3 domains of the pentafunctional AROM protein. The function of the 2 C-terminal domains may be to act as a molecular sensor that detects the presence of quinate pathway intermediates as a prerequisite for the presumed conformational changes necessary for the control of transcription regulation.
Multi-domain repressor protein that negatively regulates transcription of the quinate utilization pathway genes. May mediate its repressor activity by binding directly to the qutA activator protein.
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone (PubMed:23706169). The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non-reducing polyketide synthase pkfA (PubMed:22510154). Hydroxylation, methylation of one of the phenol groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E (PubMed:23706169). The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable).
Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
Belongs to the ERCC1/RAD10/SWI10 family.
Belongs to the methyltransferase superfamily.
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.
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. Active against carboxymethylcellulose, beta-glucan and lichenan.
Belongs to the eukaryotic ribosomal protein eS10 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.
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).
Constitutively expressed throughout the vegetative cell cycle.
Belongs to the aerobic coproporphyrinogen-III oxidase family.
Expression is strongly increased in the presence of cycloheximide, imazalil, itraconazole, hygromycin, and 4-nitroquinoline oxide (4-NQO).
Pleiotropic ABC efflux transporter involved in the protection of the cells against a wide range of toxic compounds.
Produces partial defects in sexual reproduction and suppresses an apsA deletion mutation. Changes the colony morphology and inhibits sexual spore formation.
Belongs to the actin-binding proteins ADF family.
Belongs to the eukaryotic ribosomal protein eL37 family.
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.
Polyketide synthase; part of the gene cluster that mediates the biosynthesis of emericellamides, secondary metabolites acting as antibiotics (PubMed:18559263). The biosynthesis of emericellamides initiates from the highly reducing polyketide synthase easB which catalyzes the formation of the linear polyketide chain (PubMed:18559263). EasB produces several polyketides that can be further processed by the downstream enzymes (PubMed:18559263). The polyketides are released from easB as linear polyketide carboxylic acids, which are converted to CoA thioesters by the acyl-CoA ligase easD (PubMed:18559263). The substrates are then loaded onto the acyltransferase easC, which shuttles them to the first thiolation (T) domain of the nonribosomal peptide synthetase easA (PubMed:18559263). EasA then performs condensation of the polyketides with one glycine, two alanine, one valine and one leucine residues (PubMed:18559263). A last step of cyclization leads to the production of emericellamides (PubMed:18559263).
Belongs to the methyltransferase superfamily. METL family.
Oxidoreductase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:8643646). The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK (PubMed:8962148). The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (PubMed:8643646) (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF (PubMed:10618248). 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG (PubMed:24957370). The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme (PubMed:24957370). The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone (PubMed:10618248). The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone (PubMed:24957370). The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) (PubMed:24957370). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) (PubMed:8999832). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin (PubMed:7486998). The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin (PubMed:24957370). The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP (PubMed:8900026).
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.
Impairs the synthesis of austinol and dehydroaustinol and accumulates the intermediate compound 3,5-dimethylorsellinic acid (PubMed:22329759).
Polyprenyl transferase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725).
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.
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.
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.
Interacts with ODC and thereby sterically blocks ODC homodimerization.
Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimer, and targets the monomers for ubiquitin-independent proteolytic destruction by the 26S proteasome.
ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.
Probably involved in the biogenesis of the COX complex.
Abolishes growth in the presence of gliotoxin (PubMed:32667960). Leads to reduced growth in the presence of the oxidative stress-inducing compounds allyl alcohol, t-butyl hydroperoxide, but not menadione (PubMed:32667960).
Transcription factor that is important for oxidative stress resistance and essential for gliotoxin (GT) self-protection through the regulation of a gene encoding a putative gliT homolog, even if E.nidulans does not produce gliotoxin itself.
Fatty acid synthase beta subunit; part of the pki gene cluster that mediates the biosynthesis of 2,4-dihydroxy-3-methyl-6-(2-oxoundecyl)benzaldehyde (PubMed:22510154). The first step in the pathway is the generation of the decanoyl starter unit by the FAS composed of subunits pkiB and pkiC, which is then transferred directly from the FAS to the SAT domain of the non-reducing polyketide synthase pkiA (PubMed:22510154). PkiA condenses the decanoyyl starter unit with 4 malonyl-CoA units and performs one methylation step to yield 2,4-dihydroxy-3-methyl-6-(2-oxoundecyl)benzaldehyde (PubMed:22510154).
Acetate induction mediated by the amdA regulatory gene.
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 cyclophilin-type PPIase family. PPIase H subfamily.
Belongs to the fungal Na(+)/H(+) exchanger family.
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).
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.
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).
In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.
Belongs to the RNA 3'-terminal cyclase family. Type 2 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 (By similarity).
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.
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).
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.
Belongs to the nucleoporin Nup85 family.
Component of the nuclear pore complex (NPC).
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 protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.
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). Also degrades suberin, a specialized macromolecule found in the cell wall of various plant tissues (Probable).
Induced during growth on cutin, in a manner dependent on transcription factors FarA and FarB (PubMed:30863878). Induced during growth on suberin (PubMed:25043916). Induced during growth on the lipidic carbon sources 16-hydroxyhexadecanoic acid and propyl ricinoleate (synthetic cutin monomers), triacetin and triesterate (triglycerides), and olive oil (PubMed:30863878). Repressed during growth on glucose (PubMed:30863878).
Transcription factor; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) (PubMed:22506079, PubMed:27098256). Acts as a positive regulator for the cluster gene (PubMed:22506079). Down-regulates the expression of the penicillin gene cluster, two putative polyketide clusters, and one putative nonribosomal peptide cluster (PubMed:22506079).
Fatty acid synthase beta subunit; part of the gene cluster that mediates the biosynthesis of aspercryptins, linear lipopeptides built from six amino acids including 2 highly unusual and nonproteogenic amino acids, 2-amino-octanoic acid (2aoa) and 2-amino-dodecanol (2adol) (PubMed:23248299, PubMed:27310134, PubMed:26563584). The core structure of aspercryptins is as follows: Ser/Ala-Thr-Ile/Val-2aoa-Asn-2adol (PubMed:27310134). The first step of aspercryptin biosynthesis is the generation of the fatty acid precursors, octanoic and dodecanoic acids, by the FAS subunits atnF and atnM (PubMed:27310134, PubMed:26563584). The fatty acid precursors are likely transformed into the corresponding alpha-amino fatty acids in three steps (PubMed:27310134, PubMed:26563584). First, they are hydroxylated by the cytochrome P450 monooxygenase atnE, then oxidized to the corresponding alpha-keto acids by the NAD(P)-dependent oxidoreductase atnD, and finally converted to the alpha-amino fatty acids by the PLP-dependent aminotransferases atnH or atnJ (PubMed:27310134, PubMed:26563584). the alpha-amino fatty acids, 2-amino-octanoic and 2-amino-dodecanoic acids, are recognized, activated, and covalently tethered to the NRPS atnA by its fourth and sixth adenylation domains (PubMed:27310134). The second module of atnA is the Thr module and contains an epimerase (E) domain responsible for the epimerization of Thr to D-allo-Thr (PubMed:26563584). Additionally, despite atnA having only one epimerase domain, the first amino acid of aspercryptin A1 is D-Ser, suggesting that serine is either loaded directly as D-Ser on the first module or that the epimerase domain in the threonine module epimerizes both L-Ser and L-Thr (PubMed:27310134). After condensation of the hexapeptide of aspercryptin, the C-terminal reductase (TE) domain might be involved in the reductive release and production of the aldehyde hexapeptide (PubMed:26563584). Further reduction would generate aspercryptins (PubMed:27310134, PubMed:26563584). The variety of aspercryptins produced reflects the flexibiliy of the atnA NRPS, allowing incorporation of alanine instead of serine, valine for isoleucine, and a C10 fatty amino alcohol instead of the C12 version (PubMed:27310134). AtnB seems to be involved in the selectivity for Ile versus Val by the third module (PubMed:26563584). Moreover, type B, C and D aspercryptins have an additional N-terminal cichorine, acetyl and propionyl group respectively (PubMed:27310134).
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).
Serine hydrolase involved in the detoxification of formaldehyde.
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.
Plays a central role as a glucosyl donor in cellular metabolic pathways.
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.
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).
Nuclear serine protease which mediates apoptosis.
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).
Probable esterase; part of the gene cluster that mediates the biosynthesis of asperfuranone, a probable antitumor agent (PubMed:19199437). The polyketide synthase afoG is responsible for producing the 3,5-dimethyloctadienone moiety from acetyl-CoA, three malonyl-CoA, and two S-adenosyl methionines (SAM) (PubMed:19199437). The 3,5-dimethyloctadienone moiety is then loaded onto the SAT domain of afoE and extended with four malonyl-CoA and one SAM, which leads to the formation of 2,4-dihydroxy-6-(5,7-dimethyl-2-oxo-trans-3-trans-5-nonadienyl)-3-methylbenzaldehyde (compound 2) after reductive release and aldol condensation (PubMed:19199437). AfoD is the next enzyme in the biosynthesis sequence and hydroxylates the side chain at the benzylic position of compound 2 (PubMed:19199437). After benzylic hydroxylation, a furan ring is formed after five-member ring hemiacetal formation and water elimination (PubMed:19199437). AfoF and afoC are proposed to oxidize the R-diketone proton and to reduce the unconjugated carbonyl group, respectively, to generate asperfuranone (PubMed:19199437). Since no intermediates could be isolated from afoF and afoC deletants, the sequence of these two enzymes is not fully understood (PubMed:19199437). Moreover, since afoC deletant still produces a small amount of asperfuranone, other endogenous oxidoreductases might catalyze the same reaction with much less efficiency (PubMed:19199437).
Belongs to the amino acid-polyamine-organocation (APC) superfamily. YAT (TC 2.A.3.10) family.
Required for high-affinity proline transport.
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.
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.
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.
Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage.
Belongs to the tRNA(His) guanylyltransferase family.
Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. May participate in merging the COX1 and COX2 assembly lines.
Belongs to the eukaryotic ribosomal protein eS8 family.
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).
Belongs to the proteasome subunit p55 family.
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.
Strongly decreases the production of austinol and dehydroaustinol (PubMed:22329759).
Belongs to the complex I NDUFB3 subunit family.
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, methyltransferase domains (responsible for amino acid methylation) are present within the NRP synthetase. AsqK has the following architecture:A-T-C-A-M-T-C.
Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins (PubMed:25251934). The first stage is catalyzed by the nonribosomal pepdide synthetase asqK that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (PubMed:25251934). AsqK is also able to use anthranilic acid and L-phenylalanine as substrates to produce cyclopeptin, but at a tenfold lower rate (PubMed:25251934). 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase asqJ through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (PubMed:25251934, PubMed:26553478). AsqJ also converts its first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin (PubMed:25251934). AsqJ is a very unique dioxygenase which is capable of catalyzing radical-mediated dehydrogenation and epoxidation reactions sequentially on a 6,7-benzo-diazepinedione substrate in the 4'-methoxyviridicatin biosynthetic pathway (PubMed:25251934). AsqJ is also capable of converting cyclopeptin into dehydrocyclopeptin (PubMed:25251934). The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI (PubMed:30026518). Cyclopenin can also be converted into viridicatin by asqI (PubMed:30026518). 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase asqH1 then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase asqF to yield conjugated aryl diene (By similarity). The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase asqH2 to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain (By similarity). The FAD-dependent monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin (PubMed:30026518). Finally, after dehydratation of the epoxide at C3 by asqC, the quinolone epoxide rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring system in aspoquinolone (PubMed:30026518).
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).
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.
Non-reducing polyketide synthase; part of the pkg gene cluster that mediates the biosynthesis of dihydrocitreoisocoumarin and 6,8-dihydroxy-3-(2-oxopropyl)-isocoumarin (PubMed:22510154). The non-reducing polyketide synthase pkgA performs the condensation of one acetyl-CoA starter unit with 6 and 5 malonyl-CoA units, respectively (PubMed:22510154). As pkgA lacks a releasing domain, the thioesterase pkgB is necessary to break the thioester bond and release dihydrocitreoisocoumarin and 6,8-dihydroxy-3-(2-oxopropyl)-isocoumarin from pkgA (PubMed:22510154).
Belongs to the glycosyl hydrolase 74 family.
Oligoxyloglucan-reducing end-specific xyloglucanase involved in degradation of xyloglucans. Releases the first two glycosyl segments from oligoxyloglucans. Active against cotton xyloglucan, tamarind xyloglucan and tamarind xyloglucan oligomers (Probable).
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.
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.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily.
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.
Catalyzes the Claisen rearrangement of chorismate to prephenate (PubMed:10428795). Acts at the first branch point in the aromatic amino acid pathway where it steers biosynthesis towards phenylalanine and tyrosine, and away from tryptophan (By similarity).
Each dimer has two allosteric binding sites that can bind the regulatory effectors tryptophan or tyrosine (PubMed:10428795). Can bind either one tryptophan or one tyrosine, two tryptophan or two tyrosine or one tryptophan and one tyrosine, which differentially affect the catalytic activity (By similarity). Activated by tryptophan and subject to feedback inhibition by tyrosine (PubMed:10428795). In the presence of both tryptophan and tyrosine, the enzyme is in the activated state (By similarity).
Transcription factor that positively regulates the cluster that mediate the production of aspercryptins, linear lipopeptides built from six amino acids including 2 highly unusual and nonproteogenic amino acids, 2-amino-octanoic acid (2aoa) and 2-amino-dodecanol (2adol) (PubMed:27310134, PubMed:26563584).
Belongs to the ubiquitin-conjugating enzyme family. UEV subfamily.
Belongs to the MsrA Met sulfoxide reductase family.
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
Dehydratase; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins (PubMed:25251934, PubMed:28114276). The first stage is catalyzed by the nonribosomal pepdide synthetase asqK that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (PubMed:25251934). AsqK is also able to use anthranilic acid and L-phenylalanine as substrates to produce cyclopeptin, but at a tenfold lower rate (PubMed:25251934). 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase asqJ through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (PubMed:25251934, PubMed:26553478). AsqJ also converts its first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin (PubMed:25251934). AsqJ is a very unique dioxygenase which is capable of catalyzing radical-mediated dehydrogenation and epoxidation reactions sequentially on a 6,7-benzo-diazepinedione substrate in the 4'-methoxyviridicatin biosynthetic pathway (PubMed:25251934). AsqJ is also capable of converting cyclopeptin into dehydrocyclopeptin (PubMed:25251934). The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI (PubMed:30026518). Cyclopenin can also be converted into viridicatin by asqI (PubMed:30026518). 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase asqH1 then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase asqF to yield conjugated aryl diene (By similarity). The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase asqH2 to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain (By similarity). The FAD-dependent monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin (PubMed:30026518). Finally, after dehydratation of the epoxide at C3 by asqC, the quinolone epoxide rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring system in aspoquinolone (PubMed:30026518).
FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of asperfuranone, a probable antitumor agent (PubMed:19199437). The polyketide synthase afoG is responsible for producing the 3,5-dimethyloctadienone moiety from acetyl-CoA, three malonyl-CoA, and two S-adenosyl methionines (SAM) (PubMed:19199437). The 3,5-dimethyloctadienone moiety is then loaded onto the SAT domain of afoE and extended with four malonyl-CoA and one SAM, which leads to the formation of 2,4-dihydroxy-6-(5,7-dimethyl-2-oxo-trans-3-trans-5-nonadienyl)-3-methylbenzaldehyde (compound 2) after reductive release and aldol condensation (PubMed:19199437). AfoD is the next enzyme in the biosynthesis sequence and hydroxylates the side chain at the benzylic position of compound 2 (PubMed:19199437). After benzylic hydroxylation, a furan ring is formed after five-member ring hemiacetal formation and water elimination (PubMed:19199437). AfoF and afoC are proposed to oxidize the R-diketone proton and to reduce the unconjugated carbonyl group, respectively, to generate asperfuranone (PubMed:19199437). Since no intermediates could be isolated from afoF and afoC deletants, the sequence of these two enzymes is not fully understood (PubMed:19199437). Moreover, since afoC deletant still produces a small amount of asperfuranone, other endogenous oxidoreductases might catalyze the same reaction with much less efficiency (PubMed:19199437).
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 GHMP kinase family. GalK subfamily.
Essential for vacuolar protein sorting. Required for vacuole biogenesis, stability and to maintain vacuole morphology.
Belongs to the lariat debranching enzyme family.
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 Mediator complex subunit 20 family.
Belongs to the uroporphyrinogen decarboxylase family.
Belongs to the Mrp/NBP35 ATP-binding proteins family.
Microtubule binding protein that promotes the stabilization of dynamic microtubules. Required for mitotic spindle formation (By similarity).
Chaperone required for the export of the chitin synthase chs3 from the endoplasmic reticulum.
Probable lysosomal cobalamin transporter. Required to export cobalamin from lysosomes allowing its conversion to cofactors.
Belongs to the universal ribosomal protein uS14 family.
Belongs to the acetolactate synthase small subunit 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 (By similarity). Constitutes the ATP-driven core of the motor and binds the precursor preprotein (By similarity).
Interacts with the Fe/S cluster assembly and transfer machinery (By similarity). Component of the PAM complex (By similarity).
Required for the assembly of iron-sulfur (Fe/S) clusters in mitochondria (By similarity). Assisted by the DnaJ-like co-chaperone jac1 and the nucleotide exchange factor mge1, it mediates ATP-dependent Fe-S cluster transfer from the scaffold proteins isu1/isu2 to grx5 (By similarity).
Subject to nitrate and nitrite induction, and nitrogen metabolite repression. CrnA expression is mediated by the products of nirA, areA, and niaD.
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).
Expressed in presence of xylose. Repressed in presence of glucose through the action of the creA transcription repressor.
Reduces growth on birchwod xylan, while growth is unaffected on D-xylose, xylitol and other carbon sources like D-glucose, L-arabinose or L-arabitol.
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. Binds to the DNA sequence 5'-GGNTAAA-3'.
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.
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. GliP has the following architecture: A-T-C-A-T-C-A-T-E-TE.
Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic (PubMed:2645274, PubMed:8277946, PubMed:9003303). The trimodular NRPS acvA produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine (PubMed:2645274). The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV (By similarity). Each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates (PubMed:2645274). The penicillin biosynthesis occurs via 3 enzymatic steps, the first corresponding to the production of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) by the NRPS acvA. The tripeptide ACV is then cyclized to isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase penDE to yield penicillin in the peroxisomal matrix (By similarity).
Belongs to the neutral ceramidase family.
May function both as a monomer and a homodimer.
Belongs to the WD repeat IPI3/WDR18 family.
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.
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).
May contribute to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity (By similarity).
Mg(2+) is required for catalysis and for stabilizing the dimer.
Belongs to the GTP cyclohydrolase I family.
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.
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.
Belongs to the phosphatase 2A regulatory subunit B family.
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.
Belongs to the pantothenate synthetase family.
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.
May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi.
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).
Belongs to the ribonucleoside diphosphate reductase small chain family.
Involved in the early part of the secretory 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.
Impairs the production of the xanthones shamixanthone, emericellin and epishamixanthone; and accumulates variecoxanthone A (PubMed:21351751).
Belongs to the PPP phosphatase family. PP-2A subfamily.
Belongs to the arsenical resistance-3 (ACR3) (TC 2.A.59) family.
Involved in the transport of siderophore enterobactin and so has a role in iron homeostasis.
Belongs to the eukaryotic ribosomal protein eL19 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 DASH complex DAM1 family.
Belongs to the metallo-beta-lactamase superfamily. RNA-metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:16844780). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (By similarity). Also degrades suberin, a specialized macromolecule found in the cell wall of various plant tissues (By similarity).
Constitutively expressed in a manner dependent on transcription factor FarB: levels are unaffected by varying lipidic or non-lipidic carbon source, or by oxidative stress.
Belongs to the mitochondrion-specific ribosomal protein mS29 family.
Belongs to the DNA/RNA non-specific endonuclease family.
Belongs to the DHHC palmitoyltransferase family. PFA5 subfamily.
Belongs to the proteasome subunit S11 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 pterin-4-alpha-carbinolamine dehydratase family.
Belongs to the eukaryotic ribosomal protein eL18 family.
Component of the ribosome quality control complex (RQC), composed of the E3 ubiquitin ligase ltn1, rqc1 and rqc2, as well as cdc48 and its ubiquitin-binding cofactors. RQC forms a stable complex with 60S ribosomal subunits.
Involved in spindle disassembly, degradation of ubiquitinated proteins and protein export from the endoplasmic reticulum to the cytoplasm. Acts as a chaperone that collects ubiquitinated substrates. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway. 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. Cdc48 may provide the mechanical force that dislodges the polyubiquitinated nascent peptides from the exit channel.
Mediates the transfer of lipids between membranes at organelle contact sites. May play a role in mitochondrial lipid homeostasis.
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 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 XPG/RAD2 endonuclease family. XPG subfamily.
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).
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.
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 ATPase epsilon chain family.
Belongs to the Mediator complex subunit 21 family.
eIF-5A seems to be the only eukaryotic protein to have a hypusine residue which is a post-translational modification of a lysine by the addition of a butylamino group.
Catalyzes the oxidation of various aldopyranoses and disaccharides on carbon-2 to the corresponding 2-keto sugars concomitant with the reduction of O(2) to H(2)O(2).
Belongs to the adaptor complexes medium subunit family. Delta-COP 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.
In the central section; belongs to the inositol 1,4,5-trisphosphate 5-phosphatase family.
Belongs to the endopolyphosphatase PPN1 family.
Catalyzes the hydrolysis of inorganic polyphosphate (polyP) chains of many hundreds of phosphate residues into shorter lengths.
Nonessential protein which may be part of a two-component regulatory system activated by changes in the extracellular environment.
Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A subfamily.
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.
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.
Not known. Probably involved in quinate metabolism.
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 ATPase delta chain family.
May associate with the eukaryotic translation initiation factor 3 (eIF-3) complex.
mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.
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 cyclin family. Cyclin AB subfamily.
Essential for the control of the cell cycle at the G2/M (mitosis) transition. Interacts with the CDC2 protein kinase to form MPF. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis.
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).
May participate in the translocation of oligosaccharide from the cytoplasmic side to the lumenal side of the endoplasmic reticulum membrane.
Required for multiple vacuole delivery pathways including the cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and endocytosis.
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.
Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
Belongs to the CSN7/EIF3M family. CSN7 subfamily.
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 (By similarity). The CSN complex seems to link protein degradation to sexual development. May be required for sporulation only at elevated temperatures.
Present in uninduced vegetative hyphae, induced conidiating cultures and in both conidiospores and ascospores.
Belongs to the threonine synthase family.
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.
This promotes the activity of RNA polymerase II.
Belongs to the Mediator complex subunit 11 family.
Belongs to the phytoene/squalene synthase family.
Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Active on paranitrophenyl-alpha-galactoside but not on raffinose, locust bean gum and gum guar.
Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Transcriptional coactivator that stimulates transcriptional activity by bridging regulatory proteins and TBP, thereby recruiting TBP to promoters occupied by DNA-binding regulators.
Pathway-specific regulatory gene of nitrate assimilation; it activates the transcription of the genes for nitrate and nitrite reductases (niaD and niiA).
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 phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type I sub-subfamily.
Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.
Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.
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 inorganic phosphate transporter (PiT) (TC 2.A.20) family.
Sodium-phosphate symporter which plays a fundamental housekeeping role in phosphate transport.
Belongs to the XRCC4-XLF family. XLF subfamily.
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.
Belongs to the SRP receptor beta subunit family.
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).
Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
Involved in the lipid remodeling steps of GPI-anchor maturation.
Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor.
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 flavin monoamine oxidase family.
Belongs to the replication factor A protein 3 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.
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins (PubMed:25251934). The first stage is catalyzed by the nonribosomal pepdide synthetase asqK that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (PubMed:25251934). AsqK is also able to use anthranilic acid and L-phenylalanine as substrates to produce cyclopeptin, but at a tenfold lower rate (PubMed:25251934). 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase asqJ through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (PubMed:25251934, PubMed:26553478). AsqJ also converts its first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin (PubMed:25251934). AsqJ is a very unique dioxygenase which is capable of catalyzing radical-mediated dehydrogenation and epoxidation reactions sequentially on a 6,7-benzo-diazepinedione substrate in the 4'-methoxyviridicatin biosynthetic pathway (PubMed:25251934). AsqJ is also capable of converting cyclopeptin into dehydrocyclopeptin (PubMed:25251934). The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI (PubMed:30026518). Cyclopenin can also be converted into viridicatin by asqI (PubMed:30026518). 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase asqH1 then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase asqF to yield conjugated aryl diene (By similarity). The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase asqH2 to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain (By similarity). The FAD-dependent monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin (PubMed:30026518). Finally, after dehydratation of the epoxide at C3 by asqC, the quinolone epoxide rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring system in aspoquinolone (PubMed:30026518).
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 nonaspanin (TM9SF) (TC 9.A.2) family.
Belongs to the universal ribosomal protein uL30 family.
Regulated by phosphoenolpyruvate substrate and allosteric effectors such as fructose 1,6 diphosphate and magnesium.
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.
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 ketol-acid reductoisomerase family.
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).
Belongs to the WD repeat PRL1/PRL2 family.
Involved in pre-mRNA splicing and required for cell cycle progression at G2/M.
Transcription factor required for protein utilization and degradation. Regulates transcription of major secreted proteases (By similarity).
Belongs to the Rieske iron-sulfur protein family.
The Rieske protein is a high potential 2Fe-2S protein.
Belongs to the clathrin light chain family.
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.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase 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 acetyltransferase family. GCN5 subfamily.
Belongs to the homoserine dehydrogenase family.
Increases the production of DHMBA completely loses the yellow color and instead produces red pigments (PubMed:23001671). Impairs sexual development and produces very few colorless but fertile sexual fruit bodies (cleistothecia) after 7 days of sexual growth (PubMed:23001671).
Belongs to the non-repetitive/WGA-negative nucleoporin family.
Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by PDX2. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Also plays an indirect role in resistance to singlet oxygen-generating photosensitizers.
Defects cause some indirect sensitivity to photosensitizers, due to the inability to synthesize pyridoxal 5'-phosphate. Indeed, pyridoxal 5'-phosphate is destroyed in the presence of photosensitizers, and cannot be synthesized in reaction.
Belongs to the mitochondrion-specific ribosomal protein mL49 family.
May interact with target proteins during translocation into the lumen of the endoplasmic reticulum. May protect unfolded target proteins against degradation and facilitate correct glycosylation.
Belongs to the mitochondrion-specific ribosomal protein mL41 family.
Belongs to the complex I 24 kDa subunit 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-129.
Belongs to the precorrin methyltransferase family.
Belongs to the eukaryotic ribosomal protein eL30 family.
Belongs to the NFYB/HAP3 subunit 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).
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 (By similarity). Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product (By similarity). 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 (By similarity). Occasionally, methyltransferase domains (responsible for amino acid methylation) are present within the NRP synthetase (By similarity). InpA has the following architecture: C-A-T-TE (PubMed:18804170).
Nonribosomal peptide synthase; part of the inp gene cluster that mediates the biosynthesis of fellutamide B, a mycotoxin that acts as a proteasome inhibitor (PubMed:18804170, PubMed:20952652, PubMed:27294372). In the first step of fellutabmide B biosynthesis, inpC activates 3-hydroxydodecanoic acid to generate 3-hydroxydodecanoyl-AMP that is then loaded onto the T0 domain of inpB (PubMed:27294372). The 3-hydroxydodecanoyl-S-phosphopantetheinyl-T0 is sequentially extended with L-Asn and L-Gln by the two CAT modules of inpB (PubMed:27294372). The linear lipodipeptide from inpB is then transferred onto inpA for the addition of the third amino acid, L-Leu (PubMed:27294372). Reductive releasing of the lipotripeptide by the TE domain of inpA produces (2S)-fellutamide B (PubMed:27294372). InpF might be involved in the release and transfer of the lipodipeptide from inpB to inpA (PubMed:27294372). The inp cluster-encoded proteasome subunit inpE confers resistance to internally produced fellutamides (PubMed:27294372). The MFS efflux transporter inpD may contribute to fellutamide resistance as well (PubMed:27294372).
Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
Belongs to the complex I NDUFA2 subunit family.
Required for pre-18S rRNA processing. May bind microtubules (By similarity).
Belongs to the snRNP Sm proteins family. SmF/LSm6 subfamily.
Belongs to the GST superfamily. Zeta family.
Induced by phenylalanine or phenylacetate. Not induced by glucose.
Belongs to the ferroportin (FP) (TC 2.A.100) family. SLC40A subfamily.
May be involved in iron transport and iron homeostasis.
Component of the mitochondrial large ribosomal subunit.
An additional intron is predicted in this sequence to correct a probable sequencing error.
Belongs to the formin homology family. BNI1 subfamily.
Involved in cytokinesis. Overexpression results in growth inhibition.
The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity).
Belongs to the mitochondrion-specific ribosomal protein mL43 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.
Belongs to the mitochondrion-specific ribosomal protein mL54 family.
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.
Interacts with the 40S ribosomal subunit.
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.
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 DASH complex SPC19 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.
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.
Branched-chain-amino-acid aminotransferase; part of the gene cluster that mediates the biosynthesis of aspercryptins, linear lipopeptides built from six amino acids including 2 highly unusual and nonproteogenic amino acids, 2-amino-octanoic acid (2aoa) and 2-amino-dodecanol (2adol) (PubMed:23248299, PubMed:27310134, PubMed:26563584). The core structure of aspercryptins is as follows: Ser/Ala-Thr-Ile/Val-2aoa-Asn-2adol (PubMed:27310134). The first step of aspercryptin biosynthesis is the generation of the fatty acid precursors, octanoic and dodecanoic acids, by the FAS subunits atnF and atnM (PubMed:27310134, PubMed:26563584). The fatty acid precursors are likely transformed into the corresponding alpha-amino fatty acids in three steps (PubMed:27310134, PubMed:26563584). First, they are hydroxylated by the cytochrome P450 monooxygenase atnE, then oxidized to the corresponding alpha-keto acids by the NAD(P)-dependent oxidoreductase atnD, and finally converted to the alpha-amino fatty acids by the PLP-dependent aminotransferases atnH or atnJ (PubMed:27310134, PubMed:26563584). the alpha-amino fatty acids, 2-amino-octanoic and 2-amino-dodecanoic acids, are recognized, activated, and covalently tethered to the NRPS atnA by its fourth and sixth adenylation domains (PubMed:27310134). The second module of atnA is the Thr module and contains an epimerase (E) domain responsible for the epimerization of Thr to D-allo-Thr (PubMed:26563584). Additionally, despite atnA having only one epimerase domain, the first amino acid of aspercryptin A1 is D-Ser, suggesting that serine is either loaded directly as D-Ser on the first module or that the epimerase domain in the threonine module epimerizes both L-Ser and L-Thr (PubMed:27310134). After condensation of the hexapeptide of aspercryptin, the C-terminal reductase (TE) domain might be involved in the reductive release and production of the aldehyde hexapeptide (PubMed:26563584). Further reduction would generate aspercryptins (PubMed:27310134, PubMed:26563584). The variety of aspercryptins produced reflects the flexibiliy of the atnA NRPS, allowing incorporation of alanine instead of serine, valine for isoleucine, and a C10 fatty amino alcohol instead of the C12 version (PubMed:27310134). AtnB seems to be involved in the selectivity for Ile versus Val by the third module (PubMed:26563584). Moreover, type B, C and D aspercryptins have an additional N-terminal cichorine, acetyl and propionyl group respectively (PubMed:27310134).
Eliminates approximately 40% of aspercryptin production (PubMed:26563584).
Fails to produce sterigmatocystin under conditions that supports production by wild-type. Able to grow without exogenous long-chain fatty acids.
Fatty acid synthase alpha subunit; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:8643646, PubMed:8962148). The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK (PubMed:8962148). The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (PubMed:8643646) (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF (PubMed:10618248). 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG (PubMed:24957370). The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme (PubMed:24957370). The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone (PubMed:10618248). The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone (PubMed:24957370). The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB) (PubMed:24957370). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA) (PubMed:8999832). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin (PubMed:7486998). The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin (PubMed:24957370). The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP (PubMed:8900026).
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 eukaryotic ribosomal protein eL15 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)).
Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Active against locust bean gum and gum guar (PubMed:16844780). Also has transglycosylation activity. Produces mainly mannopentaose and mannohexaose out of mannotetraose (PubMed:21867780, PubMed:24950755).
Belongs to the queuosine salvage protein family.
Transcription factor involved in regulation of gene cluster that mediates the biosynthesis of aspyridones (PubMed:17369821).
Putative mitochondrial redox protein which could be involved in the reduction of small toxic molecules.
Involved in pre-mRNA splicing and cell cycle control.
Belongs to the squalene monooxygenase family.
Belongs to the UPL family. K-HECT subfamily.
Belongs to the SMC family. SMC5 subfamily.
Belongs to the Orn/Lys/Arg decarboxylase class-II family.
Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
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.
Belongs to the small GTPase superfamily. Rab family.
Rab activation is generally mediated by a guanine exchange factor (GEF), while inactivation through hydrolysis of bound GTP is catalyzed by a GTPase activating protein (GAP).
Ypt/Rab-type GTPases are key regulators of membrane trafficking and intracellular vesicular transport. They act as molecular switches that convert between GTP-bound and GDP-bound states, and regulate virtually all steps of membrane traffic from the formation of the transport vesicle at the donor membrane to its fusion at the target membrane. In the GDP-bound state, Ypt proteins are predominantly cytosolic, solubilized through the interaction with a GDP dissociation inhibitor (GDI). In the GTP-bound state, the proteins are membrane bound and interact with specific effector proteins that select cargo, promote vesicle movement, or verify the correct site of fusion (By similarity). AvaA functions in vacuolar biogenesis (PubMed:12095681).
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).
Catalyzes the reversible hydration of CO(2) to H(2)CO(3). The main role may be to provide inorganic carbon for the bicarbonate-dependent carboxylation reactions catalyzed by pyruvate carboxylase, acetyl-CoA carboxylase and carbamoyl-phosphate synthetase (By similarity). Involved in osmoadaptation.
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 eukaryotic-type primase small subunit 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.
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 complex I 20 kDa subunit family.
Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
Regulator of type 1 phosphatases which maintains protein phosphatase activity under strict control.
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 class I-like SAM-binding methyltransferase superfamily. BUD23/WBSCR22 family.
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 NAD(P)-dependent epimerase/dehydratase family.
Belongs to the TAF9 family. CENP-S/MHF1 subfamily.
Highly induced during germination and drops to a low constant level throughout vegetative development. Repressed by ammonium. Down-regulated by endocytosis in responde to ammonia or the presence of cytosine.
This permease has a broad specificity towards purines, and also transports cytosine, but neither uracil nor thymine. Contributes very little in purine uptake. Its major role may be the uptake of cytosine.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.
Involved in chromosome segregation during meiosis and DNA damage repair.
Belongs to the F-actin-capping protein alpha subunit family.
Belongs to the chitin synthase family. Class III subfamily.
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.
Belongs to the TFIID complex together with the TBP-associated factors (TAFs). Binds DNA as monomer.
General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II.
Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
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.
Belongs to the carbohydrate esterase 1 (CE1) family. AxeA subfamily.
The C-terminal carbohydrate-binding module (CBM) extension found in some acetylxylan esterases from other species is absent.
Belongs to the uroporphyrinogen-III synthase family.
Component of the 66S pre-ribosomal particle.
Required for efficient assembly and nuclear export of the 60S ribosomal subunit.
Belongs to the GLI C2H2-type zinc-finger protein family.
C2H2-type zinc-finger transcription factor that controls the expression of the nonribosomal peptide synthases inpA and inpB, as well as of the other inp cluster-associated genes (PubMed:20952652, PubMed:27294372). Mediates also the expression of the asperfuranone biosynthesis gene cluster by binding to the afoA promoter (PubMed:20952652). Probably recognizes the 5'-CT/C/AAAAGGAT/AT/GG/CA-3' motif in the promoters of teget genes (PubMed:20952652).
FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins (PubMed:25251934). The first stage is catalyzed by the nonribosomal pepdide synthetase asqK that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin (PubMed:25251934). AsqK is also able to use anthranilic acid and L-phenylalanine as substrates to produce cyclopeptin, but at a tenfold lower rate (PubMed:25251934). 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase asqJ through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain (PubMed:25251934, PubMed:26553478). AsqJ also converts its first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin (PubMed:25251934). AsqJ is a very unique dioxygenase which is capable of catalyzing radical-mediated dehydrogenation and epoxidation reactions sequentially on a 6,7-benzo-diazepinedione substrate in the 4'-methoxyviridicatin biosynthetic pathway (PubMed:25251934). AsqJ is also capable of converting cyclopeptin into dehydrocyclopeptin (PubMed:25251934). The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI (PubMed:30026518). Cyclopenin can also be converted into viridicatin by asqI (PubMed:30026518). 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase asqH1 then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase asqF to yield conjugated aryl diene (By similarity). The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase asqH2 to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain (By similarity). The FAD-dependent monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin (PubMed:30026518). Finally, after dehydratation of the epoxide at C3 by asqC, the quinolone epoxide rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring system in aspoquinolone (PubMed:30026518).
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment (PubMed:18978088, PubMed:21866960). Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules (PubMed:18978088). Polyketide is subsequently hydrolyzed by the action of the hydrolase aptB into endocrocin-9-anthrone (PubMed:18978088). Endocrocin-9-anthrone is then oxidized into endocrocin by the monooxygenase aptC (PubMed:18978088). Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis cluster (PubMed:18978088). Finally, aptC or another endogenous oxygenase catalyzes additional oxidation steps to form asperthecin (PubMed:18978088).
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 DEAD box helicase family. DEAH subfamily. DDX11/CHL1 sub-subfamily.
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.
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.
Involved in maceration and soft-rotting of plant tissue. Active against citrus pectin.
Belongs to the complex I NDUFA5 subunit family.
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.
Eliminates the production of fellutamides (PubMed:27294372). Does not impair the production of asperfuranone (PubMed:20952652).
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 (By similarity). Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product (By similarity). 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 (By similarity). Occasionally, methyltransferase domains (responsible for amino acid methylation) are present within the NRP synthetase (By similarity). InpB has the following architecture: T0-C-A-T-C-A-T (PubMed:18804170).
Nonribosomal peptide synthase; part of the inp gene cluster that mediates the biosynthesis of fellutamide B, a mycotoxin that acts as a proteasome inhibitor (PubMed:18804170, PubMed:20952652, PubMed:27294372). In the first step of fellutabmide B biosynthesis inpC activates 3-hydroxydodecanoic acid to generate 3-hydroxydodecanoyl-AMP that is then loaded onto the T0 domain of inpB (PubMed:27294372). The 3-hydroxydodecanoyl-S-phosphopantetheinyl-T0 is sequentially extended with L-Asn and L-Gln by the two CAT modules of inpB (PubMed:27294372). The linear lipodipeptide from inpB is then transferred onto inpA for the addition of the third amino acid, L-Leu (PubMed:27294372). Reductive releasing of the lipotripeptide by the TE domain of inpA produces (2S)-fellutamide B (PubMed:27294372). InpF might be involved in the release and transfer of the lipodipeptide from inpB to inpA (PubMed:27294372). The inp cluster-encoded proteasome subunit inpE confers resistance to internally produced fellutamides (PubMed:27294372). The MFS efflux transporter inpD may contribute to fellutamide resistance as well (PubMed:27294372).
Belongs to the PAPS reductase family. CysH subfamily.
The NADP dependent reduction of PAPS into sulfite involves thioredoxin which probably plays the role of a thiol carrier.
Involved in the regulation of telomere length, clustering and has a specific role in telomere position effect (TPE).
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.
Barely detectable in asexual spores (conidia), disappears after germination, and starts to accumulate 10 hours after spore inoculation, throughout growth and conidiation.
By hydrogen peroxide, heat shock, paraquat, or uric acid catabolism but not by osmotic stress.
Belongs to the thiolase-like superfamily. HMG-CoA synthase family.
Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form HMG-CoA.
Belongs to the NiCoT transporter (TC 2.A.52) family.
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.
Part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725). AusS is necessary for austinoids production and may play a possible function as a regulator (By similarity).
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).
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.
Involved in pre-mRNA splicing and cell cycle progression. Required for the spliceosome assembly and initiation of the DNA replication (By similarity).
Required for normal levels of the cell wall 1,6-beta-glucan. Involved in a protein folding machinery chaperoning proteins acting in various physiological processes including cell wall synthesis and lysis of autophagic bodies (By similarity).
Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of cichorine, a phytotoxin active against knapweed, corn, and soybeans.
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 SLC29A/ENT transporter (TC 2.A.57) family.
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.
Belongs to the complex I 75 kDa subunit family.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
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.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type V subfamily.
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 protein kinase superfamily. CMGC Ser/Thr protein kinase family.
Has a role in a nucleosome assembly pathway that is required for the integrity of heterochromatin and proper chromosome segregation.
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.
Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
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).
3-hydroxy-3-methylglutaryl coenzyme A reductase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD) (PubMed:22506079, PubMed:27098256). Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors (PubMed:22506079, PubMed:27098256). The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes (PubMed:22506079, PubMed:27098256). Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene (PubMed:22506079, PubMed:27098256). The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable).
Belongs to the XPG/RAD2 endonuclease family.
The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Belongs to the cytochrome c oxidase subunit 6B family.
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation.
Belongs to the acetyltransferase family. ECO subfamily.
Belongs to the eukaryotic ribosomal protein eS30 family.
Expression is induced in mycelia grown in high iron medium or transferred from low iron medium into high iron medium, and repressed in mycelia grown in low iron medium or transferred from high iron medium into low iron medium (PubMed:9988696).
GATA-type transcription repressor that regulates iron- acquisition genes through specific binding GATA sequence elements of target promoters (PubMed:9988696, PubMed:11555288). 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:11555288). SreA targets include genes encoding a number of key iron-regulated factors such as those involved in siderophore biosynthesis (PubMed:11555288, PubMed:12196195, PubMed:12487628).
Leads to increased iron uptake (PubMed:9988696). leads to partial derepression of triacetylfusarinine C (TAFC) and fusigen production as well as to cellular accumulation of ferricrocin (FC) (PubMed:11555288). Leads also to increased oxidative stress (PubMed:11555288).
The conserved cystein-rich region (CRR) localized between the zinc fingers is also involved in DNA-binding and transcription repressor activity (By similarity).
May function as a GSI-related enzyme in synthesizing a small diffusible factor that acts as an extracellular signal directing asexual sporulation and perhaps other aspects of colony growth. May be involved in brlA activation (an early transcriptional regulator for conidiation specific gene).
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 (By similarity). Controls sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor.
Belongs to the major facilitator superfamily. TCR/Tet family.
Efflux pump; part of the gene cluster that mediates the biosynthesis of asperlin, a polyketide showing anti-inflammatory, antitumor and antibiotic activities (PubMed:30339758). Is probably involved in the efflux of asperlin (Probable).
Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.
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.
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.
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.
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.
Impairs the synthesis of austinol and dehydroaustinol and accumulates the intermediate compound austinolide (PubMed:22329759).
Required for 60S pre-ribosomal subunits export to the cytoplasm.
During the catalytic reaction, a sulfide is transferred from Cys-220 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.
Starch-active PMOs provide an expanded perspective on studies of starch metabolism and may have potential in the food and starch-based biofuel industries.
Starch-active polysaccharide monooxygenase that oxidizes the C1 position of starch substrates, but not in cellulose, chitin, polygalacturonan or esterified pectin, nor with Arabidopsis stem cell walls.
The CBM20 domain is involved in binding to starch.
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 (PubMed:18978088, PubMed:20479000).
Non-reducing polyketide synthase (NRPKS); part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment (PubMed:18978088, PubMed:21866960). Catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules (PubMed:18978088, PubMed:21866960). Through its product template (PT) domain, catalyzes the cyclization of the polyketide backbone via C6-C11 aldolcondensation (PubMed:20479000). Polyketide is subsequently hydrolyzed from the NRPKS by the action of the hydrolase aptB into endocrocin-9-anthrone (PubMed:18978088). Endocrocin-9-anthrone is then oxidized into endocrocin by aptC (PubMed:18978088). Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis cluster (PubMed:18978088). Finally, aptC or another endogenous oxygenase catalyzes additional oxidation steps to form asperthecin (PubMed:18978088).
Belongs to the DEAD box helicase family. DDX56/DBP9 subfamily.
Pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase.
Catalyzes the hydrolysis of inorganic orthophosphate from phytate.
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 fatty acid desaturase type 1 family. DEGS subfamily.
Delta(4)-fatty-acid desaturase which introduces a double bond at the 4-position in the long-chain base (LCB) of ceramides.
Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Active on paranitrophenyl-alpha-galactoside, raffinose, locust bean gum and gum guar.
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).
Iron/alpha-ketoglutarate-dependent dioxygenase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725).
Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.
Belongs to the eukaryotic ribosomal protein eL43 family.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. NCD subfamily.
Belongs to the eukaryotic-type N-acetylglucosamine kinase 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.
Involved in the catabolism of quinolinic acid (QA).
Belongs to the universal ribosomal protein uL24 family.
Belongs to the activator 1 large subunit family.
Catalyzes the liberation of alpha-xylose from the non-reducing terminal glucose of xyloglucan oligosaccharides.
Despite the presence of an amyR-binding consensus sequence in the promoter, is not activated by isomaltose.
Component of the GPI transamidase complex. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI.
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.
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.
Belongs to the protoporphyrinogen/coproporphyrinogen oxidase family. Protoporphyrinogen oxidase subfamily.
Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
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.
Forms a complex with an importin beta subunit (By similarity). Interacts with hsp70, hsp90, napB, nkuA, nudK, AN1413 and nimE (PubMed:17890114).
Import of proteins with classical NLS composed of one or two clusters of basic residues is initiated by binding to the importin alpha/beta heterodimer, where importin alpha acts as an adapter subunit to bridge NLS cargos to importin beta, which transports the whole complex through the nuclear envelope (PubMed:12684370). Involved in the nuclear accumulation of the light-dependent developmental regulator veA (PubMed:17163983, PubMed:19318129). Participates at different regulatory stages of asexual and sexual development, being required for the completion of both reproductive cycles with the formation of conidiospores and ascospores, respectively (PubMed:19318129). Mediates secondary metabolite gene expression with positive regulation of penicillin production and negative regulation of mycotoxin biosynthesis (PubMed:19318129).
BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation. They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (PubMed:2655931). Responsible for activating a set of genes whose products make up the final two conidial wall layers or direct their assembly and, through this activity, is responsible for acquisition of spore dormancy (PubMed:1986246, PubMed:2180753, PubMed:7704830).
Expression is induced during conidiation, after conidia had begun to form (PubMed:2823119). Positively regulated by abaA (PubMed:2655931). Negatively regulated by velC (PubMed:24587098).
Has an acidic N-terminus (AA 1-52) followed by a Ser-, Thr-, Pro-rich domain (AA 125-233) and a basic C-terminus (AA 461-555).
The wetA gene is activated only during conidiophore development, and its mRNA accumulates preferentially in mature conidia.
Required for nuclear membrane fusion during karyogamy.
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 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.
Ubiquitinated. Deubiquitinated by creB, probably to control its activity or amount (By similarity).
Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of aspyridones (PubMed:17369821, PubMed:20828130, Ref.5). The polyketide-amino acid backbone preaspyridone A is first assembled by the PKS-NRPS hybrid apdA (PubMed:17369821, PubMed:20828130). The assembly of preaspyridone A is initiated by loading of malonyl-CoA onto apdA, followed by decarboxylation to yield the acetyl starter unit (PubMed:20828130). The growing polyketide chain then elongates into a tetraketide (PubMed:20828130). The adpA PKS module catalyzes three Claisen condensations, as well as beta-keto processing and methylation (PubMed:17369821, PubMed:20828130). Alpha-methylation step during polyketide synthesis is a prerequisite and a key checkpoint for chain transfer between PKS and NRPS modules (PubMed:25494235). The downstream NRPS module contains the condensation (C), adenylation (A), and thiolation (T) domains and catalyzes the incorporation of tyrosine via the formation of the L-tyrosinyl-thioester and the amide linkage between L-tyrosinyl-thioester and the tetraketide (PubMed:20828130). The bimodular assembly line is terminated with a reductase (R) domain that facilitates formation and release of the tetramic acid product (PubMed:20828130). Because apdA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase apdC (PubMed:17369821, PubMed:20828130, Ref.5). ApdC appears to operate with different stereoselectivity in different PKS cycle (Ref.5). Combined with apdC, apdA is proposed to synthesize preaspyridone A via about 20 enzymatic steps (PubMed:20828130). A number of oxidative steps performed successively by the cytochrome P450 monooxygenases apdE and apdB are required for the conversion of preaspyridone A to aspyridone A (PubMed:17369821). The cytochrome P450 monooxygenase apdE is responsible for the oxidative dephenylation of preaspyridone A (Ref.5). Finally, the predicted FAD-dependent monooxygenase apdD and the acyl-CoA dehydrogenase apdG may be involved in the transformation of aspyridone A into aspyridone B (PubMed:17369821) (Probable).
Belongs to the thymidylate kinase family.
Belongs to the glutathione peroxidase family.
Required for nuclear positioning and completion of asexual development.
Belongs to the Mediator complex subunit 10 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.
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).
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).