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).
Belongs to the protein kinase superfamily.
Expressed in hyphae. Regulated by the EFG1 and TUP1 transcription factors.
GPI-anchored cell wall protein required for mating efficiency, biofilm formation, adhesion, filamentous growth, and oxidative stress tolerance. Involved in normal disseminated infection in a mouse systemic candidiasis model.
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 glycosyl hydrolase 31 family.
Belongs to the snRNP Sm proteins family.
Belongs to the heat shock protein 70 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 universal ribosomal protein uL16 family.
Belongs to the eukaryotic mitochondrial porin family.
Consists mainly of membrane-spanning sided beta-sheets.
Forms a channel through the cell membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective (By similarity).
Has antigenic properties. Elicits a specific immune response in systemic candidiasis human patients undergoing malignant hematological disorders.
Acts in the GPI biosynthetic pathway between GlcNAc-PI synthesis and GPI transfer to protein.
Up-regulated upon milbemycins A3 oxim derivative (A3Ox) treatment.
Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.
Belongs to the amino acid-polyamine-organocation (APC) superfamily. YAT (TC 2.A.3.10) family.
Belongs to the ribose-phosphate pyrophosphokinase family.
Belongs to the glucosamine/galactosamine-6-phosphate isomerase family.
Beta-glucan associated cell wall protein involved in cell wall structure. May serve as cross-linking or coat-forming wall protein.
Expressed in both yeast and hyphal cells at the same level, indicating that it has no morphological differential expression. Expression is slightly increased by fluconazole.
Leads to increased sensitivity to caspofungin, Congo red, calcofluor white, and zymolyase.
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.
Component of the PAN1 actin cytoskeleton-regulatory complex (By similarity). Interacts with PAN1 and CLN3.
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. Required for assembly of the cortical actin cytoskeleton and for hyphal growth.
Expression is regulated by NRG1 and MIG1.
Phosphorylated by the CDC28-CLN3 complex and by PRK1. CDC28-CLN3 phosphorylation regulates cortical actin patch dynamics, as well as PRK1 phosphorylation and SLA1 association with PAN1. Rapidly dephosphorylated upon hyphal induction.
The N-terminal SH3 domains are important for actin cytoskeleton assembly but not for localization.
Expression is induced during infection of reconstituted human oral epithelium. Expression is repressed by HOG1 and regulated by TEC1, EGF1, NTD80, ROB1, BRG1, and SSN6.
Belongs to the bacterial ribosomal protein bL27 family.
Belongs to the folylpolyglutamate synthase family.
Component of the pre-66S ribosomal particle.
Involved in the biogenesis of the 60S ribosomal subunit.
Belongs to the DNA/RNA non-specific endonuclease family.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB 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. 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.
Component of the cell wall involved in virulence which plays a role in the relationship between C.albicans and the host (By similarity). Involved in the regulation or assembly of chitin within the cell wall.
Expression is regulated upon white-opaque switch, during cell wall regeneration, and when cells are grown on lactate. Also up-regulated upon milbemycin A3 oxim derivative (A3Ox) treatment. Repressed by BCR1.
Leads to hypersensitivity to caspofungin.
Belongs to the nucleoporin interacting component (NIC) family.
Belongs to the glycosyl hydrolase 18 family. Chitinase class V subfamily.
Chitinase involved in the remodeling of chitin in the fungal cell wall. Plays a role in sporulation.
Belongs to the clathrin heavy chain family.
Copper ion-sensing transcription factor which activates transcription of the CTR1 copper transporter under low-copper conditions. Promotes filamentous and invasive growth.
Expression is inhibited in the presence of copper. Expression is increased in polymicrobial biofilms during coinfection with S.aureus.
Results in reduced growth on copper or iron depleted media and the inability to grow on media with a non-fermentable carbon source.
Belongs to the Mediator complex subunit 10 family.
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
Belongs to the phosphoglycerate mutase family.
CSA2 could be used as a new diagnostic marker of Candida albicans infection.
Expression is induced during hyphal growth, by ketoconazole, and nitric oxide. Expression is also regulated by RIM101, TSA1, HAP43 and BCR1.
Homodimer (PubMed:27617569). The possibility of a transient honotrimer assembly of the holo protein is not ruled out (PubMed:27617569).
Leads to defects in hemoglobin utilization as sole source of iron.
Secreted heme-binding protein involved in the utilization of iron from human hemoglobin during hyphal growth (PubMed:24796871, PubMed:27617569). May also play a role in non-hemoglobin iron utilization (PubMed:24796871). Heme transfer occurs between PGA7, RBT5 and CSA2 supporting a model in which the 3 CFEM proteins cooperate in a heme-acquisition system and form a cross-cell wall heme-transfer cascade (PubMed:27617569). The ability to acquire iron from host tissues is a major virulence factor of pathogenic microorganisms (PubMed:24796871).
The CFEM domain is involved in heme-binding and contains 8 cysteines and is found in proteins from several pathogenic fungi, including both human and plant pathogens (PubMed:27617569). The CFEM domain adopts a novel helical-basket fold that consists of six alpha-helices, and is uniquely stabilized by four disulfide bonds formed by its 8 signature cysteines (PubMed:27617569).
Belongs to the glycosyltransferase 39 family.
Impairs biofilm formation and shows reduced virulence in a mouse model of hematogenously disseminated candidiasis (HDC) and using reconstituted human epithelium (RHE).
Protein mannosyltransferase (PMT) involved in hyphal growth and drug sensitivity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1, PMT2 and PMT4 account for most of the protein-O-glycosylation activity, while PMT5 and PMT6 may specifically modulate a much narrower spectrum of target proteins. Accounts for the O-glycosylation of AXL2, responsible for bud site selection, as well as of the SEC20 t-SNARE component. O-glycosylation of SEC20 is essential for its stability. Required for biofilm formation.
Transcribed in the yeast form, but expression is increased two to threefold during hyphal induction. Also up-regulated more than twofold when PMT1 expression is impaired. MSB2 functions not only to secure basal levels of the PMT4 transcripts but is needed also for up-regulation of both transcripts upon PMT1 inhibition. Repressed by BCR1.
Belongs to the NFYA/HAP2 subunit family.
Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes.
Belongs to the 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 protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.
Component of the SRB8-11 complex, a regulatory module of the Mediator complex.
Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The SRB8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II (By similarity).
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.
Belongs to the carbohydrate kinase pfkB family.
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.
Lacks conserved residue(s) required for the propagation of feature annotation.
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 class-III pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.
Sterol O-acyltransferase that catalyzes the formation of stery esters.
Component of the homotypic vacuole fusion and vacuole protein sorting (HOPS) complex. Component of the class C core vacuole/endosome tethering (CORVET) complex.
Belongs to the glycosyltransferase 4 family.
Belongs to the class-II aminoacyl-tRNA synthetase family.
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.
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
In presence of estrogen; decreases binding of host complement factor H protein and increases phagocytosis of the fungus by host (PubMed:34986357). Decreases virulence in presence of estrogen in a zebrafish larval model of infection (PubMed:34986357).
Interacts with human CFH/complement factor H; the interaction is direct and enables the pathogen to evade the host innate immune system (PubMed:23204165). Interacts with human CFHR1/complement factor H-related protein 1; the interaction is direct (PubMed:23204165). Interacts with human PLG/plasminogen; the interaction is direct and provides active plasmin on the surface of fungal cells (PubMed:23204165).
May catalyze the production and accumulation of glycerol during hyperosmotic stress conditions (By similarity). Glycerol acts as a osmoregulator that prevents loss of water and turgor of the cells (By similarity). Mediates evasion of the host innate immune system by binding inhibitory components of the host alternative complement system, in a manner dependent on estrogen-induced inhibition of EBP1 (PubMed:34986357, PubMed:23204165).
Mildly induced by estrogen (17beta-estradiol).
Beta-mannosyltransferase involved in cell wall biosynthesis. Required for beta-1,2-mannose transfer on phospholipomannan.
Attenuates tolerance to oxidative stress when PEX1 is also deleted (PubMed:27473887). Leads to hypersensitivity to ER stress and causes the loss of virulence when YSY6 is also deleted (PubMed:29544880).
The C-terminal 19 residues are removed 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 (By similarity). The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). With atg4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton (By similarity). Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production (By similarity). Participates also in membrane fusion events that take place in the early secretory pathway (By similarity). Regulates autophagy-related endoplasmic reticulum stress response (PubMed:29544880, PubMed:36328097). Also involved in resistance to oxidative stress (PubMed:27473887). Is essential for virulence (PubMed:29544880).
Belongs to the intradiol ring-cleavage dioxygenase family.
Belongs to the isocitrate and isopropylmalate dehydrogenases family.
Octamer of two non-identical subunits IDH1 and IDH2.
Belongs to the C/M/P thioester hydrolase family.
Belongs to the AB hydrolase superfamily. Lipase family.
May act as a negative regulator of salt tolerance.
Beta-mannosyltransferase involved in cell wall biosynthesis. Required for beta-1,2-mannose transfer on phospholipomannan. Required for pro-inflammatory response in macrophages through phospholipomannan-induced TNF-alpha production.
Leads to the production of phospholipomannan with short truncated oligomannosidic chain and impairs induction of TNF-alpha production in macrophages.
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.
Beta-mannosyltransferase involved in cell wall biosynthesis through beta-1,2-mannosylation of cell wall phosphopeptidomannan.
Expression is induced by HAP43 and down-regulated in an azole-resistant strain.
Induced after prolonged growth with antifungal drugs such as clotrimazole, miconazole, fluconazole, itraconazole, ketoconazole, terbinafine and fenpropimorph.
Sterol 14alpha-demethylase that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (PubMed:8647850, PubMed:9559662, PubMed:10393548, PubMed:28258218). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity). In filamentous fungi, during the initial step of this module, lanosterol (lanosta-8,24-dien-3beta-ol) can be metabolized to eburicol (By similarity). Sterol 14alpha-demethylase catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of both these sterols in the form of formate, and converts eburicol and lanosterol to 14-demethyleburicol (4,4,24-trimethylergosta-8,14,24(28)-trienol) and 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, respectively, which are further metabolized by other enzymes in the pathway to ergosterol (PubMed:8647850, PubMed:10393548, PubMed:28258218, PubMed:9559662). Can also use substrates not intrinsic to fungi, such as 24,25-dihydrolanosterol (DHL), producing 4,4-dimethyl-8,14-cholestadien-3-beta-ol, but at lower rates than the endogenous substrates (By similarity).
The catalytic activity is inhibited by the binding of azoles clotrimazole, miconazole, fluconazole, ketoconazole, oteseconazole (VT-1161), tetraconazole, the triazole SCH39304, and the triazole derivative ICI 153066.
Component of the nucleoplasmic and cytoplasmic pre-60S ribosomal particles.
Probable metalloprotease involved in proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Accompanies the pre-60S particles to the cytoplasm (By similarity).
Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Belongs to the mitochondrion-specific ribosomal protein mL53 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.
Exhibits increased colonization of the murine intestinal tract, a model of commensal colonization.
Transcription factor that regulates filamentous growth through repression of EFG1. Regulates the level of colonizing fungi, favoring commensalism as opposed to candidiasis.
Catalyzes the NAD(+)-dependent cleavage of saccharopine to L-lysine and 2-oxoglutarate, the final step in the alpha-aminoadipate (AAA) pathway for lysin biosynthesis.
The coordinates of this ORF in the reference genome reflect non-intron adjustments made to compensate for presumed sequencing errors.
Belongs to the HAD-like hydrolase superfamily. SerB family.
Belongs to the universal ribosomal protein uS10 family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Component of the small ribosomal subunit (PubMed:35613268). Mature ribosomes consist of a small (40S) and a large (60S) subunit (PubMed:35613268). The 40S subunit contains about 32 different proteins and 1 molecule of RNA (18S) (PubMed:35613268). The 60S subunit contains 45 different proteins and 3 molecules of RNA (25S, 5.8S and 5S) (PubMed:35613268).
Probable metalloprotease involved in proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Accompanies the pre-60S particles to the cytoplasm.
Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs.
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.
Belongs to the eukaryotic ribosomal protein eS17 family.
Belongs to the ABC transporter superfamily.
Is 10-fold down-regulated during log phase and strongly induced at the diauxic shift. Expression remains high during the postdiauxic phase and continues into stationary phase. Is also up-regulated during the presence of cadmium ions.
Leads to decreased sublethal intraperitoneal infection in mice.
Vacuolar multi-drug resistance ABC transporter that may be involved in the transport of bilirubin and glutathione conjugates (By similarity). Plays an important role in virulence.
Belongs to the mitochondrial carrier (TC 2.A.29) family.
Mitochondrial transporter that mediates uptake of thiamine pyrophosphate (ThPP) into mitochondria.
Belongs to the archaeal rpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Belongs to the eukaryotic ribosomal protein eL18 family.
Component of the large ribosomal subunit (PubMed:35613268). Mature ribosomes consist of a small (40S) and a large (60S) subunit (PubMed:35613268). The 40S subunit contains about 32 different proteins and 1 molecule of RNA (18S) (PubMed:35613268). The 60S subunit contains 45 different proteins and 3 molecules of RNA (25S, 5.8S and 5S) (PubMed:35613268).
Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.
Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA polymerase 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.
Associated with pre-ribosomal particles.
Belongs to the DEAD box helicase family. DDX51/DBP6 subfamily.
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Belongs to the threonine synthase family.
Belongs to the Mediator complex subunit 9 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 ATPase alpha/beta chains family.
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Belongs to the prefoldin subunit beta family.
Belongs to the glycosyl hydrolase 72 family.
Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall.
ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives.
Central component of the spindle assembly checkpoint which is a feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. Plays a key role in virulence, probably through cell cycle checkpoint functions, especially those monitoring the integrity of DNA and chromosome segregation, which might be required for the pathogen to repair damage caused by host defense.
Component of the mitotic checkpoint complex (MCC).
Quickly loses viability when treated with nocodazole, which causes disassembly of mitotic spindles. Exhibits increased frequency of chromosome loss and greatly reduced virulence in mice.
Mammalian nucleoside transport inhibitors dipyridamole and NBMPR inhibit adenosine transport by NUP.
Nucleoside permease that transports adenosine and guanosine. Does not show any transport activities towards cytidine, adenine, guanine, uridine, and uracil.
Predicted to be a substrate for cleavage by KEX2.
Belongs to the PI3/PI4-kinase family. Type III PI4K subfamily.
Belongs to the TRAPP small subunits family. BET3 subfamily.
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 archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family.
Belongs to the universal ribosomal protein uL23 family.
Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability.
Belongs to the AAA ATPase family. BCS1 subfamily.
Binds HTN3/histatin-5, a peptide from human saliva, and mediates its fungicidal activity.
May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum.
Belongs to the trans-sulfuration enzymes family.
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 carnitine/choline acetyltransferase family.
Belongs to the universal ribosomal protein uS8 family.
Component of the small ribosomal subunit (SSU) (By similarity). Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 32 different proteins and 1 molecule of RNA (18S). The 60S subunit contains 45 different proteins and 3 molecules of RNA (25S, 5.8S and 5S) (Probable).
Required for pre-18S rRNA processing. May bind microtubules (By similarity).
ATP-binding RNA helicase involved in ribosome assembly.
Associates with pre-ribosomal particles.
Belongs to the DEAD box helicase family. DDX27/DRS1 subfamily.
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. cAMP subfamily.
Leads to reduced cell size and to sensitivity to rapamycin, caffeine and sodium dodecyl sulfate. Attenuates the virulence of in a mouse model of systemic candidiasis.
Protein kinase that is part of growth control pathway which is at least partially redundant with the cAMP pathway (By similarity). Plays a role in filamentous growth and virulence. Prevents hypha formation specifically under hypoxia at high CO(2) levels. Required for chlamydospore formation, distinctive morphological feature of the fungal pathogen C.albicans that can be induced to form in oxygen-limited environments and has been reported in clinical specimens.
Belongs to the bacterial ribosomal protein bL36 family.
Belongs to the thiamine pyrophosphokinase family.
Although this enzyme participates in the selenocysteinyl-tRNA(Sec) biosynthesis pathway in many taxa, this pathway has been shown in PubMed:30742068 to be lost in dikarya.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.
Catalyzes the attachment of serine to tRNA(Ser) in a two-step reaction: serine is first activated by ATP to form Ser-AMP and then transferred to the acceptor end of tRNA(Ser).
Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Homodimer. The tRNA molecule binds across the dimer (By similarity).
Belongs to the DASH complex DAM1 family.
Component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore (By similarity).
The DASH complex oligomerizes to form rings that encircle the microtubules.
Required for the proteolytic cleavage of the transcription factor RIM101 in response to alkaline ambient pH.
Belongs to the ATP-dependent DNA ligase family.
Cell cycle-regulated. Expression peaks in late G1 and during the morphological transition.
Involved in ds DNA break (DSB) repair. Has a role in non-homologous integration (NHI) pathways where it is required in the final step of non-homologous end-joining (NHEJ). Not required for the repair of DSBs induced by ionizing radiation or UV light. Has an important role in morphogenesis, positively affecting the capacity to form hyphae.
Belongs to the sirtuin family. Class I subfamily.
Expression is up-regulated and increases progressively with hyphal development. Expression is inhibited by 2-dodecanol and decreased by allicin and fluconazole.
Leads to high frequency phenotypic switching, spontaneous hyphal growth, and decreased replicative lifespan. Shows also oxidatively damaged proteins even distribution between mother and daughter cells during division.
NAD-dependent deacetylase. Heterochromatin component that silences transcription at silent mating loci, telomeres and the ribosomal DNA, and that also suppresses recombination in the rDNA and extends replicative life span. It acts as a NAD-dependent histone deacetylase, which deacetylates 'Lys-9' and 'Lys-14' of Histone H3 and 'Lys-16' of Histone H4. Functions in the distribution of oxidatively damaged proteins during cell division. Mediates phenotypic switching.
Expression is induced by fluconazole and repressed by HAP43.
Component of the mitochondrial inner membrane i-AAA protease complex required for mitochondrial inner membrane protein turnover.
Component of the mitochondrial inner membrane i-AAA protease complex.
Involved in membrane organization. Involved in a novel pathway of export of proteins that lack a cleavable signal sequence. Non-classical export pathway functions also as an alternative clearance/detoxification pathway to eliminate damaged material, when the basic repair pathway is not sufficient (By similarity). Regulates actin organization and subsequent morphogenesis and pathogenesis.
Leads to decreased virulence and forms abnormal hyphae in mice. Shows defects in forming hyphae and invading low concentrations of agar but can invade well in higher agar concentrations.
Putative mitochondrial redox protein which could be involved in the reduction of small toxic molecules.
Belongs to the methylenetetrahydrofolate reductase family.
Belongs to the arsenical resistance-3 (ACR3) (TC 2.A.59) 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.
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.
Belongs to the universal ribosomal protein uL3 family.
Activity is completely abolished by Triton X-100, deoxycholate or Cu(2+), and partially inhibited by thiol reagents, rotenone and antimycin A (PubMed:6378256). The allylamine antimycotic agents naftifine and SF 86-327are potent inhibitors and show apparently non-competitive kinetics with respect to the substrate squalene (PubMed:3877503).
Belongs to the squalene monooxygenase family.
Impairs ergosterol production and leads to increased susceptibility to terbinafine (PubMed:15845783). Leads also to susceptibility to polyenes, nystatin and amphotericin B (PubMed:15845783). Impairs the localization of the membrane-bound transporter CDR1 (PubMed:15845783). Reduces the formation of hyphae (PubMed:15845783).
Squalene epoxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:9161422, PubMed:6378256, PubMed:3877503, PubMed:15845783). Erg1 catalyzes the epoxidation of squalene into 2,3-epoxysqualene (PubMed:9161422, PubMed:6378256, PubMed:3877503, PubMed:15845783). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable).
Belongs to the class VI-like SAM-binding methyltransferase superfamily. CHO2 family.
Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
Belongs to the RNA 3'-terminal cyclase family. Type 2 subfamily.
Belongs to the class-I aminoacyl-tRNA synthetase family.
Belongs to the sphingosine N-acyltransferase family.
Belongs to the Mediator complex subunit 21 family.
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.
Belongs to the RecA family. RAD51 subfamily.
Required both for recombination and for the repair of DNA damage caused by X-rays.
Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
Belongs to the universal ribosomal protein uL4 family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. BUD23/WBSCR22 family.
Belongs to the methyltransferase superfamily. METL family.
S-adenosyl-L-methionine-dependent methyltransferase.
Substrate-binding subunit (component A) of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane.
Belongs to the purine-cytosine permease (2.A.39) family.
Key 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 (Probable).
No visible phenotype. Cells lacking both RUB1 and CAND1 show defects in morphological, growth and protein degradation, consistent with a reduction in SCF ubiquitin ligase activity.
Belongs to the prokaryotic/mitochondrial release factor family.
Belongs to the CND2 (condensin subunit 2) family.
Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes.
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.
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.
Belongs to the iron/manganese superoxide dismutase family.
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
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).
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 twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space.
Belongs to the peptidase M28 family. M28B subfamily.
Belongs to the glycogen debranching enzyme family.
Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family.
Catalyzes the hydrolysis of ATP coupled with the transport of calcium.
Involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles.
Belongs to the glycosyltransferase group 1 family.
Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Mg(2+) is required for catalysis and for stabilizing the dimer.
The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that 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. It has an ATP-dependent proteolytic activity.
Belongs to the bacterial ribosomal protein bL33 family.
Belongs to the arrestin family. PalF/RIM8 subfamily.
Required for the proteolytic cleavage of the transcription factor RIM101 in response to alkaline ambient pH. Required for hyphal development.
Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome.
Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends.
Belongs to the STXBP/unc-18/SEC1 family.
Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.
Belongs to the UPL family. TOM1/PTR1 subfamily.
Belongs to the glycosyl hydrolase 5 (cellulase A) family.
Expression is down-regulated in absence of GOA1.
GPI-anchored cell wall protein involved in cell wall organization, hyphal growth, as well as in host-fungal interaction and virulence.
Belongs to the glycosyl hydrolase 76 family.
Induced by caspofungin. Expression is also regulated by SPF1.
Leads to decreased caspofungin sensitivity.
Required for normal synthesis of the cell wall and alkaline pH-induced hypha formation.
Belongs to the class I-like SAM-binding methyltransferase superfamily. MenG/UbiE family.
Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9.
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).
Beta-mannosyltransferase involved in cell wall biosynthesis. Required for the elongation of beta-mannose chains on the acid-labile fraction of cell wall phosphopeptidomannan.
Expression in regulated by TSA1 and repressed in rat catheter biofilm.
Impairs the elongation of beta-mannose chains on the acid-labile fraction of cell wall phosphopeptidomannan.
Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
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.
May negatively regulate the SNF1 kinase.
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.
In the C-terminal section; belongs to the NAGSA dehydrogenase family.
In the N-terminal section; belongs to the acetylglutamate kinase family.
Transcription elongation factor implicated in the maintenance of proper chromatin structure in actively transcribed regions.
Belongs to the JHDM3 histone demethylase family.
Belongs to the mitochondrion-specific ribosomal protein mL54 family.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type V subfamily.
Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH. Also inhibited by ADP.
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 universal ribosomal protein uL11 family.
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 cytidylyltransferase 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.
Belongs to the eukaryotic ribosomal protein eS19 family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (Probable). RPS19A is required for proper maturation of the small (40S) ribosomal subunit (By similarity).
Cell wall protein which mediates cell-cell and cell-substrate adhesion. Required for biofilm formation and plays a role in virulence.
Expressed in white cells. Transcription is regulated by the transcription factor EFG1 and up-regulated by alpha-pheromone, by host serum, in biofilms, and in high iron conditions. Repressed by BCR1 in a/a biofilms.
The N-terminal domain mediates haploid invasive growth and yeast cell-cell adhesion.
The regions containing tandem repeats are required to project the N-terminal region into the extracellular environment and to mediate adhesion to polystyrene and to host cells. In allele CaO19.8979, the N-terminal tandem repeat region is expended and contains up to 90 repeats and the C-terminal tandem repeat region has one more repeat.
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.
Ubiquitin-protein ligase which is mainly involved pre-mRNA splicing and DNA repair. Required for pre-mRNA splicing as component of the spliceosome.
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.
Belongs to the glycosyl hydrolase 16 family. CRH1 subfamily.
Extracellular glycosidase which plays an important role in fungal pathogenesis. Involved in cell wall assembly and regeneration, filamentation, and adherence to host cells.
Leads to increased susceptibility to cell wall-perturbing agents.
Unlike CRH11, CRH12 is down-regulated during cell wall regeneration. Also regulated by NRG1, TUP1, and RIM101.
Involved in protein synthesis. Involved in microtubule stabilization (By similarity).
Belongs to the amino acid/polyamine transporter 2 family.
The ERF2-ERF4 complex is a palmitoyltransferase specific for Ras proteins. Palmitoylates RAS2, which is required for its proper plasma membrane localization (By similarity).
Belongs to the UbiA prenyltransferase family.
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate.
Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family.
Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
Catalytic activity is higher with Mg(2+).
Catalyzes the synthesis of phosphatidylinositol (PtdIns) (PubMed:8740418). Required for proper membrane dynamics and cell wall integrity (PubMed:35227874).
Inhibited by calcium and zinc ions (PubMed:8740418). Inhibited by nucleoside triphosphates and diphosphates (PubMed:8740418).
Belongs to the acyl-CoA dehydrogenase 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.
Component of the 2-(3-amino-3-carboxypropyl)histidine synthase complex composed of DPH1, DPH2, DPH3 and a NADH-dependent reductase, predominantly CBR1.
Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase, predominantly CBR1 (By similarity). Facilitates the reduction of the catalytic iron-sulfur cluster found in the DPH1 subunit (By similarity).
Belongs to the 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.
In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis.
Belongs to the putative lipase ROG1 family.
Belongs to the ERCC1/RAD10/SWI10 family.
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Maintains high levels of reduced glutathione in the cytosol.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the glycosyltransferase 8 family.
Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.
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.
E2-like enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy and nucleophagy. Acts as an E2-like enzyme that catalyzes the conjugation of ATG12 to ATG5. ATG12 conjugation to ATG5 is required for proper localization of ATG8 to the preautophagosomal structure (PAS). Likely serves as an ATG5-recognition molecule (By similarity).
Expression is decreased upon fluphenazine treatment.
Belongs to the V-ATPase e1/e2 subunit family.
Component of the ASTRA chromatin remodeling machinery complex.
Component of the ASTRA complex involved in chromatin remodeling.
Belongs to the sulfate adenylyltransferase family.
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.
The oligomerization domain is distantly related to APS kinases, but it is not functional and does not bind APS. It is required for oligomerization of the enzyme, although the oligomerization state has no effect on the catalytic activity of the enzyme.
Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter.
Cell wall protein necessary for cell wall integrity. Plays only a minor role in hyphal morphogenesis and is not critical to biofilm formation.
Induced during cell well regeneration, by fluconazole, and in high iron conditions. Expression is also induced by TBF1 and repressed by SSK1, and CYR1 or RAS1.
Leads to an altered cell wall structure with a less electron dense inner layer of the cell wall, and a disorganized outer layer.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
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.
Expression is induced during phagocytosis by host macrophages (PubMed:15470236). Expression is also induced during biofilm development (PubMed:19527170, PubMed:21414038, PubMed:22265407).
High-affinity permease for basic amino acids arginine, lysine and histidine (PubMed:8299168, PubMed:9180275).
Expression is induced by HAP43 under low iron conditions.
Transcriptional regulator of the switch between 2 heritable states, the white and opaque states. These 2 cell types differ in many characteristics, including cell structure, mating competence, and virulence. Each state is heritable for many generations, and switching between states occurs stochastically, at low frequency. WOR2 is necessary for the stability of the opaque state phenotypic switching from the white to the opaque phase is a necessary step for mating. Plays a role in cell adhesion and pseudohyphal growth.
Belongs to the deoxyhypusine synthase family.
Leads to constitutive hyphal growth and avirulence in a mouse model.
Transcription regulator that functions in both the positive and negative regulation of filamentous growth, depending upon the environmental conditions. Recruits the TUP1/SSN6 general repression complex to achieve repression. Regulates genes encoding cell wall components that are specifically expressed in the filamentous forms such as HWP1, RBT1, HYR1, ECE1, ALS1, RBT4 and RBT5.
Belongs to the PPP phosphatase family. PP-Z subfamily.
ATP-dependent DNA helicase important for chromosome transmission and normal cell cycle progression in G(2)/M (By similarity). May have a role in changing DNA topology to allow the loading of proteins involved in maintaining sister chromatid cohesion in the vicinity of the centromeres (By similarity). Has a specific role in chromosome segregation during meiosis II (By similarity).
Belongs to the DEAD box helicase family. DEAH subfamily. DDX11/CHL1 sub-subfamily.
Component of the nuclear pore complex (NPC)-associated TREX-2 complex (transcription and export complex 2), composed of at least SUS1, SAC3, THP1, SEM1, and CDC31. TREX-2 contains 2 SUS1 chains. The TREX-2 complex interacts with the nucleoporin NUP1. Component of the 1.8 MDa SAGA transcription coactivator-HAT complex. SAGA is built of 5 distinct domains with specialized functions. Within the SAGA complex, SUS1, SGF11, SGF73 and UBP8 form an additional subcomplex of SAGA called the DUB module (deubiquitination module). Interacts directly with THP1, SAC3, SGF11, and with the RNA polymerase II.
Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex required for deubiquitination of H2B and for the maintenance of steady-state H3 methylation levels. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. May also be involved in cytoplasmic mRNA decay by interaction with components of P-bodies (By similarity).
Responsible for addition of the terminal mannose residues to the outer chain of core N-linked polysaccharides and to O-linked mannotriose. Implicated in late Golgi modifications (By similarity).
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.
Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.
Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
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 ribosomal protein P1/P2 family.
Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
In the C-terminal section; belongs to the trehalose phosphatase family.
In the N-terminal section; belongs to the glycosyltransferase 20 family.
Mediates the transfer of lipids between membranes at organelle contact sites. May play a role in mitochondrial lipid homeostasis.
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.
Adaptor protein complex 3 (AP-3) is a heterotetramer composed of 2 large adaptins, a medium adaptin and a small adaptin.
Belongs to the adaptor complexes small subunit family.
Part of the AP-3 complex, an adapter-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 (By similarity). Involved in vacuolar trafficking and contributes to hyphal growth and pathogenesis.
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.
Decreases cell adherence to silicone substrate.
Transcription factor required for yeast cell adherence to silicone substrate.
Expression is negatively regulated by the transcriptional repressors NRG1 and TUP1 (PubMed:11532938, PubMed:11737641). Expression is also regulated by SSN6 (PubMed:15814841). Expression is repressed by HAP43 (PubMed:21592964). Expression is induced by antifungal agents caspofungin and flucytosine (PubMed:15917516). Finally, expression is also induced during biofilm development (PubMed:19527170, PubMed:22265407).
Probable permease for arginine and lysine.
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.
Expression is under the positive control of the hyphal regulator TEC1 and repressed by TUP1 (PubMed:15814840, PubMed:15964282). Also induced by acetic acid-stress in a MNL1-dependent manner (PubMed:18653474).
Implanted medical devices, such as venous catheters, are a serious risk factor for C.albicans infection since they are substrates for the formation of biofilms, which in turn serve as reservoirs of cells to continually seed an infection.
Phosphorylated at Thr-191 and Ser-556 by CBK1. Phosphorylation by CBK1 is required for ALS1 and ALS3 expression, adherence, and biofilm formation.
Produces poor biofilms and decreases infection on rat denture models (PubMed:20605982, PubMed:20705667). Increases phagocytosis of the fungus by host cells in presence of estrogen (PubMed:34986357). Decreases expression of GPD2 (PubMed:34986357).
Transcription factor which acts as a master regulator of biofilm formation (PubMed:15964282, PubMed:17030992, PubMed:16839200, PubMed:20223293, PubMed:19959578, PubMed:20705667, PubMed:21829325, PubMed:21283544, PubMed:21407800, PubMed:22145027, PubMed:22265407, PubMed:22882910, PubMed:22589718). Biofilms play an important role in pathogenesis and produce many infections such as oropharyngeal candidiasis or vulvovaginal candidiasis (PubMed:20705667, PubMed:21283544, PubMed:21407800, PubMed:22544909, PubMed:22265407). Controls the expression of genes that govern cell-surface properties such as ALS1, ALS3, HWP1 and HYR1 (PubMed:16839200, PubMed:17277173, PubMed:19197361, PubMed:20415594, PubMed:22145027, PubMed:22544909, PubMed:22589718). Down-stream component of the hyphal regulatory network that couples expression of cell-surface genes to hyphal differentiation (PubMed:20223293, PubMed:21407800, PubMed:22359502).
Belongs to the WD repeat G protein beta family. Ribosomal protein RACK1 subfamily.
Causes defects in hyphal development under hypha-inducing conditions and attenuates virulence in a mouse model of systemic infection.
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 (Probable). Located at the head of the 40S ribosomal subunit in the vicinity of the mRNA exit channel, it serves as a scaffold protein that can recruit other proteins to the ribosome (By similarity). Involved in the negative regulation of translation of a specific subset of proteins (By similarity). Plays a role in morphogenesis and pathogenesis (PubMed:20929924).
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.
Belongs to the adaptor complexes medium subunit family.
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 transcriptional coactivator PC4 family.
During the catalytic reaction, a sulfide is transferred from Cys-210 to a reaction intermediate, generating a dehydroalanine residue.
Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance.
Belongs to the AB hydrolase superfamily. LDAH 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.
Plays an essential role in initiation of the G0 program by preventing the degradation of specific nutrient-regulated mRNAs via the 5'-3' mRNA decay pathway.
Belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family.
Responsible for methylating the 5'-cap structure of mRNAs.
Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
Catalytic component of the ISW2 complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW2 complex is involved in coordinating transcriptional repression and in inheritance of telomeric silencing (By similarity). ISW2 is required for chlamydospore formation, distinctive morphological feature of the fungal pathogen C.albicans that can be induced to form in oxygen-limited environments and has been reported in clinical specimens.
Expression is induced by the HAP43 transcription factor and repressed in response to high doses of peroxide stress.
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
Belongs to the 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.
Belongs to the class VI-like SAM-binding methyltransferase superfamily. Isoprenylcysteine carboxyl methyltransferase family.
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 cytochrome c-type heme lyase family.
Lyase that catalyzes the covalent linking of the heme group to the cytochrome C apoprotein to produce the mature functional cytochrome.
Belongs to the beta-class carbonic anhydrase family.
Essential for vacuolar protein sorting. Required for vacuole biogenesis, stability and to maintain vacuole morphology.
Component of the GINS complex which is a heterotetramer of SLD5, PSF1, PSF2 and PSF3.
The GINS complex plays an essential role in the initiation of DNA replication. Has a role in chromosome segregation (By similarity).
Belongs to the glycosyl hydrolase 17 family.
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 histone H4 and H2A. The NuA4 complex is also involved in DNA repair (By similarity).
Belongs to the eukaryotic ribosomal protein eL19 family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (Probable). RPL19A may play a role in the last stages of translation initiation, in particular subunit joining and shedding/releasing factors (By similarity).
Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. 6-phosphogluconolactonase subfamily.
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Belongs to the WD repeat PROPPIN family.
Component of the PI(3,5)P2 regulatory complex.
The L/FRRG motif is essential for the cytoplasm to vacuole transport (Cvt) pathway, for the recruitment of ATG8 and ATG16 to the PAS in nutrient-rich medium, and for its recruitment to and dissociation from the PAS under starvation conditions.
The N-terminus might form a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2), leading to the association of the protein to the membrane.
The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Necessary for proper vacuole morphology. Plays an important role in osmotically-induced vacuole fragmentation. Required for cytoplasm to vacuole transport (Cvt) vesicle formation, pexophagy and starvation-induced autophagy. Involved in correct ATG9 trafficking to the pre-autophagosomal structure. Might also be involved in premeiotic DNA replication (By similarity).
Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport.
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.
This protein may be expected to contain an N-terminal transit peptide but none has been predicted.
Belongs to the cysteine dioxygenase family.
Cysteine dioxygenase involved in sulfite formation from cysteine. Plays an important role in filamentous growth and virulence.
Displays reduced hyphae formation in the presence of cysteine and leads to attenuated virulence.
Expression is under the control of the ZCF2 transcription factor and is regulated upon white-opaque switching. Transcription is also up-regulated in both intermediate and mature biofilms.
The thioether cross-link between Cys-157 and Tyr-221 plays a structural role through stabilizing the Fe(2+) ion, and prevents the production of highly damaging free hydroxyl radicals by holding the oxygen radical via hydroxyl hydrogen.
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 (By similarity). Required for the transition from hyphal to yeast growth.
Expressed under both yeast and hyphal conditions of growth.
Expression is positively regulated by the transcription factor PHO4 (PubMed:24114876). Induced during early phase of biofilm formation (PubMed:16151249).
Glycerophosphocholine glycerophosphodiesterase responsible for the hydrolysis of intracellular glycerophosphocholine into glycerol-phosphate and choline (PubMed:24114876). The choline is used for phosphatidyl-choline synthesis (PubMed:24114876). Required for utilization of glycerophosphocholine as phosphate source (PubMed:24114876). C.albicans can utilize GroPCho through transport and intracellular hydrolysis or through extracellular hydrolysis (PubMed:24114876).
Results in altered glycerophosphocholine catabolism (PubMed:24114876). Leads to hypersensitivity to 5-fluorouracil (5-FU) (PubMed:17604452).
Belongs to the lysophospholipase family.
Belongs to the IPP isomerase type 1 family.
Isopentenyl-diphosphate delta-isomerase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). IDI1 catalyzes the 1,3-allylic rearrangement of isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP) (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable).
Involved in nucleotide metabolism via production of dUMP, the immediate precursor of thymidine nucleotides, and decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Belongs to the WD repeat CDC20/Fizzy family.
Belongs to the nonaspanin (TM9SF) (TC 9.A.2) family.
Belongs to the aconitase/IPM isomerase family.
Catalyzes the reversible hydration of cis-homoaconitate to (2R,3S)-homoisocitrate, a step in the alpha-aminoadipate pathway for lysine biosynthesis.
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 peptidase C56 family. HSP31-like subfamily.
Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. Selective for MG, does not use glyoxal as substrate. Plays a role in detoxifying endogenously produced MG, particularly when glycerol is the principal carbon source (PubMed:24302734). Important for viability in stationary phase (By similarity).
Has a 3- to 5-fold increase in levels of intracellular methylglyoxal compared with wild-type cells grown in the same media.
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).
Belongs to the acetate uptake transporter (AceTr) (TC 2.A.96) family.
Belongs to the DNA mismatch repair MutS family. MSH3 subfamily.
Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS beta, which binds to DNA mismatches thereby initiating DNA repair. MSH3 provides substrate-binding and substrate specificity to the complex. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. Acts mainly to repair insertion-deletion loops (IDLs) from 2 to 13 nucleotides in size, but can also repair base-base and single insertion-deletion mismatches that occur during replication. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions (By similarity).
Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a ternary complex with MutL alpha (MLH1-PMS1) (By similarity).
Belongs to the glycosyltransferase 3 family.
Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.
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.
Expression is increased in opaque cells.
Histidine kinase involved in a two-component signaling pathway that regulates cell wall mannan biosynthesis. Required for hyphal formation and virulence. Plays a role in fungicides sensitivity, probably through the positive regulation of the HOG1-signaling pathway. Presumed to mediate phosphotransfer to the HOG1 MAP kinase pathway during oxidative and perhaps osmotic stress.
Impairs the hyphal formation and attenuates the virulence in a mouse systemic candidiasis model.
The HAMP domains are critical for the sensitivity to fungicides such as fludioxonil, as well as for activation of HOG1.
The phosphorelay mechanism involves the sequential transfer of a phosphate group from His-510 (H1) in the histidine kinase domain (transmitter domain) to Asp-924 (D1) of the response regulatory domain (receiver domain). This transfer probably occurs between two NIK1 molecules, rather than intramolecularly (By similarity).
Belongs to the ubiquitin-conjugating enzyme family. UEV subfamily.
Involved in pre-mRNA splicing and cell cycle control.
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.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel.
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. Minor subunit located with subunit a in the membrane.
Belongs to the LDH/MDH superfamily. MDH type 1 family.
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). Required for pseudohyphal growth and virulence in mice.
3' to 5' exoribonuclease required for proper 3' end maturation of MRP RNA and of the U5L snRNA.
Exoribonuclease involved in ribosome biosynthesis. Involved in the processing of ITS1, the internal transcribed spacer localized between the 18S and 5.8S rRNAs (By similarity).
Probable component of the endoplasmic reticulum-associated degradation (ERAD) pathway.
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 class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 2 subfamily.
In the C-terminal section; belongs to the peptidase M41 family.
In the N-terminal section; belongs to the AAA ATPase family.
Belongs to the two pore domain potassium channel (TC 1.A.1.8) family.
ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix. Necessary for type 2 peroxisome targeting signal (PTS2)-containing protein processing and facilitates peroxisome matrix protein import.
Belongs to the 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.
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).
Monomer. Component of the 2-(3-amino-3-carboxypropyl)histidine synthase complex composed of DPH1, DPH2, DPH3 and a NADH-dependent reductase, predominantly CBR1.
NADH-dependent reductase for DPH3 and cytochrome b5. Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase, predominantly CBR1. By reducing DPH3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes.
Belongs to the universal ribosomal protein uS15 family.
Belongs to the SNF2/RAD54 helicase family.
Expression is induced by HAP43 and during biofilm formation.
Transcription factor required for transcription of 5S rRNA by RNA polymerase III.
Belongs to the glycosyltransferase 34 family.
As part of the replication protein A (RPA/RP-A), a single-stranded DNA-binding heterotrimeric complex, may play an essential role in DNA replication, recombination and repair. Binds and stabilizes single-stranded DNA intermediates, preventing complementary DNA reannealing and recruiting different proteins involved in DNA metabolism.
Belongs to the replication factor A protein 1 family.
Component of the heterotrimeric canonical replication protein A complex (RPA).
In the C-terminal section; belongs to the anthranilate synthase component I family.
Belongs to the triosephosphate isomerase 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 WD repeat peroxin-7 family.
Interacts with the 35S, 23S and 20S pre-rRNAs and with the U3 snoRNA.
Involved in ribosome biogenesis. Required for normal pre-rRNA processing in internal transcribed spacer 1 (ITS1). May be involved in the movements of the replication forks.
Belongs to the DNA mismatch repair MutS family.
Component of the post-replicative DNA mismatch repair system (MMR).
Golgi membrane protein involved in vesicular trafficking.
Belongs to the acyl carrier protein (ACP) family.
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Cyclin-dependent kinase that acts as a master regulator of the mitotic and meiotic cell cycles (By similarity). May drive the G1-S transition (PubMed:7830719). Plays a role in mitotic exit (PubMed:22090345). Plays a role in the expression of morphology-related transcription factors, and especially hyphae-specific genes (PubMed:16710830, PubMed:11809828, PubMed:15659158). Binds distinct cyclin subunits as cells progress through the division cycle or flamentous growth (PubMed:15071502, PubMed:17765684, PubMed:18923418, PubMed:22787279). The CDC28-CLB2 complex regulates cytokinesis partly by phosphorylating the actomyosin ring component IQG1 (PubMed:18923418). The CDC28-CLN3 complex phosphorylates SLA1 which regulates cortical actin patch dynamics (PubMed:22787279). The CDC28-CCN1 complex phosphorylates CDC11 and SEC2 upon induction of filamentous growth (PubMed:17765684). The CDC28-HGC1 complex also phosphorylates SEC2 and maintains CDC11 phosphorylation throughout hyphal growth (PubMed:20639857). Moreover, the CDC28-HGC1 complex phosphorylates and prevents RGA2 from localizing to hyphal tips, leading to localized CDC42 activation for hyphal extension (PubMed:17673907). CDC28-HGC1 phosphorylation of EFG1 represses cell separation genes during hyphal growth (PubMed:19528234). Additional substrates for CDC28 are RFA2 in G1-phase; MOB2, which is required for the maintenance of polarisome components and for inhibition of cell separation in hyphae; and GIN4 to regulate its association to SEP7 and subsequent septin ring assembly (PubMed:23140133, PubMed:22366454, PubMed:21593210).
Expression is increased during exponential growth and repressed by the antifungal drug plagiochin E (PLE).
Forms several complexes with cyclins CCN1, CLB2, CLN3, and HGC1. The CDC28-CCN1 complex associates with septin CDC11 upon hyphal induction. Interacts with IQG1, RFA2, and HSP90.
Phosphorylated at Tyr-18 by SWE1 in a cell cycle-dependent manner. Yeast-form and hyphal cells display similar dynamics of phosphorylation and dephosphorylation of Tyr-18. Tyr-18 phosphorylation leads to inhibition of CDC28 kinase activity.
Phosphorylation at Thr-17 or Tyr-18 inactivates the enzyme, while phosphorylation at Thr-166 activates it.
Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.
In the C-terminal section; belongs to the eukaryotic ribosomal protein eS31 family.
In the N-terminal section; belongs to the ubiquitin family.
Ubiquitin is encoded by several different genes. UBI3 is a polyprotein with one copy of ubiquitin fused to ribosomal protein eS31. UBI4 is a polyprotein containing 3 exact head to tail repeats of ubiquitin.
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PDPK1 subfamily.
Belongs to the protein-tyrosine phosphatase family.
Putative tyrosine-protein phosphatase required for protection against superoxide stress.
Regulated by EFG1, NRG1, and TUP1. Expression is increased with increasing cell density and during host infection. Expression is repressed by linalool.
Transcriptional regulator involved in extension of germ tubes into elongated hyphae and maintenance of filamentous growth. Regulates expression of UME6. Acts in a pathway that regulates maintenance of hyphal growth by repressing hyphal-to-yeast transition and allows dissemination within host epithelial tissues. Dispensable for invasion into both host oral epithelial cells and enterocytes, but required for epithelial damage.
Expression is induced in opaque cells and biofilm, and is regulated by WOR1.
Stabilizes opaque cells at higher temperatures.
Transcription factor that modulates the white-opaque switch.
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 the N-acetylglucosamine catabolic cascade that phosphorylates N-acetylglucosamine (GlcNAc), and allows the unique ability to utilise GlcNAc as carbon source. Converts GlcNAc to GlcNAc-6-P. Also able to phosphorylate glucose, glucosamine (GlcN), and mannose. Galactose, fructose, N-acetylmannosamine (ManNAc), mannosamine (ManN), galactosamine (GalN), and N-acetylgalactosamine (GalNAc) are not phosphorylated by HXK1. GlcNAc metabolism is closely associated with virulence and morphogenesis, and is involved in the cell wall synthesis. Acts both as a repressor and an activator of genes involved in maintaining cellular homeostasis. Contributes to white-opaque morphological transition and plays a role as a filamentation repressor.
Expression is induced by N-acetylglucosamine (GlcNAc), by the alpha pheromone, and in filamentation-inducing media.
Greatly retards the growth of cells using GlcNAc as the sole carbon source, increases resistance against farnesol, and attenuates the virulence in a mouse systemic infection model. Leads to derepression of opaque specific gene expression, as well as to constitutive filamentous growth and hyperfilamentation in filamentation-inducing conditions.
Interacts with histone deacetylase SIR2 under filamentation-inducing conditions.
Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair (By similarity).
Component of the NuA4 histone acetyltransferase complex.
Belongs to the major facilitator superfamily. DHA1 family. Polyamines/proton antiporter (TC 2.A.1.2.16) subfamily.
Expression is induced in presence of cycloheximide and 4-nitroquinoline-N-oxide (PubMed:12589826). Expression is up-regulated during biofilm formation (PubMed:25784162).
Leads to increased susceptibility to cycloheximide, 4-nitroquinoline-N-oxide, and 1,10-phenanthroline, but not to actinomycin D, fluconazole, ketoconazole and colchicine (PubMed:12076781). Leads also to attenuated virulence in mice (PubMed:12076781).
MFS transporter involved in N-acetylglucosamine (GlcNAc) uptake (PubMed:19648376). Confers resistance to cycloheximide, 4-nitroquinoline-N-oxide, and 1,10-phenanthroline, and contributes to virulence (PubMed:12076781, PubMed:12589826).
Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).
Belongs to the eukaryotic/archaeal PrmC-related family.
Belongs to the methyltransferase superfamily. LCMT family.
Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Mediator of diverse signals that repress RNA polymerase III transcription. Inhibits the de novo assembly of TFIIIB onto DNA.
Belongs to the RNA polymerase beta' chain family.
Belongs to the histidine acid phosphatase family.
Belongs to the 2-oxoacid dehydrogenase family.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
Belongs to the V-ATPase E subunit family.
Transcriptional coactivator that stimulates GCN4-dependent transcriptional activity by bridging the DNA-binding region of GCN4 and TBP (SPT15), thereby recruiting TBP to GCN4-bound promoters. Involved in induction of the ribosome quality control (RQC) pathway; a pathway that degrades nascent peptide chains during problematic translation. Required to prevent stalled ribosomes from frameshifting.
Required for respiratory activity and maintenance and expression of the mitochondrial genome.
Belongs to the aldehyde dehydrogenase family.
G1/S-specific cyclin essential for the control of the cell cycle at the G1/S (start) transition. CLN3 may be an upstream activator of the G1 cyclins which directly catalyze start. Required for budding and for cell cycle progression and morphogenesis in environment-induced hyphae. Degradation is mediated by GRR1. Through binding to CDC28, controls the phosphorylation of SLA1 which regulates cortical actin patch dynamics.
Hyperphosphorylated. GRR1 preferentially mediates the degradation of hyperphosphorylated CLN3.
The GINS complex plays an essential role in the initiation of DNA replication.
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.
Essential transcriptional activator that binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of gene expression. Bind both the promoters of ribosomal protein genes and the rDNA locus and activates transcription at these loci. Recruits FHL1 and IFH1 to promoters.
Expression is under the control of transcription factors SWI4 and SWI6.
Belongs to the DNA polymerase epsilon subunit B family.
The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel.
Belongs to the PPP phosphatase family. PP-2A subfamily.
Inhibited by okadaic acid, a specific inhibitor of serine/threonine phosphatases of types 1, 2A and 2B.
Leads to defect in morphogenesis and reduced virulence.
Serine/threonine-protein phosphatase that plays an important role in controlling colony morphology, filament extension and agar invasion. Down-regulates expression of NRG1 and affects the expression of multiple filament-specific transcripts in response to serum and 37 degrees Celsius. Plays a crucial role in virulence in a mouse model of systemic candidiasis.
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.
Efficient DNA binding requires dimerization with another bHLH protein.
Expression is controlled by RTG1 and is down-regulated during mating process, yeast-to-hyphal transition, and in presence of benomyl, amphotericin B, and caspofungin.
Key transcriptional regulator of carbohydrate metabolism. Binds the promoter sequences of the glycolytic genes at the CANNTG motif and activates their expression during growth on either fermentable or non-fermentable carbon sources as well as under hypoxic growth conditions. Complete glycolytic activation by GAL4 and TYE7 is required for full virulence. Involved in biofilm formation and negatively regulates hyphal formation under hypoxia. Controls also the expression of the copper transport protein CTR1.
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 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).
Belongs to the DHHC palmitoyltransferase family. ERF2/ZDHHC9 subfamily.
The DHHC domain is required for palmitoyltransferase activity.
The ERF2-ERF4 complex is a palmitoyltransferase specific for Ras proteins.
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.
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''.
Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the pathogenesis of C.albicans infections (PubMed:17510860, PubMed:22321066, PubMed:22429754). Allele ALS9-2 contributes to endothelial cell adhesion, whereas ALS9-1 does not (PubMed:17600078).
Each ALS protein has a similar three-domain structure, including a N-ter domain of 433-436 amino acids that is 55-90 percent identical across the family and which mediates adherence to various materials; a central domain of variable numbers of tandemly repeated copies of a 36 amino acid motif; and a C-ter; domain that is relatively variable in length and sequence across the family.
Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Belongs to the ETF beta-subunit/FixA family.
Heterodimer of an alpha and a beta subunit.
The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).
Belongs to the SEC23/SEC24 family. SEC24 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. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
Involved in the processing of the 20S pre-rRNA.
Belongs to the bacterial ribosomal protein bL17 family.
Component of the EKC/KEOPS complex composed of at least BUD32, CGI121, GON7, KAE1 and PCC1; the whole complex dimerizes.
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. GON7 likely plays a supporting role to the catalytic subunit KAE1 in the complex. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators (By similarity).
ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping. Is involved in G1/S DNA-damage checkpoint recovery, probably through the regulation of the translational status of a subset of mRNAs. May also have a role in translation and mRNA nuclear export (By similarity).
Belongs to the DEAD box helicase family. DDX6/DHH1 subfamily.
Belongs to the cyclin family. Cyclin C subfamily.
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, transcription elongation regulation and pathogenesis of invasive candidiasis.
Component of the COMPASS (Set1C) complex.
Acts in DNA repair and mutagenesis. Involved in promoting resistance to ionizing radiation and UV light, as well as regulating cell cycle progression after irradiation.
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) via its interaction with PAM18/TIM14. May act by positioning PAM18/TIM14 in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation (By similarity).
Heterodimer with PAM18. Component of the PAM complex, at least composed of mtHsp70, MGE1, TIM44, PAM16, PAM17 and PAM18 (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 SMC family. SMC2 subfamily.
Belongs to the universal ribosomal protein uL15 family.
Catalyzes the release of fatty acids from lysophospholipids (By similarity). Phospholipase B may well contribute to pathogenicity by abetting the fungus in damaging and traversing host cell membranes, processes which likely increase the rapidity of disseminated infection (PubMed:9748287).
Expressed during candidal infection of mice.
Reduces dramatically the ability to penetrate host cells.
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.
Part of the nascent polypeptide-associated complex (NAC), consisting of EGD2 and EGD1. NAC associates with ribosomes via EGD1 (By similarity).
Component of 250-400 kDa complexes called cytochrome oxidase assembly intermediates or COA complexes.
Required for assembly of cytochrome c oxidase (complex IV).
Belongs to the XRCC4-XLF family. XLF subfamily.
Belongs to the mitochondrion-specific ribosomal protein mL50 family.
Belongs to the eukaryotic ribosomal protein eL8 family.
Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly.
Interacts with histone H3 and histone H4.
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 NDUFB7 subunit family.
Interacts with RIM101 by binding to its two YPX[LI] motifs.
Required for the proteolytic cleavage of the transcription factor RIM101 in response to alkaline ambient pH. May act as a scaffold protein that recruits the calpain-like protease RIM13 via SNF7 to its substrate RIM101 (By similarity). Required for filamentation.
Belongs to the DEAD box helicase family. DDX54/DBP10 subfamily.
E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation.
Belongs to the peptidase C19 family. PAN2 subfamily.
Binds 2 metal cations per subunit in the catalytic exonuclease domain.
Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails.
Contains a pseudo-UCH domain. This ubiquitin C-terminal hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain is predicted to be catalytically inactive because it lacks the active site catalytic triad characteristic of thiol proteases, with residues at the equivalent structural positions that are incompatible with catalysis, and it cannot bind ubiquitin. It functions as a structural scaffold for intra- and intermolecular interactions in the complex.
Forms a heterotrimer with an asymmetric homodimer of the regulatory subunit PAN3 to form the poly(A)-nuclease (PAN) deadenylation complex.
Positively regulated by the regulatory subunit PAN3.
The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with PAN3.
Belongs to the ubiquitin-conjugating enzyme family.
Probable cell wall protein that participates directly in adhesive cell-cell interactions.
The PGA6 mRNA is transported by SHE3 to the hyphal tips during filamentous growth.
Up-regulated by high iron, during biofilm development, and upon ALS2 depletion.
Belongs to the universal ribosomal protein uL29 family.
Component of the mitochondrial large ribosomal subunit (mt-LSU).
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Belongs to the uroporphyrinogen-III synthase family.
Belongs to the pterin-4-alpha-carbinolamine dehydratase family.
Putative adhesin which may be involved in cell adhesion and virulence (By similarity). Involved in the regulation of filamentous growth.
ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.
Belongs to the DEAD box helicase family. DDX5/DBP2 subfamily.
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).
Expressed during development of germ tubes, pseudohyphae and true hyphae.
Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. Induces host inflammatory cytokine production in a proteolytic activity-independent way. Plays a role in tissue damage during superficial infection. Moreover, acts toward human hemoglobin though limited proteolysis to generate a variety of antimicrobial hemocidins, enabling to compete with the other microorganisms of the same physiological niche using the microbicidal peptides generated from the host protein.
Belongs to the thiolase-like superfamily. Fungal fatty acid synthetase subunit alpha family.
Leads to avirulence using a BALB/c disseminated mouse model.
Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes. Regulates also the sphingolipid metabolism. Required for growth during anaerobiosis and sterol uptake. Plays a role in pathogenesis.
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 cell cycle progression and meiosis (By similarity).
Interacts with H3K4me3 and to a lesser extent with H3K4me2. Component of the NuA4 histone acetyltransferase complex.
The PHD-type zinc finger mediates the binding to H3K4me3.
Belongs to the group II decarboxylase 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.
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 thiolase-like superfamily. Thiolase family.
Belongs to the DHHC palmitoyltransferase family. PFA3 subfamily.
Palmitoyltransferase specific for VAC8. Palmitoylates VAC8 at one or more of its N-terminal cysteine residues, which is required for its proper membrane localization (By similarity).
ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Also required for efficient mitochondrial translation (By similarity).
Belongs to the DEAD box helicase family. DDX18/HAS1 subfamily.
Belongs to the pyridoxine kinase 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 arginase family. Agmatinase subfamily.
Belongs to the glycosyltransferase 15 family.
Involved in O-glycosylation of cell wall and secreted proteins. Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage. Mainly responsible for the addition of the second mannose residue in an O-linked mannose pentamer. Can also substitute for MNT2 by adding the third mannose residue. Important for adherence to host surfaces and for virulence.
Probable GPI-anchored cell wall protein involved in cell wall organization, hyphal growth, as well as in host-fungal interaction and virulence.
Up-regulated in biofilm, in oralpharyngeal candidasis, and upon milbemycins A3 oxim derivative (A3Ox). Down-regulated by fluconazole.
Belongs to the inositol phosphokinase (IPK) family.
Component of the fork protection complex (FPC) consisting of TOF1 and CSM3.
Forms a fork protection complex (FPC) with TOF1 and which is required for chromosome segregation during meiosis and DNA damage repair. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors (By similarity).
Belongs to the oligoribonuclease family.
Highly up-regulated by fetal bovine serum.
Plays an important role in survival in host blood through increasing tolerance to stresses such as heat, salt, or cycloheximide, which is essential for virulence.
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).
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.
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
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.
Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.
Transcription factor involved in RNA polymerase II transcription regulation. May function in both SPT15/TBP post-recruitment and recruitment steps of transcription (By similarity).
GTPase-activating protein for the ADP ribosylation factor family.
Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol.
Interacts with nucleoporin complex protein MTR2.
Involved in the export of mRNA from the nucleus to the cytoplasm.
The NTF2 domain heterodimerizes with MTR2. The formation of this heterodimer is essential for mRNA export and binds to all of the nucleoporin-FG-repeats.
The RNA-binding domain is conserved in most NXF proteins but may be absent in yeasts.
Belongs to the class I-like SAM-binding methyltransferase superfamily. UbiG/COQ3 family.
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Belongs to the 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).
Belongs to the peroxidase family. Cytochrome c peroxidase subfamily.
Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Required for vacuolar assembly and vacuolar traffic.
Belongs to the SurE nucleotidase family.
Belongs to the VAMP-associated protein (VAP) (TC 9.B.17) family.
Belongs to the eIF-2B alpha/beta/delta subunits family.
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 RNA polymerase beta chain family.
Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs (By similarity).
Belongs to the cyclophilin-type PPIase family. PPIase A subfamily.
Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.
Belongs to the class V-like SAM-binding methyltransferase superfamily. RKM1 family.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily.
Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. Plays a role in both tRNA-processing and mitochondrial metabolism. Involved in the 2-thio-modification of both 5-carboxymethylaminomethyl-2-thiouridine in mitochondrial tRNAs and 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) in cytoplasmic tRNAs.
Expression is up-regulated at high-iron conditions.
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.
Belongs to the alkaline phosphatase family.
Belongs to the complex I 75 kDa subunit family.
In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
Belongs to the DASH complex DUO1 family.
Belongs to the GTP-binding SRP family. SRP54 subfamily.
Fungal signal recognition particle consists of a 7S RNA molecule (scR1) and at least six protein subunits: srp72, srp68, srp54, sec65, srp21 and srp14.
Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the arrest of nascent chain elongation during membrane targeting. SRP54 binds to the signal sequence of presecretory protein when they emerge from the ribosomes. SRP54 interacts with the scR1 RNA and mediates the association of the resulting SRP-RNC complex with the signal recognition particle receptor (SR) via its alpha subunit SRP101. Both, SRP54 and SRP101, are locked in their GTP bound forms in the SRP-RNC-SR complex, which dissociates upon transferring the signal sequence to the protein-conducting channel (translocon). After signal sequence transfer, SRP54 and SRP101 act as reciprocal GTPase-activating proteins (GAPs), thereby resolving their association.
The M domain binds the 7SL RNA and the signal sequence of presecretory proteins.
The NG domain, also named G domain, is a special guanosine triphosphatase (GTPase) domain, which binds GTP and forms a guanosine 5'-triphosphate (GTP)-dependent complex with a homologous NG domain in the SRP receptor subunit srp101. The two NG domains undergo cooperative rearrangements upon their assembly, which culminate in the reciprocal activation of the GTPase activity of one another. SRP receptor compaction upon binding with cargo-loaded SRP and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER.
Belongs to the 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.
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).
E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8 from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8. The formation of the ATG8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity).
Monomer. Interacts with ATG8 through an intermediate thioester bond through the C-terminal Gly of ATG8. Also interacts with the 40 amino acid C-terminal region of the E1-like ATG7 enzyme. Interacts also with the ATG12-ATG5 conjugate.
The N-terminal region is involved in phosphatidylethanolamine-binding and is required for ATG8-PE conjugation.
The flexible region (FR) is required for ATG7-binding.
The handle region (HR) contains the ATG8 interaction motif (AIM) and mediates binding to ATG8. It is crucial for the cytoplasm-to-vacuole targeting pathway (By similarity).
Involved in pre-mRNA splicing and cell cycle progression. Required for the spliceosome assembly and initiation of the DNA replication (By similarity).
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 poly(A) polymerase family.
Binds 2 magnesium ions. Also active with manganese.
Polymerase that creates the 3'-poly(A) tail of mRNA's. May acquire specificity through interaction with a cleavage and polyadenylation factor (By similarity).
The C.albicans mating-type-like (MTL) locus contains, in addition to the genes for the regulatory proteins (MTLA1, MTLA2, MTLALPHA1 and MTLALPHA2), a and alpha idiomorphs of a phosphatidylinositol kinase (PIKA and PIKALPHA), a poly(A) polymerase (PAPA and PAPALPHA) and an oxysterol binding protein-like protein (OBPA and OBPALPHA).
Belongs to the peptidase S26 family. IMP2 subfamily.
Belongs to the ZIP transporter (TC 2.A.5) family.
Histone chaperone-dependent acetylase that modifies 'Lys-56' of histone H3 (H3K56ac), to promote genomic stability, DNA repair and transcriptional regulation during mitotic S-phase (PubMed:20601951, PubMed:20080646). Plays an important role in the regulation of white-opaque genotoxin induced-switching (PubMed:21749487).
Leads to a decreased pathogenicity in mice and increased susceptibility to killing by macrophages in vitro.
Belongs to the sirtuin family. Class III subfamily.
In contrast to class I sirtuins, class III sirtuins have only weak deacetylase activity. Difference in substrate specificity is probably due to a larger hydrophobic pocket with 2 residues (Tyr-67 and Arg-70) that bind to malonylated and succinylated substrates and define the specificity.
NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo.
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.
Induced via CAP1 during oxitive stress, as well as during biofilm formation.
Leads to altered sensitivity to fluconazole, LiCl, and copper.
Probable transcription factor involved in response to fluconazole, LiCl, and copper.
RNA-binding protein involved in the specific removal of group I introns in mitochondrial encoded transcripts. Maintains the stability of the small subunit mitochondrial 15S rRNA and thus the expression of the mitochondrial genome.
Belongs to the methyltransferase superfamily. Fibrillarin 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). All subunits are required for a maximal enzyme activity.
May be involved in vacuolar sorting and osmoregulation.
Belongs to the AB hydrolase superfamily. MetX family.
Belongs to the Mediator complex subunit 20 family.
Component of the cleavage factor I (CF I) involved in pre-mRNA 3'-end processing.
Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).
Belongs to the SOS response-associated peptidase family.
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.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.
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.
Heterooctamer of 4 alpha and 4 beta chains.
Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 2 subfamily.
Tetramer of two alpha and two beta subunits.
Belongs to the cytidine and deoxycytidylate deaminase family.
Belongs to the peptidase M67A family. CSN5 subfamily.
Catalytic Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes.
Component of the COP9 signalosome (CSN) complex.
The JAMM motif is essential for the protease activity of the CSN complex resulting in deneddylation of cullins. It constitutes the catalytic center of the complex (By similarity).
Belongs to the complex I 24 kDa subunit family.
A psd1 psd2 double mutant displays diminished phosphatidylethanolamine levels. It exhibits defects in cell wall integrity, mitochondrial function, filamentous growth and is less virulent than the wild-type.
Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type I sub-subfamily.
Binds 1 pyruvoyl group covalently per subunit.
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine (By similarity). Important for virulence (PubMed:20132453).
Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.
Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Belongs to the Cu-Zn superoxide dismutase family.
Belongs to the WD repeat NOL10/ENP2 family.
Belongs to the zinc-containing alcohol dehydrogenase family.
Required for translation of the mitochondrial OLI1 transcript coding for the mitochondrial ATP synthase subunit 9.
Forms a one-to-one complex with cytochrome c.
Belongs to the bZIP family. YAP subfamily.
Causes hypersensitivity to cadmium, 4-nitroquinoline N-oxide, 1,10-phenanthroline, and hydrogen peroxide. Abolishes the peroxide-mediated induction of COR33, TSA1, and many other genes involved in oxidative stress response. Inhibits trehalose accumulation upon exposure to oxidative stress. Shows significantly reduced viability when exposed to whole blood or polymorphonuclear cells, as well as to the Chinese herbal medicine baicalein. Leads also to decreased virulence in a Caenorhabditis elegans model. Increases apoptosis upon apoptotic stimulation.
Contains two cysteine rich domains (CRD), referred to as the N- and C-terminal CRD's, n-CRD (Cys-254 and Cys-261) and c-CRD (Cys-446, Cys-468 and Cys-477), respectively. A nuclear export signal is embedded in the c-CRD, with which the nuclear export protein CRM1/exportin 1 interacts only in the absence of disulfide bonds (or otherwise oxidized cysteines) within the c-CRD or between the c-CRD and the n-CRD.
Induced by oxidative stress and during contact with neutrophils. Expression is also up-regulated by the thioredoxin TRX1 and by treatment with Chinese herbal medicine baicalein.
Transcription activator involved in multidrug resistance, oxidative stress response, and redox homeostasis. Preferentially binds to promoters with the core binding site 5'-TTA[CG]TAA-3'. Involved in the oxidative stress response in via multiple pathways, including the cellular antioxidant defense system, carbohydrate metabolism and energy metabolism, protein degradation, ATP-dependent RNA helicase, and resistance pathways. The ability of the major systemic fungal pathogen of humans to sense and respond to reactive oxygen species, such as H(2)O(2) generated by the host immune system, is required for survival in the host and therefore virulence. Regulates the transcription of COR33, GLR1, GTO1, GTT1, GTT1, TRR1, TRX1, SOD1, CAT1, and the transcription regulator TSA1. Participates in the apoptosis by regulating the expression of the glutathione reductase gene and glutathione content. Also plays a role in the peroxide-mediated induction of MDR1 and other drug response genes such as PDR16, MDR1, FLU1, YCF1, and FCR1. Regulates trehalose accumulation which is important for the oxidative stress tolerance. Recruits ADA2 to its target promoters. Activity of CAP1 is controlled through oxidation of specific cysteine residues resulting in the alteration of its subcellular location. Oxidative stress induces nuclear accumulation and as a result CAP1 transcriptional activity. Nuclear export is restored when disulfide bonds are reduced by thioredoxin, whose expression is controlled by CAP1, providing a mechanism for negative autoregulation.
Upon oxidative stress, is oxidated by the peroxidase GPX3 and stabilized by YBP1 (PubMed:20679492, PubMed:23706023). Oxidative stress induces conformational changes through oxidation of cysteine residues, masking the nuclear export signal, thus abolishing nuclear export by CRM1/exportin 1 (By similarity).
Belongs to the universal ribosomal protein uS19 family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (Probable). RPS15 has a role in the late stage of the assembly of pre-40S particles within the nucleus and controls their export to the cytoplasm (By similarity).
Belongs to the NtaA/SnaA/DszA monooxygenase family.
Belongs to the homoserine dehydrogenase family.
Catalyzes the intermembrane transfer of phosphatidylglycerol and phosphatidylinositol.
Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks.
Belongs to the myo-inositol 1-phosphate synthase family.
Inositol auxotrophy (PubMed:18268031). Virulence is not affected in a mouse model of disseminated infection (PubMed:18268031). Simultaneous disruption of ITR1 results in lethality (PubMed:18268031).
Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner (PubMed:18268031). Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity).
Belongs to the Tim17/Tim22/Tim23 family.
Component of the TIM22 complex, whose core is composed of TIM22 and TIM54, associated with the 70 kDa heterohexamer composed of TIM9 and TIM10 (or TIM8 and TIM13).
Essential 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 (By similarity).
ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes (By similarity).
Belongs to the DEAD box helicase family. DDX3/DED1 subfamily.
High-conductance magnesium-selective channel that mediates the influx of magnesium into the mitochondrial matrix. Essential for the splicing of mRNA group II introns in mitochondria by affecting mitochondrial magnesium concentrations, which are critical for group II intron splicing. It also suppresses a variety of mitochondrial intron mutations and its absence may disturb the assembly of mitochondrial membrane complexes.
Homopentamer. Forms homooligomers. Interacts with MFM1.
Component of a multiprotein complex of 250 kDa composed of at least HYR1, MP65, and PRA1.
GPI-anchored hyphal cell wall protein required for hyphal growth and virulence. Involved in innate immune cell evasion through confering resistance to neutrophil killing. Binds kininogen, the proteinaceous kinin precursor, and contributes to trigger the kinin-forming cascade on the cell surface. Production of kinins is often involved in the human host defense against microbial infections.
Induced specifically in response to hyphal growth. Expression is repressed by neutrophils and purpurin. Regulated by RFG1, EFG1, NRG1, TUP1, CYR1, BCR1, and HAP43.
Leads to attenuated virulence in a mouse oral biofilm model of infection.
Belongs to the PA-phosphatase related phosphoesterase family.
Belongs to the UbiD family. UbiD-like/FDC subfamily.
Binds 1 prenylated FMN (prenyl-FMN) per subunit.
Catalyzes the reversible decarboxylation of aromatic carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives 4-vinylphenol, 4-vinylguaiacol, and styrene, respectively, which play the role of aroma metabolites.
Homodimer. May form higher order oligomers.
Transcriptional regulator of nitrogen utilization required for nitrogen catabolite repression and utilization of isoleucine, tyrosine and tryptophan as nitrogen sources. Controls expression of the MEP2 ammonium permease, the DUR1,2 urea amidolyase, and the transcription factor STP1, which in turn mediates SAP2 expression, a long-known virulence attribute of C.albicans. Influences the filamentation process depending upon the nitrogen sources available. Required for virulence in a mouse systemic infection model.
Associates with mature 80S ribosomes. Binds to the head domain of the 40S ribosomal subunit and prevents mRNA binding by inserting its alpha-helix domain towards the mRNA entry tunnel at the decoding site, where it blocks the binding of tRNA and mRNA at the A- and P-sites (Probable). Interacts with eEF2; interaction sequesters eEF2 at the A-site of the ribosome, thereby blocking the interaction sites of the mRNA-tRNA complex, promoting ribosome stabilization and hibernation (By similarity).
Phosphorylation by TORC1 upon nutrient replenishment inhibits STM1 and causes its release from dormant ribosomes.
Ribosome preservation factor that protect a small pool of nontranslating, vacant ribosomes in cells under nutrient starvation conditions. Under nutrient-limiting conditions, cells reduce ribosome biogenesis and degrade ribosomes via autophagy (ribophagy) or proteasomal degradation. To avoid excessive degradation during starvation, STM1 binds to and protects 80S ribosomes from proteasomal degradation. Under nutrient-sufficient conditions, TORC1 phosphorylates and inhibits STM1 to prevent formation of dormant 80S ribosomes. Acts as an inhibitor of mRNA translation by promoting ribosome hibernation: clamps the two ribosomal subunits, thereby preventing their dissociation, and inhibits translation by excluding mRNA-binding. Acts via its association with eEF2, promoting ribosome stabilization and storage in an inactive state. May also repress translation by preventing association of eEF3 with ribosomes. Binds specifically G4 quadruplex (these are four-stranded right-handed helices, stabilized by guanine base quartets) and purine motif triplex (characterized by a third, antiparallel purine-rich DNA strand located within the major groove of a homopurine stretch of duplex DNA) nucleic acid structures. These structures may be present at telomeres or in rRNAs.
Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. EXG2 is not heavily involved in the exoglucanase function of the adhesion process.
Induced during cell wall regeneration and repressed by HAP43.
Plays a role in maintenance of chromatin structure during RNA polymerase II transcription elongation thereby repressing transcription initiation from cryptic promoters. Mediates the reassembly of nucleosomes onto the promoters of at least a selected set of genes during repression; the nucleosome reassembly is essential for transcriptional repression (By similarity).
Belongs to the small GTPase superfamily. Rho family.
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.
Belongs to the universal ribosomal protein uL24 family.
Belongs to the activator 1 small subunits family.
SNARE required for protein transport between the ER and the Golgi complex.
Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. Required for cell surface integrity and cell separation during budding.
Abolished the utilization of glycerophosphoinositol(GroPIns) as a phosphate source (PubMed:21984707).
Glycerophosphodiester transporter that mediates uptake of glycerophosphoinositol (GroPIns) as a source of inositol and phosphate (PubMed:21984707, PubMed:24114876). Does not possess detectable glycerophosphocholine (GroPCho) transport activity (PubMed:21984707). Although no glycerophosphoinositol transport activity occurs in the absence of GIT1, C.albicans is still able to use glycerophosphoinositol as a phosphate source at pH 7.5, albeit slowly (PubMed:21984707). Thus, a second, GIT1-independent, mechanism must exist for utilizing glycerophosphoinositol as a phosphate source at physiological pH (PubMed:21984707, PubMed:24114876). The expanded ability to utilize GroPIns and GroPCho results from the organism's pathogenic nature and its need to occupy a variety of environments within its host organism (PubMed:21984707). This possibility is buttressed by the fact that GroPIns and GroPCho are present and abundant in human fluids (PubMed:21984707, PubMed:24114876).
Phosphate levels regulate glycerophosphoinositol transport activity and transcription factor PHO4 is required for GIT1 expression (PubMed:21984707). Expression profile differs significantly in isolates of high, medium, and low virulence, being the highest in the most virulent strains (PubMed:19151328).
Belongs to the CoA-transferase III family.
Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the pathogenesis of C.albicans infections.
Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function.
Component of the cell wall involved in virulence which plays a role in the relationship between C.albicans and the host.
Up-regulated upon milbemycin A3 oxim derivative (A3Ox) treatment.
Belongs to the NADH dehydrogenase family.
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 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.
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.
Belongs to the dynein light chain family.
Cytoplasmic dynein consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits which present intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs).
Belongs to the oligopeptide OPT transporter family.
Each ALS protein has a similar three-domain structure, including a N-ter domain of 433-436 amino acids that is 55-90 percent identical across the family and which mediates adherence to various materials; a central domain of variable numbers of tandemly repeated copies of a 36 amino acid motif; and a C-ter domain that is relatively variable in length and sequence across the family.
Highly expressed in biofilms and during candidiasis infection dissemination. Induced upon interaction with host macrophages.
Belongs to the DEAD box helicase family. DDX31/DBP7 subfamily.
Present with 1460 molecules/cell in log phase SD medium.
Involved in the lipid remodeling steps of GPI-anchor maturation.
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 GET1 and GET2, 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 GET1-GET2 receptor, and returning it to the cytosol to initiate a new round of targeting. Cooperates with the HDEL receptor ERD2 to mediate the ATP-dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER. Involved in low-level resistance to the oxyanions arsenite and arsenate, and in heat tolerance.
Homodimer. Component of the Golgi to ER traffic (GET) complex, which is composed of GET1, GET2 and GET3. Within the complex, GET1 and GET2 form a heterotetramer which is stabilized by phosphatidylinositol binding and which binds to the GET3 homodimer. Interacts with the chloride channel protein GEF1.
Chaperone required for the export of the chitin synthase CHS3 from the endoplasmic reticulum.
Belongs to the eukaryotic ribosomal protein eS28 family.
Belongs to the lipid-translocating exporter (LTE) (TC 9.A.26.1) family.
Belongs to the transient receptor potential (TRP) ion channel family.
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 phage and mitochondrial RNA polymerase family.
Involved in ribosome biogenesis, probably through modulation of rDNA transcription.
Performs an essential function in the repair of oxidatively damaged mtDNA that is required for the maintenance of the mitochondrial genome. Binds to DNA (By similarity).
Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.
Repressed by the HAP43 transcription regulator. Expression is also under the control of MAC1.
Transcriptional regulator of iron-responsive genes. Represses expression of SEF1 and genes for iron uptake if iron is present. Plays also a transcription-independent role in the direct inhibition of SEF1 function through protein complex formation and translocation to the cytoplasm, where SEF1 is destabilized. Promotes gastrointestinal commensalism in mice.
Belongs to the snRNP Sm proteins family. SmF/LSm6 subfamily.
Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Not involved in the GTP-dependent ribosomal translocation step during translation elongation.
NAD-dependent histone deacetylase, which could function in telomeric silencing, cell cycle progression and chromosome stability.
Belongs to the glycosyl hydrolase 81 family.
Belongs to the fungal cytochrome c oxidase subunit 7a family.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily.
Protein kinase that acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylating and inhibiting the mitosis-promoting cyclin B-bound CDC28 at 'Tyr-18'. SWE1-mediated inhibition of CDC28 acts in a cell size or morphogenesis checkpoint to delay mitosis in response to defects in growth, actin organization or bud formation. Plays an important role in filamentous growth.
Accepts electrons from ETF and reduces ubiquinone.
Belongs to the ketopantoate reductase family.
Belongs to the eukaryotic ribosomal protein eL24 family.
Component of the RIX1 complex required for processing of ITS2 sequences from 35S pre-rRNA and the nucleoplasmic transit of the pre-60S ribosomal subunits. Regulates pre-60S association of the critical remodeling factor MDN1.
Component of the RIX1 complex, composed of IPI1, RIX1/IPI2 and IPI3 in a 1:2:2 stoichiometry. The complex interacts (via RIX1) with MDN1 (via its hexameric AAA ATPase ring) and the pre-60S ribosome particles.
Belongs to the lariat debranching enzyme 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.
Belongs to the G-protein coupled receptor 4 family.
Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2 (By similarity).
The DPH-type metal-binding (MB) domain can bind either zinc or iron ions.
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly (By similarity).
Expression is regulated by changes of iron conditions with an increase in low iron. Transcription is negatively regulated by SFU1.
Phosphorylated by SSN3 under iron-depleted conditions which leads to nuclear localization.
Transcription factor which plays an essential role in virulence by activating the transcription of iron uptake genes such as FRE7 in iron-poor environments such as the host bloodstream and internal organs. Promotes commensalism in a mouse model of gastrointestinal infection.
Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.
Component of centromeric nucleosomes, where DNA is wrapped around a histone octamer core. The octamer contains two molecules each of H2A, H2B, CSE4/CENPA and H4 assembled in one CSE4-H4 heterotetramer and two H2A-H2B heterodimers. Interacts with the inner kinetochore.
Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division (By similarity).
Ubiquitinated. Is degraded through ubiquitin-mediated proteolysis when not protected by its association to the kinetochore.
Expression is induced in presence of cycloheximide, 4-nitroquinoline-N-oxide, and 1,10-phenanthroline (PubMed:12589826). Expression is up-regulated during biofilm formation (PubMed:25784162). Expression is also increased in high-iron conditions (PubMed:15387822). Expression is decreased after combined treatment with fluconazole and osthole (PubMed:28607012).
Autoacetylation at Lys-296 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.
Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for the ferulic acid decarboxylase FDC1. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.
Hyperphosphorylated. Phosphorylation is cell cycle-dependent and peaks at the time of cytokinesis. Contains 21 consensus sites for cyclin-dependent kinases (CDKs). At least some of them are phosphorylated by the CLB2-CDC28 kinase complex. Mutation of 15 of the phosphorylation sites to Ala caused both premature assembly and delayed disassembly of the actomyosin ring, blocked interaction with the actin-nucleating proteins BNI1 and BNR1, and resulted in defects in cytokinesis.
Interacts with myosin MYO1 and its light chain MLC1 (By similarity). Interacts with BNI1 (PubMed:18923418). Interacts with BNR1 (PubMed:18923418). Interacts with CLB2 (PubMed:18923418). Interacts with CLB4 (PubMed:18923418). Interacts with CDC28 (PubMed:18923418).
Required for the assembly and the contraction of the actomyosin ring at the bud neck during cytokinesis.
The IQ domains provide the interaction surface for the myosin light chain MLC1.
The Ras-GAP domain is required for contraction of the actomyosin ring. It probably does not stimulate GTPase activity (By similarity).
The calponin homology (CH) domain binds to actin filaments and is required for their recruitment to the bud neck.
Belongs to the thymidylate synthase family.
Component of the U1 snRNP particle, which recognizes and binds the 5'-splice site of pre-mRNA. Together with other non-snRNP factors, U1 snRNP forms the spliceosomal commitment complex, that targets pre-mRNA to the splicing pathway.
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).
Required for the assembly of cytochrome c oxidase.
Belongs to the glycosyltransferase 32 family.
Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration.
Belongs to the ATP-dependent AMP-binding enzyme family.
Belongs to the peroxisomal membrane protein PXMP2/4 family.
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.
Transcription factor which regulates nonfermentable carbon utilization.
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.
Belongs to the spermidine/spermine synthase family.
Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Forms a redox cycle with ERV1 that involves a disulfide relay system. Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria. The oxidized form of MIA40 forms a transient intermolecular disulfide bridge with the reduced precursor protein, resulting in oxidation of the precursor protein that now contains an intramolecular disulfide bond and is able to undergo folding in the IMS (By similarity).
The CHCH domain contains a conserved twin Cys-X(9)-Cys motif which is required for import and stability of MIA40 in mitochondria.
Belongs to the ubiquitin-activating E1 family.
Binds specifically to the 3'-terminal U-tract of U6 snRNA.
LSm subunits form a heteromer with a doughnut shape.
Belongs to the DNA mismatch repair MutL/HexB family.
Belongs to the peptidase M16 family. PreP subfamily.
Degrades mitochondrial transit peptides after their cleavage in the intermembrane space or in the matrix, and presequence peptides; clearance of these peptides is required to keep the presequence processing machinery running (By similarity). Preferentially cleaves the N-terminal side of paired basic amino acid residues (By similarity). Also degrades other unstructured peptides (By similarity). May function as an ATP-dependent peptidase as opposed to a metalloendopeptidase (By similarity).
Monomer and homodimer; homodimerization is induced by binding of the substrate.
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 (PubMed:26101253). 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 bacterial ribosomal protein bL12 family.
Belongs to the MIP/aquaporin (TC 1.A.8) family.
Ceramide-binding protein that may transfer ceramides from the endoplasmic reticulum membrane to the cis-Golgi network membrane, and is thereby required for the biosynthesis of complex sphingolipids.
Component of the PEX2-PEX10-PEX12 retrotranslocation channel, composed of PEX2, PEX10 and PEX12.
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. Involved in salt tolerance (By similarity).
Belongs to the Mediator complex subunit 18 family.
Belongs to the tellurite-resistance/dicarboxylate transporter (TDT) family.
Secreted protein that acts as a virulence factor during infections.
Highly expressed in biofilms with down-regulation during later stages of biofilm formation. Expression is repressed by TPK1 and SFL1, and induced by TPK2. Also under the control of TOR1. Expression is down-regulated by Riccardin D, a macrocyclic bisbibenzyl isolated from Chinese liverwort D.hirsute, which has an inhibitory effect on biofilms and virulence. Induced by caspofungin.
Involved in nonsense-mediated decay of mRNAs containing premature stop codons.
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.
Induced in hyphae and up-regulated during oral infection. Expression is higher in white cells.
reduces capacity to damage oral epithelial cells.
Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-14' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Component of the HAT-B complex composed of at least HAT1 and HAT2. The HAT-B complex binds to histone H4 tail (By similarity).
Amino-acid permease that is able to transport phenylalanine (PubMed:21764911, PubMed:28028545).
Expression is under control of the CSY1 amino-acid sensor (PubMed:28028545). Expression is also regulated by PLC1 and GCN4 (PubMed:16207920, PubMed:16215176). Expression is induced during development of biofilm (PubMed:22265407).
Component of the U1 snRNP particle, a subcomplex of the spliceosome.
Component of the U1 snRNP particle, which recognizes and binds the 5'-splice site of pre-mRNA. Together with other non-snRNP factors, U1 snRNP forms the spliceosomal commitment complex, that targets pre-mRNA to the splicing pathway (By similarity).
Belongs to the mitochondrial pyruvate carrier (MPC) (TC 2.A.105) family.
Mediates the uptake of pyruvate into mitochondria.
Belongs to the universal ribosomal protein uS13 family.
Catalytic component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond. Functions also as a dipeptidase with high specificity for Cys-Gly and no activity toward tri- or tetrapeptides (By similarity).
Homodimer. Component of the GSH degradosomal complex.
Heterodimers with GPN1 or GPN2. Binds to RNA polymerase II (RNAPII).
Small GTPase required for proper nuclear import of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import.
Belongs to the universal ribosomal protein uS17 family.
Homotrimerization occurs through formation of a three-stranded coiled-coil structure generated by intermolecular interactions between HR-A/B regions allowing DNA-binding activity.
Leads to sensitivity to H(2)O(2) in vitro, but only mildly attenuated virulence.
Phosphorylated by the phosphorelay intermediate protein YPD1.
Transcription factor that is part of a SLN1-YPD1-SKN7 two-component regulatory system, which controls gene expression in response to changes in the osmolarity of the extracellular environment. Under low osmotic conditions, phosphorylated and activated by the phosphorelay intermediate protein YPD1. Also activated in response to oxidative stress, independent on the two-component regulatory system. Regulates heat shock genes in response to oxidative stress and genes involved in cell wall integrity in response to osmotic changes.
Belongs to the WD repeat LIS1/nudF family.
Positively regulates the activity of the minus-end directed microtubule motor protein dynein. Plays a central role in positioning the mitotic spindle at the bud neck during cell division. Targets cytoplasmic dynein to microtubule plus ends, thereby promoting dynein-mediated microtubule sliding along the bud cortex and consequently the movement of the mitotic spindle to the bud neck.
Self-associates. Interacts with NDL1 and dynein.
Belongs to the uroporphyrinogen decarboxylase family.
Essential for respiratory growth and required for maintenance of mtDNA. Required for cell survival in the absence of prohibitins.
Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Belongs to the MsrA Met sulfoxide reductase family.
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.
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).
Expressed in limited copper conditions. Expression is positively controlled by MAC1 and TYE7. Induced during biofilm formation and contact with macrophages as well as by alkaline pH via RIM101. Expression is down-regulated by 17-beta-estradiol.
Impairs growth on solid low-copper and low-iron medium and displays altered morphology in response to copper-depleted conditions.
Required for high affinity copper (probably reduced Cu I) transport into the cell.
Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase 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.
Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily.
Nonessential protein required for the fusion of transport vesicles derived from the endocytic pathway with the Golgi complex.
Belongs to the phosphoenolpyruvate carboxykinase (ATP) family.
Involved in rRNA-processing at A0, A1 and A2 sites and regulates negatively telomerase.
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 phytoene/squalene synthase family.
Expression is induced by lovastatin and fluconazole and is repressed by amphotericin B and caspofungin (PubMed:14653518). Expression is repressed during spider biofilm formation (PubMed:22265407).
Squalene synthase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (By similarity). ERG9 produces squalene from 2 farnesyl pyrophosphate moieties (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable).
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Homohexamer or homoheptamer. Organized in a ring with a central cavity.
Belongs to the damage-control phosphatase family. Sugar phosphate phosphatase III subfamily.
Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism.
Subfamily III proteins have a conserved RTxK motif about 40-50 residues from the C-terminus; the threonine may be replaced by serine or cysteine.
Belongs to the snRNP core protein family.
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.
May mediate the reduction of outer membrane cytochrome b5.
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.
Putative adhesin which is involved in cell adhesion and virulence.
Essential component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. Required for the maturation of extramitochondrial Fe/S proteins.
Regulated in response to carbon source, temperature, growth phase, and physical environment. Expression is up-regulated by rapamycine, and thus is under the regulation of the TOR pathway. Binds its own promoter and is also under the control of EFG1.
Transcriptional regulator of the switch between 2 heritable states, the white and opaque states. These 2 cell types differ in many characteristics, including cell structure, mating competence, and virulence. Each state is heritable for many generations, and switching between states occurs stochastically, at low frequency. Contributes to formation of the opaque state, but is not necessary for heritability of the opaque state. Plays a role in cell adhesion and pseudohyphal growth. Involved in acquisition of drug resistance and acts as a repressor of beta-glucan synthesis, thus negatively regulating cell wall integrity. Plays a role in adherence, invasion and damage to oral epithelial cells.
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.
Component of the TIM23 complex, at least composed of TIM23, TIM17, TIM50 and TIM21.
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Required to keep the TOM and the TIM23 complexes in close contact. At some point, it is released from the TOM23 complex to allow protein translocation into the mitochondrial matrix (By similarity).
Defective in filamentation and invasive growth in response to environmental cues. Defective in the formation of biofilms. Displays decreased virulence in the greater wax moth Galleria mellonella infection model.
Interacts with FLO8 and MSS11, both morphogenetic transcription factors binding directly to the FLO11 promoter.
Transcriptional regulator with a general role in all morphogenetically distinct forms of filamentous growth, namely invasive growth and biofilm formation. May control FLO11 gene expression as part of a promoter-bound complex with FLO8 and MSS1. Important for virulence.
Belongs to the PDK/BCKDK protein kinase family.
Belongs to the formin homology family. BNI1 subfamily.
Homodimer, and possibly also homotetramer (By similarity). Interacts with actin via the FH2 domain (By similarity). Interacts with IQG1.
Leads to swollen cells, increased random budding pattern, and severe defect in cytokinesis with enlarged bud necks.
Required for the assembly of F-actin structures, such as actin cables and stress fibers. Nucleates actin filaments. Binds to the barbed end of the actin filament and acts as leaky capper, slowing both polymerization and depolymerization. Protects the growing actin fiber from tight capping proteins and so increases the time of elongation and the total amount of F-actin. May organize microtubules by mediating spindle positioning and movement in the budding process. Required for the maintenance of polarized hyphal growth. BNI1-mediated actin cables are necessary for positioning the Golgi complex to a putative site of germ tube emergence and for coordinating the transport and deposition of membrane and cell wall material to a growing hypha. Plays a key role in virulence.
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 Mediator complex subunit 31 family.
Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm.
Involved in nucleolar processing of pre-18S ribosomal RNA.
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.
Component of the ESCRT-I complex (endosomal sorting complex required for transport I), a regulator of vesicular trafficking process.
Expression is repressed by amphotericin B and caspofungin (PubMed:15917516). Expression is also repressed during biofilm formation (PubMed:22265407).
Heterotetramer of ERG25, ERG26, ERG27 and ERG28 (By similarity). ERG28 acts as a scaffold to tether ERG27 and other 4,4-demethylation-related enzymes, forming a demethylation enzyme complex, in the endoplasmic reticulum (By similarity).
Sterol-4-alpha-carboxylate 3-dehydrogenase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:12702354). ERG26 is a catalytic component of the C-4 demethylation complex that catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group (PubMed:12702354). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable).
N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.
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).
Cell surface beta-glucosidase involved in cell wall maintenance and cytokinesis. Plays a role redundant to SUN41.
Expression is up-regulated during biofilm formation and down-regulated by RIM101, CYR1, RAS1, as well as by host macrophages.
GPI-linked hyphal surface heme-binding protein involved in heme-iron utilization (PubMed:25275454, PubMed:27617569). Heme transfer occurs between PGA7, RBT5 and CSA2 supporting a model in which the 3 CFEM proteins cooperate in a heme-acquisition system and form a cross-cell wall heme-transfer cascade (PubMed:25275454, PubMed:27617569). The ability to acquire iron from host tissues is a major virulence factor of pathogenic microorganisms. Required for biofilm formation (PubMed:25275454).
Induced by hypoxia, ketoconazole, fluconazole, nitric oxide, ciclopirox olamine, during cell wall regeneration following protoplasting, during adhesion, and during biofilm formation. Regulated by UPC2, BCR1, HAP43, and RIM101.
Leads to defects in hemoglobin utilization as sole source of iron and decreased virulence on a mouse model of systemic candidiasis.
The CFEM domain is involved in heme-binding and contains 8 cysteines and is found in proteins from several pathogenic fungi, including both human and plant pathogens (PubMed:12633989, PubMed:22145027, PubMed:25275454). The CFEM domain adopts a novel helical-basket fold that consists of six alpha-helices, and is uniquely stabilized by four disulfide bonds formed by its 8 signature cysteines (By similarity).
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 (Probable). RPL25 is a major component of the universal docking site for these factors at the polypeptide exit tunnel (By similarity).
Belongs to the eukaryotic ribosomal protein eL15 family.
Expressed in greater amounts in the mature biofilms compared to early biofilms during inflammatory disorder of the palatal mucosa among denture wearers.
Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. Serves as a major regulator of MSB2-processing which activates CEK1 MAPK-signaling affecting biofilm formation and oropharyngeal candidiasis. Moreover, acts toward human hemoglobin though limited proteolysis to generate a variety of antimicrobial hemocidins, enabling to compete with the other microorganisms of the same physiological niche using the microbicidal peptides generated from the host protein.
Belongs to the pseudouridine synthase RluA family.
Pseudouridylate synthase responsible for the pseudouridine-2819 formation in mitochondrial 21S rRNA. May modulate the efficiency or the fidelity of the mitochondrial translation machinery.
Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
Regulator of type 1 phosphatases which maintains protein phosphatase activity under strict control.
Belongs to the eukaryotic ribosomal protein eS25 family.
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 FKBP-type PPIase family. FKBP1 subfamily.
Belongs to the alkylbase DNA glycosidase AlkA family.
Component of the mitochondrial small ribosomal subunit (mt-SSU).
Mitochondrial transcription factor that confers selective promoter recognition on the core subunit of the yeast mitochondrial RNA polymerase. Interacts with DNA in a non-specific manner.
Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
Homodimer; disulfide-linked, upon oxidation.
Results in delayed hyphal development and enhanced sensitivity to cell wall-perturbing agents, yet does not impair virulence in vivo.
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Also involved in the correct composition of the hyphal cell wall.
Belongs to the transferase hexapeptide repeat family.
Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint (By similarity).
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.
Predicted GPI-anchored protein which may have a role during host infection.
Substrate for cleavage by KEX2 in vitro.
Up-regulated upon milbemycins A3 oxim derivative (A3Ox) treatment, upon interaction of cells with host macrophages, and during oralpharyngeal candidiasis. Repressed by alpha pheromone.
Belongs to the palmitoyl-protein thioesterase family.
Involved in chitin synthesis and also required for mating.
Regulates the cell cycle in a nutrient dependent manner.
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 eukaryotic ribosomal protein eL39 family.
Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins.
Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family.
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 ribonucleoside diphosphate reductase large chain family.
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
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).
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 fungal Na(+)/H(+) exchanger family.
Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus.
Belongs to the universal ribosomal protein uL5 family.
Belongs to the SLC26A/SulP transporter (TC 2.A.53) 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 MID2 like cell wall stress sensor family.
Cell-surface associated glycoprotein that acts as a plasma membrane receptor-type protein which senses the presence of matrix. Binds to calmodulin in response to environmental conditions and initiates a signaling cascade that activates CEK1, thus promoting invasive filamentation. Involved in the maintenance of the cell wall.
Cross-linked to the carbohydrate polymers of the cell wall.
O-glycosylated by MNT1 and MNT2. Also N-glycosylated.
Shows defects in invasion of agar medium and attenuated virulence in a murine model of disseminated candidiasis. Leads to hypersensibility to the glucan synthase inhibitor capsofungin and the cell wall disturbing agents Congo red and calcofluor white.
The GxxxG glycophorin motif in the transmembrane domain is required for CEK1 activation and subsequent invasive filamentation on agar medium.
The cytoplasmic C-terminal calmodulin-binding motif (residues 301 to 317) is important for CEK1 activation and subsequent invasive filamentation on agar medium.
Required for cytoplasm to vacuole transport (Cvt), pexophagy and mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Functions in protein retrieval from the endocytic pathway (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 a complex that contains SEC61, SEC62, SEC63, SEC66 and SEC72.
Expression is detected as early as 1 hour after infection of reconstituted human esophageal tissue and increases thereafter up to 48 hours postinfection.
Final receptor of the SLN1-YPD1-SSK1 two-component regulatory system, which controls activity of the HOG1 pathway in response to oxidative stress and probably also to the osmolarity of the extracellular environment. Involved in cell wall biosynthesis, hyphal growth, and virulence. Regulates the expression of CHK1, as well as of a subset of genes whose functions are associated with cell wall biosynthesis and adaptation to oxidative stress. Provides at least partial adaptive functions for the survival following encounter with human neutrophils.
Leads to flocculation, attenuated virulence towards reconstituted human esophageal tissue, and to hypersensitivity to fluconazole and voriconazole.
Belongs to the complex I NDUFA5 subunit 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.
Mannosyltransferase involved in outer chain elongation of asparagine-linked oligosaccharides of the type Man(9)GlcNAc(2). Adds the first alpha-1,6-mannose to the Man(8)GlcNAc(2) and Man(9)GlcNAc(2), but not Man(5)GlcNAc(2), endoplasmic reticulum intermediates (By similarity). Represents the first enzymatic event required for synthesis of outer chain mannose linkages on yeast secretory proteins. N-glycan outer chain epitopes play a crucial role in the host-fungal interaction, virulence, and host immune response such as interleukin synthesis or phagocytosis by neutrophils.
Results in a temperature-sensitive growth defect, cellular aggregation, loss of outer chain elongation of N-glycans, hypersensitivity to a range of cell wall perturbing agents, as well as to constitutively activated cell wall integrity pathway. Finally, leads to attenuated virulence in a mouse model of systemic infection and affects inflammatory response and the efficiency of neutrophil phagocytosis by the host.
The conserved DXD motif is involved in enzyme activity.
Component of the TIM23 complex, at least composed of TIM23, TIM17, TIM50 and TIM21. Interacts with preproteins in transit (By similarity).
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Required to direct preproteins in transit and direct them to the channel protein TIM23, and possibly facilitates transfer of the translocating proteins from the TOM complex to the TIM23 complex (By similarity).
Belongs to the glycosyl hydrolase 47 family.
Involved in the assembly of the cytochrome c oxidase complex.
Heme-binding protein involved in heme-iron utilization. The ability to acquire iron from host tissues is a major virulence factor of pathogenic microorganisms. Involved in biofilm formation.
Induced by RIM101 at pH8, hypoxia, ketoconazole, ciclopirox, and during hyphal growth. Regulated by UPC2 and BCR1.
The CFEM domain is involved in heme-binding and contains 8 cysteines and is found in proteins from several pathogenic fungi, including both human and plant pathogens (PubMed:12633989). The CFEM domain adopts a novel helical-basket fold that consists of six alpha-helices, and is uniquely stabilized by four disulfide bonds formed by its 8 signature cysteines (By similarity).
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 phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
Belongs to the OMP decarboxylase 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).
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. This subunit can bind 18S rRNA.
Belongs to the STE12 transcription factor family.
Transcription factor involved in the formation of pseudohyphae and hyphae. It is likely to play a role in the developmental switch between yeast and mycelial forms. May be involved in a signal transduction system, strengthening the possibility of a sexual phase up to now undetected, and similar to that of the yeast mating pathway.
Belongs to the alpha-IPM synthase/homocitrate synthase family. Homocitrate synthase LYS20/LYS21 subfamily.
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.
Belongs to the Mediator complex subunit 19 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.
May be involved in the modulation of rDNA transcription.
Cell surface protein required for proper cell wall integrity and for the correct assembly of the mannoprotein outer layer of the cell wall.
Expression is induced by growth in hypoxic conditions and by caspofungin and ketoconazole. Expression is negatively regulated by BCR1, HOG1, PLC1, RIM101, SSN6, and SUR7.
Is probably involved in a pathway contributing to genomic integrity.
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 eukaryotic/archaeal RNase P protein component 3 family.
Induced in biofilms and in oralpharyngeal candidasis. Repressed by alpha pheromone.
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).
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
Constitutively expressed and not cell-cycle regulated like its S.cerevisiae ortholog.
Decreases virulence in murine infection models.
Plays a role in resistance to host antimicrobial peptides such as protamine, RP-1, or human beta-defensin-2; allowing colonization of human tissues. Required for resistance to membrane permeabilization and maintenance of mitochondrial membrane potential upon exposure to RP-1.
Component of the outer cell wall layer required for stability of the cell wall and specifically for cell wall rigidity.
Covalently linked to beta-1,3-glucan of the inner cell wall layer via an alkali-sensitive ester linkage between the gamma-carboxyl group of glutamic acids, arising from specific glutamines within the PIR1/2/3 repeats, and hydroxyl groups of glucoses of beta-1,3-glucan chains.
Expression varies during the cell-cycle with a peak at the beginning of G1. Expression increases in hypoxic and acidic conditions and is down-regulated during the switch from yeast to hyphal growth and under low-iron conditions. The promoter contains E-box consensus sequences (CANNTG) suggesting that PIR1 is directly regulated by EFG1. Expression is also regulated by ACE2, HOG1, and RIM101.
Highly O-glycosylated by PMT1 and contains one N-mannosylated chain.
Increases sensitivity to calcofluor white and Congo red.
The PIR1/2/3 repeats are required for covalent linkage to the cell wall.
Putative adhesin which may be involved in cell adhesion and virulence.
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.
Belongs to the bacterial ribosomal protein bS16 family.
Belongs to the alternative oxidase family.
Catalyzes cyanide-resistant oxygen consumption. May increase respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures.
Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity.
Belongs to the peptidase M24 family. SPT16 subfamily.
Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II (By similarity).
Forms a stable heterodimer with POB3. The SPT16-POB3 dimer weakly associates with multiple molecules of NHP6 to form the FACT complex (By similarity).
Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.
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).
Appears to play a crucial role in the insertion of secretory and membrane polypeptides into the ER. It is required for assembly of membrane and secretory proteins and is essential for cell growth. It interacts with other membrane proteins required for protein translocation. Upon binding to SEC62/63 complex, secretory precursor polypeptides may engage SEC61 to begin membrane penetration event. A cycle of assembly and disassembly of SEC62/63 from SEC61 may govern the activity of the translocase (By similarity).
Heterotrimeric complex composed of SEC61-alpha, SEC61-beta and SEC61-gamma.
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 ubiquitin-activating E1 family. UBA3 subfamily.
Catalytic subunit of the dimeric E1 enzyme, which activates NEDD8.
Belongs to the Mediator complex subunit 14 family.
Binds 1 thiamine pyrophosphate per subunit.
Predicted to be a cleavage substrate for KEX2.
Putative adhesin which is involved in cell adhesion and virulence (By similarity). Plays a role in Candida-bacterial interactions and subsequent regulation of filamentation.
Belongs to the Mediator complex subunit 15 family.
Microtubule binding protein that promotes the stabilization of dynamic microtubules. Required for mitotic spindle formation (By similarity).
Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1 subfamily.
Belongs to the helicase family. UvrD subfamily.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily.
Expression is increased in low iron conditions.
GTPase activating protein (GAP) for RSR1 which is involved in the polarization of yeast and hyphal cells. Directs the site of new daughter cell growth in yeast and hyphal cells. Important for hyphae to maintain linear growth and necessary for hyphal responses to directional cues in the environment (tropisms). Required for correct localization of the septin rings and stabilization of the polarisome at hyphal tips. Involved in cell adhesion.
Belongs to the ribulose-phosphate 3-epimerase family.
Binds 1 divalent metal cation per subunit.
Leads to increased drug susceptibility. Displays decreased colonization of mouse kidneys. Shows decreased yeast cell adherence to silicone substrate.
Transcription factor that controls the expression of CDR1, the major multidrug efflux pump. Required for yeast cell adherence to silicone substrate and plays a role in virulence.
Belongs to the universal ribosomal protein uL18 family.
C-22 sterol desaturase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (Probable). ERG5 converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable).
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CHEK2 subfamily.
Controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints. Phosphorylates proteins on serine, threonine, and tyrosine. Prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.
Belongs to the protein kinase superfamily. RIO-type Ser/Thr kinase family.
Belongs to the eukaryotic-type primase small subunit family.
Required for replication-independent chromatin assembly and for the periodic repression of histone gene transcription during the cell cycle.
Belongs to the FIT family. Fungal FIT2B/SCS3 subfamily.
Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate. Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen. This catalytic activity is required for maintaining ER structure and for lipid droplets (LDs) biogenesis, which are lipid storage organelles involved in maintaining lipid and energy homeostasis. May directly bind to diacylglycerol (DAGs) and triacylglycerol, which is also important for LD biogenesis. May support directional budding of nacent LDs from the ER into the cytosol by reducing DAG levels at sites of LD formation. May play a role in the regulation of cell morphology and cytoskeletal organization. Involved in phospholipid biosynthesis.
Belongs to the XPG/RAD2 endonuclease family. FEN1 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.
Interacts with PCNA. Three molecules of RAD27 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.
Mediates inactivation of the TORC1 complex in response to amino acid starvation. Required for meiotic nuclear division (By similarity).
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.
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.
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.
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.
Belongs to the glycosyltransferase 2 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.
Acts as a cytolytic peptide toxin that directly damages host epithelial membranes, triggers a danger response signaling pathway and activates epithelial immunity (PubMed:27027296, PubMed:35073742). Probably acts similarly to cationic antimicrobial peptide toxins, inducing lesions after binding to target cell membranes and causing an inward current associated with calcium influx (PubMed:27027296).
Cleavage by KEX2 generates 8 peptides ECE1-I to ECE1-VIII, all terminating in Lys-Arg (PubMed:18625069, PubMed:27027296). Only peptide ECE1-III, called candidalysin, shows toxin activity (PubMed:27027296).
Expressed in elongating hyphae but not in budding yeast cells (PubMed:8359888).
Expression is induced by human serum and epithelial cells (PubMed:24673895). Expression is regulated by the transcription factor EFG1 (PubMed:10464197, PubMed:10790384). Expression is also regulated by the transcription factor BCR1 (PubMed:16839200).
Impairs damaging of epithelia and induction of p-MKP1/c-Fos-mediated danger responses and cytokine secretion (PubMed:27027296).
Secreted protein cleaved by KEX2 in 8 similar peptides (ECE1-I to ECE1-VIII) (PubMed:27027296). Stimulates biofilm formation (PubMed:16839200).
The N-terminal alpha-helix of peptide ECE1-III allows insertion of the toxin into host epithelial cells membranes (PubMed:27027296).
Expression is induced in biofilm and repressed by fluconazole. Expression is also regulated by SS1.
Belongs to the PAPS reductase family. CysH subfamily.
Small GTPase required for proper nuclear import of RNA polymerase II (RNAPII). May act at an RNAP assembly step prior to nuclear import.
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.
Probable helicase, member of the UBC2/RAD6 epistasis group. Functions with DNA repair protein RAD18 in error-free postreplication DNA repair. Involved in the maintenance of wild-type rates of instability of simple repetitive sequences such as poly(GT) repeats. Seems to be involved in maintaining a balance which acts in favor of error-prone non-homologous joining during DNA double-strand breaks repairs (By similarity).
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
Expressed under acidic conditions. Expression is positively regulated by HAP43 and NRG1, and repressed by RIM101. Expression is also controlled by SUR7.
Probable cell wall protein required for filamentation at low pH.
Belongs to the dihydroxyacetone kinase (DAK) family.
Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde.
Cell surface beta-glucosidase involved in cytokinesis, cell wall biogenesis, adhesion to host tissue, and biofilm formation; thus playing an important role in the host-pathogen interaction. Has hydrolytic activity on linear (1->3)-beta-D-glucans such as laminaribiose and other laminarioligosaccharides.
Leads to increased cell size, cytokinesis defects, altered sensitivity to the cell wall-modifying substance Congo red, defects in adhesion, and reduced biofilm formation.
Strongly up-regulated under hypoxic conditions and in white but not opaque cells (PubMed:16854431, PubMed:19798425). Repressed by exposure to caspofungin (PubMed:15917516). Expression is probably regulated by EFG1 since SUN41 has 9 E-boxes in its promoter (PubMed:12492856).
Belongs to the universal ribosomal protein uL13 family.
Expression is induced by CPH2 which directly binds to the two sterol regulatory element 1-like elements upstream of TEC1. Expression is also regulated by the histone deacetylase complex HDAC3, as well as by TOR1 and EFG1. Moreover, heat shock factor-type transcriptional regulator SFL1 represses expression whereas SFL2 induces expression. In white cells, is up-regulated in the presence of alpha-pheromone. Expression is induced during oropharyngeal candidiasis (OPC). Competitors Escherichia coli, Pseudomonas aeruginosa, and Salmonella typhimurium secreted factors decrease TEC1 expression to impair biofilm formation. Expression is also down-regulated by linoleic acid and tetrandrine.
Impairs the formation of germ tubes and true hyphae; and decreases virulence in a mouse model of systemic candidiasis. Leads to defective biofilm under normoxic conditions but not under hypoxic conditions.
Transcription factor which regulates genes involved in hyphal development, cell adhesion, biofilm development, and virulence. Plays a role in the formation of 'finger' morphology, a unique multicellular morphology of C.albicans induced by carbon dioxide. Regulates gene expression during intestinal colonization. Required for the expression of the secreted aspartyl proteinases SAP4, SAP5, and SAP6; but also of BCR1, PGA4, and CDC24. Moreover, a positive feedback loop between CDC24 and TEC1 contributes to an increase in active CDC42 at the tip of the germ tube which is important for hyphae formation. Regulates also the pheromone response of the white cell phenotype.
Belongs to the major facilitator superfamily. Proton-dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
Belongs to the acetyltransferase family.
N-acetylglutamate synthase involved in arginine biosynthesis.
Up-regulated in cells treated with farnesol and grown at high cell density in N-acetyl-D-glucosamine medium. Expression is regulated by the general amino acid control response transcription factor GCN4.
Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
Belongs to the small GTPase superfamily. SAR1 family.
COPII is composed of at least 5 proteins: the SEC23/24 complex, the SEC13/31 complex and SAR1.
Small GTPase component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SAR1 controls the coat assembly in a stepwise manner. Activated SAR1-GTP binds to membranes first and recruits the SEC23/24 complex. These SEC23/24-SAR1 prebudding intermediates are then collected by the SEC13/31 complex as subunits polymerize to form coated transport vesicles. Conversion to SAR1-GDP triggers coat release and recycles COPII subunits (By similarity).
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 (By similarity). Plays an important role in resistance to several stresses, as well as in autophagy and virulence (PubMed:25038082).
Results in the inability to grow at alcaline pH and altered resistance to calcium, osmotic stress, cold temperature, antifungal drugs and growth on non-fermentable carbon sources. Leads also to unability to fully assemble the V-ATPase at the vacuolar membrane and impairs its proton transport and ATPase activities. Finally, leads to autophagy defect and avirulence in a Caenorhabditis elegans infection model.
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).
Expression is increased with increased iron.
Transcription factor involved in iron utilization and virulence.
Attenuates virulence in a mouse model of systemic infection.
Transcription factor required for hyphal growth, biofilm formation, and virulence. Promotes formation of both conventional and pheromone-stimulated biofilms. Binds and recruits HDA1 to promoters of hypha-specific genes in a rapamycin-dependent manner. Involved in the switch between two heritable states, the white and opaque states. These two cell types differ in many characteristics, including cell structure, mating competence, and virulence. Each state is heritable for many generations, and switching between states occurs stochastically at low frequency.
Up-regulation during the yeast-to-hypha transition is dependent upon the function of YAK1. HOG1 represses the expression of BRG1 via the transcriptional repressor SKO1. Regulated by TYE7 during late-stage biofilm formation.
Belongs to the Mediator complex subunit 1 family.
Component of the Golgi to ER traffic (GET) complex, which is composed of GET1, GET2 and GET3. Within the complex, GET1 and GET2 form a heterotetramer which is stabilized by phosphatidylinositol binding and which binds to the GET3 homodimer.
Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Together with GET2, acts as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. The GET complex cooperates with the HDEL receptor ERD2 to mediate the ATP-dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER.
Fails to undergo filamentation under a range of hypha-inducing conditions and attenuates the virulence towards reconstituted human oral epithelium and in a mouse model of gastrointestinal colonization and dissemination.
Induced at high temperature and during human oral epithelium infection.
Transcription factor that plays a role of activator of filamentous growth and which is involved in invasive growth at a high temperature. Required for human oral epithelium colonization and damage. Promotes filamentous growth in EFG1- and FLO8-dependent manners. Antagonizes functions of SFL1.
Belongs to the eukaryotic ATPase epsilon family.
Belongs to the class-I DAHP synthase family.
Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
Required for proper homologous chromosome pairing and efficient cross-over and intragenic recombination during meiosis.
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.
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).
Belongs to the eukaryotic GSH synthase family.
Belongs to the bacterial ribosomal protein bL32 family.
Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment.
Belongs to the PIGG/PIGN/PIGO family. PIGN subfamily.
Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor (By similarity).
Belongs to the DNA polymerase type-B family.
Belongs to the ABC transporter superfamily. ABCG family. PDR (TC 3.A.1.205) subfamily.
Multidrug efflux transporter. Confers resistance to azole antifungal agents, to other antifungals (terbinafine, amorolfine) and to a variety of metabolic inhibitors.
Acetyl-CoA acetyltransferase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity). ERG10 catalyzes the formation of acetoacetyl-CoA from acetyl-CoA (By similarity). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase ERG10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthase ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase HMG1 finally reduces HMG-CoA to produce mevalonate (Probable).
Expression is up-regulated in azole resistant clinical isolates (PubMed:15215138). Expression is induced by exposure to arole antifungals such as fluconazole, ketoconazole or itraconazole (PubMed:11353609, PubMed:15820985).
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 universal ribosomal protein uS9 family.
Belongs to the eukaryotic RPA49/POLR1E RNA polymerase subunit family.
Catalyzes the ferrous insertion into protoporphyrin IX.
Belongs to the mitochondrion-specific ribosomal protein mL67 family.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. mL67/MHR1 also has extraribosomal functions, being involved in regulation of mitochondrial DNA recombination, maintenance and repair, and generation of homoplasmic cells. mL67/MHR1 also acts as transcription factor involved in regulation of RNA polymerase II-dependent transcription.
Involved in the partitioning of the mitochondrial organelle and mitochondrial DNA (mtDNA) inheritance.
Belongs to the eukaryotic AdoMetDC family.
Component of the 7-subunit TFIIH core complex composed of XPB/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is active in NER. The core complex associates with the 3-subunit CTD-kinase module TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription.
Belongs to the Mediator complex subunit 17 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 TIM8 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity).
Binds the 3'-UTR of mitochondrial mRNAs (By similarity). Involved in the processing or stability of mitochondrial mRNAs (By similarity).
Phosphorylated. Phosphorylation promotes binding to RNA.
Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by the MOCS3 homolog UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates.
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.
Belongs to the universal ribosomal protein uL2 family.
Belongs to the oxidase-dependent Fe transporter (OFeT) (TC 9.A.10.1) family.
Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells. Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy, mitophagy, and pexophagy.
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.
Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA (By similarity).
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family.
Catalyzes methylation of the sphingoid base component of glucosylceramides (GluCers) at the C9-position. Sphingolipid C9-methylation requires 4,8-desaturated ceramides as substrates. Glucosylceramides play important roles in growth, differentiation and pathogenicity. The methyl group at the C9-position distinguishes fungal glucosylceramides from those of plants and animals, and may thus play a role in host-pathogen interactions enabling the host to recognize the fungal attack and initiate specific defense responses. Not necessary for vegetative growth at low temperatures, but plays a role in hyphal formation on solid medium.
Produces only non-methylated glucosylceramides. Has a decreased hyphal growth rate.
Component of the transcription regulatory histone acetylation (HAT) complex SAGA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation and deubiquitination. SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs) (By similarity). SPT20 plays a role in nuclear division and regulates hyphal and biofilm formation, which are crucial steps for virulence.
Expression is down-regulated by flucytosine and upon adherence to polystyrene.
Impairs proper nucleus dividing and distribution to the dividing cells. Leads to hypersensitivity to amphotericin B, fluconazole and caspofunginreduced; and to reduced virulence in the C.elegans and the G.mellonella infection models.
Required for gamma-tubulin complex recruitment to the microtubule organizing center (MTOC).
Belongs to the ATPase delta chain family.
Belongs to the eukaryotic ribosomal protein eL13 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.
The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER).
Cell wall protein that plays a role in adaptation and resistance to cell wall stress.
Expression is induced in high iron conditions.
Belongs to the aspartate-semialdehyde dehydrogenase family.
Belongs to the NFYB/HAP3 subunit family.
Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Transcriptional corepressor that acts in conjunction with ALPHA2 to repress transcription both of homozygote-specific genes and of genes necessary for the white-opaque switch, a prerequisite for mating.
Moderately repressed by HBR1 in response to hemoglobin and growth signals.
Most C.albicans strains are heterozygous at the MTL locus and do not readily undergo white-opaque switching and mating, but mating occurs in hemi- or homozygous strains. Mating takes place in opaque cells, produces tetraploid progeny and seems to occur rarely, if at all, in nature. Conservation of mating capacity is rather thought to be due to the simultaneously regulated white-opaque switch, which seems to play an important role in host commensalism.
Belongs to the XPG/RAD2 endonuclease family.
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Homodimer. Component of the ER-mitochondria encounter structure (ERMES) or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34. A MMM1 homodimer associates with one molecule of MDM12 on each side in a pairwise head-to-tail manner, and the SMP-LTD domains of MMM1 and MDM12 generate a continuous hydrophobic tunnel for phospholipid trafficking.
The SMP-LTD domain is a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM61 family.
Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA.
Heterotetramer; composed of two copies of TRM6 and two copies of TRM61.
Belongs to the complex I 23 kDa subunit family.
Cleaves A-5'-PPP-5'A to yield AMP and ADP. Can cleave all dinucleoside polyphosphates, provided the phosphate chain contains at least 3 phosphates and that 1 of the 2 bases composing the nucleotide is a purine. Is most effective on dinucleoside triphosphates. Negatively regulates intracellular dinucleoside polyphosphate levels, which elevate following heat shock.
May be involved in a process influencing telomere capping.
Belongs to the archaeal/bacterial/fungal opsin family.
Cleaves internal linkages in 1,3-beta-glucan (PubMed:16328626). Involved in the cell separation process. Plays no essential role in growth, nor is it involved in hyphal morphogenesis (PubMed:16328626).
Expression is decreased during the hyphal transition, in biofilm, as well as by heat stress, caspofungin, fluconazole, and alpha pheromone. Transcription is also regulated by ACE2 and SIT4.
Leads to clusters of growing cells that have not completed separation.
Activity is inhibited by squash aspartic peptidase inhibitor (SQAPI).
Expressed during development of germ tubes, pseudohyphae and true hyphae. Induced during host infection. Expression is suppressed by fluconazole.
Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. Activates host systemic immunity. During infection, plays an important role in penetration into deeper tissues and interaction with host defense. Moreover, acts toward human hemoglobin though limited proteolysis to generate a variety of antimicrobial hemocidins, enabling to compete with the other microorganisms of the same physiological niche using the microbicidal peptides generated from the host protein.
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.
Associates in the nucleolus with the 60S and pre-60S ribosomal subunits.
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).
Belongs to the DNA repair enzymes AP/ExoA family.
Probably binds two magnesium or manganese ions per subunit.
Belongs to the peptidase M16 family. UQCRC2/QCR2 subfamily.
Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 3 respiratory subunits cytochrome b, cytochrome c1 and Rieske protein, 2 core protein subunits, and additional low-molecular weight protein subunits. The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with cytochrome c oxidase (complex IV, CIV).
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Does not seem to have protease activity as it lacks the zinc-binding site.
Component of the cell wall involved in virulence. Does not seem to have a major role in maintaining cell wall integrity but plays a role in the relationship between C.albicans and the host.
Down-regulated during yeast-to-hyphal transition and by fluconazole. Induced during cell wall regeneration following protoplasting and highly overexpressed after treatment with micafungin.
Leads to a significant reduction of cell wall mannan and to decreased virulence with a diminished induction of host pro-inflammatory cytokines.
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.
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).
Component of the ribosomal small subunit (SSU) processome.
Involved in nucleolar processing of pre-18S ribosomal RNA. Involved in ribosome biosynthesis (By similarity).
Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
Binds 1 dipyrromethane group covalently.
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
The porphobilinogen subunits are added to the dipyrromethan group.
Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.
Belongs to the DASH complex DAD4 family.
Present with 3460 molecules/cell in log phase SD medium.
Required for normal beta-1,6-glucan synthesis, for hyphal morphogenesis, adhesion and virulence.
Belongs to the universal ribosomal protein uL22 family.
Belongs to the DEAD box helicase family. DEAH subfamily. DDX15/PRP43 sub-subfamily.
Belongs to the F-actin-capping protein alpha 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 NUP186/NUP192/NUP205 family.
Belongs to the glutathione peroxidase family.
Involved in oxidative stress response and redox homeostasis. Functions as a sensor and transducer of hydroperoxide stress. In response to hydroperoxide stress it oxidizes (activates) the transcription activator CAP1, which is involved in transcription activation of genes of the oxidative stress response pathway (PubMed:23706023). May also play a direct role in hydroperoxide scavenging. The enzyme is not required for the glutaredoxin-mediated antioxidant function. In the presence of peroxides, GPX3 is directly oxidized at Cys-43 to form a cysteine sulfenic acid (-SOH). Cys-43-SOH then forms either an intramolecular disulfide bond (Cys-43 with Cys-89) or a transient, intermolecular disulfide bond with 'Cys-446' of CAP1, which is further resolved into a CAP1 intramolecular disulfide bond ('Cys-303' with 'Cys-598'), which causes its nuclear accumulation and activation, and a reduced Cys-43 in GPX3 (By similarity). Required for C.albicans-mediated macrophage killing (PubMed:23706023).
Sensitive to hydrogen peroxide. Unable to filament and thus, escape from murine macrophages after phagocytosis. Also displays defective virulence in the Galleria mellonella infection model.
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this atypical 2-Cys peroxiredoxin, C(R) is present in the same subunit to form an intramolecular disulfide.
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) (By similarity).
Heterodimer with PAM16. Component of the PAM complex, at least composed of mtHsp70, MGE1, TIM44, PAM16, PAM17 and PAM18 (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 helicase family. PIF1 subfamily.
DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance of telomeric DNA. Inhibits telomere elongation, de novo telomere formation and telomere addition to DSBs via catalytic inhibition of telomerase. Reduces the processivity of telomerase by displacing active telomerase from DNA ends. Releases telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid that is the intermediate in the telomerase reaction. Involved in the maintenance of ribosomal (rDNA). Required for efficient fork arrest at the replication fork barrier within rDNA. Involved in the maintenance of mitochondrial (mtDNA). Required to maintain mtDNA under conditions that introduce dsDNA breaks in mtDNA, either preventing or repairing dsDNA breaks. May inhibit replication progression to allow time for repair. May have a general role in chromosomal replication by affecting Okazaki fragment maturation. May have a role in conjunction with DNA2 helicase/nuclease in 5'-flap extension during Okazaki fragment processing.
Belongs to the cytochrome c oxidase VIIc 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. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII).
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.
Required for the addition of the long alpha 1,6-mannose backbone of N-linked glycans on cell wall and periplasmic proteins.
Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
Expression is regulated by SEF1, SFU1, and HAP43.
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/SPO72 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/SPO72 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.
Belongs to the ThrE exporter (TC 2.A.79) family.
Belongs to the SEC23/SEC24 family. SEC23 subfamily.
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 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.
eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least eIF4A, eIF4E and eIF4G. eIF4E is also known to interact with other partners (By similarity).
Belongs to the TPT transporter family. SLC35D subfamily.
Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen. Involved in hyphal formation.
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.
In eukaryotes there are two forms of the enzymes: a cytosolic one and a mitochondrial one.
Belongs to the acetyltransferase family. GCN5 subfamily.
Acts on phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol 1,4,5,-trisphosphate.
Consists of at least two heavy chains and a number of intermediate and light chains.
Abolishes D-arabinono-1,4-lactone oxidase activity and impairs the production of D-erythroascorbic acid (PubMed:11349062). Leads to increased sensitivity towards oxidative stress, defective hyphal growth and attenuated virulence (PubMed:11349062).
Belongs to the oxygen-dependent FAD-linked oxidoreductase family.
D-arabinono-1,4-lactone oxidase that catalyzes the final step of biosynthesis of D-erythroascorbic acid, an important antioxidant and one of the virulence factors enhancing the pathogenicity (PubMed:11349062, PubMed:7957197). Is also able to oxidize L-galactono-1,4-lactone, L-xylono-1,4-lactone and L-gulono-1,4-lactone (PubMed:7957197).
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 (PubMed:25220074). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:25220074). Mediates oxidative stress response, filamentous growth, and plays an important role in virulence (PubMed:25220074).
Leads to a defect in vacuolar acidification and higher sensitivity to oxidants such as H(2)O(2) or menadione. Reduces strongly virulence in mice.
Belongs to the ubiquitin-activating E1 family. ULA1 subfamily.
Regulatory subunit of the dimeric UBA3-ULA1 E1 enzyme.
Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.
Decreases phagocytosis of the fungus by host cells (PubMed:34986357). Increases expression of GPD2 (PubMed:34986357).
Oxidoreductase that binds mammalian estrogens with high affinity.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
Belongs to the copper/topaquinone oxidase family.
Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
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.
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-7; H2AS128ph = phosphorylated Ser-129.
Belongs to the ribose 5-phosphate isomerase family.
Involved in the first step of the non-oxidative branch of the pentose phosphate pathway. It catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Belongs to the proteasome subunit S11 family.
Required for establishment of the axial budding pattern in yeast cells. May be involved in the selection of future sites of septation in hyphal cells. Contributes to morphogenesis and is important for induction of hyphal growth. Also plays a role in epithelial adherence, and is involved in intestinal colonization and systemic infection. The role in adhesion is probably minor compared with its role in morphogenesis.
Catalyzes the dephosphorylation of the nucleoside 5'-monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and deoxythymidine monophosphate (dTMP).
Binds human HTN3/histatin-5, a peptide from saliva, and mediates its fungicidal activity.
Belongs to the 5-formyltetrahydrofolate cyclo-ligase 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.
5' to 3' DNA replicative helicase recruited to paused replisomes to promote fork progression throughout nonhistone protein-DNA complexes, naturally occurring impediments that are encountered in each S phase where replication forks pauses. Required for timely replication of the telomere and subtelomeric DNA and for wild-type levels of telomeric silencing. Involved in DNA repair during stalled replication fork, regulation of fragile sites expression and essential for genome stability. Plays also a role in mtDNA replication. Has G-quadruplex (G4) unwinding activity and can suppress G4-induced genome instability when PIF1 levels are low.
Belongs to the pantothenate synthetase family.
E3 RING-finger protein, member of the UBC2/RAD6 epistasis group. Associates to the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA.
Interacts with E2 UBC2, forming a complex with ubiquitin ligase activity.
Expression is specific for the white growth phase. Down-regulation under hyphal induction depends on the presence of EFG1 itself which plays a role of autoinhibitor and the protein kinase A isoforms TPK1 and TPK2.
Thr-208 is a phosphorylation target to promote hyphal induction by a subset of environmental cues. Phosphorylation at Thr-181 by the CDc28/HGC1 complex represses cell separation genes and leads to hyphal chain formation.
Transcriptional regulator of the switch between 2 heritable states, the white and opaque states. These 2 cell types differ in many characteristics, including cell structure, mating competence, and virulence. Each state is heritable for many generations, and switching between states occurs stochastically, at low frequency. Antagonizes the action of WOR1, WOR2 and CZF1, and promotes the white state. In white cells, EFG1 represses WOR1 indirectly through WOR2 to maintain white cell identity. Binds target gene promoters at the EFG1 recognition sequence (EGRbox) TATGCATA. Acts as a major regulator of cell wall dynamics and plays a role in interactions with extracellular matrices. Required for TOR1-dependent cellular aggregation and adhesin expression. Required for both normoxic and hypoxic biofilm formation. Hypoxic biofilm formation is a major cause of perseverance and antifungal resistance during infections. Contributes to virulence by regulating hyphal formation and the factors that enable C.albicans to invade and injure endothelial cells. Required for the formation of thick-walled big resting spores called chlamydospores, which survive in unfavorable conditions. Mediates the expression of virulence factors SAP4, SAP5and SAP6 during infection. Involved in drug resistance by regulating the expression of ERG3.
Amino-acid permease involved in S-adenosylmethionine (SAM) transport and required for SAM-induced morphogenesis (PubMed:28028545). GAP4 is also able to transport arginine and thialysine, and thus probably also lysine (PubMed:21764911).
Expression is under control of the CSY1 amino-acid sensor (PubMed:28028545). Expression is also regulated by HAP43, GCN2, GCN4 and SSN6 (PubMed:16215176, PubMed:15814841, PubMed:21592964). Induced during biofilm development (PubMed:22265407).
Belongs to the eukaryotic RPB4 RNA polymerase subunit family.
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37.
RNA-binding protein involved in post-transcriptional regulation through transcript degradation.
Belongs to the glycosyl hydrolase 3 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.
In the C-terminal section; belongs to the NAD synthetase 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 helicase family. SKI2 subfamily.
Belongs to the phosphatidylethanolamine-binding protein family.
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Belongs to the Mediator complex subunit 4 family.
Belongs to the universal ribosomal protein uS12 family.
Involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs.
Belongs to the ATP phosphoribosyltransferase family.
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of the enzymatic activity (By similarity).
Belongs to the phosphohexose mutase family.
Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, which is a biosynthetic precursor of chitin and also supplies the amino sugars for N-linked oligosaccharides of glycoproteins.
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.
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.
Belongs to the TRAFAC class YlqF/YawG GTPase family. GEP3 subfamily.
May be involved in the mitochondrial lipid metabolism.
Probable rhomboid-type serine protease that catalyzes intramembrane proteolysis.
Impairs the transport and degradation of ATG8 (PubMed:31284951). Suppresses also the degradation of both LAP41 (the indicator of the cytoplasm-to-vacuole pathway) and CSP37 (the indicator of mitophagy) (PubMed:31284951).
Plays an essential role in both non-selective and selective autophagy such as mitophagy (PubMed:31284951). Recruits mitochondria for their selective degradation via autophagy (mitophagy) during starvation, through its interaction with ATG32 (By similarity). Works as scaffold proteins that recruit ATG proteins to the pre-autophagosome (PAS), the site of vesicle/autophagosome formation (By similarity). Required for ATG9 anterograde transport from the mitochondria to the PAS (By similarity).
Belongs to the GcvT family. CAF17 subfamily.
Belongs to the ETF alpha-subunit/FixB family.
Induced during biofilm formation and Up-regulated in response to treatment with MUC7 12-mer, a cationic antimicrobial peptide derived from the N-terminal region of human low-molecular-weight salivary mucin.
Belongs to the class IV-like SAM-binding methyltransferase superfamily.
Induced in biofilm, by caspofugin, as well as by 17-beta-estradiol and ethynyl estradiol. Expression is regulated by SSN6.
Probable transcription factor involved in response to cell wall damage.
Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.
Belongs to the PPP phosphatase family. PP-5 (PP-T) subfamily.
Belongs to the NADPH-dependent diflavin oxidoreductase NDOR1 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.
Belongs to the diphosphomevalonate decarboxylase family.
Diphosphomevalonate decarboxylase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (PubMed:12073030). MVD1 converts diphosphomevalonate into isopentenyl diphosphate (PubMed:12073030). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable).
Expression is high in media supplemented with glucose, moderate in acetate, galactose and low in maltose medium (PubMed:12073030). Expression is higher in the yeast phase than in the hyphal phase of growth as well as higher in the exponential than in the stationary phase (PubMed:12073030). Expression is affected by antifungals (PubMed:15917516). Expression is repressed during biofilm formation (PubMed:19527170, PubMed:22265407).
Component of the ER membrane protein complex (EMC).
Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins.
Belongs to the protein prenyltransferase subunit beta family.
Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX.
Component of the large ribosomal subunit (By similarity). Mature ribosomes consist of a small (40S) and a large (60S) subunit (By similarity). The 40S subunit contains about 32 different proteins and 1 molecule of RNA (18S) (By similarity). The 60S subunit contains 45 different proteins and 3 molecules of RNA (25S, 5.8S and 5S) (By similarity).
Belongs to the metallo-dependent hydrolases superfamily. NagA family.
Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit.
Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Belongs to the proteasome subunit S2 family.
Promotes the exchange of Ras-bound GDP by GTP. This protein positively controls the level of cellular cAMP at start, the stage at which the yeast cell division cycle is triggered.
Belongs to the DHHC palmitoyltransferase family. PFA5 subfamily.
Targets a different set of genes than S.cerevisiae ADR1.
Transcription factor involved in the regulation of hyphal growth.
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 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.
RNA-binding protein involved in the specific removal of group I introns in mitochondrial encoded transcripts. Maintains the stability of the small subunit mitochondrial 15S rRNA and thus the expression of the mitochondrial genome (By similarity).
Belongs to the helicase family. RecQ subfamily.
Belongs to the mitochondrion-specific ribosomal protein mL40 family.
Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
Belongs to the FPP/GGPP synthase family.
Belongs to the small GTPase superfamily. Rho family. CDC42 subfamily.
Involved in hyphal formation, virulence, morphogenesis.
Plays an important role in the cellular response to the nitrogen source. URE2 gene plays a major part in the repression of GLN1 and GDH2 genes by glutamine, and is required for the inactivation of glutamine synthetase. URE2 gene product may catalytically inactivate GLN3 in response to an increase in the intracellular concentration of glutamine (By similarity).
Hypha-specific G1 cyclin-related protein involved in regulation of morphogenesis and opaque cells filamentous growth, and required for both conventional and pheromone-stimulated biofilm formation. Required to maintain hyphal tip localization of actin and SPA2. Regulates the CDC28 kinase during hyphal growth. The CDC28-HGC1 complex phosphorylates and prevents RGA2 from localizing to hyphal tips, leading to localized CDC42 activation for hyphal extension. The CDC28-HGC1 complex also phosphorylates SEC2 and maintains CDC11 phosphorylation throughout hyphal growth. Moreover CDC28-HGC1 phosphorylation of EFG1 represses cell separation genes during hyphal growth. Also partially controls SEP7 phosphorylation status and subsequent septin ring dynamics. Required for virulence and especially mediates dynamic adhesion to endothelium of blood vessels during circulation.
Transcript is detected only in the apical cells of hyphae, suggesting that HGC1 is transcribed in the apical cell. Induced during hyphal formation and upon exposure to host serum. Expression is regulated by the cAMP/PKA pathway, EFG1, FLO8, SSN6, RAD52, TUP1, and UME6. Repressed by farnesol and linalool.
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 protein disulfide isomerase family.
Induced by HAP43 and up-regulated in absence of CYR1.
Probable mannosidase required for normal synthesis of the cell wall.
Belongs to the mitochondrion-specific ribosomal protein mL43 family.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. Also has an extraribosomal function, being essential for mitochondrial genome integrity. May interact with MHR1 to take part in the mtDNA repair mechanism.
Belongs to the proteasome subunit S14 family.
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Involved in nuclear export, actin cytoskeleton organization and vesicular transport.
Belongs to the metallo-beta-lactamase superfamily. RNA-metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations.
Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio.
Expression is positively regulated by the CAP1 transcription activator (PubMed:19395663). Expression is also regulated by the MRR1 transcription factor (PubMed:28953977). Expression is inhibited by tetrandrine (TET), a compound known to act in a synergistic manner with fluconazole (PubMed:19420894, PubMed:23527892). Expression is increased in clinical azole-resistant isolates (PubMed:23769565, PubMed:24962255).
Increases the susceptibility to mycophenolic acid, fuconazole, ketoconazole and itraconazole (PubMed:11065353). Reduces the efflux of spermidine as well as of histatin 5, a salivary human antimicrobial peptide that is toxic to the opportunistic yeast C.albicans (PubMed:23380720). Leads also to reduced biofilm formation (PubMed:23380720).
Major facilitator superfamily transporter that mediates resistance to structurally and functionally unrelated compounds including cycloheximide but also azoles such as fuconazole, ketoconazole and itraconazole (PubMed:11065353, PubMed:11181345). Mediates also efflux of histatin 5, a salivary human antimicrobial peptide, and is responsible for reduction of its toxicity in C.albicans (PubMed:23380720, PubMed:28953977).
Transcription factor necessary to sustain growth on non-fermentative carbon sources such as sodium acetate, acetic acid, or ethanol. Plays a role in hyphal formation.
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.
Belongs to the universal ribosomal protein uL30 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 (By similarity).
Cleaves the gamma-glutamyl peptide bond of glutathione and glutathione conjugates.
Expression is negatively regulated by NRG1, and by the contact with host oral epithelial cells. Up-regulated during the yeast-to-hypha transition through the function of YAK1. Also regulated by SWI4, SWI6, and WOR1, a transcriptional regulator of white-opaque switching.
Leads to increased resistance to UV-killing, derepression of various stress-related genes, hyperfilamentous growth, and overexpression of hypha-specific genes.
Transcriptional repressor which regulates DNA damage responses, morphogenesis, and virulence. Involved in the regulation of filamentous growth through its repression of hyphal-specific genes such as HWP1, ALS3, HYR1, ECE1, and CEK1.
Belongs to the bacterial ribosomal protein bL34 family.
Cells are resistant to rapamycin and display reduced TOR signaling.
Protease activity is induced in response to various mitochondrial stress.
Protease that is part of the quality control system in the inner membrane of mitochondria (By similarity). Cleaves and thereby promotes the turnover of mistranslated or misfolded membrane protein (By similarity). Required for TOR signaling (PubMed:27325672).
Belongs to the actin-binding proteins ADF family. Twinfilin subfamily.
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).
Activated through phosphorylation of Thr-211 and Tyr-213 from the TXY motif (By similarity). Phosphorylated in a PKC1-dependent manner in response to cell wall perturbations, oxidative stress, osmotic stress, and low temperatures. Also activated in response to physical contact leading to contact-dependent cellular behaviors such as invasive hyphal growth and biofilm development. Phosphorylation is also PBS2- and HOG1-dependent.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.
Expression is up-regulated by caspofungin.
Leads to thermosensitive growth, enhanced caffeine and caspofungin sensitivity, and alterations of cell surfaces. Leads also to a decreased pathogenicity in mice through displaying a greater susceptibility to nitric oxide (NO), a reduced inhibitory effect on macrophage NO production, and an increased capacity of macrophage stimulation by cell wall extracts.
Serine/threonine protein kinase component of the cell integrity pathway, a signal transduction pathway that plays a role in yeast cell morphogenesis and cell growth. Participates in cell wall construction, azole resistance, and host interaction. Required for the signaling for invasive filamentous growth and biofilm formation, and plays a crucial role in virulence.
The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Belongs to the ketol-acid reductoisomerase family.
Beta-mannosyltransferase involved in cell wall biosynthesis. Required for addition of the second beta-mannose residue to acid-stable fraction of cell wall phosphopeptidomannan, and in elongation of beta-mannose chains on the phosphopeptidomannan acid-labile fraction.
Expression is induced in biofilm and by HAP43.
Belongs to the eukaryotic ribosomal protein eS12 family.
C-24(28) sterol reductase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (By similarity). Catalyzes the last step of ergosterol biosynthesis by converting ergosta-5,7,22,24(28)-tetraen-3beta-ol into ergosterol (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable).
Expression is induced by fluconazole and repressed by caspofungin (PubMed:15917516). Expression is also repressed during biofilm formation (PubMed:19527170).
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Belongs to the acetyltransferase family. NAA40 subfamily.
In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.
In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.
Belongs to the Mediator complex subunit 12 family.
The active site is a redox-active disulfide bond.
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).
In contrast to the other glycerophosphodiester transporters, expression is largely unresponsive to phosphate levels (PubMed:24114876).
Probable glycerophosphodiester transporter (PubMed:24114876). Does not possess detectable glycerophosphoinositol (GroPIns) transport activity (PubMed:24114876). Might be involved in the uptake of glycerophosphocholine (GroPCho) (PubMed:24114876). The expanded ability to utilize GroPIns and GroPCho results from the organism's pathogenic nature and its need to occupy a variety of environments within its host organism (PubMed:24114876). This possibility is buttressed by the fact that GroPIns and GroPCho are present and abundant in human fluids (PubMed:24114876).
Triple deletion of GIT2, GIT3 and GIT4 impairs the uptake of glycerophosphocholine (GroPCho) and reduces virulence in a mouse model of blood stream infection (PubMed:24114876).
Belongs to the NADPH--cytochrome P450 reductase family.
This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis.
Belongs to the actin family. ARP6 subfamily.
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.
F-box protein probably involved in ubiquitin conjugation pathway.
Hydrophilin which is essential to overcome the simple stress of the desiccation-rehydration process.
Induced during cell wall regeneration and upon milbemycins A3 oxim derivative (A3Ox) treatment. Expression is also regulated by SSN6.
Belongs to the PNP/MTAP phosphorylase family.
The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
Probable GPI-anchored cell wall protein that may be involved in cell wall organization, hyphal growth, as well as in virulence.
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-7; H2AS128ph = phosphorylated Ser-128.
Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage.
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 eukaryotic RPB7/RPC8 RNA polymerase subunit family.
DNA-dependent RNA polymerase which catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Required for multiple vacuole delivery pathways including the cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and endocytosis.
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.
Affects filamentous growths and leads to hypersensitivity to caspofungin.
Probable transcription factor involved in the regulation of filamentous growth.
Belongs to the mitochondrion-specific ribosomal protein mL46 family.
Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Component of a cytoskeletal structure that is required for the formation of endocytic vesicles at the plasma membrane level. Plays an important role in virulence.
Leads to defects in actin polarization, endocytosis, bud morphogenesis, as well as altered abundance and distribution of the cortical actin patches and increased sensitivity to calcofluor white and Congo red. Shows also attenuated virulence.
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. Required for the formation of the monounsaturated sphingoid base (E)-sphing-4-enine during glucosylceramide (GluCer) biosynthesis.
Belongs to the eukaryotic ribosomal protein eL20 family.
Endoplasmic reticulum-Golgi intermediate compartment membrane
Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Although the beta-barrel of Cu/Zn SODs is largely preserved, SOD5 is a monomeric copper protein that lacks a zinc-binding site and is missing the electrostatic loop element proposed to promote catalysis through superoxide guidance. Without an electrostatic loop, the copper site of SOD5 is not recessed and is readily accessible to bulk solvent (PubMed:24711423).
Induced during yeast-to-hyphal transition and by osmotic and oxidative stresses. Expression is also increased when cells were grown on nonfermentable substrates as the only carbon source, in serum, and in the presence of neutrophils. Down-regulated by shikonin. Expression is controlled by EFG1, NRG1 and RIM101.
Leads to sensitivity to hydrogen peroxide when cells were grown in nutrient-limited conditions.
Secreted in a disulfide-oxidized form and apo-pools of secreted SOD5 can readily capture extracellular copper for rapid induction of enzyme activity.
Superoxide dismutases serve to convert damaging superoxide radicals, a key form of ROS, to less damaging hydrogen peroxide that can be converted into water by catalase action. Degrades host-derived reactive oxygen species to escape innate immune surveillance. Involved in the occurrence of miconazole-tolerant persisters in biofilms. Persisters are cells that survive high doses of an antimicrobial agent. The unusual attributes of SOD5-like fungal proteins, including the absence of zinc and an open active site that readily captures extracellular copper, make these SODs well suited to meet challenges in zinc and copper availability at the host-pathogen interface.
Belongs to the TFIIF beta subunit family.
Belongs to the ATG13 family. Fungi subfamily.
Expression is induced during biofilm formation.
Interacts with ATG1 to form the ATG1-ATG13 kinase complex.
Plays a key role in autophagy (PubMed:36476055). Activates the atg1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy (By similarity). Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation (By similarity). Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy (By similarity). Finally, plays an important role in biofilm formation and resistance to antifungal compounds such as fluconazole, itraconazole, terbinafine and caspofungin (PubMed:36476055).
Reduces the formation of biofilms (PubMed:36476055). Significantly decreases the resistance of biofilms to fluconazole, itraconazole, terbinafine and caspofungin (PubMed:36476055). Leads to autophagosomes with shrunken membranes with undefined edges (PubMed:36476055). Results also in partially dissolved contents of autophagosomes (PubMed:36476055).
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).
Amino-acid permease with broad substrate specificity (PubMed:21764911, PubMed:28028545). GAP2 is the only amino-acid permease with very broad substrate specificity, none of the other GAP permeases is able to transport such a variety of amino acids (PubMed:21764911, PubMed:28028545). GAP2 is also able to transport thialysine, and thus probably also lysine (PubMed:21764911). Functions as a sensor via detection of some amino acids including methionine, leading to a rapid activation of trehalase, a downstream target of PKA (PubMed:21764911).
Expression is under control of the CSY1 amino-acid sensor (PubMed:14871944, PubMed:28028545). Induced during biofilm development (PubMed:22265407). Expression is repressed by nitrogen sources (PubMed:28028545). Expression is repressed by the antifungal agents ketoconazole and flucytosine (PubMed:15917516). Expression is also regulated by NRG1 and TUP1 (PubMed:15814841).
Leads to a growth defect on medium containing phenylalanine, valine, leucine, or methionine as sole nitrogen source (PubMed:28028545).
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 (By similarity).
Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome.
Belongs to the chloride channel (TC 2.A.49) family.
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 nucleoporin NSP1/NUP62 family.
May form heterododecamers with RVB2. Component of the SWR1 chromatin remodeling complex, the INO80 chromatin remodeling complex, and of the R2TP complex (By similarity).
Belongs to the glycosyltransferase 22 family.
In complex with IFH1, acts as a transcriptional regulator of rRNA and ribosomal protein genes. The FHL1-IFH1 complex is targeted to the ribosomal protein genes by the DNA-binding factor TBF1.
Nucleoside permease that transports adenosine and guanosine.
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 plasma membrane SPS (SSY1-PTR3-SSY5) amino acid sensor complex.
Protease component of the SPS-sensor system, which regulates the expression of several amino acid-metabolizing enzymes and amino acid- and peptide-permeases in response to extracellular amino acid levels by controlling the activity of two transcription factors, STP1 and STP2. Catalyzes the activation of these transcription factors, which are synthesized as latent cytoplasmic precursors, by proteolytic removal of an N-terminal inhibitory domain containing cytoplasmic retention motifs. SSY5 binds as an inactive protease complex to STP1. In response to extracellular amino acids and dependent on the other SPS-sensor components, the inhibitory propeptide is induced to dissociate, and thereby enables the catalytic domain to process STP1.
Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Required for hyphal growth.
Unknown. The enzyme has no activity toward sorbose.
Belongs to the proteasome subunit p55 family.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
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).
Consists of two distinct domains; a N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.
Expression is under the control of the CDA4 transcription factor. Induced by nitric oxide, high-iron conditions, during transition to filamentous growth, by contact with host macrophages, and during oral infection. Expression is repressed by HAP43 and CWT1.
Leads to increased susceptibility to neutrophils.
Nitric oxide dioxygenase involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the fungus from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. Plays a role in virulence since nitric oxide is generated by macrophages of the host immune system.
Required for the maintenance of the structure of the mitochondrial inner membrane. Involved in mitochondrial morphology. Causes growth arrest when highly overexpressed (By similarity).
Heterodimer with ALG13 to form a functional enzyme.
Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity).
Belongs to the mitochondrion-specific ribosomal protein mS23 family.
Down-regulated during filament induction and in response to serum at 37 degrees Celsius. Expression of NRG1 is also repressed by RIM101 and under conditions that repress CDC28 expression. The bacterial signaling molecules indole and its derivate indole-3-acetonitrile (IAN) increase NRG1 expression.
Exhibits a high degree of filamentous growth and leads to avirulence in a mouse model.
Transcriptional repressor that binds NRG1 response elements (NRE) of target promoters. Involved in regulation of chlamydospore formation, hyphal growth, virulence, and stress response. Plays a key role in regulating true hyphal growth, but does not regulate pseudohyphal growth in the same fashion. Directs transcriptional repression of a subset of filament-specific genes such as HWP1, HYR1, ALS8, HWP1, or ECE1; via the TUP1 pathway. Functions with UME6 in a negative feedback loop to control the level and duration of filament-specific gene expression in response to inducing conditions. Plays a key role in biofilm formation and dispersion. Also plays the role of a negative regulator of virulence in mice models. Required for the expression of the cell wall genes RBR1.
Belongs to the glycosyl hydrolase 65 family.
Cell wall acid trehalase that catalyzes hydrolysis of the disaccharide trehalose and required for growth on trehalose as carbon source. Plays a role in dimorphic conversion and virulence.
Expression is repressed by glucose and by HAP43.
Lacks acid trehalase activity and decreases hypha formation and infectivity.
Belongs to the peroxisomal targeting signal receptor family.
Interacts (via WxxxF/Y and LVxEF motifs) with PEX14; promoting translocation through the PEX13-PEX14 docking complex.
Monoubiquitinated at Cys-10 by PEX2 during PEX5 passage through the retrotranslocation channel: monoubiquitination acts as a signal for PEX5 extraction and is required for proper export from peroxisomes and recycling. When PEX5 recycling is compromised, polyubiquitinated at Lys-22 by PEX10 during its passage through the retrotranslocation channel, leading to its degradation.
Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX14 docking complex along with cargo proteins. PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle.
The TPR repeats mediate interaction with proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type).
The WxxxF/Y motifs mediate interaction with PEX14, promoting association with the PEX13-PEX14 docking complex.
The amphipathic helix 1 and 2 (AH1 and AH2, respectively) are required for PEX5 retrotranslocation and recycling. AH2 mediates interaction with lumenal side of the PEX2-PEX10-PEX12 ligase complex, while AH1 is required for extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex.
Belongs to the mitochondrion-specific ribosomal protein mL41 family.
Belongs to the terpene cyclase/mutase family.
Expression is induced in the presence of fluconazole (PubMed:15820985). Expression is up-regulated when ERG6, CYP51/ERG11 or ERG24 are deleted (PubMed:15473366).
Lanosterol synthase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:8486282, PubMed:2185141). ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core (PubMed:2185141). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable).
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.
Inclusion body (IB) resident protein that interacts strongly with lipid droplet (LD) proteins. Involved in LD-mediated IB clearing after protein folding stress, probably by enabling access to the IBs of an LD-stored soluble sterol derivative that acts as chaperone in inclusion clearing.
Belongs to the actin-binding proteins ADF family.
Involved in pre-mRNA splicing. Binds and is required for the stability of snRNA U1, U2, U4 and U5 which contain a highly conserved structural motif called the Sm binding site. Involved in cap modification.
Belongs to the replication factor A protein 3 family.
Belongs to the acetolactate synthase small subunit family.
Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Belongs to the small GTPase superfamily. Rab family.
Involved in exocytosis. Maybe by regulating the binding and fusion of secretory vesicles with the cell surface. The GTP-bound form of SEC4 may interact with an effector, thereby stimulating its activity and leading to exocytotic fusion. SEC4 may be an upstream activator of the 19.5S SEC8/SEC15 particle. SEC4 probably interacts directly with SEC8; it could serve as the attachment site for the SEC8/SEC15 particle (By similarity).
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.
Common component of the spliceosome and rRNA processing machinery.
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.
Phosphorelay intermediate protein that is part of the bifurcated SLN1-YPD1-SKN7/SSK1 two-component regulatory system, which controls activity of the HOG1 pathway and gene expression in response to oxidative stress and probably to changes in the osmolarity of the extracellular environment. Catalyzes the phosphoryl group transfer from the membrane-bound histidine kinase SLN1 to two distinct response regulators SSK1 and SKN7.
Expression is increased in during infection. Expression is also regulated by CDC28, SKO1, and SSK1.
Induces filamentous growth and leads to decreased HWP1 expression.
Transcriptional activator that binds to the RPG box and to telomeres. Involved in the regulation of the transition between yeast and filamentous forms and plays a role in virulence. Induces expression of HWP1, a major hyphal cell protein and virulence factor.
May participate in the translocation of oligosaccharide from the cytoplasmic side to the lumenal side of the endoplasmic reticulum membrane.
Cell wall protein which plays an anti-adhesive role and promotes dispersal of yeast forms, which allows the organism to seek new sites for colonization.
Cleaved by SAP9 and SAP10, which leads to its release from the cell wall.
Expression is greatest during yeast exponential-phase growth, but down-regulated in stationary phase and upon filamentation. Expression is also increased during growth in hypoxic conditions. Expression decreases in biofilm cultures and becomes undetectable through late stage biofilm formation. Up-regulated when the extracellular phosphate concentration is low or in presence of Cis-2-dodecenoic acid (BDSF). Repressed during cell wall regeneration. Expression is positively regulated by EFG1 and EFH1, and negatively regulated by SSN6 and SSK1.
Leads to increased adhesion and biofilm formation.
Belongs to the PPP phosphatase family. PP-2B subfamily.
Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity.
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 AB hydrolase superfamily. AB hydrolase 4 family.
Activated by tyrosine and threonine phosphorylation.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily.
Dually phosphorylated on Thr-174 and Tyr-176, which activates the enzyme (By similarity). Phosphorylated in response to oxidative and salt stress.
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. Regulates stress-induced production and accumulation of glycerol and D-arabitol. HOG1 is also involved in virulence, morphogenesis and oxidative stress response especially through its role in chlamydospore formation, an oxygen-dependent morphogenetic program.
Beta-mannosyltransferase involved in cell wall biosynthesis. Required for addition of the first beta-mannose residue to acid-stable fraction of cell wall phosphopeptidomannan. Plays a key role in reducing host inflammatory response.
Impairs the mannosylation of beta-mannose chains on the acid-stable fraction of cell wall phosphopeptidomannan.
Required for synthesis of 60S ribosomal subunits and the transport of pre-ribosomes from the nucleoplasm to the cytoplasm.
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 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).
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.
Belongs to the proteasome subunit S5A family.
Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily.
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 eukaryotic ribosomal protein eL6 family.
Belongs to the bacterial ribosomal protein bL35 family.
Belongs to the glycosyltransferase 48 family.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Belongs to the membrane magnesium transporter (TC 1.A.67) family.
Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.
The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. COT1 subfamily.
Serine/threonine-protein kinase required for wild-type hyphal growth and transcriptional regulation of cell-wall-associated genes. Involved in the biofilm formation through phosphorylation of the master regulator of biofilm formation BCR1.
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 Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family.
Belongs to the iron/ascorbate-dependent oxidoreductase 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.
Belongs to the glycosyl hydrolase 63 family.
Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor.
Expression is induced by HAP43, by osmotic stress, by oxidative stress, by heavy metal stress, and during biofilm formation.
Transcriptional activator of a number of genes encoding proteasomal subunits. Binds to the DNA sequence 5'-GAAGGCAAAA-3', enriched in regions upstream of proteasome genes.
Belongs to the casein kinase 2 subunit beta family.
Regulatory subunit of casein kinase II/CK2 (By similarity). As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine.
Regulatory subunit of casein kinase II/CK2. As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine.
Negative regulator of the mitotic exit network (MEN), required for multiple cell cycle checkpoints. Required for daughter cell separation and chromosome stability. Involved in copper sensitivity.
Nuclear serine protease which mediates apoptosis.
Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage.
Belongs to the tRNA(His) guanylyltransferase family.
Belongs to the DASH complex SPC19 family.
Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are bound between subunits.
Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Belongs to the proteasome subunit S3 family.
Belongs to the precorrin methyltransferase family.
Belongs to the universal ribosomal protein uS11 family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (Probable). RPS14B is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (By similarity).
Belongs to the prephenate/arogenate dehydrogenase family.
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).
Alpha-1,2-mannosyltransferase required for cell wall integrity. Responsible for addition of the first alpha-1,2-linked mannose to form the branches on the mannan backbone of oligosaccharides. Addition of alpha-1,2-mannose is required for stabilization of the alpha-1,6-mannose backbone and hence regulates mannan fibril length; and is important for both immune recognition and virulence.
Belongs to the DHHC palmitoyltransferase family. AKR/ZDHHC17 subfamily.
Palmitoyltransferase specific for casein kinase 1.
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 (Probable). RPL3 plays a role in coordinating processes of accommodating the aminoacyl-tRNA in the PTC (By similarity).
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.
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 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.
General activator of RNA polymerase III transcription. Interacts with TBP. Binds to Pol III subunit C34 and to the TAU135 component of TFIIIC.
TFIIIB comprises the TATA-binding protein (TBP), the B-related factor (BRF) and a 70 kDa polypeptide.
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.
Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription (By similarity).
The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors.
Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm. Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix.
Belongs to the enhancer of polycomb family.
Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Involved in gene silencing by neighboring heterochromatin, blockage of the silencing spreading along the chromosome, and required for cell cycle progression through G2/M (By similarity).
Belongs to the complex I NDUFB3 subunit family.
Beta-mannosyltransferase involved in cell wall biosynthesis. Required for the addition of beta-mannose to the acid-labile fraction of cell wall phosphopeptidomannan.
Regulated on yeast-hypha and white-opaque switches, and repressed in biofilm.
Belongs to the Mediator complex subunit 5 family.
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
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).
Central component of the spindle assembly checkpoint which is a feedback control that prevents cells with incompletely assembled spindles from leaving mitosis.
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.
Belongs to the universal ribosomal protein uL1 family.
Component of the large ribosomal subunit (LSU) (By similarity). Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 32 different proteins and 1 molecule of RNA (18S). The 60S subunit contains 45 different proteins and 3 molecules of RNA (25S, 5.8S and 5S) (Probable). uL1 forms part of the L1 stalk (By similarity).
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. uL1 forms part of the L1 stalk, a mobile element that plays a role in evacuating the exit-site tRNA.
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 D-isomer specific 2-hydroxyacid dehydrogenase family.
Belongs to the anthranilate synthase component I family.
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.
Expression is decreased at the stationary phase (PubMed:17588813). Expression in suppressed in the presence of Pseudomonas aeruginosa lipopolysaccharide (LPS) (PubMed:23194472).
Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2.
Belongs to the fungal fatty acid synthetase subunit beta family.
Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.
[Alpha(6)beta(6)] hexamers of two multifunctional subunits (alpha and beta).
Belongs to the actin-binding proteins ADF family. GMF subfamily.
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'.
Belongs to the CND3 (condensin subunit 3) family.
Belongs to the universal ribosomal protein uL6 family.
Induced during the switch from the yeast form to filamentous growth and by fluconazole. Expression is negatively regulated by CPH2, EFG1, RFG1, and TUP1.
Secreted protein that acts as a virulence factor during infections such as in posttraumatic corneal infections. Acts as an important antigen in patients with systemic candidiasis and plays a role in the protection against phagocyte attack.
Belongs to the eukaryotic ribosomal protein eL14 family.
Belongs to the complex I LYR family. SDHAF1 subfamily.
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.
Repressed by HAP43. Down-regulated during oral epithelial infection. Up-regulated in response to galactose.
Belongs to the FKBP-type PPIase family. FKBP2 subfamily.
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 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.
Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has also a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides.
Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
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.
Expressed in presence of 2 percent glucose (PubMed:12187386). Expression is induced by progesterone and drugs such as cycloheximide, benomyl and chloramphenicol (PubMed:10612724).
High-affinity glucose transporter (PubMed:10612724, PubMed:12187386). Acts as a multifunctional complement-evasion molecule that causes down-regulation of complement activation by acquisition of human complement factors FH and C4BP (PubMed:21844307). Functions also as a human immunodeficiency virus (HIV) receptor via binding the viral gp160 protein (PubMed:21844307). Modulates hyphae formation (PubMed:21844307).
Interacts with the human complement factors FH and C4BP (PubMed:21844307). Binds also human immunodeficiency virus (HIV) protein gp160 (PubMed:21844307).
Reduces the binding of human FH and C4Bp as well as of human immunodeficiency virus (HIV) gp160 protein onto C.albicans cell surface (PubMed:21844307). Reduces ability to form hyphae (PubMed:21844307).
Belongs to the eukaryotic release factor 1 family. Pelota subfamily.
Component of the Dom34-Hbs1 complex, a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway (PubMed:20890290). In the Dom34-Hbs1 complex, dom34 recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel. Following ribosome-binding, the Dom34-Hbs1 complex promotes the disassembly of stalled ribosomes, followed by degradation of damaged mRNAs as part of the NGD pathway.
Up-regulated during cell wall regeneration and down-regulated in kidney lesions. Expression is also regulated by HAP43 and SSN6.
Belongs to the archaeal Rpo12/eukaryotic RPC10 RNA polymerase subunit family.
Belongs to the tRNA pseudouridine synthase TruA family.
Formation of pseudouridine at positions 27 and 28 in the anticodon stem and loop of transfer RNAs; at positions 34 and 36 of intron-containing precursor tRNA(Ile) and at position 35 in the intron-containing tRNA(Tyr). Catalyzes pseudouridylation at position 44 in U2 snRNA. Also catalyzes pseudouridylation of mRNAs.
Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP2/CFD1 subfamily.
Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NBP35 and two labile, bridging clusters between subunits of the NBP35-CFD1 heterotetramer.
Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Required for biogenesis and export of both ribosomal subunits, which may reflect a role in assembly of the Fe/S clusters in RLI1, a protein which performs rRNA processing and ribosome export.
Heterotetramer of 2 NBP35 and 2 CFD1 chains.
Belongs to the mitochondrion-specific ribosomal protein mS41 family.
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. mS41 is involved in telomere length regulation.
Belongs to the eukaryotic ribosomal protein eL42 family.
Candida albicans is resistant to cycloheximide (CHX), which binds to the ribosomal E-tRNA binding site (E-site). This resistance is caused by a natural substitution P56Q in ribosomal protein RPL42, which decreases the volume of the binding pocket and prevents the binding of inhibitors such as CHX.
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 glycosyl hydrolase 37 family.
Expression is regulated by FKH2 and repressed upon adherence to polystyrene and interaction with macrophages.
Transcription factor involved in the expression of a broad class of genes including snRNAs. Required for sporulation and DNA-damage repair. Prevents the spreading of SIR silencing at telomeres and protects histone H4, but not H3, from deacetylation (By similarity).
Belongs to the peptidase S8 family. Furin subfamily.
Transcription factor which mediates CO(2) sensing. Required for CO(2)-induced white-to-opaque switching, as well as for filamentous growth and virulence. Required for both normoxic and hypoxic biofilm formation. Hypoxic biofilm formation is a major cause of perseverance and antifungal resistance during infections.
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).
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 (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 by IPL1 to form H3S10ph. H3S10ph promotes subsequent H3K14ac formation and is required for transcriptional activation through TBP recruitment to the promoters (By similarity).
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 (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.
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.
Can cleave 4-methylcatechol at lower rates than catechol, but has no activity with 3-methylcatechol, 4-chlorocatechol, 4-carboxycatechol or hydroxyquinol.
Inhibited by Ag(+), Cu(+), Hg(2+) and Pb(2+).
Catalyzes the addition of a phosphorylinositol group onto ceramide to form inositol phosphorylceramide, an essential step in sphingolipid biosynthesis.
Inhibited by aureobasidin A (AbA), khafrefungin and rustmicin.
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.
Component of the RPD3C(L) histone deacetylase complex (HDAC) 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 (By similarity). UME6 controls the level and duration of gene expression in the filamentous growth program such as HGC1; and is specifically important for hyphal elongation and germ tube formation. Promotes filamentous biofilms and is required for adherence to surfaces such as plastic. Plays an important role in virulence.
Leads to attenuated virulence and defective hyphal extension in a mouse model of systemic candidiasis.
Up-regulated during growth in alkaline conditions, in response to various filament-inducing conditions, and during oropharyngeal candidiasis. Induced in both white and opaque cells. Induced by SFL2 and repressed by RFG1, SFL1, and by NRG1 under non-filament-inducing conditions. Also repressed by linalool. Expression is also regulated by BRG1 and EFG1.
Belongs to the SMC family. SMC1 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 (PubMed:17185534). 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 (By similarity).
Phosphorylated by ATG1. ATG1 phosphorylation is required for preautophagosome elongation.
Belongs to the V-ATPase D 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 (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity).
Intracellular phospholipase B that catalyzes the double deacylation of phosphatidylcholine (PC) to glycerophosphocholine (GroPCho). Plays an important role in membrane lipid homeostasis. Responsible for the rapid PC turnover in response to inositol, elevated temperatures, or when choline is present in the growth medium (By similarity).
Plays a role in vesicular protein sorting.
Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET5 subfamily.
Putative protein lysine methyltransferase.
ATP-dependent DNA helicase important for chromosome transmission and normal cell cycle progression in G(2)/M (By similarity). May have a role in changing DNA topology to allow the loading of proteins involved in maintaining sister chromatid cohesion in the vicinity of the centromeres (By similarity). Has a specific role in chromosome segregation during meiosis II.
Belongs to the helicase family. RAD3/XPD subfamily.
Belongs to the 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.
Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites.
GPI-anchored protein involved in proper cell wall integrity. Does not seem to be directly involved in the synthesis of the cell wall. Required for normal virulence in a mouse model of disseminated candidiasis.
Induced during cell wall regeneration. Expression is also increased under high-iron conditions. Repressed by the HAP43 transcription factor.
Leads to hyperfilamentation, increased biofilm formation and reduced virulence in a mouse model of disseminated candidiasis. Leads also to increased susceptibility to antifungals (fluconazol, posaconazol or amphotericin B) that target the plasma membrane and to altered sensitivities to environmental (heat, osmotic and oxidative) stresses.
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.
Involved in cell wall metabolism and required for the separation of the mother and daughter cells.
Belongs to the Mrp/NBP35 ATP-binding proteins family.
Expressed at higher levels in cells growing as hyphae than in those growing as budding yeasts.
Plays a role in the cell cycle. Involved in the formation of the ring of filaments in the neck region at the mother-bud junction during mitosis.
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.
Component of the telomerase complex involved in telomere replication. Stimulates RNA/DNA heteroduplex unwinding which favors the telomere replication by the telomerase (By similarity).
Involved in cell wall beta(1->6) glucan synthesis.
Causes defects in hyphal development, reduced resistance to osmotic and oxidative stress, and severe virulence attenuation in the mouse model of disseminated candidiasis.
Required for stress adaptation, morphogenesis and virulence.
Induced by fluconazole and down-regulated in absence of GOA1.
Involved in cell wall, plasma membrane, and cytoskeletal organization. Plays a role in endocytosis and hyphal morphogenesis. Required to restrict septin proteins to the bud neck and prevents intracellular growth of cell wall. Contributes to secretion, biofilm formation, and macrophage killing. Essential for resistance to stressful conditions and for invasive growth and virulence.
Leads to defective tolerance to cell wall stress and antifungal agents targeting cell wall components, defective plasma membrane structure, defective endocytosis, impaired lipase secretion, SAP2 over-production, increased adherence, aberrant biofilm formation, defective macrophage killing, and decreased virulence in a mouse infection model.
Belongs to the glycosyltransferase 28 family.
Sterol glycosyltransferase responsible for the glycosylation of ergosterol to form ergosterol-glucoside.
Belongs to the cyclophilin-type PPIase family. PPIase D subfamily.
Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.
Belongs to the mitochondrion-specific ribosomal protein mS35 family.
Involved in cell wall 1,6-beta-glucan assembly possibly by the addition of linear side chains of 1,6-linked Glc units to a highly branched 1,6- and 1,3-linked glucan backbone.
Extracellular glycosidase which plays an important role in fungal pathogenesis. Involved in cell wall assembly and regeneration, filamentation, and adherence to host cells. Plays a role of cell surface antigen in acute candidemia patients.
Leads to increased susceptibility to cell wall-perturbing agents, defect in filamentation, reduction in adherence to mammalian cells in an in vitro adhesion assay, and a prolongation of survival in an immunocompetent mouse model of disseminated candidiasis.
Up-regulated by heat stress, calcineurin, micafungin, and fluconazole. Protein abundance is increased at pH 4 compared to pH 7. Expression is also regulated by RCH1.
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. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates the YNG2 subunit of NuA4 histone acetyltransferase (HAT) module, leading to the reduction of YNG2 and NuA4 HAT at the promoters of hypha-specific genes. Plays a key role in the regulation of filamentous growth and virulence. Involved in the switch between two heritable states, the white and opaque states. These two cell types differ in many characteristics, including cell structure, mating competence, and virulence. Each state is heritable for many generations, and switching between states occurs stochastically at low frequency.
May function both as a monomer and a homodimer.
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.
Belongs to the protoporphyrinogen/coproporphyrinogen oxidase family. Protoporphyrinogen oxidase subfamily.
Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Substrate-binding subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA.
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.
Plays a role in transport between endoplasmic reticulum and Golgi.
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. NIM1 subfamily.
Phosphorylated throughout the cell cycle, except for the G1 phase.
Protein kinase involved in determination of morphology during the cell cycle of both yeast-form and hyphal cells via regulation of SWE1 and CDC28. Regulates pseudohypha formation, but is not required for septin ring organization or septum formation. Plays an essential role in virulence in a mouse model.
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.
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.
Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole. Vacuole inheritance has a role in the regulation of hyphal cell division.
Belongs to the Nudix hydrolase family. DCP2 subfamily.
Belongs to the SMC family. SMC3 subfamily.
In the central section; belongs to the inositol 1,4,5-trisphosphate 5-phosphatase family.
Belongs to the DHHC palmitoyltransferase family. PFA4 subfamily.
Mediates the reversible addition of palmitate to target proteins, thereby regulating their membrane association and biological function.
Belongs to the SAICAR synthetase family.
Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity.
Forms a complex with Hsp90. Interacts with a number of kinases such as crk1.
Single strand DNA specific 5' exonuclease involved in mitochondrial DNA replication and recombination. Releases dinucleotides as main products of catalysis. Has the capacity to slide across 5'double-stranded DNA or 5'RNA sequences and resumes cutting two nucleotides downstream of the double-stranded-to-single-stranded junction or RNA-to-DNA junction, respectively (By similarity).
Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
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).
Cell surface protein involved in the ability to sense and respond to changes in the host environment. Required for stress response and confers partial antifungal drug resistance. Contributes to the DNA damage response. Required for the flocculation response stimulated by 3-aminotriazole-induced amino acid starvation.
Expression is induced during filamentation, biofilm formation, after UV exposure, as well as by benomyl, caspofungin, and ketoconazole. Also enriched in azole-resistant strains and in stationary phase. Expression is repressed by SKO1, HOG1, RFX2, farnesol, and in alkaline conditions. Expression is also controlled by the filamentous growth regulators CPH1, CPH2, and EFG1.
leads to reduced flocculation stimulated by 3-aminotriazole-induced amino acid starvation.
Causes greater curvature of cells growing in a filamentous manner and morphological defects in suspensor cells and chlamydospores. Leads to reduced tissue penetration and non-invasive fungal masses in mice infected kidneys. Leads also to hypersusceptibility to caspofungin.
Component of the septin complex which consists of CDC3, CDC10, CDC11, CDC12 and probably SEP7. The purified septin complex appeared to have a stoichiometry of 2 CDC3, 1 to 2 CDC10, 1 CDC11, 2 CDC12, and 1 or none SEP7 subunit. Interacts with HSL1.
Hyphal induction causes immediate phosphorylation at Ser-395 by GIN4 and at Ser-394 by CDC28-CCN1. GIN4 phosphorylation at Ser-395 primes CDC11 for further phosphorylation by CDC28-CCN1. CDC28-HGC1 then maintains CDC11 phosphorylation throughout hyphal growth. Ser-4 is also phosphorylated in yeast cells but not hyphal cells.
Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinase GIN4. Septins are also involved in cell morphogenesis, chlamydospores morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization, and spore wall formation. CDC11 is required for the correct localization of SEC3 at bud tips and bud necks. Plays a key role in invasive growth and virulence.
Disruption of both alleles leads to letality. Disruption of only one allele impairs filamentation and leads to an altered cell wall composition with reduced amounts of beta-1,6-glucan and shows reduced virulence in a mouse model of hematogenously disseminated candidiasis (HDC) and using reconstituted human epithelium (RHE).
PMT1 and PMT2 form a functional heterodimer.
Protein mannosyltransferase (PMT) involved in hyphal growth and drug sensitivity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1, PMT2 and PMT4 account for most of the protein-O-glycosylation activity, while PMT5 and PMT6 may specifically modulate a much narrower spectrum of target proteins. Essential protein that plays an important role in virulence.
Transcribed in the yeast form, but expression is increased two to threefold during hyphal induction. Also induced during cell wall regeneration. Up-regulated more than twofold when PMT1 expression is impaired. MSB2 functions not only to secure basal levels of the PMT2 transcripts but is needed also for up-regulation of both transcripts upon PMT1 inhibition.
Belongs to the PI3/PI4-kinase family. ATM subfamily.
Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Recruited to DNA lesions in order to initiate the DNA repair by homologous recombination. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of DNA damage, also involved in the regulation of DNA damage response mechanism. Required for cell growth and meiotic recombination (By similarity).
Late secretory t-SNARE protein required for secretion and proper cytokinesis. Plays an important role in the secretion of virulence-associated extracellular enzymes and vesicle-mediated polarized hyphal growth.
Leads to defects in secretion of degradative enzymes and defects in hyphal extension. Leads also to the Spitzenkoerper dissipation and accumulation of secretory vesicles.
Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)) (By similarity).
The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
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.
Part of the multisubunit TRAPP (transport protein particle) complex.
Plays a key role in the late stages of endoplasmic reticulum to Golgi traffic.
Belongs to the multicopper oxidase family.
Involved in nucleolar integrity and required for processing of the pre-rRNA for the 60S ribosome subunit.
Probable mitochondrial mRNA stabilization factor.
Belongs to the Rieske iron-sulfur protein family.
The Rieske protein is a high potential 2Fe-2S protein.
Expression is positively regulated by the transcription factor PHO4 (PubMed:24114876).
Glycerophosphodiester transporter that mediates uptake of glycerophosphocholine (GroPCho) with GIT3 (PubMed:24114876). Does not possess detectable glycerophosphoinositol (GroPIns) transport activity (PubMed:24114876). The expanded ability to utilize GroPIns and GroPCho results from the organism's pathogenic nature and its need to occupy a variety of environments within its host organism (PubMed:24114876). This possibility is buttressed by the fact that GroPIns and GroPCho are present and abundant in human fluids (PubMed:24114876).
This promotes the activity of RNA polymerase II.
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.
GPI-linked hyphal surface heme-binding protein involved in heme-iron utilization (PubMed:15306022, PubMed:17042757, PubMed:18466294, PubMed:21205162, PubMed:25275454, PubMed:27617569). Heme transfer occurs between PGA7, RBT5 and CSA2 supporting a model in which the 3 CFEM proteins cooperate in a heme-acquisition system and form a cross-cell wall heme-transfer cascade (PubMed:15306022, PubMed:17042757, PubMed:18466294, PubMed:21205162, PubMed:25275454, PubMed:27617569). The ability to acquire iron from host tissues is a major virulence factor of pathogenic microorganisms. Required for biofilm formation (PubMed:15306022, PubMed:17042757, PubMed:18466294, PubMed:21205162, PubMed:25275454).
Induced by iron starvation, hypoxia, amphotericin B, and during hyphal growth. Repressed by ketoconazole and caspofungin. Regulated by BCR1, HOG1, SFU1, TUP1, and UPC2.
Leads to defects in hemin and hemoglobin utilization as sole source of iron.
Component of the autophagy-specific VPS34 PI3-kinase complex I composed of at least VPS15, VPS30, VPS34, and of the VPS34 PI3-kinase complex II composed of VPS15, VPS30, VPS34 and VPS38 (By similarity). Interacts with VMNA7 (PubMed:15861817).
Expression is increased up to 12-fold during exponential growth, followed by a decline upon entry into stationary phase.
Leads to defective acidification of the vacuoles and a lack of growth at pH 8.0 (PubMed:15861817). Vacuoles are considerably enlarged and electron-transparent (PubMed:11223944). Shows aberrant patch-like accumulation of vesicles, which are localized in the periplasm close to the plasma membrane (PubMed:11223944). Shows a staining of punctuate structures, possibly multivesicular bodies (MVB), that are scattered all over the cell, the result of a late block in endocytic vesicle transport (PubMed:11223944). Results in significantly lower carboxypeptidase Y activity (PubMed:11223944). Causes disturbance of normal nuclear migration (PubMed:11223944). Leads also to avirulence in mice (PubMed:15632428).
Multifunctional phosphatidylinositol 3-kinase involved in acidification of vacuoles, pH-dependent cell growth, and autophagocytosis (PubMed:15861817, PubMed:15632428). Plays an important role in protein transport and virulence (PubMed:11223944, PubMed:15632428). Component of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure (By similarity). Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II (By similarity). This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes) (By similarity). Finally, it might also be involved in ethanol tolerance and cell wall integrity (By similarity).
Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Component of the PAM complex, at least composed of mtHsp70 (SSC1), MGE1, TIM44, PAM16, PAM17 and PAM18.
Involved in mitochondrial migration along actin filaments.
Belongs to the WD repeat coronin 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).
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).
Component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Belongs to the heat shock protein 90 family.
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.
Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity. Mediates resistance to oxidative stress. Controls the activation of the CEK1 MAP kinase. Influences the molecular weight and polymer distribution of cell wall mannan. Involved in invasive filamentation into semi-solid medium and plays a role in morphological dimorphic transition which is a differentiation program characteristic of C.albicans and which is known to play a major role in pathogenesis.
Adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
Belongs to the universal ribosomal protein uS14 family.
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).
Expression is regulated upon white-opaque switch (PubMed:12397174). Expression is repressed by HAP43 (PubMed:21592964).
Belongs to the 5'-AMP-activated protein kinase beta subunit family.
Expression is negatively regulated by RIM101. Expression is also increased in absence of SUR7, as well as CHK1 and NIK1.
Belongs to the DEAD box helicase family. DDX56/DBP9 subfamily.
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.
DNA polymerase II participates in chromosomal DNA replication.
Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Expressed during development of germ tubes, pseudohyphae and true hyphae. Induced during host infection.
Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. During infection, plays an important role in penetration into deeper tissues and interaction with host defense. Moreover, acts toward human hemoglobin though limited proteolysis to generate a variety of antimicrobial hemocidins, enabling to compete with the other microorganisms of the same physiological niche using the microbicidal peptides generated from the host protein.
Involved in DNA double-strand break repair (DSBR). Possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity. Also involved in meiotic DSB processing.
Belongs to the proteasome subunit S9 family.
Belongs to the WD repeat DCAF13/WDSOF1 family.
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).
Belongs to the TRAPP small subunits family.
Part of the multisubunit transport protein particle (TRAPP) complex.
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.
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 threonine aldolase family.
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 eukaryotic ribosomal protein eS21 family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (Probable). RPS21B is required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits and has a physiological role leading to 18S rRNA stability (By similarity).
Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane (By similarity).
Belongs to the universal ribosomal protein uS4 family.
Belongs to the transglutaminase-like superfamily. PNGase family.
Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins (By similarity).
Expression is induced by cell wall damage caused by caspofungin, and by osmotic stress through the HOG1 pathway. Expression is positively regulated by MNL1.
Leads to caspofungin hypersensitivity and increases filamentation.
Transcription repressor involved in cell wall damage response. Regulates 79 caspofungin-responsive genes, including several cell wall biogenesis genes such as CRH11, MNN2, and SKN1. Controls also the expression of pathogenesis and hyphal related genes and represses the yeast-to-hypha transition. Mediates the response to oxidative stress.
Undergoes HOG1-dependent phosphorylation after osmotic stress.
Component of the 20S proteasome chaperone.
Abolishes hyphal formation and impairs biofilm formation (PubMed:28743811). Sensitive to thermal stress (PubMed:28743811).
Belongs to the glycosyltransferase 20 family.
Inhibited by validoxylamine A, a non-reactive trehalose analog.
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 protein kinase superfamily. ADCK protein kinase family.
Belongs to the succinate/malate CoA ligase alpha subunit family.
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
Belongs to the U2 small nuclear ribonucleoprotein A family.
Sensitive to cell wall-damaging agents SDS and Congo red.
Serine/threonine-protein kinase which is part sphingolipid-mediated signaling pathway that is required for the internalization step of endocytosis by regulating eisosome assembly and organization, and modulating the organization of the plasma membrane. Phosphorylates and activates PKC1. Activates YPK1 and YPK2, 2 components of signaling cascade required for maintenance of cell wall integrity. Required for stress-induced P-body assembly and regulates global mRNA decay at the deadenylation step.
The PIF-pocket is a small lobe in the catalytic domain required by the enzyme for the binding to the hydrophobic motif of its substrates. It is an allosteric regulatory site that can accommodate small compounds acting as allosteric inhibitors.
Belongs to the transient receptor (TC 1.A.4) family.
Expression is down-regulated in response to alkaline pH when CRZ1 or RIM101 are deleted.
Leads to hypersensitivity to oxidative stress, increased sensitivity to killing by macrophages, reduced ability to invade epithelium cells, and attenuated virulence in a mouse model. Shows defects in hyphal maintenance, hyphal growth and flocculation. Prevents the localization of the Spitzenkoerper to hyphal tips. Enhances mitochondrial depolarization and apoptosis.
Vacuolar calcium channel involved in the release of calcium ions from the vacuole in response to hyperosmotic or alkaline stress. Required for activation of CAP1-related transcription of oxidative stress response (OSR) genes, but also for maintaining the stability of both the mitochondria and the vacuole in a potassium- and calcium-dependent manner. Contributes to pathogenicity. Plays a key role in hyphal polarized growth and re-orientation to host-signals through its contribution to the localization of the Spitzenkoerper to the hyphal tips.
Belongs to the major facilitator superfamily. CAR1 family.
Expression is repressed by caspofungin and during chlamydospore formation. Also regulated during white-opaque switch, and by NRG1, TUP1 and HAP43.
Leads to defects in biofilm architecture.
MFS antiporter that does not display functional linkage as drug transporter and performs functions that significantly affect biofilm development and virulence. No substrate for transport has been identified yet, but plays an important role in the growth in the host.
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.
Up-regulated by UV radiation, heat shock, osmotic stress and nitrogen starvation.
Involved in vacuolar transport and vacuole pH homeostasis. Also required for cytokinesis (By similarity).
Belongs to the GHMP kinase family. Homoserine kinase subfamily.
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
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.
Belongs to the V-ATPase F subunit family.
Belongs to the eukaryotic ribosomal protein eL27 family.
Belongs to the eukaryotic ribosomal protein eS26 family.
Constitutive, high-level transcription is commonly observed in laboratory and clinical strains of Candida albicans that are resistant to the antifungal drug fluconazole. Multiple cis-acting sequences within the promoter mediate its activation. One, a benomyl response element (BRE), is situated at position -296 to -260. It is required for benomyl-dependent MDR1 up-regulation and is also necessary for constitutive high expression of MDR1. A second element, termed H(2)O(2) response element (HRE), is situated at position -561 to -520. The HRE is required for H(2)O(2)-dependent MDR1 up-regulation, but dispensable for constitutive high expression. Two potential binding sites (TTAG/CTAA) for the transcription factor CAP1 lie within the HRE. Expression is induced by fluconazole, rifampicin, methotrexate, diethylmaleate, diamide, 4-nitroquinoline-N-oxide, benomyl, o-phenanthroline (OP), hydrogen peroxide, methyl methanesulfonate, and sulfometuron methyl. Expression is down-regulated by tetrandrine and levofloxacin derivatives. Transcription is positively regulated by ADA2, CAP1, MRR1, UPC2, and TAC1; and negatively regulated by REP1. Transcription is also regulated by the general transcription factor MCM1. MCM1 is dispensable for up-regulation by H(2)O(2) but is required for full induction by benomyl.
Leads to enhanced susceptibility against fluconazole, methotrexate, 4-nitroquinoline-N-oxide, and cycloheximide.
Plasma membrane multidrug efflux pump that confers resistance to numerous chemicals including azoles such as fluconazole, voriconazole, and benztriazoles, as well as to benomyl, cycloheximide, methotrexate, 4-nitroquinoline-N-oxide, sulfometuron methyl, cerulenin, and brefeldin A.
The central cytoplasmic loop (residues 295 to 350) is critical for the function, but unlike other homologous proteins, has no apparent role in imparting substrate specificity or in the recruitment of the transporter protein.
The overexpression of MDR1 is a frequent cause of resistance to the widely used antimycotic agent fluconazole and other toxic compounds in the pathogenic yeast Candida albicans.
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 eukaryotic ribosomal protein eL32 family.
Belongs to the mannose-6-phosphate isomerase type 1 family.
Expression is induced by host macrophages.
Leads to increased chitin content in the cell wall, hyperfilamentation, and resistance to sodium dodecyl sulfate, hydrogen peroxide, and sodium chloride. Shows also an increased virulence in a mouse model.
O-glycosylated. Extensively O-mannosylated.
Probable structural component of the cell wall involved in cell wall integrity and virulence.
Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine at position 1191 (Psi1191) in 18S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA.
Belongs to the TDD superfamily. TSR3 family.
Catalyzes the 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 adaptor complexes medium subunit family. Delta-COP subfamily.
Beta-mannosyltransferase involved in cell wall biosynthesis through beta-1,2-mannosylation of cell wall phosphopeptidomannan (By similarity). Plays a role in the ability to produce hyphae in the presence of three bacterial species.
Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase complex; essential for the ER localization.
Belongs to the GTP cyclohydrolase II family.
Essential component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as external driving force (By similarity).
Component of the RPD3C(L) histone deacetylase complex (HDAC). 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 (By similarity). Controls filamentous growth and required for full virulence in a mouse model of disseminated candidiasis.
Expression is controlled by the transcription factor ACE2.
Leads to defects in responding to some filament-inducing conditions and to reduced virulence.
The ASH1 mRNA is transported to the daughter cell before cytokinesis where translation produces the protein to block mating-type switching, as well as to the hyphal tips during filamentous growth.
Belongs to the PPP phosphatase family. PP-6 (PP-V) subfamily.
Causes growth retardation and leads to significant reduction in virulence.
Serine/threonine protein phosphatase which is involved in the dephosphorylation of the large subunit of RNA polymerase II. Is required in late G1 for normal G1 cyclin expression, bud initiation and expression of certain genes that are periodically expressed during late G1 (By similarity). Plays a role during hyphal growth through the regulation of cell wall biogenesis, osmosensing and protein translation. Involved in virulence in a mouse systemic infection model.
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.
Belongs to the clathrin light chain family.
Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family.
Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone.
In contrast to other lysine histone methyltransferases, it does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones.
Ubiquitination of histone H2B to form H2BK123ub1 is required for efficient DOT1 methyltransferase activity on histone H3.
Belongs to the SRP receptor beta subunit family.
Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Involved in nucleotide excision repair.
Belongs to the glutaminase PdxT/SNO family.
Probable cell surface protein involved in the process of adhesion and early events of invasion.
Up-regulated when cells are growing in an adherent manner and upon milbemycins A3 oxim derivative (A3Ox) treatment. Expression is also regulated by CYR1, RIM101 and SSN6.
Leads to auxotrophy for sulfur amino acids.
Transcription factor that binds ribosomal protein gene promoters and rDNA locus with TBF1. Necessary for the expression of genes involved in assimilation of inorganic sulfate. Also required for the expression of respiratory genes and glycolytic genes. Does not bind to centromeres and is not necessary for efficient chromosome segregationas as does S.cerevisiae CBF1.
Belongs to the complex I NDUFA2 subunit family.
Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation.
Belongs to the imidazoleglycerol-phosphate dehydratase family.
mRNA-binding protein which stimulates mRNA decapping.
Glycerophosphodiester transporter that mediates uptake of glycerophosphocholine (GroPCho) with GIT4 (PubMed:24114876). GIT3 acts as the major GroPCho permease (PubMed:24114876). Does not possess detectable glycerophosphoinositol (GroPIns) transport activity (PubMed:24114876). The expanded ability to utilize GroPIns and GroPCho results from the organism's pathogenic nature and its need to occupy a variety of environments within its host organism (PubMed:24114876). This possibility is buttressed by the fact that GroPIns and GroPCho are present and abundant in human fluids (PubMed:24114876).
Belongs to the indoleamine 2,3-dioxygenase family.
Belongs to the glycosyltransferase 22 family. PIGB subfamily.
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI during GPI precursor assembly (By similarity).
Belongs to the bacterial ribosomal protein bL9 family.
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 three sequential steps of tetrahydrofolate biosynthesis.
In the C-terminal section; belongs to the DHPS family.
In the N-terminal section; belongs to the DHNA family.
In the central section; belongs to the HPPK family.
Master transcriptional regulator of the switch between 2 heritable states, the white and opaque states. These 2 cell types differ in many characteristics, including cell structure, mating competence, and virulence. Each state is heritable for many generations, and switching between states occurs stochastically, at low frequency. WOR1 Binds the intergenic regions upstream of the genes encoding three additional transcriptional regulators of white-opaque switching, CZF1, EFG1, and WOR2. Phenotypic switching from the white to the opaque phase is a necessary step for mating. Plays a role in cell adhesion and pseudohyphal growth.
Only expressed in opaque cells, in which it forms a positive feedback loop since it binds its own DNA regulatory region and activates its own transcription leading to the accumulation of high levels of WOR1.
Belongs to the universal ribosomal protein uS5 family.
Expression is induced in biofilm and repressed by alpha pheromone.
Required for growth under high-pressure and low-temperature conditions.
Forms a fork protection complex (FPC) with CSM3 and which is required for chromosome segregation during meiosis and DNA damage repair. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors (By similarity).
Involved in the second step of GPI biosynthesis. De-N-acetylation of N-acetylglucosaminyl-phosphatidylinositol.
Amino-acid permease that coordinates external nitrogen source response and morphogenesis (PubMed:12949183, PubMed:21764911, PubMed:28028545). Is capable of transporting several structurally unrelated amino acids such as leucine and phenylalanine, though with a lower capacity than the GAP2 and GAP6 permeases (PubMed:21764911). Has citrulline import activity (PubMed:12949183). GAP1 is also able to transport thialysine, and thus probably also lysine (PubMed:21764911). Functions as a sensor via detection of some amino acids including methionine, leading to a rapid activation of trehalase, a downstream target of PKA (PubMed:21764911).
Decreases two fold the citrulline uptake (PubMed:12949183). Leads to defective hyphal formation in solid hyphal-inducing media and exhibits less hyphal clumps when induced by N-acetylglucosamine (PubMed:12949183).
Expression is under control of the CSY1 amino-acid sensor (PubMed:28028545). Expression is induced by N-acetylglucosamine (PubMed:12949183). Expression is also regulated by CPH1-mediated RAS1 signaling but is independent of EFG1 (PubMed:12949183). Induced during biofilm development (PubMed:21414038, PubMed:22265407, PubMed:23572557). Induced upon internalization by host macrophages (PubMed:15470236). Expression is down-regulated by growth in alkaline conditions (PubMed:15554973). Expression is also controlled by the nitrogen-dependent GATA-type transcriptional activator GAT1 (PubMed:14617156).
Belongs to the nucleoporin Nup133 family.
Belongs to the eukaryotic RPC34/RPC39 RNA polymerase subunit family.
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.
Opaque-specific transcript. Repressed by HAP43 and induced by macrophages.
Forms homooligomers. Interacts with MRS2.
Mitochondrial inner membrane magnesium transporter required for mitochondrial magnesium homeostasis. Modulates the conductance of the MRS2 channel. Involved in the splicing of mRNA group II introns in mitochondria by affecting mitochondrial magnesium concentrations, which are critical for group II intron splicing.
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.
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).
May be involved in cellular response to stress. Required to maintain mitochondrial DNA (mtDNA) integrity and stability (By similarity).
Belongs to the ammonia transporter channel (TC 1.A.11.2) family.
Required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Constitutes the ATP-driven core of the motor and binds the precursor preprotein (By similarity).
Belongs to the gluconokinase GntK/GntV family.
Belongs to the complex I NDUFA12 subunit family.
Homodimer; may form higher order oligomers. Interacts with the large RNA polymerase II subunit RPO21; the interaction is direct and serves to bridge RPO21 to the Elongin complex in a manner dependent on transcription stress. Interacts with RAD26.
Proteolytically cleaved by the proteasome in response to transcription stress; the resulting N-terminal form constitutes the activated nuclear form and the C-terminal portion is degraded.
Recruits the ubiquitination machinery to RNA polymerase II for polyubiquitination, removal and degradation, when the transcription-coupled repair (TCR) factor RAD26 fails to efficiently displace stalled RNA polymerase II. Also involved in telomere length regulation. Binds DNA.
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.
Involved in the early part of the secretory pathway.
Belongs to the bacterial ribosomal protein bL28 family.
Belongs to the glycosyl hydrolase 18 family. Chitinase class III subfamily.
Chitinase involved in the remodeling of chitin in the fungal cell wall. Plays a role in cell separation.
Expression is positively regulated by BCR1 and FKH2. Transcription is greater during growth of the yeast form as compared to the mycelial form, and down-regulated by micafungin treatment.
Leads to the clumping or clusterings of cells from early exponential phase, and to increased hyphal growth on solid media.
Proteolytic cleavage by SAP9 and SAP10 leads to the cell wall release of CHT2 and increased chitinase activity, suggesting a direct influence of SAP9 and SAP10 on CHT2 function.
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 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 (Probable). RPS2 is important for the assembly and function of the 40S ribosomal subunitand is nvolved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (By similarity).
Belongs to the Clp1 family. NOL9/GRC3 subfamily.
Polynucleotide 5'-kinase involved in rRNA processing.
Decreases MDR1 expression and leads to greater fluconazole and cerulenin susceptibility.
Expression is coordinately up-regulated with MDR1 in drug-resistant, clinical isolates. Expression is induced by HAP43.
Transcription factor that acts as the central regulator of the MDR1 efflux pump. Other target genes include those encoding oxidoreductases, whose up-regulation in fluconazole-resistant isolates may help to prevent cell damage resulting from the generation of toxic molecules in the presence of fluconazole and thereby contribute to drug resistance.
Belongs to the glycosyl hydrolase 15 family.
Belongs to the PheA/TfdB FAD monooxygenase family.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. KIN-5/BimC subfamily.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c.
Belongs to the 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 prefoldin subunit alpha 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.
Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs.
Component of the endosomal sorting complex required for transport II (ESCRT-II).
Belongs to the complex I NDUFA1 subunit family.
Expression is under the control of RAS1. Up-regulated during colonization of the cecum and invasion of host tissue. Down-regulation correlates with clinical development of fluconazole resistance.
Involved in the control of energetic metabolism and significantly contribute to cell fitness, especially under respiratory growth conditions.
Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Transcriptional activator that induces the transcription of a-specific mating genes.
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 eukaryotic ribosomal protein eS30 family.
Heterohexamer; composed of 3 copies of TIM9 and 3 copies of TIM10, named soluble 70 kDa complex. Associates with the TIM22 complex, whose core is composed of TIM22 and TIM54. Interacts with the transmembrane regions of multi-pass transmembrane proteins in transit (By similarity).
Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity).
The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIM9 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity).
Belongs to the choline monooxygenase family.
Catalyzes the first step of the osmoprotectant glycine betaine synthesis.
Leads to increased hyphal growth on solid media.
Transcription is greater during growth of the yeast form as compared to the mycelial form and up-regulated by micafungin treatment.
Belongs to the Mediator complex subunit 13 family.
Component of the SRB8-11 complex, which itself associates with the Mediator complex.
Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex (By similarity).
Belongs to the nucleoporin Nup85 family.
Component of the nuclear pore complex (NPC).
Functions as a component of the nuclear pore complex (NPC).
Transcription factor that binds the promoters of genes involved in biofilm formation, which include several key adhesion genes, and recruits MCM1 to these sites. Plays an important role in hyphal growth and virulence. Promotes conversion of opaque cells to white phase, but needs existence of EFG1, a key regulator required for maintenance of the white state.
Phosphorylation of the TEDS site (Ser-366) is required for the polarization of the actin cytoskeleton. Phosphorylation probably activates the myosin-I ATPase activity.
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). The IQ domain and the TH1 region are essential for hyphal growth and for endocytosis. The SH3 domain together with the TH3 region are required for the organization of the cortical actin.
Type-I myosin implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. 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 a role in chitin deposition in the cell wall, in determination of the budding pattern, and is required for hyphae formation.
Belongs to the sterol desaturase family.
C-4 methylsterol oxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:10783002). ERG25 is a catalytic component of the C-4 demethylation complex that catalyzes the conversion of 4,4-dimethylfecosterol into fecosterol via 4-methylfecosterol (PubMed:10783002). Catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols (PubMed:10783002). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable).
Essential gene; conditional lethal mutations decrease the production of ergosterol and accumulate 4,4-dimethylzymosterol.
Expression is induced by fluconazole and in azole-resistant strains (PubMed:15273122, PubMed:15820985). Expression is induced during biofilm formation (PubMed:15075282). Expression is up-regulated when ERG6, CYP51/ERG11 or ERG24 are deleted (PubMed:15473366).
The histidine box domains may contain the active site and/or be involved in metal ion binding.
Lys-51 undergoes hypusination, a unique post-translational modification that consists in the addition of a butylamino group from spermidine to lysine side chain, leading to the formation of the unusual amino acid hypusine. eIF-5As are the only known proteins to undergo this modification, which is essential for their function.
Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts. Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome. Acts as ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step.
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site.
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.
NAD-dependent histone deacetylase that is involved in nuclear silencing events. Derepresses subtelomeric silencing and increases repression in nucleolar (rDNA) silencing. Its function is negatively regulated by active nuclear export (By similarity).
Belongs to the methyltransferase superfamily. Trimethylguanosine synthase family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
Leads to defects in secretion of degradative enzymes and defects in hyphal extension.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Erg6/SMT family.
Does not affect the susceptibility to azoles (PubMed:9593144). Leads to hypersensitivity to cyclosporin A (CsA) and FK506, inhibitors of the protein phosphatase calcineurin (PubMed:11847103).
Expression is induced in the presence of fluconazole and up-regulated in azole-resistant strain (PubMed:15820985). Expression is positively regulated by the transcription regulator HAP43 (PubMed:21592964). Expression is also induced by N-acetyl-D-glucosamine (PubMed:22406769). Expression is repressed during spider biofilm formation (PubMed:22265407).
Sterol 24-C-methyltransferase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:9593144, PubMed:20946868). ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol (PubMed:9593144, PubMed:20946868). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable).
Substrate analogs 25-azalanosterol and 24(R,S),25-epiminolanosterol act as inhibitors.
Belongs to the eukaryotic ribosomal protein eS4 family.
Belongs to the eukaryotic ribosomal protein eL30 family.
Required for apical cell growth and plays an essential role in morphogenesis. May be integral to the pathogenic ability of the organism.
Strongly expressed under conditions of alkaline pH but not expressed at any pH below 5.5.
Transcription factor involved in the RAM (regulation of ACE2 transcription factor and polarized morphogenesis) signaling network that regulates polarized morphogenesis. Regulates expression of genes involved in cell separation such as CHT3, DSE1, and SCW11; or other cell wall genes such as ASH1, DSE4, PIR1, PRY2, and RME1. Required for regulation of morphogenesis, cell separation, adherence, biofilm formation, invasion, as well as virulence in a mouse model of infection.
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.
Belongs to the phosphoglycerate kinase family.
Heme-binding protein involved in heme-iron utilization. The ability to acquire iron from host tissues is a major virulence factor of pathogenic microorganisms. Required for biofilm formation.
Preferentially expressed during the mycelial growth phase with only low levels of transcript detected in the yeast form. Induced by iron starvation and ciclopirox. Positively regulated by BCR1 and RIM101, and repressed by TUP1. Expression is also regulated by EFG1, CPH1, HAP43, and SEF1.
The CFEM domain is involved in heme-binding. It contains 8 cysteines and is found in proteins from several pathogenic fungi, including both human and plant pathogens.
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.
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).
Expression is induced by HOG1 and during biofoilm formation, and repressed by caspofungin. Also regulated by SSN6.
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Together with GET1, acts as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. The GET complex cooperates with the HDEL receptor ERD2 to mediate the ATP-dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER.
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.
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 eukaryotic RPA43 RNA polymerase subunit family.
Plays a key role in autophagy (PubMed:36476055). Effector of VPS34 phosphatidylinositol 3-phosphate kinase signaling (By similarity). Regulates the cytoplasm to vacuole transport (Cvt) vesicle formation (By similarity). Plays a role in ATG protein retrieval from the pre-autophagosomal structure (PAS) and is especially required for autophagy-dependent cycling of ATG9 (By similarity). Finally, plays an important role in biofilm formation and resistance to antifungal compounds such as fluconazole, itraconazole, terbinafine and caspofungin (PubMed:36476055).
Belongs to the TrkH potassium transport family.
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 universal ribosomal protein uS2 family.
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 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).
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.
Contains 2 cytoplasmic nucleotide binding domains (NBDs). The N-terminal NBD has ATPase activity. The 2 NBDs are asymmetric and non-exchangeable and the drug efflux by CDR1 involves complex interactions between the two halves of the protein.
Disulfiram reverses CDR1-mediated drug resistance by interaction with both ATP and substrate-binding sites of the transporter and may be useful for antifungal therapy.
Leads to hypersusceptibility to the antifungal agents terbinafine and amorolfine, and to the metabolic inhibitors cycloheximide, brefeldin A, and fluphenazine. Shows a decreased number of germ tube-forming cells in the presence of estradiol when CDR2 is also deleted.
Pleiotropic ABC efflux transporter that confers resistance to numerous chemicals including anisomycin, cycloheximide, fluconazole, miconazole, ketoconazole, itriconazole, nystatin, terbinafine, amorolfine, brefeldin A, amphotericin B, fluphenazine, as well as estrogen. Plays a role in farnesol-induced apoptotic process through glutathione efflux activity. Mediates in-to-out translocation of membrane phospholipids including aminophospholipids and thus regulates asymmetric distribution of phosphatidylethanolamine. Exhibits nucleoside triphosphatase activity.
The distal promoter mediates the miconazole response whereas the proximal promoter (-345/+1) contains all the regulatory domains required for its induction by various other stresses. The promoter also contains a steroid responsive region (SRR) conferring beta-oestradiol and progesterone inducibility. Transcription is positively regulated by NCB2, NTD80 and TAC1 and repressed by FCR1. Expression is up-regulated during biofilm development, by heat-shock, and by benomyl, doxorubicin, miconazole, vinblastine, adriamycin, fluphenazine, cycloheximide, calcofluor, canavanine, 5'-fluorcytosine, cilofungin and caffeine. Expression is repressed by serum and inhibited by tetrandrine. Transcription is also reduced during in vitro fluconazole exposure but in the postexposure period, the mRNA abundance increases.
Necessary for the splicing of pre-mRNA. Has a role in the recognition of the branch site (5'-UACUAAC-3'), the pyrimidine tract and the 3'-splice site at the 3'-end of introns (By similarity).
Belongs to the DASH complex ASK1 family.
Belongs to the diacylglycerol acyltransferase family.
GPI-anchored cell wall protein involved in cell wall organization, hyphal growth, as well as in host-fungal interaction and virulence. Plays a role in adherence to plastic and to host epithelial cells. Promotes the tissue fungal burden during murine vaginal candidiasis. Increases also susceptibility to neutrophil-mediated killing. Furthermore, contributes to the severity of hematogenously disseminated candidiasis in normal mice, but not in neutropenic mice.
Leads to decreased adherence of germ tubes to plastic and epithelial cells, but not endothelial cells.
Repressed by HAP43 and in absence of GOA1.
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.
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins.
Expression is induced by N-acetylglucosamine (GlcNAc).
Leads to increased resistance to the chitin synthase inhibitor nikkomycin Z.
N-acetylglucosamine-induced protein which plays a role in the N-acetylglucosamine metabolic pathway.
Heterotetramer of ERG25, ERG26, ERG27 and ERG28. ERG28 acts as a scaffold to tether ERG27 and other 4,4-demethylation-related enzymes, forming a demethylation enzyme complex, in the endoplasmic reticulum. Interacts with ERG25, ERG26 and ERG27. Also interacts with ERG1, ERG3, ERG5, ERG6 and ERG11.
Part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (By similarity). ERG28 has a role as a scaffold to help anchor the catalytic components of the C-4 demethylation complex ERG25, ERG26 and ERG27 to the endoplasmic reticulum (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable).
Catalyzes the isomerization of citrate to isocitrate via cis-aconitate, a step in the citric acid cycle.
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 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).
Component of the septin complex which consists of CDC3, CDC10, CDC11, CDC12 and probably SEP7. The purified septin complex appeared to have a stoichiometry of 2 CDC3, 1 to 2 CDC10, 1 CDC11, 2 CDC12, and 1 or none SEP7 subunit. Induction of hyphal growth brings about important modifications in septin ring dynamics, because the rings were found in a different state from those of yeast cells. This hyphal-specific state contains a core of stable septins (SEP7, CDC3, and CDC12), and it shows a high CDC10 turnover between the ring and the cytoplasm. Interacts with GIN4.
Leads to a minor reduction in agar invasion ability.
Phosphorylated by GIN4 which stabilizes the GIN4-SEP7 interaction.
Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinase GIN4. Septins are also involved in cell morphogenesis, chlamydospores morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation. SEP7 is required to convert hyphal septin rings into the hyphal-specific state and is necessary for CDC10 turnover during hyphal growth.
Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity).
Catalyzes 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.
Transcription factor that activates stress response genes via SLE (STRE-like) elements. Required for adaptation to weak acid stress such as acetic acid stress, but seems not involved in the response to heat, osmotic, ethanol, nutrient, oxidative, or heavy-metal stress. Activates a subset of the genes that are repressed by NRG1.
Highly expressed in biofilms with down-regulation during later stages of biofilm formation. Expression is repressed by TPK1 and SFL1, and induced by TPK2. Also under the control of TOR1. Down-regulated by Riccardin D, a macrocyclic bisbibenzyl isolated from Chinese liverwort D.hirsute which has an inhibitory effect on biofilms and virulence. Induced by caspofungin.
Major cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Acts as a downstream effector of the EFG1 regulatory pathway. Required for rapamycin-induced aggregation of C.albicans. Binds glycans and mediates adherence to endothelial and epithelial cells, thereby playing an important role in the pathogenesis of C.albicans infections.
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.
Expression is negatively regulated by the TUP1 transcriptional repressor. Also regulated by EFG1, RFG1 and RIM101. Induced during hyphal growth, during mating process, under alkaline conditions, and by farnesol. Repressed by fluconazole.
GPI-anchored cell wall protein required for mating efficiency, biofilm formation, and virulence. Involved in normal disseminated infection, but not in intestinal colonization.
Leads to hypersensitivity to calcofluor white (CFW).
Belongs to the Mediator complex subunit 11 family.
Up-regulated upon milbemycin A3 oxim derivative (A3Ox) treatment. Expression is also regulated by CWT1.
Involved in DNA replication and cell separation.
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). Acts by mediating the C-terminal thiocarboxylation of sulfur carrier URM1. Its N-terminus first activates URM1 as acyl-adenylate (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 to form thiocarboxylation (-COSH) of its C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.
Belongs to the eukaryotic ribosomal protein eL22 family.
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.
Belongs to the myo-inositol oxygenase family.
Belongs to the peroxiredoxin family. Prx6 subfamily.
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively.
Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation.
Component of the heptameric LSM1-LSM7 complex that forms a seven-membered ring structure with a donut shape.
Belongs to the 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 (By similarity). Induces transcription of mating-type proteins ALPHA1 and ALPHA2 and moderately represses transcription of mating-type protein A1 in response to hemoglobin and growth signals. Involved in the induction of a high affinity fibronectin receptor by sub-inhibitory dosages of caspofungin.
Induced in the presence of exogenous hemoglobin and during the exponential growth phase and by cold-stress.
Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
Histone methyltransferase that trimethylates histone H3 'Lys-36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression.
The AWS and SET domains are necessary for transcription repression.
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 class I-like SAM-binding methyltransferase superfamily. EFM5 family.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that trimethylates elongation factor 1-alpha at 'Lys-79'.
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.
May be used as a target for the development of some new fungicide, due the fact the presence of a fourth mannose in GPI-anchor proteins is essential for viability in fungi but not in mammals.
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.
Has a decreased hyphal growth rate and is highly sensitive to SDS and fluconazole.
Belongs to the eukaryotic ribosomal protein eL36 family.
Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
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).
Component of the RIX1 complex required for processing of ITS2 sequences from 35S pre-rRNA.
Catalytic subunit of an S-adenosyl-L-methionine-dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nucleotide at position 10 (m2G10) in tRNAs.
Belongs to the protein-tyrosine phosphatase family. Non-receptor class myotubularin subfamily.
Belongs to the pyrroline-5-carboxylate reductase family.
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 DASH complex SPC34 family.
Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate.
Belongs to the 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.
Belongs to the peptidase C2 family. PalB/RIM13 subfamily.
Belongs to the eukaryotic RPC7 RNA polymerase subunit family.
Component of the RNA polymerase III (Pol III) complex.
Belongs to the DEAD box helicase family. DDX24/MAK5 subfamily.
Involved in oxidative stress response and redox homeostasis. Required for hydrogen peroxide-induced oxidation and nuclear localization (activation) of CAP1. Functions probably in concert with GPX3, the actual CAP1 modifying enzyme.
Leads to decreased virulence in a Galleria mellonella model.
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.
S-glutathionylation is reversible and dependent on a glutaredoxin.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.
Leads to sensitivity to calcofluor white and SDS, as well as to thermosensitivity.
Golgi membrane protein involved in vesicular trafficking and spindle migration.
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.
Belongs to the methyltransferase superfamily. NTM1 family.
Expression is regulated upon white-opaque switching. Repressed by RIM101 and alpha pheromone, and up-regulated upon interaction with macrophages.
Probable cell wall protein which may have esterase activity, with a preference for esters of fatty acids from 4 to 16 carbon atoms.
Belongs to the Orn/Lys/Arg decarboxylase class-II family.
Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.
Homodimer (By similarity). Only the dimer is catalytically active, as the active sites are constructed of residues from both monomers (By similarity).
Inhibited by antizyme (AZ) OAZ1 in response to polyamine levels. AZ inhibits the assembly of the functional homodimer by binding to ODC monomers and targeting them for ubiquitin-independent proteolytic destruction by the 26S proteasome.
Belongs to the histone deacetylase family. HD Type 1 subfamily.
Belongs to the SIMIBI class G3E GTPase family. ZNG1 subfamily.
Belongs to the bacterial ribosomal protein bL19 family.
Necessary for protein synthesis in mitochondria. Functions as a ribosome recycling factor in mitochondria.
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.
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).
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).
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.
Involved in O-glycosylation of cell wall and secreted proteins. Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage. Mainly responsible for the addition of the third mannose residue in an O-linked mannose pentamer. Can also substitute for MNT1 by adding the second mannose residue. Important for adherence to host surfaces and for virulence.
Repressed at pH values above 6 and progressively induced at more acidic pH values.
Required for apical cell growth and plays an essential role in morphogenesis. May be integral to the pathogenic ability of the organism (By similarity).
Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type II sub-subfamily.
Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit. Interacts with pstB2. This interaction may be a means to structurally tether the donor membrane (ER) harboring PstB2 to acceptor membranes (Golgi/endosomes) harboring PSD2 during PtdSer transport to the site of PtdEtn synthesis.
The C2 domains have an essential, but non-catalytic function. They may facilitate interaction with PstB2 and are required for lipid transport function.
Required for transport of secretory proteins from the Golgi complex. Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes in vitro (By similarity).
Belongs to the complex I 20 kDa subunit family.
Belongs to the cytochrome c oxidase subunit 6A family.
Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Leads to increased caspofungin sensitivity.
Protein kinase involved in regulation of actin cytoskeleton organization and endocytosis. Phosphorylates the endocytic protein SLA1. The CDC28-CLN3 complex phosphorylation of SLA1 enhances its further phosphorylation by PRK1, weakening SLA1 association with PAN1, an activator of the actin-nucleating ARP2/3 complex. Plays a role in cell wall regulation and required for oxidative stress survival.
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 copper transporter (Ctr) (TC 1.A.56) family. SLC31A 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.
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.
Catalyzes the hydrolytic deamination of cytosine to uracil or 5-methylcytosine to thymine. Is involved in the pyrimidine salvage pathway, which allows the cell to utilize cytosine for pyrimidine nucleotide synthesis.
Decreases myo-inositol import into cell (PubMed:18268031). Virulence is not affected in a mouse model of disseminated infection (PubMed:18268031). Simultaneous disruption of INO1 results in lethality (PubMed:18268031).
Activated by the amino acid-induced proteolytic removal of an N-terminal inhibitory domain.
Expression is down-regulated in presence of extracellular amino acids.
Impairs expression of SAP2 and OPT1. Impairs virulence in Drosophila as a host model.
Transcription factor that activates genes required for degradation of extracellular protein and uptake of peptides such as the secreted aspartyl protease SAP2 or the oligopeptide transporter OPT1. Required for virulence. Synthesized as latent cytoplasmic precursor, which, upon a signal initiated by the plasma membrane SPS amino acid sensor system (including CSY1 and CSH3), becomes proteolytically activated and relocates to the nucleus, where it induces the expression of SPS-sensor-regulated genes.
Cell wall protein which mediates cell-cell and cell-substrate adhesion. Required for biofilm formation and plays a role in virulence (By similarity).
Expression in regulated by NRG1 and TUP1.
Belongs to the polyprenol kinase family.
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.
As a major cell surface protein expressed during infection, HWP1 detection can be used for diagnosis of invasive candidiasis. HWP1 epitopes can also be used to develop vaccines for protection against candidiasis.
Major hyphal cell wall protein which plays a role of adhesin and is required for mating, normal hyphal development, cell-to-cell adhesive functions necessary for biofilm integrity, attachment to host, and virulence. Promotes interactions with host and bacterial molecules, thus leading to effective colonization within polymicrobial communities. Plays a crucial role in gastrointestinal colonization, in mucosal symptomatic and asymptomatic infections, in vaginitis, as well as in lethal oroesophageal candidiasis, caused by the combined action of fungal virulence factors and host inflammatory responses when protective immunity is absent.
Reduces the overall mating frequency in both liquid and solid media. Impairs stable attachments to human buccal epithelial cells and reduces capacity to cause systemic candidiasis in mice. Produces a thin biofilm that lacks much of the hyphal mass found in the wild type cell.
Serves as a substrate for mammalian transglutaminases which are necessary for cross-linking between HWP1 and host epithelial cells. Also predicted to be a substrate for cleavage by KEX2.
The promoter contains a 368 bp region, the HWP1 control region (HCR), which is target of transcription factors and is critical for activation under hypha-inducing conditions. Expression is positively regulated by BCR1, EFG1, FLO8, GPA2, GPR1, MSS11, RBF1, and RFG1; and negatively regulated by NRG1 and TUP1. Transcription is induced in an adhesion-dependent manner and in presence of human serum or hemoglobin. Expression is down-regulated by hypoxic conditions, allicine, ethylenediaminetetra-acetic acid (EDTA), farnesol, linalool, riccardin D, purpurin, filastatin, phorbasin H, Ocimum sanctum essential oil (OSEO), as well as many substances belonging to chemical classes such as methyl aryl-oxazoline carboxylates, dihydrobenzo-d-isoxazolones, and thiazolo-4,5-e-benzoisoxazoles. Moreover, the competitors Saccharomyces boulardii or Streptococcus mutans secrete respectively capric acid and trans-2-decenoic acid (SDSF) which also suppress HWP1 expression.
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.
Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. Dihydroflavonol-4-reductase subfamily.
Catalyzes the irreversible reduction of the cytotoxic compound methylglyoxal (MG, 2-oxopropanal) to (S)-lactaldehyde. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation.
Belongs to the DNA polymerase type-A family.
Belongs to the UTP23/FCF1 family. FCF1 subfamily.
Cell wall glucan 1,3-beta-glucosidase involved in cell wall biosynthesis and virulence. Crucial for delivery of beta-1,3-glucan to the biofilm matrix and for accumulation of mature matrix biomass. Plays a role as a major antigen in human systemic candidiasis patients.
Exhibits diminished extracellular biofilm material, renders cells more dependent on chitin for wall integrity, and attenuates virulence in mice.
Induced during biofilm formation and by fluconazole and micafungin. Expression is also regulated by RCK2.
Belongs to the TFIIF alpha subunit family.
TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation.
Belongs to the eukaryotic ribosomal protein eL31 family.
Belongs to the steroid 5-alpha reductase family.
Adds the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(1)Man(9)GlcNAc(2)-PP-Dol (By similarity).
Belongs to the ALG6/ALG8 glucosyltransferase family.
Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate functions as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes (By similarity).
Belongs to the 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.
Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
Belongs to the phosphatase 2A regulatory subunit B family.
Component of the checkpoint clamp complex involved in the surveillance mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes.
Expressed in cell walls of both yeast and hyphae cells. Up-regulated by growth in hypoxic conditions, during cell wall regeneration, by heat stress, as well as by calcineurin, caspofungin, and fluconazole. Expression is also regulated by CAS5, RLM1, and SPF1.
Divalent metal ions. Mg(2+) is the most effective.
Superoxide dismutases serve to convert damaging superoxide radicals, a key form of ROS, to less damaging hydrogen peroxide that can be converted into water by catalase action. May be involved protection against extracellular stress.
Unlike SOD4 and SOD5, SOD6 is not regulated during yeast to hyphae transition or by temperature. Up-regulated during biofilm formation and expression is controlled by HAP43.
Belongs to the EF-1-beta/EF-1-delta family.
Expression is high in white-phase cells and low in opaque-phase cells.
Transcription factor that is recruited by AHR1 to the promoters of genes involved in biofilm formation, which include several key adhesion genes. Plays an important role in cell adhesion, hyphal growth and virulence. Implicated in the regulation of opaque-phase-specific gene expression.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. uL10 forms part of the P stalk that participates in recruiting G proteins to the ribosome.
Expression is very weak and pH-independent.
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 spore wall assembly (By similarity).
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.
Required for exosome-dependent processing of pre-rRNA and small nucleolar RNA (snRNA) precursors. Involved in processing of 35S pre-rRNA at the A0, A1 and A2 sites.
Belongs to the eukaryotic ribosomal protein eS7 family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (Probable). RPS7A is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (By similarity).
Belongs to the eukaryotic ribosomal protein eS27 family.
Expressed during development of germ tubes, pseudohyphae and true hyphae. Expressed in greater amounts in the mature biofilms compared to early biofilms during inflammatory disorder of the palatal mucosa among denture wearers.
Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. During infection, plays an important role in penetration into deeper tissues and interaction with host defense. Activates host systemic immunity and induces host inflammatory cytokine production in a proteolytic activity-independent way. Contributes to corneal pathogenicity. Moreover, acts toward human hemoglobin though limited proteolysis to generate a variety of antimicrobial hemocidins, enabling to compete with the other microorganisms of the same physiological niche using the microbicidal peptides generated from the host protein.
Belongs to the phospholipid scramblase family.
Catalyzes the final step in the biosynthesis of the membrane lipid glucosylceramide (GluCer), the transfer of glucose to ceramide. Glucosylceramides play important roles in growth, differentiation and pathogenicity.
Results in complete loss of glucosylceramides (GluCers) in mutant cells (PubMed:11443131). Has a decreased hyphal growth rate and increased susceptibility to SDS and fluconazole, suggesting defects in the cell membrane structure (PubMed:20019081). Shows increased resistance to plant defensin RsAFP2, and to heliomicin, a defensin-like peptide from the insect Heliothis virescens (PubMed:14604982).
The D1, D2, D3, (Q/R)XXRW motif is a critical part of the GCS active site, involved in catalysis and UDP-sugar binding.
Confers pleiotropic effects like an increased sensitivity to mild heat shock, increased formation of colony morphology variants and induction of hyphal and pseudohypal development (PubMed:12742065). Induces cell cycle defects, as well as sensitivity to thermal, oxidative and cell wall stresses. Rapidly lose viability under starvation conditions (PubMed:21269335).
For the sake of clarity sequence features are annotated only for the first chain, and are not repeated for each of the following chains.
Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). Involved in the negative control of switching, as well as in maintaining the yeast cell morphology (PubMed:12742065, PubMed:21269335).
Belongs to the chorismate synthase family.
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).
Belongs to the Mediator complex subunit 8 family.
In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
Belongs to the TFIIE alpha subunit family.
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.
Belongs to the DNA2/NAM7 helicase family.
Involved in the regulation of telomere length, clustering and has a specific role in telomere position effect (TPE).
Cell cycle-regulated with a peak during M/G1.
Ser/Thr-protein kinase involved in the mitotic exit network (MEN) and required after the metaphase to anaphase cell cycle transition. Required for proper nuclear segregation, mitotic spindle organization, actomyosin ring contraction, primary septum assembly, and normal hyphal morphogenesis.
Belongs to the mitochondrion-specific ribosomal protein mS33 family.
This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Expression is under control of the CSY1 amino-acid sensor (PubMed:28028545).
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 eukaryotic/archaeal RNase P protein component 2 family.
Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Belongs to the proteasome subunit S5B/HSM3 family.
Involved in DNA mismatch repair in slow-growing cells. Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the 19S regulatory complex (RC) (By similarity).
Belongs to the bacterial ribosomal protein bS6 family.
NAD(+)-dependent glutamate dehydrogenase which degrades glutamate to ammonia and alpha-ketoglutarate.
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 mS37 family.
Component of the mitochondrial small ribosomal subunit.
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).
Forms constitutive pseudohyphae. Impairs ability to damage human epithelial or human endothelial cells in vitro.
Induced during host epithelium infection. Expression is positively regulated by CDC28.
Transcription factor required for the morphogenesis of true hyphal as well as yeast cells. Contributes to virulence.
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
Transcription factor involved in DNA damage responses, morphogenesis, and virulence.
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. CGI121 acts as an allosteric effector that regulates the t(6)A activity of the complex. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators. CGI121 is not required for tRNA modification (By similarity).
Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration.
Leads to enhanced sensitivity to both cysteine and sulfite.
Sulfite efflux pump required for the secretion of sulfite as a reducing agent (By similarity). Plays a role in resistance to neutrophils during infection. Involved in transition to filamentous growth, which is believed to be central to the virulence of this human pathogen.
Up-regulated by cysteine, nitic oxide, and in response to neutrophil phagocytosis. Expression is under the control of GCN2, GCN4 and ZCF2.
Alpha-1,2-mannosyltransferase required for cell wall integrity. Responsible for addition of the first alpha-1,2-linked mannose to form the branches on the mannan backbone of oligosaccharides. Addition of alpha-1,2-mannose is required for stabilization of the alpha-1,6-mannose backbone and hence regulates mannan fibril length; and is important for both immune recognition and virulence. Promotes iron uptake and usage along the endocytosis pathway under iron-limiting conditions.
Decreases the ability to extend O-linked, and possibly also N-linked, mannans. Leads to hypersensitivity to cell wall-damaging agents, and to a reduction of cell wall mannosylphosphate. Leads also to resistance to killing by the iron-chelating protein lactoferrin.
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).
Belongs to the proteasome subunit p27 family.
Belongs to the eukaryotic ribosomal protein eL40 family.
Belongs to the GHMP kinase family. Mevalonate kinase subfamily.
Expression is up-regulated in response to terbinafine.
Mevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). ERG12 converts mevalonate into 5-phosphomevalonate (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable).
Constitutive expression independent of white/opaque switching or mating type locus.
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.
Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
May be involved in protection from oxidative damage.
Cell surface protein involved in the host-parasite interaction during candidal infection. With MP65, represents a major component of the biofilm matrix. Sequesters zinc from host tissue and mediates leukocyte adhesion and migration. As a surface protein, binds the two human complement regulators CFH and CFHR1, as well as plasminogen PLG, mediates complement evasion and extra-cellular matrix interaction and/or degradation. As a released protein, enhances complement control in direct vicinity of the yeast and thus generates an additional protective layer which controls host complement attack, assisting the fungus in escaping host surveillance. Binds to host fluid-phase C3 and blocks cleavage of C3 to C3a and C3b, leading to inhibition of complement activation. Mediates also human complement control and complement evasion through binding to C4BPA, another human complement inhibitor, as well as through binding to host integrin alpha-M/beta-2. Decreases complement-mediated adhesion, as well as uptake of C.albicans by human macrophages.
Component of a multiprotein complex of 250 kDa composed of at least HYR1, MP65, and PRA1. Interacts with host Integrin alpha-M/beta-2 heterodimer. Binds also human factor H (CFH), CFHR1, plasminogen (PLG), complement C3, and C4BPA.
Differentially expressed in response to changes in the pH with aximal expression at neutral pH and no expression detected below pH 6.0. Expression is controlled by RIM101. Expression is also increased during adhesion onto human epithelia.
Impairs hypha formation. Protects the fungus against leukocyte killing in vitro and in vivo, impedes the innate immune response to the infection, and increases fungal virulence and organ invasion in vivo.
N- and O-glycosylated. The N- and 0-glycosidically linked carbohydrates represent 18 to 20 percent and 3 to 4 percent, respectively, of the molecular mass of PRA1. 0-linked sugar residues may be involved in the interaction with fibrinogen. Contributes highly to the carbohydrate component of the matrix. Treatment with tunicamycin impairs glycosylation.
Histidine kinase involved in a two-component signaling pathway that regulates cell wall mannan biosynthesis. Part of the bifurcated SLN1-YPD1-SKN7/SSK1 two-component regulatory system, which controls activity of the HOG1 pathway and gene expression in response to oxidative stress and probably also to changes in the osmolarity of the extracellular environment. Plays a role in the regulation of alternative oxidase (AOX) gene family expression. Required for hyphal formation and virulence.
The phosphorelay mechanism involves the sequential transfer of a phosphate group from His-515 (H1) in the histidine kinase domain (transmitter domain) to Asp-1300 (D1) of the response regulatory domain (receiver domain). This transfer probably occurs between two SLN1 molecules, rather than intramolecularly (By similarity).
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.
Belongs to the mitochondrial Rho GTPase family.
Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution.
Belongs to the DNA polymerase type-B-like family.
C-14 sterol reductase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:11897574). ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol (PubMed:11897574). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable).
Leads to the accumulation of ignosterol (ergosta-8,14-dienol), and of a new sterol, ergosta-8,14,22-trienol (PubMed:11897574). Results in slow growth and significant increased sensitivity to an allylamine antifungal and to selected cellular inhibitors including cycloheximide, cerulenin, fluphenazine, and brefeldin A (PubMed:11897574). Slightly increases resistance to azoles (PubMed:11897574). Significantly reduces pathogenicity in a mouse model system and fails to produce germ tubes upon incubation in human serum (PubMed:11897574).
Belongs to the eukaryotic ribosomal protein eL37 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.
IFF11 differs from other HYR1/IFF family members in lacking a GPI-anchor.
Leads to hypersensitivity to cell wall-damaging agents and highly attenuated in a murine model of systemic infection.
Transcription factor that binds upstream of hexose and ergosterol metabolism, as well as cell cycle genes. Activates pseudohyphal growth.
Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase subunit family.
Belongs to the DNA polymerase delta/II small subunit family.
Converts proline to delta-1-pyrroline-5-carboxylate.
Guanine nucleotide-exchange factor (GEF) required for the formation or budding of transport vesicles from the ER.
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.
Expressed predominantly by the mycelial cells. Also induced during cell wall regeneration and biofilm formation. Repressed by fluconazole.
Glycosylated protein with a polysaccharide moiety composed exclusively of mannose and glucose at a ratio of 12.7 to 1. Contributes highly to the carbohydrate component of the matrix. Treatment with tunicamycin impairs glycosylation.
Impairs germ tube formation and suppresses hyphal formation. Decreases also pathogenicity and adherence to polystyrene plates.
Surface mannoprotein required for hyphal morphogenesis, surface adherence, and pathogenicity. Contributes in a high proportion to the carbohydrate component of the matrix due to high levels of glycosylation and may play important roles during biofilm development and maintenance. Acts as a major antigen target of host cell-mediated immune response. Induces extensive T-cell proliferation of human peripheral blood mononuclear cells. Facilitates host dendritic cells maturation and promotes cytokine production through its glycosylated portion while its protein core is essentially involved in induction of T-cell response.
The presence of the MP65 gene can be used as a diagnostic marker to distinguish C.albicans from other yeast or Candida species by PCR.
Belongs to the Mediator complex subunit 7 family.
Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
Component of the HAT-B complex composed of at least HAT1 and HAT2. The HAT-B complex binds to histone H4 tail.
Regulatory subunit of the histone acetylase B (HAT-B) complex. The complex acetylates 'Lys-14' of histone H4 which is required for telomeric silencing.
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 (By similarity). Required for yeast cell adherence to silicone substrate, but nor required not required for buccal epithelial cell adherence or virulence in mouse systemic infection.
Decreases cell adherence to silicone substrate. Decreases slightly filamentation.
Decreases cell adherence to silicone substrate. Blocks biofilm formation.
Expression is down-regulated during growth at pH 8 by the pH-responsive transcription factor RIM101. Induced during exposure to the weak acid stress of acetic acid, through the regulation by the transcription factor MNL1.
Transcription factor that regulates pH-induced filamentation with RIM101. Required for yeast cell adherence to silicone substrate and biofilm formation.
Belongs to the eukaryotic/archaeal RNase P protein component 1 family.
Pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase.
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 small GTPase superfamily. Arf family.
GTP-binding protein involved in protein trafficking; modulates vesicle budding and uncoating within the Golgi apparatus.
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.
Positive regulator of phosphatidylinositol 4,5-bisphosphate turnover and negatively regulates signaling through the cell integrity pathway. Involved in rDNA silencing (By similarity).
Induced by farnesol and ciclopirox. Expression is higher in opaque cells compared to white cells.
Superoxide dismutases serve to convert damaging superoxide radicals, a key form of ROS, to less damaging hydrogen peroxide that can be converted into water by catalase action. Degrades host-derived reactive oxygen species to escape innate immune surveillance. Involved in the occurrence of miconazole-tolerant persisters in biofilms. Persisters are cells that survive high doses of an antimicrobial agent.
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.
Highly specific phosphatase involved in the metabolism of ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of tRNA splicing.
Involved in gross chromosomal rearrangements (GCRs) and telomere healing.
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).
Expression is specific to in opaque cells, in presence of lactate, and during hyphal growth. Expression is repressed in response to alpha pheromone.
Enhances flocculation, filamentous growth, and hypha-specific gene expression in several media and at several growth temperatures.
Transcription factor that plays a role of repressor of filamentous growth and flocculation. Antagonizes functions of SFL2 and FLO8. Plays a role in the hyphal repression induced by secreted factors like dodecanol by competitors such as Pseudomonas aeruginosa and Burkholderia cenocepacia.
In the C-terminal section; belongs to the TrpB family.
In the N-terminal section; belongs to the TrpA family.
Belongs to the eukaryotic ribosomal protein eL21 family.
Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.
Leads to defects in biofilm architecture and attenuated virulence.
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.
Lacks the C-terminal half of the classical GPI inositol-deacylases.
May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi.
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.
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.
Common component of the spliceosome and rRNA processing machinery. In association with the spliceosomal U4/U6.U5 tri-snRNP particle, required for splicing of pre-mRNA. In association with box C/D snoRNPs, required for processing of pre-ribosomal RNA (rRNA) and site-specific 2'-O-methylation of substrate RNAs. Essential for the accumulation and stability of U4 snRNA, U6 snRNA, and box C/D snoRNAs (By similarity).
Component of the U3 snoRNP particle. Binds to the C'/D and B/C motifs in U3 snoRNA. Component of the 25S U4/U6.U5 tri-snRNP particle, a subcomplex of the spliceosome. Binds to the 5' stem-loop of U4 snRNA (By similarity).
Has a role in the initiation of DNA replication. Required at S-phase checkpoint (By similarity).
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
Belongs to the 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 (via N-terminus) 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. Further stabilizes spliceosome conformation for 3'-splice site docking (via C-terminus) promoting exon ligation.
In the C-terminal section; belongs to the histidinol dehydrogenase family.
Belongs to the eukaryotic ribosomal protein eL34 family.
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 (By similarity).
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.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase 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 GatFAB amidotransferase (AdT) complex, composed of A, B and F subunits.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily.
In the C-terminal section; belongs to the AIR carboxylase family. Class I subfamily.
Belongs to the amidase family. GatA subfamily.
Serine hydrolase involved in the detoxification of formaldehyde.
Belongs to the DASH complex DAD2 family.
Belongs to the concentrative nucleoside transporter (CNT) (TC 2.A.41) family.
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.
Non-catalytic component of the proteasome.
Belongs to the galactose-1-phosphate uridylyltransferase type 1 family.
Expression is regulated by the transcription factor NRG1.
Phosphomevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (PubMed:11243736). ERG8 converts 5-phosphomevalonate to 5-diphosphomevalonate (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable).
Has a role in a nucleosome assembly pathway that is required for the integrity of heterochromatin and proper chromosome segregation.
Expression is higher in white cells than opaque cells. Induced during exposure to the weak acid stress of acetic acid, through the regulation by the transcription factor MNL1.
Leads to hypersensitivity to ion stress.
Probably phosphorylated in a calcineurin-dependent manner.
Transcription factor involved in the regulation of calcium ion homeostasis and required for the maintenance of membrane integrity. Binds to the calcineurin-dependent response element. Plays a role in azole tolerance.
Belongs to the MICOS complex subunit Mic10 family.
Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Belongs to the SMC family. SMC5 subfamily.
Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
May organize microtubules by mediating spindle positioning and movement in the budding process. Required for cytokinesis and the maintenance of polarized hyphal growth.
2/mitotic-specific cyclin essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis. Degradation is necessary for the cell to exit from mitosis. Plays a role in morphogenesis by negatively regulating polarized growth. Through binding to CDC28 regulates cytokinesis, partly by phosphorylation of the actomyosin ring component IQG1.
Belongs to the cyclin family. Cyclin AB subfamily.
Expressed from S phase through G2 and M phases and is degraded at the end of mitosis. Expression is down-regulated by the anti-fungal agent plagiochin E (PLE).
Leads to completely attenuated virulence in a mouse keratitis model.
Required for intron-independent turnover and processing of mitochondrial RNA. It is a key control element in nuclear-mitochondrial interactions (By similarity). Required for embedded hyphal growth, for wild-type respiratory growth, and biofilm development. Required for chlamydospore formation, distinctive morphological feature of the fungal pathogen C.albicans that can be induced to form in oxygen-limited environments and has been reported in clinical specimens. Plays am important role in virulence.
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
Acidic protein, which assembles histones into an octamer (By similarity). Involved in the regulation of the localization and the function of the septins during mitosis.
Belongs to the nucleosome assembly protein (NAP) family.
Component of the GIN4 complex which forms a ring at the bud neck.
Leads to constitutive filamentous growth and abnormalities in both septin localization and organization. Exhibits greatly reduced virulence in a mouse model of systemic candidiasis.
Phosphorylation is cell cycle dependent and is important for its bud neck localization. Phosphorylation is highest in newly collected G1 cells, declines when the cells are traversing through the G1 phase, and reaches the lowest level around the time of bud emergence. Phosphorylation increases and remains high through the rest of the cell cycle until the beginning of the next one, when it decreases again. Phosphorylation involves two septin ring-associated kinases, CLA4 and GIN4, and its dephosphorylation occurs at the septin ring in a manner dependent on the phosphatases PP2A and CDC14.
Belongs to the ferric reductase (FRE) family.
Ferric reductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane. Also participates in Cu(2+) reduction and Cu(+) uptake (By similarity). Involved in maintenance of cell wall integrity (CWI), mitochondrial function, and interaction between the pathogen and the host.
Leads to abnormal cell wall composition, decreased ability of adhesion, and hypersensitivity to cell wall stresses. Increases mitochondrial activity and shows abnormal mitochondrial morphology. Results also in up-regulation of the expression of the cell wall integrity (CWI) genes PGA13 and CRH11, enhanded secretion, and decreased ability to invade HeLa cells.
Transcription is negatively regulated by SFU1, copper, amphotericin B, and caspofungin; and induced by ciclopirox olamine.
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.
Involved in ribosomal large subunit assembly.
Belongs to the 2H phosphoesterase superfamily. CPD1 family.
Involved in the metabolism of ADP-ribose 1',2'-cyclic phosphate which is produced as a consequence of tRNA splicing.
TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity.
Belongs to the HAD-like hydrolase superfamily. MasA/MtnC family.
Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Belongs to the eukaryotic ribosomal protein eL33 family.
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).
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 WD repeat PRL1/PRL2 family.
Involved in pre-mRNA splicing and required for cell cycle progression at G2/M.
Component of several multiprotein Golgi SNARE complexes.
Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor.
Component of the 66S pre-ribosomal particle.
Required for efficient assembly and nuclear export of the 60S ribosomal subunit.
Functions as an activator subunit for the CBK1 protein kinase. Part of the regulation of ACE2 activity and cellular morphogenesis (RAM) signaling network. The RAM network is critically required for hyphal growth as well as normal vegetative growth, and for polarization of lipid rafts and the actin cytoskeleton. It play an essential role in biofilm formation. The RAM network also plays a role in serum- and antifungal azoles-induced activation of ergosterol biosynthesis genes, especially those involved in the late steps of ergosterol biosynthesis.
Interacts with protein kinase CBK1 to form the RAM CBK1-MOB2 kinase complex.
Leads to hypersensitivity to cell-wall- or membrane-perturbing agents, cell-separation defects, a multinucleate phenotype, and loss of cell polarity.
Phosphorylated by CDC28 at Ser-44, Ser-51, Ser-67, and Ser-97. Phosphorylation occurs during bud emergence and is maintained until the G2/M transition. Dephosphorylated at the end of mitosis. Phosphorylation is required for the maintenance of polarisome components in hyphae.
Required for proper 27S pre-rRNA processing and 60S ribosome subunit assembly.
Expression is regulated by GCN2 and GCN4.
Leads to defects in endocytosis. Displays a characteristic class E vacuolar morphology and multilamellar structures consistent with an aberrant prevacuolar compartment. Missorts several vacuolar proteins to the extracellular space, including carboxypeptidase (CPY), vacuolar protease A (PrA), and vacuolar protease B (PrB). In addition, certain soluble secretory proteins, such as invertase and acid phosphatase, are missorted from the pre-vacuolar compartment (PVC) to the general secretory pathway prior to exocytosis. Results also in a decrease of canonically secreted proteins. Shows increased biofilm formation. Causes reduced tissue damage in an in vitro oral epithelial model (OEM) of tissue invasion, and defects in macrophage killing in vitro. Shows also attenuated virulence in an in vivo Caenorhabditis elegans model representative of intestinal epithelial infection.
Monomer or homodimer (in nucleotide-free form). Decamer, dodecamer or tetradecamer of two stacked respective homooligomeric rings (when bound to ATP); the dodecameric form seems to be predominant.
Pre-vacuolar protein sorting protein involved in the transport of biosynthetic membrane proteins from the prevacuolar/endosomal compartment to the vacuole. Required for multivesicular body (MVB) protein sorting. Catalyzes the ATP-dependent dissociation of class E VPS proteins from endosomal membranes, such as the disassembly of the ESCRT-III complex. Required for extracellular secretion of the secreted aspartyl proteases SAP2, SAP4, SAP5, and SAP6. Its regulation of the pre-vacuolar secretory pathway is critical for virulence.
Amines and amino acids act as activators of catalytic activity, whereas natural product-based phenols, dithiocarbamates, aliphatic and aromatic carboxylates, boronic acids, and sulfonamides act as inhibitors of enzymatic activity. Also inhibited by anions such as cyanide and carbonate, and to a lesser extent by sulfate, phenylboronic, and phenyl arsonic acid.
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. Involved in protection against oxidative damage. Acts as a CO(2) chemosensor and induces CO(2)-mediated filamentation. Essential for pathological growth in niches where sufficient CO(2) is not supplied by the host. Necessary for white-to-opaque switching at low CO(2) concentrations.
Strongly expressed when cells are grown in ambient air but non-detectable when cultured in air enriched with CO(2). Up-regulated by MNL1, HAP43, RCA1, and during early stages of biofilm development.
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.
Inactivated by metal-chelating agents phenanthroline and EDTA. Inhibited by bestatin, an aminopeptidase inhibitor. Not inhibited by pepstatin A and PMSF, inhibitors of aspartic and the serine proteases, respectively. Not inhibited by carboxypeptidase inhibitor.
Metalloprotease that specifically hydrolyzes peptides with N-terminal alanine, arginine and leucine residues.
Associates with the NTC complex (or PRP19-associated complex). The NTC complex associates with the spliceosome after the release of the U1 and U4 snRNAs and forms the CWC spliceosome subcomplex reminiscent of a late-stage spliceosome.
Involved in pre-mRNA splicing. May function at or prior to the first catalytic step of splicing at the catalytic center of the spliceosome. May do so by stabilizing the catalytic center or the position of the RNA substrate (By similarity).
Belongs to the WD repeat G protein beta family.
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.
May be required for lysis of autophagic vesicles after delivery to the vacuole.
Expression is induced during infection and decreased by benomyl treatment.
Leads to strong defects in host cell damage in a model of human oral epithelial cells. Exhibits reduced survival following co-incubation with a human macrophage cell line and causes more severe kidney pathology following intravenous murine infection. Leads also to higher levels of interleukin-1 beta (IL1B), following incubation with murine macrophages.
Virulence factor involved in pathogen-host interaction. Modulates host pro-inflammatory cytokine interleukin-1 beta (IL1B) expression.
Necessary for protein translocation in the endoplasmic reticulum.
Belongs to the eukaryotic ribosomal protein eS10 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.
Required for the regulation of both a MAP kinase signaling pathway and a cAMP signaling pathway. The activation of these pathways contributes to the pathogenicity of the cells through the induction of the morphological transition from the yeast to the polarized filamentous form (By similarity).
Leads to small cell wall defects but displays a severe attenuation of virulence in a murine infection model.
Responsible for addition of the terminal mannose residues to the outer chain of core N-linked polysaccharides and to O-linked mannotriose. Implicated in late Golgi modifications (By similarity). Involved in virulence.
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.
Regulated by GCN4 and induced in response to amino acid starvation.
Belongs to the glycosyl hydrolase 38 family.
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.
Second step of mRNA capping. Transfer of the GMP moiety of GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction intermediate.
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 dynactin subunit 4 family.
Activated by phosphorylation of at least Ser-570, Thr-574, Ser-576 and Thr-577 in response to heat shock. Additional unidentified residues are also phosphorylated in response to heat shock.
DNA-binding transcription factor that specifically binds heat shock promoter elements (HSE) and activates transcription. With HSP90, is required for the modulation of the chaperone levels in response to growth temperature, rather than the activation of acute responses to sudden thermal transitions. Activated during infection and contributes to full virulence.
Homotrimer (By similarity). Homotrimerization increases the affinity of HSF1 to DNA (By similarity). Interacts with HSP90 (PubMed:23300438).
Induced during exposure to the weak acid stress of acetic acid, through the regulation by the transcription factor MNL1.
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.
In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.
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.
The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
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.
This protein appears to have acquired a second function as a laminin receptor specifically in the vertebrate lineage. A 67 kDa form similar to the human laminin receptor (67LR) has been isolated from the cell walls of blastoconidia, but it does not bind laminin.
Component of the mitochondrial large ribosomal subunit.
Belongs to the aerobic coproporphyrinogen-III oxidase family.
Belongs to the cysteine synthase/cystathionine beta-synthase family.
Nuclear chaperone required for maturation and nuclear export of pre-60S ribosome subunits.
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 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.
Guanine nucleotide exchange factor for SEC4, catalyzing the dissociation of GDP from SEC4 and also potently promoting binding of GTP. Activation of SEC4 by SEC2 is needed for the directed transport of vesicles to sites of exocytosis (By similarity). Required for filamentous growth.
Phosphorylated at Ser-584 and Ser-598. Phosphorylation at Ser-584 by the CDC28-CCN1 and CDC28-HGC1 complexes is required to support hyphal growth. In stationary phase and growing yeast cells, is constitutively phosphorylated, probably on more than one residue, but the pattern of phosphorylation rapidly changes upon hyphal induction and precedes the appearance of hyphal germ tubes.
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.
Belongs to the eukaryotic ribosomal protein eS8 family.
Cell wall protein which contributes to cell wall synthesis and is important for acquiring normal surface properties. Required for virulence in a mouse infection model.
Induced by caspofungin, tunicamycin, during chlamydospore formation and during cell wall regeneration following protoplasting. Repressed by NRG1 and TUP1. Also regulated by TSA1.
leads to increased sensitivity to Congo red, Calcofluor white, and zymolyase, delayed filamentation, a higher surface hydrophobicity, increased adherence and flocculation; as well as to a diminished ability of protoplasts to recover their cell wall.
Belongs to the eukaryotic ribosomal protein eL29 family.
Belongs to the universal ribosomal protein uS3 family.
Up-regulated upon interaction of cells with host macrophages and upon milbemycins A3 oxim derivative (A3Ox) treatment.
Belongs to the Mediator complex subunit 22 family.
The glycine cleavage system catalyzes the degradation of glycine.
Transcription factor that regulates pseudohyphal differentiation, invasive growth, floculation, adhesion and starch metabolism in response to nutrient availability.
Probably involved in the biogenesis of the COX complex.
Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.
Catalyzes the NADP dependent reduction of L-sorbose to D-glucitol. Can also convert fructose to mannitol, but less efficiently.
Belongs to the ATPase gamma chain family.
Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the pathogenesis of C.albicans infections. Forms amyloid structures, essential for cell-cell association and cell-substrate adhesion to polystyrene.
Forms homodimers through the tandem repeats. Aggregates in amyloid-like structures, with self-propagating secondary-structure changes, amyloid-characteristic dye binding, and induced birefringence.
Highly expressed in biofilms and during candidiasis infection dissemination.
Surface antigen mediating adhesion and aggregation in S.cerevisiae.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.
Belongs to the CTL (choline transporter-like) family.
Probably involved in transport through the plasma membrane.
Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA.
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 monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family.
In the central section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.
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 protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.
Interacts (via the CRIB domain) with CDC42.
Leads to defects in morphology and hyphal formation, impaired chlamydospore formation, reduced colonization of the kidneys in infected mice and suppressed virulence in the mouse model.
Ser/Thr kinase required for wild-type filamentous growth, chlamydospore formation, and virulence in mouse systemic infection.
The CRIB domain is involved in the interaction with CDC42.
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 complex I NDUFS5 subunit family.
Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family.
MAP4K component of the MAPK pathway required for the mating pheromone response, and the regulation of cell polarity and cell cycle. Phosphorylates histone H2B to form H2BS10ph (By similarity). Required for hyphal formation and virulence.
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.
Belongs to the AB hydrolase superfamily.
Demethylates proteins that have been reversibly carboxymethylated. Demethylates the phosphatase PP2A catalytic subunit (By similarity). Involved in the regulation of filamentous growth.
Acetylated by GCN5 to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription (By similarity).
Monoubiquitinated by the UBC2-BRE1 complex to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and H3K79me formation. H2BK123ub1 also modulates the formation of double-strand breaks during meiosis and is a prerequisite for DNA-damage checkpoint activation (By similarity).
Phosphorylated by STE20 to form H2BS10ph during progression through meiotic prophase. May be correlated with chromosome condensation (By similarity).
Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su or H2BK17su, occurs preferentially near the telomeres and represses gene transcription.
To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H2BK6ac = acetylated Lys-7; H2BK6su = sumoylated Lys-7; H2BK7ac = acetylated Lys-8; H2BK7su = sumoylated Lys-8; H2BS10ph = phosphorylated Ser-11; H2BK11ac = acetylated Lys-12; H2BK16ac = acetylated Lys-17; H2BK16su = sumoylated Lys-17; H2BK17su = sumoylated Lys-18; H2BK123ub1 = monoubiquitinated Lys-124.
Recruits the lipid transfer protein VPS13 to endosomal and vacuolar membranes.
The PX domain binds phosphatidylinositol 3-phosphate (PtdIns(3)P) which is necessary for peripheral membrane localization.
In the N-terminal section; belongs to the FGAMS family.
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Contains ambiguous sequence between ORF C6_01010W_A and C6_01020W_A. Used assembly 19 sequence to merge the 2 ORFs.
Required for nuclear membrane fusion during karyogamy.
Involved in amino sugar synthesis (formation of chitin, supplies the amino sugars of asparagine-linked oligosaccharides of glycoproteins).
Expression is up-regulated during oropharyngeal candidiasis (OPC) infection and during stationary phase. Repressed by HOG1, BCR1 and hydrogen peroxide.
Plays a central role as a glucosyl donor in cellular metabolic pathways.
Present with 17200 molecules/cell in log phase SD medium.
Belongs to the membrane-bound acyltransferase family.
Changes ergosterol plasma membrane constitution and distribution and presents an increased resistance to azoles. Impairs the development of hyphae, adhesion, to invasion, and formation of biofilms, all of which are significant virulence factors.
Membrane-bound O-acyltransferase involved in the remodeling of glycosylphosphatidylinositol (GPI) anchors. Acts only on GPI-anchored proteins, but not on free GPI lipids. Also involved in lipid metabolism, having profound effects on sphingolipid-sterol-ordered domains integrity and assembly. Involved in cell integrity and apoptosis (By similarity). Plays a role in virulence and antifungal resistance (PubMed:20843317).
Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family.
Belongs to the dynactin subunits 5/6 family. Dynactin subunit 5 subfamily.
Belongs to the universal ribosomal protein uL14 family.
Belongs to the gamma-glutamylcyclotransferase family.
Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
Up-regulated by TBF1 and upon milbemycins A3 oxim derivative (A3Ox) treatment.
Belongs to the ATPase epsilon chain family.
Belongs to the pseudouridine synthase TruD family.
Interacts with the 40S ribosomal subunit.
Belongs to the eukaryotic ribosomal protein eL38 family.
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 acetyltransferase family. ECO subfamily.
Belongs to the mitochondrion-specific ribosomal protein mS29 family.
Has 2 AAA ATPase type nucleotide-binding domains (NBDs) per monomer. NBD1 is primarily responsible for ATP hydrolysis. NBD2 is crucial for oligomerization (By similarity).
Homohexamer, forming a ring with a central pore.
Required, in concert with mitochondrial Hsp70, for the dissociation, resolubilization and refolding of aggregates of damaged proteins in the mitochondrial matrix after heat stress. May extract proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by the Hsp70 chaperone system. Required for resumption of mitochondrial respiratory function, DNA synthesis and morphology after heat stress (By similarity).
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. NOG subfamily.
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1), a complex that is involved in endosomal cargo sorting.
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.
Belongs to the methyltransferase TRM13 family.
tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His).
Expression is up-regulated by ergosterol depletion, by azoles, and in anaerobic conditions. Transcript is repressed during co-incubated with macrophages, a condition that induces filamentous growth. Promotes positive auto-regulation through binding to its own promoter.
Gain-of-function mutations in UPC2 are more prevalent among clinical isolates than previously thought and make a significant contribution to azole antifungal resistance.
Shows increased susceptibility to the azole drugs ketoconazole, itraconazole, and fluconazole; drugs that act on ergosterol biosynthesis such as terbinafine, fenpropimorph, and lovastatin; as well as malachite green. Leads to lower ergosterol levels. Decreases pyroptosis but has little effect on filamentation in the macrophage.
Transcription factor involved in the regulation of ergosterol biosynthetic genes such as ERG2 and ERG11 through direct binding to sterol response elements (SREs) in the promoters. Binds also to its own promoter on 2 cis-acting elements to promote autoregulation. Regulates sterol uptake across the plasma membrane. Acts as a major regulator of ascorbic acid-induced response. Plays a role in the triggering of pyroptosis, an inflammasome-mediated programmed cell death pathway in macrophages, allowing macrophages escaping.
Component of an histone acetyltransferase complex.
Component of an histone acetyltransferase complex. Interacts with H3K4me3 and to a lesser extent with H3K4me2.
Expression is increased in the presence of fluconazole and decreased in the presence of lovastatin.
Farnesyl pyrophosphate synthase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (PubMed:14653518). ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (PubMed:14653518). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable).
ATP-dependent DNA helicase involved in DNA damage repair by homologous recombination and in genome maintenance. Capable of unwinding D-loops. Plays a role in limiting crossover recombinants during mitotic DNA double-strand break (DSB) repair. Component of a FANCM-MHF complex which promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork.
Belongs to the DEAD box helicase family. DEAH subfamily. FANCM sub-subfamily.
Interacts with the MHF histone-fold complex to form the FANCM-MHF complex.
Belongs to the universal ribosomal protein uS7 family.
Belongs to the GTP cyclohydrolase I family.
Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone KAR2 (By similarity).
Belongs to the RecA family. DMC1 subfamily.
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.
Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 3 respiratory subunits cytochrome b, cytochrome c1 and Rieske protein, 2 core protein subunits, and additional low-molecular weight protein subunits.
Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate.
Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily.
Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose (By similarity).
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.
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).
Required for 60S pre-ribosomal subunits export to the cytoplasm.
Heterodimer with ALG14 to form a functional enzyme.
Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity).
Exhibits reduced capacity to take up amino acids and to switch to the hyphal form, and impairs response to farnesol.
Proteolytically cleaved: activated by the amino acid-induced proteolytic removal of an N-terminal inhibitory domain.
Transcription factor involved in the regulation of gene expression in response to extracellular amino acid levels. Synthesized as latent cytoplasmic precursor, which, upon a signal initiated by the plasma membrane SPS amino acid sensor system (including CSY1 and CSH3), becomes proteolytically activated and relocates to the nucleus, where it induces the expression of SPS-sensor-regulated genes. Required for efficient alkalinization through the release of ammonia from the cells produced during the breakdown of amino acids, and subsequent switch to the hyphal form.
Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Substrate specificity requires an N-terminal glycine in the nascent polypeptide substrates. Ser is present at position 5 in almost all known N-myristoyl proteins and Lys is commonly encountered at postion 6. Basic residues are preferred at positions 7 and 8.
Competitively inhibited by SC-58272, a peptidomimetic derived from the N-terminal sequence of a natural substrate.
Has an ordered Bi-Bi kinetic mechanism, with myristoyl-CoA binding taking place prior to peptide binding and CoA release occurring before acylated peptide release. Cooperative interactions between the acyl-CoA and peptide binding sites of NMT contribute to its extraordinary chain-length specificity.
Belongs to the acid sphingomyelinase family.
Catalytic subunit in the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.
ALS7 gene corresponds to a hypermutable contingency locus meaning that the diversity of ALS7 proteins provide C.albicans with a large and flexible repertoire of similar but non-identical surface proteins which may be important not only for adhesion but also for evasion of host defenses.
Involved in the catabolism of quinolinic acid (QA).
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 (By similarity). Required for virulence and resistance to cycloheximide.
Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
In the de novo pyrimidine biosynthesis pathway, catalyzes the stereospecific oxidation of (S)-dihydroorotate to orotate with reduction of flavin and the transfer of electrons to ubiquinone, which is part of the respiratory chain. Does not use fumarate and NAD as electron acceptors.
Inhibited by the dianisidine derivative redoxal and by brequinar.
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.
Expression is detected as early as 1 hour after infection of reconstituted human esophageal tissue and increases thereafter up to 48 hours postinfection. Expression is also increased when cells are exposed to several types of stress. Expression is decreased by Pseudomonas aeruginosa secretions. Moreover, expression is regulated by NGR1 and BCR1.
Histidine kinase involved in a two-component signaling pathway that regulates cell wall mannan and glucan biosynthesis. Regulates quorum sensing as well as hyphal formation, biofilm formation, chlamidospore formation, and virulence. Plays a prominent role in phagocyte activation. Involved in the covering of the most potent pro-inflammatory cell wall molecules, the beta-glucans, underneath a dense mannan layer, so that the pathogen becomes partly invisible for immune cells such as phagocytes.
Impairs the hyphal formation and attenuates the virulence in a mouse systemic candidiasis model and towards reconstituted human esophageal tissue. Leads to extensive flocculation under conditions that stimulate germ-tube formation. Leads also to increased growth-inhibitory and killing effect by human neutrophils (polymorphonuclear leukocytes) and to hypersensitivity to fluconazole and voriconazole.
The phosphorelay mechanism involves the sequential transfer of a phosphate group from His-2007 (H1) in the histidine kinase domain (transmitter domain) to Asp-2394 (D1) of the response regulatory domain (receiver domain). This transfer probably occurs between two CHK1 molecules, rather than intramolecularly (By similarity).
The protein kinase domain is predicted to be catalytically inactive.
Involved in the repair of double-strand breaks in DNA during vegetative growth via recombination and single-strand annealing. Anneals complementary single-stranded DNA.
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.
May associate with the eukaryotic translation initiation factor 3 (eIF-3) complex.
mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.
Contains a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2).
Required for cytoplasm to vacuole transport (Cvt) vesicles formation and mitophagy. Involved in binding of phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated cleavage (By similarity).
The L/FRRG motif is essential for the cytoplasm to vacuole transport (Cvt) pathway and for the recruitment of ATG8 and ATG16 to the PAS in nutrient-rich medium and in both its recruitment to and dissociation from the PAS under starvation conditions.
Belongs to the small heat shock protein (HSP20) family.
Heat shock protein required for pathogenicity. Mediates thermotolerance and adaptation to oxidative stress and ethanol-induced stress. Required for invasive growth and filament formation under various filament inducing conditions. Plays a role in the capacity of damaging human-derived endothelial and oral epithelial cells during infection. Potentiates resistance to antifungal drugs, as well as resistance to killing by human neutrophils. Plays a major role in trehalose homeostasis in response to elevated temperatures. Regulates CEK1 activation by phosphorylation in response to elevated temperatures.
Only expressed in stationary phase. Expression is increased in the absence of adenylyl cyclase and in biofilms.
Belongs to the eukaryotic ribosomal protein eS24 family.
Belongs to the activator 1 large subunit family.
Belongs to the glutamine synthetase family.
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).
Component of a cytoskeletal structure that is required for membrane curvature.
Does not display the endocytic, hyphal growth, virulence, or cell wall defects exhibited by disruption in related RVS161 or RVS167.
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Affects sucrose utilization and alpha-glucosidase activity. Probable transcriptional activator.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase NEP1 family.
Induced by fluconazole. Expression is regulated by growth phase, temperature, and white-opaque switch.
Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. Involved in triggering host polymorphonuclear neutrophils chemotaxis toward germ tubes. Moreover, acts toward human hemoglobin though limited proteolysis to generate a variety of antimicrobial hemocidins, enabling to compete with the other microorganisms of the same physiological niche using the microbicidal peptides generated from the host protein. Required for cell surface integrity and cell separation during budding.
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.
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).
Component of SAGA complex, SALSA complex, and ADA complex.
Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and ADA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. ADA preferentially acetylates nucleosomal histones H3 (to form H3K14ac and H3K18ac) and H2B. Required for expression of many CAS5-dependent genes. Plays a key role in cell wall integrity, cell adhesion, hyphal development and pathogenesis.
Leads to sensitivity to weak organic acids and decreases cell adherence to silicone substrate.
Transcription factor required for yeast cell adherence to silicone substrate. Plays a role in resistance to weak organic acids such as acetate and sorbate. Binds in vitro to a nitric oxide-responsive element (NORE) but seems not to be involved in response to nitrosative stress.
Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.
Proteolytically removes the C-terminal three residues of farnesylated proteins.
Has a role in transport between endoplasmic reticulum and Golgi.
Probably involved in transcription regulation via its interaction with the INO80 complex, a chromatin remodeling complex.
Belongs to the GMC oxidoreductase family.
Long-chain fatty alcohol oxidase involved in the omega-oxidation pathway of lipid degradation.
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).
Associates with nucleolar pre-ribosomal particles.
Required for efficient biogenesis of the 60S ribosomal subunit.
Catalyzes the exchange of ADP and ATP across the membrane.
Belongs to the UPL family. K-HECT subfamily.
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.
Acts as an inhibitor of cap-dependent translation. Competes with eIF4G1 and EAP1 for binding to eIF4E and interferes with the formation of the eIF4F complex, inhibiting translation and stabilizing mRNA (By similarity).
Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits.
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.
Belongs to the nucleoporin Nup84/Nup107 family.
Induced during cell wall regeneration following protoplasting.
Plays a role in cell wall stability and rigidity. Required for normal adhesion to host cells and for adherence during biofilm formation. Necessary for proper oxidative stress response.
Belongs to the complex I 49 kDa subunit family.
3-keto-steroid reductase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:15552648). ERG27 is a catalytic component of the C-4 demethylation complex that catalyzes the reduction of the keto group on the C-3 (PubMed:15552648). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable).
Belongs to the short-chain dehydrogenases/reductases (SDR) family. ERG27 subfamily.
Expression is increased by itraconazole (which targets the lanosterol demethylase CYP51/ERG11) and by zaragozic acid A (which targets the squalene synthase ERG9).
Facilitates the association of ERG7 with lipid particles preventing its digestion in the endoplasmic reticulum and the lipid particles.
Heterotetramer of ERG25, ERG26, ERG27 and ERG28 (By similarity). ERG28 acts as a scaffold to tether ERG27 and other 4,4-demethylation-related enzymes, forming a demethylation enzyme complex, in the endoplasmic reticulum. Interacts with ERG25 and ERG28. Also interacts with ERG7, but only in lipid particles (By similarity).
Leads to complete loss of both 3-keto reductase and oxidosqualene cyclase (performed by ERG7) activities, compromising all sterol synthesis.
After transfer of sugars to endogenous macromolecular acceptors, the enzyme converts nucleoside diphosphates to nucleoside monophosphates which in turn exit the Golgi lumen in a coupled antiporter reaction, allowing entry of additional nucleotide sugar from the cytosol.
Has a role in cell wall morphogenesis during the transition of budding growth into hyphal growth, a process known as dimorphism.
Cell wall protein involved in cell wall integrity and which plays a role in virulence.
Induced by ketoconazoland fluconazole; and repressed by EFG1, RIM101, SSN6, and alkaline conditions. Enriched in the media of yeast form-containing cultures. Expression is also regulated by HAP43, SEF1, and SFU1.
Required for correct translation termination and probably involved in regulation of hypoxic gene expression.
Expressed during development of germ tubes, pseudohyphae and true hyphae. Expressed in greater amounts in the mature biofilms compared to early biofilms during inflammatory disorder of the palatal mucosa among denture wearers. Induced by fluconazole.
Inhibited by squash aspartic peptidase inhibitor (SQAPI).
Belongs to the DNA polymerase type-Y family.
Belongs to the AP endonuclease 2 family.
Has three domains each corresponding to an enzymatic activity, namely in N- to C-terminal order: ligase, kinase and cyclic phosphodiesterase (CPDase).
One of the two proteins required for the splicing of precursor tRNA molecules containing introns. The ligation activity requires three enzymatic activities: phosphorylation of the 5' terminus of the 3' half-tRNA in the presence of ATP, opening of the 2'3'-cyclic phosphodiester bond of the 5' half-tRNA leaving a 2'-phosphomonoester and ligation of the two tRNA halves in an ATP-dependent reaction.
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). Required for proper protein synthesis within the mitochondrion.
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 ubiquitin conjugation factor E4 family.
Cell surface GPI-anchored protein required for virulence. Mediates hyphal ramification which is important for the interaction with host cells.
Leads to strong defects in host cell damage in a model of human oral epithelial cells, increased survival of infected mice, and aberrant filamentous morphology.
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of an adenine present in helix 65 in 25S rRNA.
Activated by C-terminal proteolytic cleavage. At neutral to alkaline ambient pH, the signaling protease (probably RIM13) cleaves RIM101 to yield the 74 kDa functional form. Also exists as a 65 kDa form at acidic pH, which may govern pH-independent processes.
Binds to DNA. Interacts with RIM20, which binds to the YPX[LI] motifs and is required for proteolytic processing (By similarity).
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 RIM101 itself) and represses transcription of acid-expressed genes. Specifically recognizes and binds the consensus sequence 5'-CCAAGAA-3'. Required for the control of alkaline pH-induced filamentation (dimorphic switch) and virulence.
Negatively regulates early sporulation-specific genes (By similarity). TOR signaling pathway component that contributes to morphogenesis as a regulator of this key morphogenetic pathway. Required for growth and hyphal formation at pH 9, for full virulence in a mouse model of systemic infection and for biofilm formation. Involved in chlamydospore formation, distinctive morphological feature of the fungal pathogen C.albicans that can be induced to form in oxygen-limited environments and has been reported in clinical specimens.
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 proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Accompanies the pre-60S particles to the cytoplasm (By similarity).
A component of the endosomal sorting required for transport complex III (ESCRT-III).
Required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB). Also required for the proteolytic cleavage of the transcription factor RIM101 in response to alkaline ambient pH.
Belongs to the DASH complex DAD1 family.
Involved in the proteasome-dependent degradation of fructose-1,6-bisphosphatase.
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.
GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
Component of the 1.8 MDa SAGA transcription coactivator-HAT complex. SAGA is built of 5 distinct domains with specialized functions. Within the SAGA complex, SUS1, SGF11, SGF73 and UBP8 form an additional subcomplex of SAGA called the DUB module (deubiquitination module). Interacts directly with SGF73, SUS1 and UBP8.
Functions as component of the transcription regulatory histone acetylation (HAT) complex SAGA. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation and deubiquitination. SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). Involved in transcriptional regulation of a subset of SAGA-regulated genes. Within the SAGA complex, participates in a subcomplex, that specifically deubiquitinates histones H2B.
The C-terminal SGF11-type zinc-finger domain together with the C-terminal catalytic domain of UBP8 forms the 'catalytic lobe' of the SAGA deubiquitination module.
The long N-terminal helix forms part of the 'assembly lobe' of the SAGA deubiquitination module.
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.
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in endosomal cargo sorting.
Protein mannosyltransferase (PMT) involved in hyphal morphogenesis and drug sensitivity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1, PMT2 and PMT4 account for most of the protein-O-glycosylation activity, while PMT5 and PMT6 may specifically modulate a much narrower spectrum of target proteins. Required for biofilm formation.
Shows altered cell wall composition with a significant decrease in wall mannoproteins, and reduced virulence in a mouse model of hematogenously disseminated candidiasis (HDC) and using reconstituted human epithelium (RHE).
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IID subfamily.
Divalent metal cations. Prefers magnesium or manganese.
Induced during chlamydospore formation and filamentous growth. Expression is regulated by the NRG1 and TUP1 transcription factors.
Predicted GPI-ancored adhesin-like protein which may be involved in filamentous growth and chlamydospore formation.
The PGA55 mRNA is transported by SHE3 to bud in yeast cells, as well as to the hyphal tips during filamentous growth.
Has a role in nuclear-cytoplasmic transport of proteins and mRNAs.
Belongs to the acetyltransferase family. ARD1 subfamily.
Belongs to the eukaryotic release factor 1 family.
Belongs to the biotin--protein ligase family.
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 mitochondrion-specific ribosomal protein mL49 family.
Leads to sensitivity to caspofungin and affects expression of many genes including caspofungin-responsive genes. Results in hyphal defect during C.elegans infection and exhibits attenuated virulence in flies and mice models for candidiasis.
Transcription factor involved in the cell wall damage response. Acts with ADA2 to promote cell wall integrity. Required for expression of numerous cell wall biosynthesis inhibitor caspofungin-responsive genes. Plays a key role in adherence, hyphal development, and virulence.
Belongs to the dihydrofolate reductase 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 biosynthesis and morphogenesis. Plays a key role in virulence.
Transcript levels are elevated during host infection, and transiently increased after induction of hyphal formation with serum. Expression is controlled by CWT1 and induced by fluconazole.
Expression peaks at G1/S. CCN1 is stabilized during germ tube formation.
G1/S-specific cyclin essential for the control of the cell cycle at the G1/S (start) transition and for maintenance of filamentous growth. Through binding to CDC28 controls the phosphorylation of CDC11 and SEC2 upon induction of filamentous growth.
Interacts with CDC28. The CDC28-CCN1 complex associates with septin CDC11 upon hyphal induction.
Belongs to the class-II aminoacyl-tRNA synthetase family. Alax-L subfamily.
Belongs to the CND1 (condensin subunit 1) family.
Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.
Belongs to the HMG-CoA reductase family.
Expression is not affected by lovastatin or fluconazole.
HMG-CoA reductase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity). HMG1 catalyzes the reduction of hydroxymethylglutaryl-CoA (HMG-CoA) to mevalonate (By similarity). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase ERG10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthase ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase HMG1 finally reduces HMG-CoA to produce mevalonate (Probable).
Contrary to other SAPs, SAP7 is insensitive to pepstatin A inhibition, which is due restriction of the accessibility of pepstatin A to the active site by Met-242 and Thr-467.
Expression is regulated by SSN6 and induced during host infection.
Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense.
Component of the large ribosomal subunit (LSU) (By similarity). Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 32 different proteins and 1 molecule of RNA (18S). The 60S subunit contains 45 different proteins and 3 molecules of RNA (25S, 5.8S and 5S) (Probable). The 5 acidic ribosomal P-proteins form the stalk structure of the 60S subunit. They are organized as a pentameric complex in which uL10/P0 interacts with 2 heterodimers, P1A-P2B and P1B-P2A (By similarity).
Belongs to the acetyltransferase family. MAK3 subfamily.
Belongs to the complex I NDUFA8 subunit family.
Belongs to the DASH complex DAD3 family.
Belongs to the eukaryotic RPC9 RNA polymerase subunit family.
Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ("psi") residues may serve to stabilize the conformation of rRNAs.
Belongs to the alkaline ceramidase family.
Belongs to the PIGG/PIGN/PIGO family. PIGO subfamily.
Ribosome-dependent ATPase that functions in cytoplasmic translation elongation (By similarity). Required for the ATP-dependent release of deacylated tRNA from the ribosomal E-site during protein biosynthesis (By similarity). Stimulates the eEF1A-dependent binding of aminoacyl-tRNA to the ribosomal A-site, which has reduced affinity for tRNA as long as the E-site is occupied (By similarity).
Belongs to the PHP hydrolase family. HisK 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).
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.
Causes an allergic reaction in human. Binds to IgE.
Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily.
Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins (By similarity). Hydrolyzes ATP (By similarity). Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound (By similarity).
Belongs to the DODA-type extradiol aromatic ring-opening dioxygenase 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 (By similarity).
Belongs to the ribonucleoside diphosphate reductase small chain family.
Belongs to the eukaryotic NMN adenylyltransferase family.
C-5 sterol desaturase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathwa (PubMed:9000517, PubMed:10433965, PubMed:20733039). ERG3 catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol (PubMed:10433965). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable).
Defects in C-5 sterol desaturation results in antibiotic and azole resistance of Candida albicans during infection, particularly in AIDS patients.
Expression is repressed during spider biofilm formation (PubMed:22265407).
Belongs to the eIF-2B gamma/epsilon subunits family.
Complex of five different subunits; alpha (GCN3), beta (GCD7), gamma (GCD1), delta (GCD2) and epsilon (GCD6).
Subunit of the guanine nucleotide exchange factor for eIF-2.
Belongs to the protein-tyrosine phosphatase family. Non-receptor class CDC14 subfamily.
Both during budding and hyphal growth, no detectable levels are observed in G1 cells but, as cells passe through S-phase, begins to accumulate with a peak being reached during mitosis.
Leads to defective cell separation and impairs hyphal growth.
Mainly phosphorylated as the cells are passing through mitosis in yeast form cells. Phosphorylation is delayed in hyphal-induced cells, indicating that the timing of cell-cycle progression occurs with different kinetics in hyphae and in yeast cells.
Protein phosphatase which antagonizes mitotic cyclin-dependent kinase CDC28, 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). Plays a role in the expression of hydrolase genes such as CHT3 and ENG1 involved in septum degradation after cytokinesis. Also required for ACE2 localization to the daughter nucleus. Required for invasive and hyphal growth.
Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
Belongs to the eukaryotic ribosomal protein eS6 family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (Probable). RPS6A is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (By similarity).
Induced in biofilms and by alpha factor. Repressed by HAP43.
Belongs to the alpha-ketoglutarate dehydrogenase family.
Belongs to the bile acid:sodium symporter (BASS) (TC 2.A.28) family.
Leads to modest tolerance to azoles and terbinafine, but not to amphotericin B and nystatin (PubMed:22530691). Elevates the intracellular Ca(2+) and leads to the activation of the calcium/calcineurin signaling pathway (PubMed:22530691).
Solute carrier protein that negatively regulates the cytosolic homeostasis in response to high levels of extracellular calcium.
Belongs to the glutamate--cysteine ligase type 3 family.
Belongs to the complex I NDUFS4 subunit family.
Belongs to the thymidylate kinase family.
May be a flavoprotein with enzymatic activity.
Transcription factor involved in yeast cell adherence to silicone substrate, filamentous growth, and biofilm formation.
Expression is more than fourfold higher in white-phase cells than in opaque-phase cells. Up-regulated by farnesol in biofilm.
Represses transcription by RNA polymerase II. Represses genes responsible for initiating filamentous growth such as HWP1, RBT1, RBT2, RBT4, RBT5, RBT7 and WAP1; and this repression is lifted under inducing environmental conditions. Represses also genes which participate in pathogenesis. Crucial component of the response to farnesol. Plays an important role in the regulation of white-opaque switching.
Belongs to the protein kinase superfamily. PAN3 family.
Contains a pseudokinase domain. The protein kinase domain is predicted to be catalytically inactive because some of the residues important for catalytic activity are substituted and it lacks the equivalent of the binding site for a peptide substrate. However, it has retained an ATP-binding site and ATP-binding is required for mRNA degradation, stimulating the activity of the PAN2 nuclease in vitro. The nucleotide-binding site is juxtaposed to the RNase active site of PAN2 in the complex and may actually bind nucleosides of a poly(A) RNA rather than ATP, feeding the poly(A)-tail to the active site of the deadenylase and thus increasing the efficiency with which this distributive enzyme degrades oligo(A) RNAs.
Homodimer. Forms a heterotrimer with a catalytic subunit PAN2 to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts (via PAM-2 motif) with poly(A)-binding protein PAB1 (via PABC domain), conferring substrate specificity of the enzyme complex.
Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and with PAB1.
The N-terminal zinc finger binds to poly(A) RNA.
The pseudokinase domain, the coiled-coil (CC), and C-terminal knob domain (CK) form a structural unit (PKC) that forms an extensive high-affinity interaction surface for PAN2.
Belongs to the complex I 30 kDa subunit family.
Amino-acid permease with rather broad substrate specificity (PubMed:21764911). Transports many amino acids including proline, methionine, leucine, valine, isoleucine, phenylalanine, tryptophan, threonine and tyrosine, but not basic ones (arginine) and citrulline (PubMed:21764911, PubMed:28028545). Functions as a sensor via detection of some amino acids including methionine, leading to a rapid activation of trehalase, a downstream target of PKA (PubMed:21764911).
Expression is under control of the CSY1 amino-acid sensor (PubMed:28028545). Expression is also regulated by PLC1 and GCN4 (PubMed:16207920, PubMed:16215176). Expression is induced during development of rat catheter biofilm (PubMed:19527170).
Belongs to the eukaryotic ribosomal protein eL43 family.
Component of the large ribosomal subunit (PubMed:35613268). Mature ribosomes consist of a small (40S) and a large (60S) subunit (PubMed:35613268). The 40S subunit contains 32 different proteins and 1 molecule of RNA (18S) (PubMed:35613268). The 60S subunit contains 45 different proteins and 3 molecules of RNA (25S, 5.8S and 5S) (PubMed:35613268).
Converts protoheme IX and farnesyl diphosphate to heme O.
Irreversibly catalyzes the reduction of fumarate to succinate.
Belongs to the peptidase M28 family. M28A subfamily.
Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
This enzyme catalyzes only one turnover and therefore is not strictly catalytic. According to one definition, an enzyme is a biocatalyst that acts repeatedly and over many reaction cycles.
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 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).
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.
Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
Catalyzes the synthesis of activated sulfate.
Essential protein which may be involved in threonine biosynthesis.
Leads to hypersensitivity to oxidative stress.
Transcription factor involved in iron metabolism, oxidative stress, surface adhesion, hyphal development and virulence. Functions as a negative regulator of MRS4 expression through the CACCC AFT-type sequence in a gene dose-dependent fashion. Acts as a repressor in flocculation, plastic adhesion, and surface hydrophobicity.
Belongs to the WD repeat BOP1/ERB1 family.
Belongs to the neutral sphingomyelinase family.
Accessory subunit of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis.
Belongs to the DNA polymerase alpha subunit B family.
Belongs to the fluoride channel Fluc/FEX (TC 1.A.43) family.
Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
Highly sensible to fluoride. Growth is inhibited at more than a 300-fold lower fluoride concentration than in the wild-type. Has increased intracellular fluoride concentrations.
Component of the endoplasmic reticulum-associated protein degradation (ERAD) pathway. Recruits the soluble ubiquitin-conjugating enzyme UBC7 to the cytoplasmic face of the endoplasmic reticulum membrane where it functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Targets the E2 conjugating enzyme UBC7 to the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains, and to the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M) (By similarity).
Belongs to the helicase family. RAD25/XPB subfamily.
Binding of human antimicrobial peptide LL-37 decreases the catalytic activity, which leads to the decrease of cell adhesion.
Expression is maximal during the early rapid growth phase and increases during biofilm growth. Induced by caspofungin. Transcripts is also regulated by RCK2, SIT4, and HTG4.
Leads to enhanced susceptibility to the commonly used antifungal, fluconazole, during biofilm growth only.
Major glucan 1,3-beta-glucosidase required for cell wall integrity. Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. Can also function biosynthetically as a transglycosylase. Functions to deliver glucan from the cell to the extracellular matrix. Does not appear to impact cell wall glucan content of biofilm cells, nor is it necessary for filamentation or biofilm formation. Involved in cell-substrate and cell-cell adhesion. Adhesion to host-cell surfaces is the first critical step during mucosal infection. XOG1 is target of human antimicrobial peptide LL-37 for inhibition of cell adhesion.
Monomer. Interacts with the human antimicrobial peptide LL-37.
Associates with the septin complex which consists of CDC3, CDC10, CDC11, CDC12, and SEP7.
Hyperphosphorylated during mitosis at dozens of sites. Among these, 7 have perfect or minimal CDK consensus sites and are CDC28 targets.
Serine/threonine-protein kinase which regulates the localization and the function of the septins during mitosis. Involved in the formation of the septin ring but not the basal septin band. Phosphorylates septins CDC11 and SEP7. Required for the transition from pseudohyphae to hyphae. Acts upstream of IRS4 and INP51 in regulating cell wall integrity responses. Involved in propolis-induced cell death.
Belongs to the protein kinase superfamily. BUD32 family.
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.
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).
Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.
Belongs to the adenosylhomocysteinase family.
Belongs to the glycosyl hydrolase 20 family.
Belongs to the GHMP kinase family. GalK subfamily.
Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.
Belongs to the acetyltransferase family. GNA1 subfamily.
Derepresses filamentous growth and decreases virulence and resistance to cell wall and osmotic stress.
Protein tyrosine phosphatase that acts as a repressor of the yeast-hyphal switch. Plays an important role in virulence. Negatively regulates CST20-HST7-CEK1-CPH1 filamentous growth pathway. Represses hyphal genes such as SAP4, SA5, SAP6, and HYR1, by acting through a CEK1-independent mechanism.
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.
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).
Belongs to the acetyl-CoA hydrolase/transferase family.
Presumably involved in regulating the intracellular acetyl-CoA pool for fatty acid and cholesterol synthesis and fatty acid oxidation.
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).
Expression is induced in absence of HOG1 under non-stressed conditions.
Leads to defects in actin polarization, endocytosis, bud morphogenesis, as well as increased sensitivity to calcofluor white and Congo red. Shows also a strong defect of hyphal morphogenesis and attenuated virulence.
Leads to hypersensitivity to toxic ergosterol analog, amphotericin B, calcofluor white, and to thermosensitivity.
Belongs to the mitochondrion-specific ribosomal protein mS38 family.
Protein mannosyltransferase (PMT) involved in hyphal growth and drug sensitivity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1, PMT2 and PMT4 account for most of the protein-O-glycosylation activity, while PMT5 and PMT6 may specifically modulate a much narrower spectrum of target proteins. Accounts for the O-glycosylation of the cell wall proteins KRE9, PIR2, RHD3, and ALS1, as well as the SEC20 t-SNARE component. O-glycosylation of SEC20 is essential for its stability. Required for filamentation and early phases of biofilm formation.
Shows altered cell wall composition with a significant decrease in wall mannoproteins. Impairs biofilm formation and shows reduced virulence in a mouse model of hematogenously disseminated candidiasis (HDC) and using reconstituted human epithelium (RHE) or engineered human oral mucosa (EHOM).
Transcript levels are increased at least twofold by tunicamycin and Congo red. Both MSB2 and CEK1 are required to down-regulate PMT1 transcript levels in cells with intact glycostructures.
Belongs to the DDOST 48 kDa subunit family.
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER).
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 serine/threonine dehydratase family.
Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the biofilm formation and pathogenesis of C.albicans infections. Necessary for C.albicans to bind to N-cadherin on endothelial cells and E-cadherin on oral epithelial cells and subsequent endocytosis by these cells. During disseminated infection, mediates initial trafficking to the brain and renal cortex and contributes to fungal persistence in the kidneys.
Expression is under the positive control of the biofilm regulator BCR1, RLM1, TOR1 and TPK2; and under the negative control of SFL1. Induced during germ tube formation. Highly expressed in oropharyngeal candidiasis (OPC), a biofilm-like infection of the oral mucosa. Induced in the initial stages of biofilm formation. Down-regulated by human serum, as well as by bacterial quorum sensing quencher thiazolidinedione-8, pterostilbene, lipopeptides biosurfactant produced by B.amyloliquefaciens, and Riccardin D, a macrocyclic bisbibenzyl isolated from Chinese liverwort D.hirsute, which has an inhibitory effect on biofilms and virulence.
Reduces adhesion and damage to both human umbilical vein endothelial cells (HUVEC) and oral epithelial cells.
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.
Belongs to the thiolase-like superfamily. HMG-CoA synthase family.
Expressed during exponential and stationary growth phase (PubMed:17588813). Expression is repressed by amphotericin B and caspofungin (PubMed:15917516). Expression is also repressed during biofilm formation (PubMed:22265407).
Hydroxymethylglutaryl-CoA synthase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity). ERG13 condenses acetyl-CoA with acetoacetyl-CoA to form hydroxymethylglutaryl-CoA (HMG-CoA) (By similarity). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase ERG10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthase ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase HMG1 finally reduces HMG-CoA to produce mevalonate (Probable).
Belongs to the endopolyphosphatase PPN1 family.
Catalyzes the hydrolysis of inorganic polyphosphate (polyP) chains of many hundreds of phosphate residues into shorter lengths.
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 metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family. Adenine deaminase type 2 subfamily.
Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism.
Belongs to the cyclic nucleotide phosphodiesterase class-II 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.
Expression is repressed by HAP4 and BCR1.
Leads to supersensitivity to hygromycin B. Impairs filamentation, significantly reduces adherence to endothelial cells, and shows reduced virulence in a mouse model of hematogenously disseminated candidiasis (HDC) and using reconstituted human epithelium (RHE).
Protein mannosyltransferase (PMT) involved in hyphal morphogenesis and drug sensitivity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1, PMT2 and PMT4 account for most of the protein-O-glycosylation activity, while PMT5 and PMT6 may specifically modulate a much narrower spectrum of target proteins. Required for biofilm formation and virulence.
Belongs to the glucose-6-phosphate 1-epimerase family.
Catalyzes the interconversion between the alpha and beta anomers from at least three hexose 6-phosphate sugars (Glc6P, Gal6P, and Man6P).
Required for the assembly of mitochondrial cytochrome c oxidase.
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.
Activated by threonine and tyrosine phosphorylation.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily.
Belongs to the MICOS complex subunit Mic12 family.
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.
Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor.
Belongs to the aldo/keto reductase family.
Belongs to the bacterial ribosomal protein bS21 family.
Impairs expression of hypha-specific transcripts and leads to a medium-specific impairment in hyphal development.
Transcription factor that positively controls filamentous growth, virulence, and invasiveness. Binds directly to the two SRE-1-like elements upstream of TEC1 and thus regulates positively expression of this important hyphal growth regulator. Functions independently of known signaling cascades involving EFG1. Regulates also gene expression during intestinal colonization but is not involved in host cell adhesion.
Up-regulated during the yeast-to-hypha transition and in virulent strains during intestinal colonization. Also induced upon exposure to fluconazole. Expression is down-regulated by tetrandrine and by Escherichia coli biofilm secretory products.
Belongs to the non-repetitive/WGA-negative nucleoporin family.
C-8 sterol isomerase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (By similarity). ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable).
Expression is repressed during biofilm formation.
Increases the susceptibility to 4-nitroquinoline oxide, terbinafine, o-phenanthroline, itraconazole, and ketoconazole (PubMed:15105135). Affects the proper surface localization of the drug transporter CDR1 (PubMed:15105135).
Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family.
Expression is positively regulated by ACE2. Transcription is greater during growth of the yeast form as compared to the mycelial form, and down-regulated by micafungin treatment.
Leads to strong decrease of secreted chitinase activity, as well as to the clumping or clusterings of cells from early exponential phase.
Belongs to the Mediator complex subunit 16 family.
Belongs to the MsrB Met sulfoxide reductase family.
Expressed during development of germ tubes, pseudohyphae, true hyphae and opaque cells. Expressed in greater amounts in the mature biofilms compared to early biofilms during inflammatory disorder of the palatal mucosa among denture wearers. Regulated by growth phase and alpha-pheromones.
Inhibited by pepstatin A analogs and squash aspartic peptidase inhibitor (SQAPI).
Belongs to the low molecular weight phosphotyrosine protein phosphatase 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.
Belongs to the CDP-alcohol phosphatidyltransferase class-II family.
Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class II DHOase subfamily.
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily.
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 TAF9 family. CENP-S/MHF1 subfamily.
The MHF histone-fold complex is a heterotetramer of 2 MHF1-MHF2 heterodimers. Together with MPH1/FANCM, forms the FANCM-MHF complex. Component of the inner kinetochore constitutive centromere-associated network (CCAN).
dsDNA-binding component of a FANCM-MHF complex involved in DNA damage repair and genome maintenance (By similarity). FANCM-MHF promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork (By similarity). Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly (By similarity).
2/mitotic-specific cyclin essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis. Degradation is necessary for the cell to exit from mitosis. Plays a role in morphogenesis by negatively regulating polarized growth. Through binding to CDC28 regulates cytokinesis, partly by phosphorylation of the actomyosin ring component IQG1. Also involved in the phosphorylation of CDC6 and CDC54.
Expressed from S phase through G2 and M phases and are degraded at the end of mitosis. Expression is down-regulated by the anti-fungal agent plagiochin E (PLE).
Impairs macrophage killing during infection.
Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA polymerase subunit family.
GPI-anchored cell wall protein that may be involved in cell wall organization, hyphal growth, as well as in virulence.
Induced during yeast to hyphae transition, during biofilm formation, during oralpharyngeal candidasis, and in response to serum. Regulated BY FLO8, NRG1, RFG1, RGT1, TUP1, TSA1, and UME6.
Dually phosphorylated on Thr-230 and Tyr-232, which activates the enzyme.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.
Required for high-fidelity chromosome segregation during the later part of each cell cycle. Acts in opposition to the phosphatase PP1. Has a role in attaching the kinetochores to the microtubules and ensuring that sister kinetochores connect to opposite poles. The promotion of bi-orientation is achieved by selectively detaching kinetochore-microtubule attachments that are not under tension. Phosphorylates histone H3 to form H3S10ph during mitosis and meiosis (By similarity).
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 cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A 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.
Belongs to the glutamate synthase family.
Belongs to the major facilitator superfamily.
Expression is induced by nitric oxide (NO) and HOG1; and repressed by osmotic stress, oxidative stress, and heavy metal stress. Expression is also regulated by TSA1.
Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (Probable). RPS9B is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (By similarity).