Expression is low in meronts, but becomes induced in sporonts and spores.
May be involved in the degradation of proteins for nutrient acquisition or possess a regulatory function by proteolytic activation of proproteins.
Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA 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.
Belongs to the activator 1 small subunits family.
Component of ATP-dependent clamp loader (RFC and RFC-like) complexes for DNA clamps. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA. Component of the replication factor C (RFC or activator 1) complex which acts during elongation of primed DNA templates by DNA polymerase delta and epsilon. RFC has an essential but redundant activity in sister chromatid cohesion establishment (By similarity).
Component of the replication factor C (RFC) complex.
Present with 2760 molecules/cell in log phase SD medium.
Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family.
Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB9 is part of the upper jaw surrounding the central large cleft and thought to grab the incoming DNA template. Involved in the regulation of transcription elongation (By similarity).
Acts as a regulatory subunit of the 26S proteasome which 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 (By similarity).
Belongs to the proteasome subunit S2 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 (By similarity).
Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination (By similarity).
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 assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. It must be involved intimately in the translocation of a wide variety of protein substrates (By similarity).
Belongs to the diphosphomevalonate decarboxylase family.
Belongs to the SEC23/SEC24 family. SEC23 subfamily.
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity).
Belongs to the ubiquitin-conjugating enzyme family.
ATP transporter involved in the uptake of ATP from the host cell cytoplasm. Provides the microsporidian cell with host ATP in exchange for ADP. This is an obligate exchange system. This energy acquiring activity is an important component of microsporidian parasitism.
Belongs to the ADP/ATP translocase tlc family.
Belongs to the class VI-like SAM-binding methyltransferase superfamily. Isoprenylcysteine carboxyl methyltransferase family.
Lacks conserved residue(s) required for the propagation of feature annotation.
Essential role in pre-mRNA splicing. Also essential for entry into mitosis (G2/M progression) as well as for chromosome segregation during mitosis.
Involved in amino sugar synthesis (formation of chitin, supplies the amino sugars of asparagine-linked oligosaccharides of glycoproteins).
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
Component of the SMC5-SMC6 complex, that promotes sister chromatid alignment after DNA damage and facilitates double-stranded DNA breaks (DSBs) repair via homologous recombination between sister chromatids.
Belongs to the 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).
Belongs to the universal ribosomal protein uL29 family.
Component of the large ribosomal subunit.
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Belongs to the eukaryotic ribosomal protein eS25 family.
Belongs to the acetyltransferase family. GCN5 subfamily.
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).
Belongs to the reduced folate carrier (RFC) transporter (TC 2.A.48) family.
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.
Non-catalytic component of the proteasome which 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 (By similarity).
Belongs to the DHHC palmitoyltransferase family.
The DHHC domain is required for palmitoyltransferase activity.
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.
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).
Probably involved in mitosomal protein import.
Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family.
Septins are GTPases involved in cytokinesis. The septins localize to the site of cleavage and act as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Septins are also involved in cell morphogenesis, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation (By similarity).
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 (By similarity).
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 class-II aminoacyl-tRNA synthetase family.
TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity.
Belongs to the DNA repair enzymes AP/ExoA family.
Belongs to the STE12 transcription factor family.
Belongs to the pseudouridine synthase TruD family.
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 DEAD box helicase family.
Belongs to the universal ribosomal protein uL3 family.
Nonessential protein required for the fusion of transport vesicles derived from the endocytic pathway with the Golgi complex.
Belongs to the snRNP core protein family.
Belongs to the DEAD box helicase family. DEAH subfamily. DDX11/CHL1 sub-subfamily.
Belongs to the DNA mismatch repair MutL/HexB family.
Belongs to the universal ribosomal protein uS19 family.
Belongs to the adaptor complexes large subunit family.
Component of the T-complex protein 1 (TCP1) complex.
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis.
Belongs to the small GTPase superfamily. Arf family.
Belongs to the dynein heavy chain 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.
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
Belongs to the eukaryotic ribosomal protein eS12 family.
Belongs to the Clp1 family. NOL9/GRC3 subfamily.
Belongs to the class-I aminoacyl-tRNA synthetase family.
Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA polymerase subunit family.
Component of the RNA polymerase I (Pol I), RNA polymerase II (Pol II) and RNA polymerase III (Pol III) complexes consisting of 14, 12 and 17 subunits, respectively.
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 a small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, RBP10 is part of the core element with the central large cleft (By similarity).
Possesses 5'->3' exoribonuclease activity. Required for the processing of nuclear mRNA and rRNA precursors. May promote termination of transcription by RNA polymerase II.
Belongs to the eukaryotic ribosomal protein eL34 family.
Belongs to the TPT transporter family. SLC35D subfamily.
Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen.
Belongs to the WD repeat CDC20/Fizzy family.
Belongs to the DNA polymerase type-B family.
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.
Component of the autophagy-specific VPS34 PI3-kinase complex I composed; and of the VPS34 PI3-kinase complex II.
Phosphatidylinositol 3-kinase required for cytoplasm to vacuole transport (Cvt) and autophagy as a part of the autophagy-specific VPS34 PI3-kinase complex I. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II (By similarity).
Phospholipid scramblase involved in autophagy. 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.
Component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs).
Non-catalytic component of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP), which catalyzes pseudouridylation of rRNA and is required for ribosome biogenesis. 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. The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs. The H/ACA snoRNP complex mediates pseudouridylation at position 93 in U2 snRNA.
Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity.
Component of the NDC80 complex, which consists of at least NDC80 and NUF2.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
Belongs to the protein kinase superfamily. BUD32 family.
Component of the EKC/KEOPS complex composed of at least BUD32, CGI121, GON7, KAE1 and PCC1; the whole complex dimerizes.
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
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).
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.
Belongs to the eukaryotic ribosomal protein eS26 family.
Component of the small ribosomal subunit.
Belongs to the histidine acid phosphatase family.
Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family.
Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins (By similarity).
May be inactive since it lacks one cysteine involved the redox-active disulfide bond.
Belongs to the acetyltransferase family. GNA1 subfamily.
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 an H2A variant 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.
The coiled-coil domain is required for assembly into the NuA4 complex.
Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family.
Belongs to the universal ribosomal protein uL1 family.
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.
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.
Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit.
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 6-phosphogluconate dehydrogenase family.
Belongs to the TRAPP small subunits family.
Part of the multisubunit transport protein particle (TRAPP) complex.
Belongs to the deoxyhypusine hydroxylase family.
Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.
Belongs to the CDP-alcohol phosphatidyltransferase class-II family.
Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Belongs to the eukaryotic ribosomal protein eL20 family.
Belongs to the heat shock protein 70 family.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily.
Negative regulator of the cell cycle acting downstream of the cAMP-dependent protein kinase. Part of a glucose-sensing system involved in growth control in response to glucose availability (By similarity).
Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs.
Belongs to the ATPase alpha/beta chains family.
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). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity).
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and VOA1).
Belongs to the amino acid/polyamine transporter 2 family.
Belongs to the splicing factor SR family.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
Component of the eukaryotic elongation factor 1 complex (eEF1).
GTP-binding component of the eukaryotic elongation factor 1 complex (eEF1). In its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be recycled by its guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) before binding another molecule of aminoacyl-tRNA. Required for nuclear export of aminoacyl-tRNAs. May also be involved in translational quality control by targeting cotranslationally damaged proteins to the proteasome (By similarity).
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.
Belongs to the activator 1 large subunit family.
Belongs to the DEAD box helicase family. DDX54/DBP10 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 eukaryotic ribosomal protein eL39 family.
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.
Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). In microsporidia, the second signature motif differs slightly and is Asn-Pro-Gly (NPG).
Belongs to the MIP/aquaporin (TC 1.A.8) family.
Water channel required to facilitate the transport of water across membranes. Involved in osmotolerance.
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.
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.
Belongs to the diphthine synthase family.
S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis.
Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily.
Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily.
Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine.
Tetramer composed of two alpha chains, one beta chain and one beta' chain.
Belongs to the WD repeat PRL1/PRL2 family.
Belongs to the thymidylate kinase family.
Belongs to the RNA polymerase beta' chain family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.
Catalytic subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. Involved in RNA polymerase II transcriptional elongation and pre-mRNA 3'-end processing (By similarity).
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.
May play a role in the initiation and completion of mitosis.
Belongs to the eukaryotic ribosomal protein eL24 family.
As a subunit of eukaryotic initiation factor 2 (eIF-2), involved in the early steps of protein synthesis. In the presence of GTP, eIF-2 forms a ternary complex with initiator tRNA Met-tRNAi and then recruits the 40S ribosomal complex and initiation factors eIF-1, eIF-1A and eIF-3 to form the 43S pre-initiation complex (43S PIC), a step that determines the rate of protein translation. The 43S PIC binds to mRNA and scans downstream to the initiation codon, where it forms a 48S initiation complex by codon-anticodon base pairing. This leads to the displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF-5-mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release of Pi, which makes GTP hydrolysis irreversible, causes the release of the eIF-2-GDP binary complex from the 40S subunit, an event that is essential for the subsequent joining of the 60S ribosomal subunit to form an elongation-competent 80S ribosome. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP exchange factor (GEF) eIF-2B.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EIF2G subfamily.
Eukaryotic translation initiation factor 2 (eIF-2) is a heterotrimeric G-protein composed of an alpha, a beta and a gamma subunit. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-tRNAi form a multifactor complex (MFC) that may bind to the 40S ribosome.
Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
Tetramer of two alpha and two beta subunits.
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 in mitosomes.
Belongs to the type II topoisomerase family.
Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.
Belongs to the universal ribosomal protein uS4 family.
May function both as a monomer and a homodimer.
Belongs to the STXBP/unc-18/SEC1 family.
Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
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.
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 ATP-dependent AMP-binding enzyme family.
TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation.
TFIIA is a heterodimer of the large subunit and the small subunit gamma.
Belongs to the eukaryotic ribosomal protein eL6 family.
Monoubiquitinated to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and H3K79me formation (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: H2BK123ub1 = monoubiquitinated Lys-122.
Belongs to the cytidylyltransferase family.
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 TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.
Belongs to the SMC family. RAD50 subfamily.
Involved in DNA double-strand break repair (DSBR). The RAD50/MRE11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific exonuclease activity. RAD50 provides ATP-dependent control of MRE11 by unwinding and/or repositioning DNA ends into the MRE11 active site (By similarity).
The zinc-hook, which separates the large intramolecular coiled coil regions, contains 2 Cys residues that coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another RAD50 molecule, thereby forming a V-shaped homodimer.
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.
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
Belongs to the NFYB/HAP3 subunit family.
Belongs to the glycosyltransferase 39 family.
Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily.
Involved in DNA repair. May regulate the activity of protein(s) involved in double strand break repair caused by gamma rays (By similarity).
Belongs to the pseudouridine synthase TruB family.
Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.
Sterol O-acyltransferase that catalyzes the formation of stery esters.
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). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity).
Belongs to the snRNP Sm proteins family.
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 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).
Belongs to the universal ribosomal protein uL30 family.
Belongs to the major facilitator superfamily. Proton-dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
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 V-ATPase V0D/AC39 subunit family.
Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments. This subunit is a non-integral membrane component of the membrane pore domain and is required for proper assembly of the V0 sector. Might be involved in the regulated assembly of V1 subunits onto the membrane sector or alternatively may prevent the passage of protons through V0 pores.
V-ATPase is a heteromultimeric enzyme made up of two complexes: the ATP-hydrolytic V1 complex and the proton translocation V0 complex.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily.
Belongs to the eukaryotic ribosomal protein eS8 family. Ribosome biogenesis protein NSA2 subfamily.
Component of the pre-66S ribosomal particle.
Involved in the biogenesis of the 60S ribosomal subunit. May play a part in the quality control of pre-60S particles.
Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. NIM1 subfamily.
Serine/threonine protein kinase involved in regulation of exocytosis.
Belongs to the eukaryotic ribosomal protein eL8 family.
Common component of the spliceosome and rRNA processing machinery.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.
Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) (By similarity).
Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Homodimer. The tRNA molecule probably binds across the dimer (By similarity).
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase NEP1 family.
As part of the replication protein A (RPA/RP-A), a single-stranded DNA-binding heterotrimeric complex, may play an essential role in DNA replication, recombination and repair. Binds and stabilizes single-stranded DNA intermediates, preventing complementary DNA reannealing and recruiting different proteins involved in DNA metabolism.
Belongs to the replication factor A protein 1 family.
Component of the heterotrimeric canonical replication protein A complex (RPA).
Belongs to the universal ribosomal protein uS11 family.
Belongs to the cyclophilin-type PPIase family.
PPIases accelerate the folding of proteins. They catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Belongs to the DHHC palmitoyltransferase family. AKR/ZDHHC17 subfamily.
Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Belongs to the ubiquitin-activating E1 family.
Associates with TFIID-IIA (DA complex) to form TFIID-IIA-IIB (DAB-complex) which is then recognized by polymerase II.
General factor that plays a major role in the activation of eukaryotic genes transcribed by RNA polymerase II.
Belongs to the universal ribosomal protein uS13 family.
Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA.
Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family.
Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle.
Belongs to the class I fructose-bisphosphate aldolase family.
Belongs to the eukaryotic ribosomal protein eL21 family.
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Although it contains a polysaccharide deacetylase domain, the protein does not display any chitin deacetylase activity.
Binds 1 divalent metal cation per subunit.
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.
Belongs to the WD repeat DCAF13/WDSOF1 family.
Belongs to the universal ribosomal protein uL2 family.
Belongs to the eukaryotic ribosomal protein eL27 family.
Belongs to the metallo-dependent hydrolases superfamily. TatD-type hydrolase family.
Binds 2 divalent metal cations per subunit.
Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly.
Interacts with histone H3 and histone H4.
Belongs to the universal ribosomal protein uL23 family.
Belongs to the metallo-beta-lactamase superfamily. RNA-metabolizing metallo-beta-lactamase-like family. INTS11 subfamily.
Belongs to the peptidase M24 family. SPT16 subfamily.
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.
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, suggesting that it is involved in the minus-end nucleation of microtubule assembly (By similarity).
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.
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).
Belongs to the universal ribosomal protein uL13 family.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).
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.
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.
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.
Belongs to the helicase family. SKI2 subfamily.
Required for proper 27S pre-rRNA processing and 60S ribosome subunit assembly.
Required for proper homologous chromosome pairing and efficient cross-over and intragenic recombination during meiosis.
Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping.
Belongs to the small GTPase superfamily. Ran family.
Found in a nuclear export complex with RanGTP, exportin and pre-miRNA (By similarity).
GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export (By similarity).
Cis-prenyl transferase that adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP).
Belongs to the methyltransferase superfamily. Fibrillarin family.
Component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles.
S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ105me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (By similarity).
Belongs to the eukaryotic ribosomal protein eL31 family.
Component of the ribosome quality control complex (RQC), composed of the E3 ubiquitin ligase LTN1, RQC1 and RQC2, as well as CDC48 and its ubiquitin-binding cofactors. RQC forms a stable complex with 60S ribosomal subunits.
Involved in spindle disassembly, degradation of ubiquitinated proteins and protein export from the endoplasmic reticulum to the cytoplasm. Acts as a chaperone that collects ubiquitinated substrates. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway. Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. CDC48 may provide the mechanical force that dislodges the polyubiquitinated nascent peptides from the exit channel.
Glutarylation at Lys-94 (H4K91glu) destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes.
Component of the TFIID and SAGA complexes. TFIID is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs) (By similarity).
TAFs are components of the transcription factor IID (TFIID) complex that are essential for mediating regulation of RNA polymerase transcription. Regulates the genes involved in ubiquitin-dependent proteolysis during the progression of M-phase of mitosis (By similarity).
Belongs to the histone deacetylase family. HD Type 1 subfamily.
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 (By similarity).
Component of the SWR1 chromatin remodeling complex, the INO80 chromatin remodeling complex, and of the R2TP complex.
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).
Belongs to the universal ribosomal protein uL14 family.
Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits.
Belongs to the protein kinase superfamily. RIO-type Ser/Thr kinase family.
Involved in the second step of GPI biosynthesis. De-N-acetylation of N-acetylglucosaminyl-phosphatidylinositol.
Belongs to the adaptor complexes small subunit 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. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity). 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 (By similarity).
Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand.
Belongs to the universal ribosomal protein uL15 family.
Belongs to the DNA glycosylase MPG family.
Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM5/TYW2 family.
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.
ATP-dependent 3'-5' DNA helicase, 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. The ATPase activity of XPB/SSL2, but not its helicase activity, is required for DNA opening. 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. The ATP-dependent helicase activity of XPB/SSL2 is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
Belongs to the helicase family. RAD25/XPB subfamily.
Belongs to the universal ribosomal protein uS2 family.
Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (25S, 5.8S and 5S). Interacts with RPS21.
Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits.
Belongs to the major facilitator superfamily. MFSD6 family.
Intracellular phospholipase B that catalyzes the double deacylation of phosphatidylcholine (PC) to glycerophosphocholine (GroPCho). Plays an important role in membrane lipid homeostasis. Responsible for the rapid PC turnover in response to inositol, elevated temperatures, or when choline is present in the growth medium (By similarity).
Belongs to the universal ribosomal protein uS7 family.
Belongs to the proteasome subunit S9 family.
Belongs to the ERCC1/RAD10/SWI10 family.
Belongs to the universal ribosomal protein uL5 family.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Belongs to the eukaryotic ribosomal protein eS6 family.
Protein kinase component of transcription factor IIH (TFIIH) which phosphorylates the C-terminal domain of RNA polymerase II during transition from transcription to elongation after preinitiation complex (PIC) formation, thereby positively regulating transcription. Essential for both basal and activated transcription, and is involved in nucleotide excision repair (NER) of damaged DNA (By similarity).
Belongs to the WD repeat G protein beta family.
Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. LSM2 binds specifically to the 3'-terminal U-tract of U6 snRNA. Required for processing of pre-tRNAs, pre-rRNAs and U3 snoRNA (By similarity).
LSm subunits form a heteromer with a doughnut shape.
Belongs to the eukaryotic ribosomal protein eS17 family.
Belongs to the helicase family. RecQ subfamily.
Belongs to the universal ribosomal protein uS14 family.
Belongs to the SMC family. SMC1 subfamily.
Catalyzes the ATP-dependent ligation of glycine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (Gly-AMP). Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. Thereby, may play a special role in Ap4A homeostasis.
Transcription elongation factor implicated in the maintenance of proper chromatin structure in actively transcribed regions.
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.
Belongs to the eukaryotic ribosomal protein eL33 family.
Belongs to the adrenodoxin/putidaredoxin family.
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
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 1 Fe-S cluster but is otherwise mostly in an intrinsically disordered conformation.
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 dihydrofolate reductase family.
Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit family.
Belongs to the ubiquitin conjugation factor E4 family.
Belongs to the helicase family. RAD3/XPD subfamily.
Catalytic component of the tRNA-splicing ligase complex.
Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs.
Ligation probably proceeds through 3 nucleotidyl transfer steps, with 2',3'-cyclic phosphate termini being hydrolyzed to 3'-P termini in a step that precedes 3'-P activation with GMP. In the first nucleotidyl transfer step, RTCB reacts with GTP to form a covalent RTCB-histidine-GMP intermediate with release of PPi; in the second step, the GMP moiety is transferred to the RNA 3'-P; in the third step, the 5'-OH from the opposite RNA strand attacks the activated 3'-P to form a 3',5'-phosphodiester bond and release GMP.
Belongs to the universal ribosomal protein uL6 family.
Belongs to the universal ribosomal protein uS17 family.
May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
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.
Belongs to the snRNP Sm proteins family. SmF/LSm6 subfamily.
Belongs to the MMR1/HSR1 GTP-binding protein family.
Required for normal processing of ribosomal pre-rRNA. Required for cell proliferation. Binds GTP (By similarity).
GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
Belongs to the glycosyltransferase 15 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.
Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.
Belongs to the thymidylate synthase family.
Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids.
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.
Belongs to the universal ribosomal protein uL10 family.
Belongs to the IPP isomerase type 1 family.
Belongs to the phosphohexose mutase family.
Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, which is a biosynthetic precursor of chitin and also supplies the amino sugars for N-linked oligosaccharides of glycoproteins.
Belongs to the eukaryotic ribosomal protein eS30 family.
Belongs to the C/M/P thioester hydrolase family.
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 KTI11/DPH3 and a NADH-dependent reductase, predominantly CBR1. Acts as an electron donor to reduce the Fe-S cluster in DPH1-DPH2 keeping the [4Fe-4S] clusters in the active and reduced state. Restores iron to DPH1-DPH2 iron-sulfur clusters which have degraded from [4Fe-4S] to [3Fe-4S] by donating an iron atom to reform [4Fe-4S] clusters, in a manner dependent on the presence of elongation factor 2 and SAM. Associates with the elongator complex and is required for tRNA Wobble base modifications mediated by the elongator complex. The elongator complex is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine).
The DPH-type metal-binding (MB) domain can also bind zinc. However, iron is the physiological binding partner as zinc binding impairs the protein electron donor function.
Belongs to the PA-phosphatase related phosphoesterase family.
Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins.
Belongs to the SMC family. SMC5 subfamily.
Belongs to the acetyltransferase family. ARD1 subfamily.
Belongs to the methyltransferase superfamily.
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.
Belongs to the eukaryotic ribosomal protein eL37 family.
Belongs to the triosephosphate isomerase family.
Belongs to the eukaryotic ribosomal protein eS27 family.
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
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 universal ribosomal protein uS12 family.
Belongs to the V-ATPase F subunit family.
Belongs to the archaeal rpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family.
Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (RPB1). This promotes the activity of RNA polymerase II.
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).
Belongs to the glycosyltransferase 2 family.
Component of the dolichol-phosphate mannose (DPM) synthase complex.
Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins.
Belongs to the phosphoglycerate kinase family.
Belongs to the ABC transporter superfamily.
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.
Belongs to the protein prenyltransferase subunit beta family.
Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX.
Belongs to the CND1 (condensin subunit 1) family.
Cleaves the gamma-glutamyl peptide bond of glutathione and glutathione conjugates.
Belongs to the eukaryotic ribosomal protein eS8 family.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC7 subfamily.
Serine/threonine-protein kinase. Needed for the initiation of DNA synthesis during mitosis as well as for synaptonemal complex formation and commitment to recombination during meiosis (By similarity).
Belongs to the ubiquitin-activating E1 family. UBA3 subfamily.
Catalytic subunit of the dimeric E1 enzyme, which activates NEDD8.
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.
Belongs to the adaptor complexes medium subunit family. Delta-COP subfamily.
Belongs to the universal ribosomal protein uS15 family.
Belongs to the universal ribosomal protein uL4 family.
Belongs to the DNA polymerase type-B-like family.
Expressed during merogony and a large part of sporogony.
Heparin-binding motifs (HBMs) are characterized by an XBBXBX or XBBBXXBX sequence, where X is any neutral amino acid and B is a positively charged basic amino acid, and are defined as the consensus sequence necessary for protein-heparin interactions. HBM1 motif is necessary for spore adherence to host cells.
Spore wall protein involved in the adhesion to host cells surface glycoaminoglycans (GAGs). Microsporidian spore adherence is an integral part of activation and host cell invasion which requires the extrusion at the spore apex of a very long and coiled structure, the polar tube, through which the sporoplasm is pushed to enter into the potential host cell.
Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment.
Belongs to the proteasome subunit S5A family.
Belongs to the TALE/KNOX homeobox family.
Involved in nucleolar processing of pre-18S ribosomal RNA.
First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.
Heterodimer. The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an mRNA 5'-triphosphate monophosphatase.
Belongs to the chitin synthase family. Class IV subfamily.
Expression is low in meronts, but becomes induced when meronts start to differentiate into sporonts.
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Belongs to the TRAPP small subunits family. BET3 subfamily.
May play a role in vesicular transport from endoplasmic reticulum to Golgi.
Part of the multisubunit TRAPP (transport protein particle) complex.
Found in spores. Expression is high during polar tube formation.
Involved in the sporoblast-to-spore polar tube biogenesis. Plays a role in the control of the polar tube extrusion as part of a specific response to ionic stimuli.
Belongs to the eukaryotic release factor 1 family. Pelota subfamily.
Belongs to the thiolase-like superfamily. Thiolase family.
Belongs to the TFIIF beta subunit 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.
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.
Component of the DNA-binding general transcription factor complex TFIID. Component of histone acetyl transferase (HAT) complexes such as SAGA (By similarity).
Functions as a component of the DNA-binding general transcription factor complex TFIID. May also function as a component of transcription regulatory histone acetyl transferase (HAT) complexes such as SAGA. 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, facilitation of DNA opening and initiation of transcription (By similarity).
Belongs to the class I-like SAM-binding methyltransferase superfamily. BUD23/WBSCR22 family.
Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle.
Important for the export of protein containing nuclear export signal (NES) out of the nucleus.
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 universal ribosomal protein uL16 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) (By similarity).
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB2 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template (By similarity).
The binding of ribonucleoside triphosphate to the RNA polymerase II transcribing complex probably involves a two-step mechanism. The initial binding seems to occur at the entry (E) site and involves a magnesium ion coordinated by three conserved aspartate residues of the two largest RNA Pol II subunits (By similarity).
Belongs to the reverse transcriptase family. Telomerase subfamily.
Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Belongs to the tRNA-intron endonuclease family.
Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
Regulatory subunit of the histone acetylase B (HAT-B) complex. The complex acetylates histone H4 which is required for telomeric silencing (By similarity).
Belongs to the FPP/GGPP synthase family.
Cyclin-dependent kinase that acts as a master regulator of the mitotic and meiotic cell cycles.
Belongs to the sirtuin family. Class I subfamily.
Involved in the lipid remodeling steps of GPI-anchor maturation.
Belongs to the eukaryotic ribosomal protein eS28 family.
Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs.
Acetylation of histone H3 leads to transcriptional activation.
Mono-, di- and trimethylated 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. H3K36me represses gene expression (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; 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-39; H3K36me1/2/3 = mono-, di- and trimethylated Lys-39; H3K56ac = acetylated Lys-58.
Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 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).
Mono-, di- and trimethylated 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 (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; H3K14ac = acetylated Lys-15; H3K14me2 = dimethylated Lys-15; H3K18ac = acetylated Lys-19; H3K18me1 = monomethylated Lys-19; H3K23ac = acetylated Lys-24; H3K23me1 = monomethylated Lys-24; H3K56ac = acetylated Lys-56; H3K64ac = acetylated Lys-64.
Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes.
Regulates also the sphingolipid metabolism.
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.
Belongs to the aldo/keto reductase family.
Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
DNA-binding transcription factor that specifically binds heat shock promoter elements (HSE) and activates transcription.
Homotrimer (By similarity). Homotrimerization increases the affinity of HSF1 to DNA (By similarity).
Belongs to the eukaryotic ribosomal protein eS7 family.
Plays a role in determining ER morphology.
The C4-type zinc finger motif is necessary both for its ER three-way tubular junction localization and formation.
Belongs to the eukaryotic-type primase large subunit family.
Involved with PTP2 and PTP3 in the formation of the polar tube through which the infectious agent is passed on to the host cell. Accounts for at least 70 percent of the mass of the polar tube.
Component of the core Fe-S cluster (ISC) assembly machinery.
Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitosomes, which is required for maturation of both [2Fe-2S] and [4Fe-4S] proteins (PubMed:18311129). First, a [2Fe-2S] cluster is transiently assembled on the scaffold protein ISU1. In a second step, the cluster is released from ISU1, transferred to a glutaredoxin, followed by the formation of [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and their target-specific insertion into the recipient apoproteins. Cluster assembly on ISU1 depends on the function of the cysteine desulfurase complex NFS1-ISD11, which serves as the sulfur donor for cluster synthesis, the iron-binding protein frataxin as the putative iron donor, and the electron transfer chain comprised of ferredoxin reductase and ferredoxin, which receive their electrons from NADH (By similarity).
Proteolytically removes the C-terminal three residues of farnesylated proteins.
Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 2 subfamily.
Belongs to the metallo-beta-lactamase superfamily. RNA-metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair.
Belongs to the XPG/RAD2 endonuclease family. EXO1 subfamily.
Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Belongs to the eukaryotic RPB8 RNA polymerase subunit family.
Belongs to the ribonucleoside diphosphate reductase small chain family.
Heterodimer of a large and a small subunit.
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).
Belongs to the V-ATPase H subunit family.
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
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).
Acts as catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover (By similarity). Ccr4 has 3'-5' RNase activity with a strong preference for polyadenylated substrates and also low exonuclease activity towards single-stranded DNA (By similarity).
Belongs to the eukaryotic initiation factor 4G family.
Component of the eIF4F complex, which composition varies with external and internal environmental conditions.
Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome.
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 eukaryotic ribosomal protein eL19 family.
Belongs to the universal ribosomal protein uS3 family.
Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA polymerase subunit family.
Belongs to the eukaryotic ribosomal protein P1/P2 family.
Plays an important role in the elongation step of protein synthesis.
Belongs to the CND2 (condensin subunit 2) family.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type V subfamily.
Belongs to the universal ribosomal protein uL18 family.
Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily.
Lacks transmembrane domains and is probably not involved in transport.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.
Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
Associates with the 60S ribosomal subunit.
May be involved in the biogenesis of the 60S ribosomal subunit and translational activation of ribosomes.
In the C-terminal section; belongs to the trehalose phosphatase family.
In the N-terminal section; belongs to the glycosyltransferase 20 family.
Belongs to the proteasome subunit S1 family.
Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing (By similarity).
The C-terminal domain (CTD) serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing.
The binding of ribonucleoside triphosphate to the RNA polymerase II transcribing complex probably involves a two-step mechanism. The initial binding seems to occur at the entry (E) site and involves a magnesium ion temporarily coordinated by three conserved aspartate residues of the two largest RNA Pol II subunits. The ribonucleoside triphosphate is transferred by a rotation to the nucleotide addition (A) site for pairing with the template DNA. The catalytic A site involves three conserved aspartate residues of the RNA Pol II largest subunit which permanently coordinate a second magnesium ion.
The tandem 7 residues repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphatase, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed (By similarity).
Belongs to the eukaryotic-type primase small subunit family.
Belongs to the V-ATPase D subunit family.
Ribosomal protein P0 is the functional equivalent of E.coli protein L10.
Belongs to the eukaryotic ribosomal protein eL42 family.
Small GTPase required for proper nuclear import of RNA polymerase II (RNAPII). May act at an RNAP assembly step prior to nuclear import.
Belongs to the eukaryotic/archaeal RNase P protein component 3 family.
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 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 (By similarity).
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 glycosyltransferase 20 family.
Component of the trehalose synthase complex.
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. Can function independently of the complex (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.
Component of the cleavage factor I (CF I) involved in pre-mRNA 3'-end processing.
Belongs to the eukaryotic ribosomal protein eL22 family.
Belongs to the DNA polymerase delta/II small subunit family.
Heterotrimeric complex composed of SEC61-alpha, SEC61-beta and SEC61-gamma.
Necessary for protein translocation in the endoplasmic reticulum.
Belongs to the DNA polymerase alpha subunit B family.
Required for normal growth at various temperatures.
Belongs to the tRNA pseudouridine synthase TruA family.
Associates with pre-60S ribosomal particles; released from the pre-60S particle very early in the cytoplasm.
Belongs to the ZNF593/BUD20 C2H2-type zinc-finger protein family.
Involved in pre-60S ribosomal particles maturation by promoting the nuclear export of the 60S ribosome.
Binds specifically to the 3'-terminal U-tract of U6 snRNA.
Belongs to the glucose-6-phosphate dehydrogenase family.
Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis (By similarity).
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity).
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.
Belongs to the histone deacetylase family. HD type 1 subfamily.
Plays a central role as a glucosyl donor in cellular metabolic pathways.
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.
Belongs to the DNA2/NAM7 helicase family.
Key enzyme involved in DNA replication and DNA repair. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair by mediating the cleavage of 5'-ssDNA.
Belongs to the eukaryotic ribosomal protein eS24 family.
Expressed in all stages of development including spores.
Belongs to the Nudix hydrolase family. DCP2 subfamily.
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.
In the N-terminal section; belongs to the ubiquitin family.
Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Involved in vesicular transport between the endoplasmic reticulum and the Golgi.
Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
Belongs to the eukaryotic release factor 1 family.
Belongs to the eukaryotic ribosomal protein eS4 family.
Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.
Belongs to the heat shock protein 90 family.
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. 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. Required for growth at high temperatures (By similarity).
The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.
May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi.
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 small GTPase superfamily. SAR1 family.
COPII is composed of at least 5 proteins: the SEC23/24 complex, the SEC13/31 complex and SAR1.
Small GTPase component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SAR1 controls the coat assembly in a stepwise manner. Activated SAR1-GTP binds to membranes first and recruits the SEC23/24 complex. These SEC23/24-SAR1 prebudding intermediates are then collected by the SEC13/31 complex as subunits polymerize to form coated transport vesicles. Conversion to SAR1-GDP triggers coat release and recycles COPII subunits (By similarity).
Belongs to the eukaryotic ribosomal protein eL36 family.
Catalyzes the covalent attachment of ubiquitin to other proteins so as to signal them for selective protein degradation. Involved in the formation of multiubiquitin chains.
Belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family.
mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC.
Belongs to the universal ribosomal protein uS5 family.
Belongs to the methyltransferase superfamily. RRP8 family.
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of adenine in helix 25.1 in 25S rRNA. Required both for ribosomal 40S and 60S subunits biogenesis. Required for efficient pre-rRNA cleavage at site A2.
Belongs to the proteasome subunit S3 family.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the AB hydrolase superfamily. AB hydrolase 4 family.
Belongs to the protein prenyltransferase subunit alpha family.
Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to cysteines occuring in specific C-terminal amino acid sequences.
Belongs to the iron/ascorbate-dependent oxidoreductase family.
Component of the telomerase complex involved in telomere replication. Stimulates RNA/DNA heteroduplex unwinding which favors the telomere replication by the telomerase.
Belongs to the eukaryotic initiation factor 4E family.
Belongs to the Mediator complex subunit 6 family.
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
DNA polymerase II participates in chromosomal DNA replication.
Has a role in transport between endoplasmic reticulum and Golgi.
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 deoxyhypusine synthase family.
Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Belongs to the glycosyl hydrolase 37 family.
Required for the final endonucleolytic cleavage at site D converting 20S pre-rRNA into the mature 18S rRNA. Required for the final steps of cytoplasmic maturation of the 40S ribosomal subunit. Despite the protein kinase domain is proposed to act predominantly as an ATPase. Has a role in the cell cycle where it is required for entrance into S-phase and in the control of the onset of anaphase. Appears to also be involved in the maintenance of chromosome stability and correct mitotic segregation (By similarity).
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 eukaryotic ribosomal protein eL15 family.
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. cAMP subfamily.
ATP transporter involved in the uptake of ATP from the parasite cell cytoplasm into the mitosome matrix. Equilibrates nucleotide pools across a concentration gradient between both sides of the mitosome membrane.
Acts on phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol 1,4,5,-trisphosphate.
Belongs to the PI3/PI4-kinase family. Type III PI4K subfamily.
ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair.
Belongs to the SNF2/RAD54 helicase family.
Component of the INO80 chromatin-remodeling complex.
The DBINO region is involved in binding to DNA.
Preferentially synthesized during differentiation from meronts to sporonts in early sporogony.
SWP1 is a major antigen recognized during host infection and might be a target for microsporidian infection diagnosis in the case of immunocompetent persons.
Belongs to the AP endonuclease 2 family.
Belongs to the BPG-independent phosphoglycerate mutase family.
Belongs to the ATP-dependent DNA ligase family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family.
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (By similarity).
Belongs to the HMG-CoA reductase family.
May be involved in 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).
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 TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. NOG subfamily.
Involved in the biogenesis of the 60S ribosomal subunit.
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.
Belongs to the glutathione peroxidase family.
Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione.
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. 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 (By similarity).
Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein.
Belongs to the Mediator complex subunit 31 family.
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
Belongs to the universal ribosomal protein uL11 family.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.
Protein kinase required for the cell cycle where it is involved in mitotic exit. Required to form a bipolar spindle, the actin ring and septum. Functions upstream of the whole septum formation pathway, including actin ring formation (regulated by late septation genes) and septal material deposition (regulated by early septation genes). Behaves as a 'septum-promoting factor', and could also be involved in inducing other late events of cell division (By similarity).
Belongs to the ribose 5-phosphate isomerase family.
Belongs to the eukaryotic RPB4 RNA polymerase subunit family.
Belongs to the class-II aminoacyl-tRNA synthetase family. Alax-L subfamily.
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Belongs to the SLC41A transporter family.
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.
Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalytic tRNA acetyltransferase subunit of the elongator complex, which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs.
Belongs to the thiolase-like superfamily. HMG-CoA synthase family.
Belongs to the ribonucleoside diphosphate reductase large chain family.
Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the large subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site (By similarity).
Required for correct functioning of the GINS complex, a complex that plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex seems to bind preferentially to single-stranded DNA.
Belongs to the RNase HII family. Eukaryotic subfamily.
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Belongs to the eukaryotic ribosomal protein eS19 family.
Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.
Belongs to the CTL (choline transporter-like) family.
Probably involved in transport through the plasma membrane.
Promotes the assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways.
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.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
Homodimer; disulfide-linked, upon oxidation.
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.
May play a role in the control of the eukaryotic cell cycle.
Involved in ribosomal large subunit assembly.
Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase subunit family.
Component of the ribosome quality control complex (RQC).
E3 ubiquitin-protein ligase. Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation.
Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 2 subfamily.
Belongs to the eukaryotic ribosomal protein eL32 family.
Component of the 60S subunit of the ribosome.
Involved in formation of a polar tube through which the infectious agent is passed on to the host cell.
Belongs to the nucleoporin interacting component (NIC) 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.
Belongs to the protein kinase superfamily.
Belongs to the GTP-binding SRP family. SRP54 subfamily.
Belongs to the UTP23/FCF1 family. FCF1 subfamily.
Belongs to the cytidylate kinase family. Type 1 subfamily.
Belongs to the eukaryotic ribosomal protein eL18 family.
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 protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.
Belongs to the ribulose-phosphate 3-epimerase family.
Binds 1 divalent metal cation per subunit. Active with Co(2+), Fe(2+), Mn(2+) and Zn(2+).
Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
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.
Active in protein import into the nucleus.
Belongs to the V-ATPase 116 kDa subunit family.
Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Belongs to the 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''.
Component of the cytosolic Fe/S protein assembly machinery. May play a role in the transfer of pre-assembled Fe/S clusters to target apoproteins (By similarity).
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 class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Belongs to the universal ribosomal protein uL22 family.
Belongs to the RNA 3'-terminal cyclase family. Type 2 subfamily.
Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles (By similarity).
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Involved in the regulation of the onset of mitosis. Involved in a pathway that coordinates cell proliferation and differentiation. Implicated in spindle pole body (SPD) duplication. Dual specificity kinase that can phosphorylate serine, threonine and tyrosine residues (By similarity).
Belongs to the PPP phosphatase family. PP-1 subfamily.
Belongs to the universal ribosomal protein uS8 family.
Belongs to the eukaryotic ribosomal protein eL43 family.
Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.
Interacts with PCNA. Three molecules of FEN1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Phosphorylated. Phosphorylation upon DNA damage induces relocalization to the nuclear plasma.
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.