Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Belongs to the protein kinase superfamily.
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 DNA/RNA non-specific endonuclease family.
Belongs to the phosphatase 2A regulatory subunit B family.
Belongs to the pyridoxine kinase family.
VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
May be involved in photoreceptor outer segment disk morphogenesis.
Belongs to the eukaryotic ribosomal protein eL36 family.
Component of the RNA editing complex (editosome), a 1600 kDa complex composed of at least 20 proteins (By similarity). Interacts with terminal uridylyltransferase MEAT1 (By similarity).
Essential for RNA editing. RNA editing in kinetoplastid mitochondria inserts and deletes uridylates at multiple sites in pre-mRNAs as directed by guide RNAs.
Could act as a receptor for an unknown ligand.
Belongs to the mitochondrial pyruvate carrier (MPC) (TC 2.A.105) family.
Mediates the uptake of pyruvate into mitochondria.
Belongs to the GPI inositol-deacylase family.
Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.
Belongs to the dynein light chain family.
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER).
Belongs to the helicase family. PIF1 subfamily.
DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of mitochondrial (kinetoplast) genome stability. Involved in processing of minicircle Okazaki fragments.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.
Lacks conserved residue(s) required for the propagation of feature annotation.
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.
Catalytic subunit of a heterodimeric structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Forms a heterodimer with a member of the SLX4 family.
Transcription elongation factor implicated in the maintenance of proper chromatin structure in actively transcribed regions.
Belongs to the universal ribosomal protein uL13 family.
Belongs to the eukaryotic ribosomal protein eL37 family.
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Belongs to the aldehyde dehydrogenase family.
Accepts electrons from ETF and reduces ubiquinone.
DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of genome stability.
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 RecA family. DMC1 subfamily.
Belongs to the mitochondrial carrier (TC 2.A.29) family.
Belongs to the adaptor complexes small subunit family.
Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits.
The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
Required for maturation of ribosomal RNAs and formation of the large ribosomal subunit.
Belongs to the acetyltransferase family. GNAT subfamily.
ATP-dependent RNA helicase that unwinds RNA in a 3' to 5' direction and that plays an important role in mitochondrial mRNA editing, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA (PubMed:19850921, PubMed:26769962, PubMed:31034523). As part of the RET2-containing gRNA-binding (RET2-GRBC) complex, acts as a scaffold for the assembly of mRNA-gRNA hybrids and the recruitment of the RNA editing core (RECC) complex (PubMed:25928631, PubMed:26769962). Regulates several steps of mRNA editing by the MRBC3010/GRBC6 containing gRNA-binding (MRBC3010-GRBC) complex including loading of unedited mRNA, editing in the first sequence block and subsequent editing progression across multiple sequence blocks (PubMed:25928631). Also, regulates the RNA substrate content of the MRBC3010-GRBC complex as well as the association of this complex with mitoribosomes (PubMed:25928631).
Belongs to the DEAD box helicase family. DEAH subfamily.
Component of the REH2-associated complex (REH2C) composed of helicase REH2, associated factors H2F1 and H2F2, and mRNAs at various editing stages; the formation of the complex is RNA-independent (PubMed:26769962, PubMed:31034523). Within the complex, interacts with H2F1; the interaction is direct (PubMed:26769962, PubMed:31034523). Interacts transiently, in a RNA-dependent manner, with various editing complexes including the RNA editing core (RECC) complex, the gRNA-binding (GRBC) complex (also known as the MRB1 complex) and the RNA editing mediator (REMC) complex (PubMed:19850921, PubMed:25928631, PubMed:26769962, PubMed:31034523). Interacts with GAP1/GRBC2 via RNA forming a variant of the GRBC complex known as REH2-GRBC complex (PubMed:19850921, PubMed:25928631, PubMed:26769962, PubMed:31034523). Interacts with mitochondrial ribosomes (PubMed:19850921).
Expressed at the procyclic stage (at protein level).
RNAi-mediated knockdown at the procyclic stage causes a loss of RNA unwinding activity (PubMed:26769962). Reduces association of H2F1 and abolishes H2F2 association with components of various editing complexes (PubMed:26769962). RNAi-mediated knockdown at the procyclic stage inhibits editing at early 3' sites on pre-mRNA substrates without affecting the interactions between MRB3010/GRBC6, GAP1/GRBC2, RGG2, REL1 and gRNA (PubMed:25928631). Decreases the ratio of unedited mRNA substrates in the MRB3010/GRBC6-MRB complex and the association of never-edited mRNA and 9SrRNA with the MRB3010-MRB complex (PubMed:25928631). Also, causes a decrease in the steady-state levels of guide RNA (gRNA) (PubMed:19850921).
The DRBM domain is required for binding to guide RNAs (gRNA) and mRNAs which facilitates the association with the GRBC complex.
Belongs to the complex I 24 kDa subunit family.
Belongs to the FPP/GGPP synthase family.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.
Belongs to the dynein heavy chain family.
Belongs to the succinate/malate CoA ligase alpha subunit family.
Heterodimer of an alpha and a beta subunit.
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
Belongs to the isocitrate and isopropylmalate dehydrogenases family.
Binds 1 Mg(2+) or Mn(2+) ion per subunit.
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.
Belongs to the eIF-2B alpha/beta/delta subunits family.
Belongs to the poly(A) polymerase family.
Binds 2 magnesium ions. Also active with manganese.
Polymerase that creates the 3'-poly(A) tail of mRNA's.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase NEP1 family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
May contribute to the rapid motility of the trypanosomes, playing a role either in flagellar structure or in calcium metabolism. Could alternate between a GDP-bound inactive form to a calcium/GTP-bound active form.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
Phosphatidylethanolamine (PE) is a direct precursor of the ethanolamine-phosphoglycerol (EPG) moiety.
The Kennedy pathway is the major route for phosphatidylethanolamine (PE) synthesis, as shown by reduced levels after using RNAi against the first two enzymes of the Kennedy pathway.
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Belongs to the universal ribosomal protein uL16 family.
Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
Belongs to the threonine synthase family.
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
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 proteasome is 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.
Belongs to the universal ribosomal protein uS5 family.
Belongs to the ATP:guanido phosphotransferase family.
Belongs to the alternative oxidase family.
Belongs to the V-ATPase proteolipid subunit family.
Belongs to the tRNA pseudouridine synthase TruA family.
Belongs to the DPH1/DPH2 family. DPH1 subfamily.
Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2.
Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.
Belongs to the eukaryotic ribosomal protein eL43 family.
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.
Belongs to the sirtuin family. Class III subfamily.
In contrast to class I sirtuins, class III sirtuins have only weak deacetylase activity. Difference in substrate specificity is probably due to a larger hydrophobic pocket with 2 residues (Tyr-57 and Arg-60) that bind to malonylated and succinylated substrates and define the specificity.
NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo.
This protein may be expected to contain an N-terminal transit peptide but none has been predicted.
The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
The glycine cleavage system is composed of four proteins: P, T, L and H.
Belongs to the class-I aminoacyl-tRNA synthetase family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family.
Belongs to the cyclophilin-type PPIase family.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Belongs to the trans-sulfuration enzymes family.
Belongs to the fatty acid desaturase CarF family.
Catalyzes the exchange of ADP and ATP across the membrane.
Belongs to the universal ribosomal protein uL14 family.
Belongs to the glycosyltransferase 31 family.
Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling.
Belongs to the DHHC palmitoyltransferase family.
The DHHC domain is required for palmitoyltransferase activity.
Belongs to the PPP phosphatase family. PP-5 (PP-T) subfamily.
Belongs to the small GTPase superfamily. Rab family.
Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix.
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.
Belongs to the bacterial ribosomal protein bL17 family.
Activated by threonine and tyrosine phosphorylation.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily.
In the N-terminal section; belongs to the NADH:flavin oxidoreductase/NADH oxidase family.
Belongs to the iron/ascorbate-dependent oxidoreductase family.
Belongs to the UPL family. K-HECT subfamily.
Belongs to the adaptor complexes medium subunit family.
Belongs to the deoxyhypusine hydroxylase family.
Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.
Belongs to the eukaryotic ribosomal protein eS8 family.
Expressed at low levels in the bloodstream form (at protein level) (PubMed:31743541, PubMed:32532821). Expressed in the procyclic form (PubMed:31743541).
Induced during differentiation of bloodstream form to procyclic form.
Interacts (via MKT1-binding motif) with MKT1.
RNA-binding protein involved in regulation of mRNA stability (PubMed:31743541). Promotes mRNA stabilization by recruiting MKT1 and PBP1 (By similarity). Stabilizes mRNA required for differentiation from the bloodstream form to the procyclic form, and maintenance of the procyclic form (PubMed:31743541). Stabilizes transcripts encoding membrane and mitochondrial proteins, including AQP1 and GPEET2 procyclin (PubMed:31743541).
RNAi-mediated knockdown causes abnormal differentiation of the bloodstream form into the procyclic form, a reduction in the expression of several mRNA including differentiation protein PAD1, and premature death (PubMed:31743541). RNAi-mediated knockdown at the procyclic stage causes a decrease in growth rate (PubMed:31743541). Simultaneous RNAi-mediated knockdown of ZC3H20 and ZC3H21 at the bloodstream stage is lethal (PubMed:31743541). Simultaneous RNAi-mediated knockdown of ZC3H20 and ZC3H21 at the procyclic stage causes a severe growth defect and a shift towards a bloodstream form (PubMed:31743541).
Belongs to the eukaryotic initiation factor 4E family.
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.
Belongs to the DEAD box helicase family. eIF4A subfamily.
eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G.
Interacts with the flavoprotein subunit within the SDH catalytic dimer.
Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit of the SDH catalytic dimer.
Belongs to the proteasome subunit S5A family.
Belongs to the myo-inositol 1-phosphate synthase family.
Belongs to the polyadenylate-binding protein type-1 family.
Belongs to the ribose-phosphate pyrophosphokinase family.
Belongs to the eukaryotic ribosomal protein P1/P2 family.
P1 and P2 exist as dimers at the large ribosomal subunit.
Plays an important role in the elongation step of protein synthesis.
Belongs to the eukaryotic ribosomal protein eL8 family.
Belongs to the prefoldin subunit alpha family.
Belongs to the inositol monophosphatase superfamily.
Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit.
Belongs to the universal ribosomal protein uS19 family.
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X' sub-subfamily.
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Belongs to the phospholipase B-like family.
Belongs to the carnitine/choline acetyltransferase family.
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 STXBP/unc-18/SEC1 family.
Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family.
Has a role in nuclear-cytoplasmic transport of proteins and mRNAs.
Belongs to the major facilitator superfamily. RibJ family.
Transporter involved in riboflavin (vitamin B2) uptake. Also transports FMN and FAD.
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
Belongs to the UbiA prenyltransferase family.
Converts protoheme IX and farnesyl diphosphate to heme O.
Belongs to the TRAPP small subunits family. BET3 subfamily.
ATP-dependent 3'-5' DNA helicase, component of the general transcription factor IIH (TFIIH) core complex, involved in spliced leader RNA (SL RNA) gene transcription by RNA polymerase II (PubMed:17259543). 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 is required for promoter opening and promoter escape (By similarity).
Belongs to the helicase family. RAD25/XPB subfamily.
Component of the 7-subunit TFIIH core complex composed of XPB, XPD, SSL1, TFB1, TFB2, TFB4 and TFB5.
Belongs to the Rieske iron-sulfur protein family.
Belongs to the ATPase delta chain family.
Belongs to the DEAD box helicase family. DDX21/DDX50 subfamily.
Belongs to the class-II aminoacyl-tRNA synthetase family.
Expressed in the procyclic form and the bloodstream form at low levels.
Induced during the response to misfolded or unfolded cytoplasmic proteins; including during thermal stress, sodium arsenite, or acidic pH (at protein level) (PubMed:23592996, PubMed:27002830). Not induced by endoplasmic reticulum stress (PubMed:27002830).
Interacts (via MKT1-binding motif) with MKT1 (PubMed:23592996, PubMed:24470144). Interacts with PBP1 (via C-terminus); the interaction is direct (PubMed:23592996, PubMed:24470144).
Phosphorylated at the N-terminus (PubMed:23592996, PubMed:27002830). CK1.2-dependent phosphorylation may lead to proteasome-dependent degradation of ZC3H11 in absence of stress (PubMed:27002830).
RNA-binding protein involved in regulation of mRNA stability (PubMed:23592996). Binds AU-rich regions in the 3'-UTR of mRNAs and promotes their stabilization by recruiting a MKT1-containing complex (PubMed:23592996, PubMed:24470144). Stabilizes chaperone mRNAs during stress that causes an accumulation of misfolded or unfolded proteins in the cytoplasm (PubMed:23592996, PubMed:24470144, PubMed:27002830).
RNAi-mediated knockdown in the bloodstream form is lethal and causes a reduction in chaperone mRNA levels in response to heat-induced stress (PubMed:23592996). RNAi-mediated knockdown in the procyclic form causes sensitivity to cytoplasmic protein folding stress (induced by high temperature, puromycin, arsenite, MG132 or ethanol), characterized by a reduction in chaperone mRNA levels (PubMed:23592996, PubMed:27002830).
The zinc finger domain binds AU-rich regions in the 3'-UTR of mRNAs.
Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.
In the N-terminal section; belongs to the dsDNA virus mRNA guanylyltransferase family.
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 activator 1 small subunits family.
Belongs to the heat shock protein 70 family.
Major surface antigen of procyclic forms.
Belongs to the helicase family. RecQ subfamily.
Belongs to the group II decarboxylase family.
Required for the function of coenzyme Q in the respiratory chain. May serve as a chaperone or may be involved in the transport of Q6 from its site of synthesis to the catalytic sites of the respiratory complexes.
Belongs to the glycosyl hydrolase 47 family.
Belongs to the small GTPase superfamily. Ran family.
GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle.
Belongs to the protein prenyltransferase subunit beta family.
Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding.
Belongs to the WD repeat DCAF13/WDSOF1 family.
Belongs to the methyltransferase superfamily. Fibrillarin family.
Belongs to the KIF-binding protein family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. SPB1 subfamily.
Probable methyltransferase involved in the maturation of rRNA and in the biogenesis of ribosomal subunits.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily.
Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.
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.
Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.
Heterohexamer of two PFD-alpha type and four PFD-beta type subunits.
Belongs to the polypeptide deformylase family.
Removes the formyl group from the N-terminal Met of newly synthesized proteins.
Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase subunit family.
Belongs to the Rab3-GAP catalytic subunit family.
Belongs to the eukaryotic ribosomal protein eL24 family.
Involved in nucleolar processing of pre-18S ribosomal RNA.
Belongs to the universal ribosomal protein uS15 family.
Belongs to the tubulin--tyrosine ligase family.
Belongs to the pseudouridine synthase TruD family.
Belongs to the chloride channel (TC 2.A.49) family.
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network.
Belongs to the nonaspanin (TM9SF) (TC 9.A.2) family.
Flagellar protein involved in flagellum axoneme organization and function.
Belongs to the glutathione peroxidase family.
Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.
Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Interacts with PCNA. Three molecules of 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.
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 adaptor complexes large subunit family.
Belongs to the sphingomyelin synthase family.
Bidirectional lipid inositolphosphotransferase capable of converting phosphatidylinositol (PI) and ceramide to inositol-phosphorylceramide (IPC) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphoinositol acceptors. Does not function strictly as a SM synthase. Essential for viability of the pathogenic bloodstream stage of this human protozoan parasite and, consequently, can be considered as potential drug target (By similarity).
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.
Inhibited by cyclin kinase 2 (CDK2) inhibitors, including GW8510.
Was identified as a drug target for the treatment of African sleeping sickness. RNA interference leads to growth arrest and altered parasite morphology, demonstrating requirement for cell survival.
Belongs to the AAA ATPase family. BCS1 subfamily.
Belongs to the actin-binding proteins ADF family. Twinfilin subfamily.
Belongs to the CTL (choline transporter-like) family.
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/UBA4 homolog. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins. 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 the MOCS3/UBA4 homolog, then thiocarboxylated (-COSH) via the rhodanese domain of the MOCS3/UBA4 homolog.
Belongs to the methyltransferase superfamily. RRP8 family.
Probable methyltransferase required to silence rDNA.
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 cyclic nucleotide phosphodiesterase family.
Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Belongs to the eukaryotic ribosomal protein eL13 family.
Belongs to the sirtuin family. Class I subfamily.
NAD-dependent protein deacetylase, which is involved in repression of RNA polymerase I-mediated expression immediately adjacent to telomeres. It is however not involved in antigenic variation and subtelomeric variant surface glycoprotein (VSG) gene silencing. Plays a role in DNA damage response. Also has ADP-ribosylation activity in vitro.
Belongs to the glycosyl hydrolase 38 family.
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively.
Belongs to the transferase hexapeptide repeat family.
Belongs to the universal ribosomal protein uL3 family.
Belongs to the DNA polymerase type-X family.
DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities. Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
Belongs to the enoyl-CoA hydratase/isomerase family.
Belongs to the RNase HII family. Eukaryotic subfamily.
Belongs to the major facilitator superfamily. Spinster (TC 2.A.1.49) family.
In the C-terminal section; belongs to the eukaryotic ribosomal protein eS31 family.
In the N-terminal section; belongs to the ubiquitin family.
Required for the maintenance of mitochondrial (kinetoplast) genome stability. Essential for cell viability. Has probably no helicase activity, missing at least two of seven conserved helicase motifs.
Plays a role in vesicular protein sorting.
Belongs to the universal ribosomal protein uL11 family.
Belongs to the aconitase/IPM isomerase family.
Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
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.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily.
Belongs to the DNA photolyase class-1 family.
Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Belongs to the snRNP Sm proteins family.
Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome.
Belongs to the eukaryotic ribosomal protein eS25 family.
Belongs to the adaptor complexes medium subunit family. Delta-COP subfamily.
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. 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 DEAD box helicase family. DDX54/DBP10 subfamily.
Belongs to the class I fructose-bisphosphate aldolase family.
Associates with the NTC complex (or PRP19-associated complex) (By similarity). The NTC complex associates with the spliceosome after the release of the U1 and U4 snRNAs and forms the CWC spliceosome subcomplex reminiscent of a late-stage spliceosome (By similarity). Associates specifically with U5-containing snRNPs.
Essential protein involved in pre-mRNA cis- and trans-splicing. May function at or prior to the first catalytic step of splicing at the catalytic center of the spliceosome. May do so by stabilizing the catalytic center or the position of the RNA substrate.
Belongs to the DEAD box helicase family.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
Belongs to the EF-1-beta/EF-1-delta family.
Belongs to the V-ATPase H subunit family.
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments.
V-ATPase is a heteromultimeric enzyme made up of two complexes: the ATP-hydrolytic V1 complex and the proton translocation V0 complex.
Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate.
Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate.
Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
Belongs to the OMP decarboxylase family. Type 2 subfamily.
Belongs to the universal ribosomal protein uL18 family.
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.
Belongs to the tRNA methyltransferase O family.
Belongs to the replication factor A protein 3 family.
Bidirectional lipid cholinephosphotransferase capable of converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. Directly and specifically recognizes the choline head group on the substrate. Also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Does not function strictly as a SM synthase. Essential for viability of the pathogenic bloodstream stage of this human protozoan parasite and, consequently, can be considered as potential drug target (By similarity).
Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position.
Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2)) required for protein glycosylation.
Belongs to the glycosyltransferase 22 family.
Belongs to the eukaryotic GSH synthase family.
Belongs to the ubiquitin-conjugating enzyme family.
Belongs to the eukaryotic ribosomal protein eL39 family.
Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
Probable GTP-binding protein that may be involved in cell development.
Belongs to the snRNP Sm proteins family. SmF/LSm6 subfamily.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.
Belongs to the prefoldin subunit beta family.
Belongs to the eukaryotic ribosomal protein eL38 family.
Belongs to the universal ribosomal protein uS17 family.
Belongs to the DNA2/NAM7 helicase family.
Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family.
Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family.
Belongs to the mitochondrion-specific ribosomal protein mL46 family.
Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.
Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor. Molecular oxygen can replace fumarate in vitro.
Belongs to the protease inhibitor I11 (ecotin) family.
Belongs to the universal ribosomal protein uS12 family.
Belongs to the eukaryotic ribosomal protein eL19 family.
Belongs to the asfivirus helicase A859L family.
Belongs to the DNA polymerase delta/II small subunit family.
Belongs to the snRNP core protein family.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Erg6/SMT family.
Belongs to the methyltransferase superfamily. RsmH family.
Belongs to the eukaryotic ribosomal protein eS30 family.
Component of the ribosomal small subunit (SSU) processome.
Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
Belongs to the SNF2/RAD54 helicase family.
Belongs to the diphosphomevalonate decarboxylase family.
Catalyzes the ATP dependent decarboxylation of (R)-5-diphosphomevalonate to form isopentenyl diphosphate (IPP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoids and sterol synthesis.
Belongs to the tubulin polyglutamylase family.
Belongs to the nucleosome assembly protein (NAP) family.
Belongs to the proteasome subunit S2 family.
Belongs to the V-ATPase V0D/AC39 subunit family.
Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment.
Belongs to the PPP phosphatase family. PP-2B subfamily.
Belongs to the DEAD box helicase family. DEAH subfamily. DDX11/CHL1 sub-subfamily.
Belongs to the multicopper oxidase family.
Belongs to the proteasome subunit S9 family.
Belongs to the peptidase M24 family. SPT16 subfamily.
Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II.
Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
Belongs to the lariat debranching enzyme family.
DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of mitochondrial (kinetoplast) genome stability.
Belongs to the WD repeat peroxin-7 family.
Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family.
Sodium-phosphate symporter which plays a fundamental housekeeping role in phosphate transport.
Belongs to the universal ribosomal protein uL1 family.
Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Belongs to the 2-oxoacid dehydrogenase family.
Belongs to the universal ribosomal protein uS13 family.
Belongs to the polyprenol kinase family.
Belongs to the acetyltransferase family. MAK3 subfamily.
Belongs to the small GTPase superfamily. Arf family.
Belongs to the eukaryotic ribosomal protein eS12 family.
Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the glycosyltransferase 28 family.
Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has also a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides.
Component of a multi-subunit COQ enzyme complex.
Belongs to the archaeal rpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family.
Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits.
Belongs to the ATP-dependent AMP-binding enzyme family.
Belongs to the AAA ATPase family. Katanin p60 subunit A1 subfamily.
Severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays.
Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity.
Belongs to the major facilitator superfamily. Folate-biopterin transporter (TC 2.A.71) family.
Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
Belongs to the LDH/MDH superfamily. MDH type 1 family.
Component of the nuclear pore complex (NPC)-associated TREX-2 complex (transcription and export complex 2). Component of the SAGA transcription coactivator-HAT complex. Within the SAGA complex, participates to a subcomplex of SAGA called the DUB module (deubiquitination module).
Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. The transcription regulatory histone acetylation (HAT) complex SAGA is a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates to a subcomplex that specifically deubiquitinates histones. The SAGA complex is recruited to specific gene promoters by activators, where it is required for transcription. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery.
Belongs to the protein disulfide isomerase family.
Belongs to the clathrin heavy chain family.
Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
Belongs to the fatty acid desaturase type 1 family.
GTP-binding protein involved in protein trafficking; modulates vesicle budding and uncoating within the Golgi apparatus.
Belongs to the GHMP kinase family. Mevalonate kinase subfamily.
Belongs to the NUP186/NUP192/NUP205 family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. BUD23/WBSCR22 family.
Dioxygenase that catalyzes the first step of DNA base J (beta-d-glucosyl-HOMedU) biosynthesis by converting thymine to 5-hydroxymethyluracil (HOMedU). DNA base J is a hypermodified thymidine residue found in the genome of kinetoplastid parasites, which is localized primarily to repetitive DNA, namely the telomeres, and is implicated in the regulation of antigenic variation. Probably also acts as a DNA helicase. Recognizes and binds specific regions of the genome, hydrolyzes ATP and allows the DNA base J de novo synthesis. Involved in initial synthesis of DNA base J, JBP1 being able to act via the basal level of DNA base J and propagate further synthesis. In contrast to JBP1, it does not specifically bind DNA base J, however it binds chromatin.
Dioxygenase that catalyzes the first step of DNA base J (beta-d-glucosyl-HOMedU) biosynthesis by converting thymine to 5-hydroxymethyluracil (HOMedU). DNA base J is a hypermodified thymidine residue found in the genome of kinetoplastid parasites, which is localized primarily to repetitive DNA, namely the telomeres, and is implicated in the regulation of antigenic variation. Probably also acts as a DNA helicase. Recognizes and binds specific regions of the genome, hydrolyzes ATP and allows the DNA base J de novo synthesis. Involved in initial synthesis of DNA base J, JBP1 being able to act via the basal level of DNA base J and propagate further synthesis. In contrast to JBP1, it does not specifically bind DNA base J, it however binds chromatin.
In the C-terminal section; belongs to the SNF2/RAD54 helicase family.
In the N-terminal section; belongs to the TET family. JBP2 subfamily.
The genome contains reduced level of DNA base J in the DNA. Cells lacking both JBP1 and JBP2 show a complete absence of base J.
Belongs to the Nudix hydrolase family. CPSF5 subfamily.
Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs.
Homodimer (via N- and C-terminus); binds RNA as homodimer. Component of the cleavage factor Im (CFIm) complex.
Belongs to the MPDU1 (TC 2.A.43.3) family.
Belongs to the NADH dehydrogenase family.
Belongs to the glutamine synthetase family.
Belongs to the eukaryotic ribosomal protein eS10 family.
Associates with 90S and pre-40S pre-ribosomal particles.
Component of the 90S pre-ribosome involved in the maturation of rRNAs. Required for early cleavages of the pre-RNAs in the 40S ribosomal subunit maturation pathway.
Proteolytically removes the C-terminal three residues of farnesylated proteins.
Belongs to the methyltransferase superfamily. METL family.
S-adenosyl-L-methionine-dependent methyltransferase.
tRNA nucleus export receptor which facilitates tRNA translocation across the nuclear pore complex.
Belongs to the mitochondrion-specific ribosomal protein mS41 family.
Belongs to the eukaryotic ATPase epsilon family.
Belongs to the ATPase gamma chain family.
Belongs to the eukaryotic AdoMetDC family.
Binds 1 pyruvoyl group covalently per subunit.
AP-4 forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system.
Adaptor protein complex 4 (AP-4) is a heterotetramer composed of two large adaptins, a medium adaptin and a small adaptin.
Induced during the differentiation of the bloodstream form to the procyclic form.
RNA-binding protein involved in regulation of mRNA stability (PubMed:31743541). Promotes mRNA stabilization by recruiting MKT1 and PBP1 (By similarity). Stabilizes transcripts encoding mitochondrial proteins (PubMed:31743541).
RNAi-mediated knockdown in procyclic form does not affect growth rate (PubMed:31743541). Simultaneous knockdown of ZC3H20 and ZC3H21 in the procyclic form results in a severe population growth defect and a shift towards the bloodstream form transcriptome (PubMed:31743541). Simultaneous knockdown of ZC3H20 and ZC3H21 in the bloodstream form is lethal (PubMed:31743541).
Belongs to the universal ribosomal protein uL30 family.
Belongs to the cyclophilin-type PPIase family. PPIL4 subfamily.
Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family.
Belongs to the MICOS complex subunit Mic10 family.
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Belongs to the methyltransferase TRM13 family.
tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His).
Belongs to the metallo-dependent hydrolases superfamily. ATZ/TRZ family.
Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
Belongs to the PI3/PI4-kinase family. Type III PI4K subfamily.
Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins.
Belongs to the selenophosphate synthase 1 family. Class I subfamily.
RNAi-mediated knock down in procyclic and blood stream forms (strain 29-13) impairs growth following prolonged exposure to oxidative stress.
Synthesizes selenophosphate from selenide and ATP.
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.
May play a role in vesicular transport from endoplasmic reticulum to Golgi.
Belongs to the thiolase-like superfamily. HMG-CoA synthase family.
In the C-terminal section; belongs to the peptidase M41 family.
In the N-terminal section; belongs to the AAA ATPase family.
Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Involved in nucleotide excision repair.
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 peptidase M67A family. BRCC36 subfamily.
Belongs to the methyltransferase superfamily. L-isoaspartyl/D-aspartyl protein methyltransferase family.
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
Belongs to the prokaryotic/mitochondrial release factor family.
Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
Belongs to the MIP/aquaporin (TC 1.A.8) family.
Belongs to the peroxisomal targeting signal receptor family.
Belongs to the succinate/malate CoA ligase beta subunit family.
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Belongs to the eukaryotic ribosomal protein eL22 family.
Belongs to the eukaryotic ribosomal protein eS7 family.
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Belongs to the complex I NDUFB7 subunit family.
Belongs to the SMC family. SMC2 subfamily.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Belongs to the universal ribosomal protein uL22 family.
Belongs to the SLC35F solute transporter family.
Belongs to the eukaryotic ribosomal protein eL30 family.
Belongs to the fatty acid desaturase type 1 family. DEGS subfamily.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.
Belongs to the universal ribosomal protein uL15 family.
In T.brucei, PIGM has a different substrate specificity compared to mammalian. Given that the protozoan parasite evades the immune response of mammalian hosts and digestion in the gut of the insect vector by means of its coat proteins tethered to the cell surface via GPI-anchors, it may be a good candidate for chemotherapy against African trypanosomiasis.
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-PI during GPI precursor assembly (By similarity).
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly.
Belongs to the eukaryotic ribosomal protein eL32 family.
Belongs to the DNA polymerase type-B family.
Belongs to the PA-phosphatase related phosphoesterase family.
Component of the ER membrane protein complex (EMC).
Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins.
Component of the REH2-associated complex (REH2C) composed of helicase REH2, associated factors H2F1 and H2F2, and mRNAs at various editing stages; the formation of the complex is RNA-independent (PubMed:26769962). Interacts with various editing complexes including the RNA editing core (RECC) complex, the gRNA-binding (GRBC) complex (also known as the MRB1 complex) and the RNA editing mediator (REMC) complex (PubMed:26769962).
May play a role in mitochondrial mRNA editing by facilitating the association of the gRNA-binding (GRBC) complex with the RNA editing core (RECC) complex (PubMed:26769962). However, appears to be dispensable for mRNA editing per se (PubMed:26769962).
RNAi-mediated knockdown at the procyclic stage does not cause defects in RHE2 interaction with H2F1 or their association with components of the RECC and GRBC editing complexes; however, causes a slight decrease in the association of the GRBC complex with the RECC complex (PubMed:26769962). No defect in mitochondrial mRNA editing (PubMed:26769962).
Substrate-binding subunit of tRNA (adenine-N1-)-methyltransferase, which catalyzes the formation of N1-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA.
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).
eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G (By similarity).
Belongs to the major facilitator superfamily. MFSD6 family.
Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Belongs to the thiolase-like superfamily. Thiolase family.
Belongs to the eukaryotic ribosomal protein eL34 family.
Belongs to the GTR/RAG GTP-binding protein family.
Belongs to the phosphohexose mutase family.
Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family.
In plastids the minimal PEP RNA polymerase catalytic core is composed of four subunits: alpha, beta, beta', and beta''. When a (nuclear-encoded) sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
DNA polymerase II participates in chromosomal DNA replication.
Belongs to the eukaryotic ribosomal protein eS24 family.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. GDP-mannose 4,6-dehydratase subfamily.
TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.
Component of the peroxisomal translocation machinery.
May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex.
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.
Non-catalytic component of the proteasome.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. TRM7 subfamily.
Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs.
Belongs to the heat shock protein 90 family.
Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration.
Belongs to the eukaryotic ribosomal protein eL20 family.
Belongs to the methyltransferase superfamily. NTM1 family.
Although it belongs to the XPG/RAD2 endonuclease family, only one of the seven Asp residues involved in Mg(2+) binding is conserved suggesting that it has no nuclease activity.
Belongs to the XPG/RAD2 endonuclease family.
Expressed in the procyclic and bloodstream forms (at protein level).
Forms a complex composed of at least MKT1L, PBP1, XAC1 and LSM12.
Involved in post-transcriptional regulation of gene expression.
RNAi-mediated knockdown in both the procyclic and the bloodstream form is lethal.
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.
Belongs to the cytidylyltransferase family.
Belongs to the eukaryotic ribosomal protein eL18 family.
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.
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).
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Ungrouped subfamily.
ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives.
Belongs to the carbohydrate kinase PfkB family.
Belongs to the auxin efflux carrier (TC 2.A.69.2) family.
Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
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.
Involved in the early part of the secretory pathway.
Belongs to the DNA polymerase epsilon subunit B family.
Belongs to the U2 small nuclear ribonucleoprotein A family.
Belongs to the tyrosyl-DNA phosphodiesterase family.
Belongs to the universal ribosomal protein uL6 family.
A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex (HslVU) is dependent on binding of ATP (By similarity).
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis (By similarity). The HslVU protease complex functions in mitochondrial DNA replication by regulating DNA helicase PIF2 protein levels.
Belongs to the ClpX chaperone family. HslU subfamily.
Belongs to the fatty acyl-CoA reductase family.
Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
Belongs to the GTP-binding elongation factor family. EF-G/EF-2 subfamily.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Probable S-adenosyl-L-methionine-dependent methyltransferase.
Belongs to the eukaryotic ribosomal protein eL6 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 universal ribosomal protein uS3 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 exonuclease superfamily. TREX family.
Catalyzes the dephosphorylation of the nucleoside 5'-monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and deoxythymidine monophosphate (dTMP).
Small GTPase required for proper nuclear import of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import.
Belongs to the DEAD box helicase family. DEAH subfamily. DDX15/PRP43 sub-subfamily.
Belongs to the ATPase alpha/beta chains family.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c.
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes.
Regulates also the sphingolipid metabolism.
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes.
Belongs to the protein-tyrosine phosphatase family.
Belongs to the CND2 (condensin subunit 2) family.
Belongs to the V-ATPase G subunit family.
Bidirectional lipid ethanolaminephosphotransferase capable of converting phosphatidylethanolamine (PE) and ceramide to ethanolamine-phosphorylceramide (EPC) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphoethanolamine acceptors. Does not function strictly as a SM synthase. Essential for viability of the pathogenic bloodstream stage of this human protozoan parasite and, consequently, can be considered as potential drug target (By similarity).
Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors.
The PAL motif is required for normal active site conformation.
Belongs to the ribulose-phosphate 3-epimerase family.
Binds 1 divalent metal cation per subunit.
Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family.
Catalyzes the hydrolysis of ATP coupled with the transport of calcium.
Belongs to the chaperonin (HSP60) family.
Belongs to the mitochondrion-specific ribosomal protein mS29 family.
Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP2/CFD1 subfamily.
Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NUBP1 and two labile, bridging clusters between subunits of the NUBP1-NUBP2 heterotetramer.
Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins.
Heterotetramer of 2 NUBP1 and 2 NUBP2 chains.
In the C-terminal section; belongs to the glutathionylspermidine synthase preATP-grasp family.
Belongs to the glycosyltransferase 8 family.
Belongs to the folylpolyglutamate synthase family.
Belongs to the opioid growth factor receptor family.
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.
Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport.
The vault ribonucleoprotein particle is a huge (400 A x 670 A) cage structure of 12.9 MDa. It consists of a dimer of half-vaults, with each half-vault comprising 39 identical major vault protein (MVP) chains, PARP4 and one or more vault RNAs (vRNAs).
Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIA subfamily.
A component of FAZ filament that is required for correct FAZ assembly and attachment. Not essential for new flagellum growth.
Assembly of a compromised FAZ and defects in flagellum attachment and cytokinesis in procyclic trypanosomes resulting in generation of 0N1K cells (zoids) and multinucleated cells, demonstrates the role of an attached flagellum in cellular morphogenesis.
Belongs to the inositol phosphokinase (IPK) family.
Forms a complex composed of at least MKT1, PBP1, XAC1 and LSM12 (PubMed:24470144). Forms a complex composed of at least MKT1L, PBP1, XAC1 and LSM12 (PubMed:32532821). Within the complex, interacts with PBP1; the interaction is direct (PubMed:24470144, PubMed:32532821).
Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.
Belongs to the phosphoglycerate kinase 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.
Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways.
Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome.
Belongs to the mitochondrion-specific ribosomal protein mL43 family.
Adaptor protein complex 3 (AP-3) is a heterotetramer.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily.
Required for proper 27S pre-rRNA processing and 60S ribosome subunit assembly.
Converts proline to delta-1-pyrroline-5-carboxylate.
Belongs to the eukaryotic ribosomal protein eS28 family.
Forms a complex composed of at least MKT1, PBP1, XAC1 and LSM12 (PubMed:32532821). Forms a complex composed of at least MKT1L, PBP1, XAC1 and LSM12 (PubMed:32532821). Within the complex, interacts with MKT1 (via C-terminus); the interaction is direct (PubMed:24470144, PubMed:32532821). Interacts (via C-terminus) with ZC3H11; the interaction is direct (PubMed:24470144).
Involved in post-transcriptional regulation of gene expression (PubMed:24470144). Promotes mRNA stabilization by bridging poly(A)-binding protein to mRNAs (PubMed:24470144).
Belongs to the pterin-4-alpha-carbinolamine dehydratase family.
Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.
Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Binds 1 thiamine pyrophosphate per subunit.
Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Belongs to the very long-chain fatty acids dehydratase HACD family.
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).
Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This 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.
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.
Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
In the C-terminal section; belongs to the NnrD/CARKD family.
In the N-terminal section; belongs to the NnrE/AIBP family.
Activated by Ca(2+) (PubMed:18005666, PubMed:23506317, PubMed:28089596, PubMed:22529389). In response to calcium binding, the 280-loop, a disordered loop consisting of residues 269-275, undergoes a conformational change which stabilizes substrates in the active site (PubMed:22529389). The binding to the substrate triggers the release of the N-terminal region resulting in the activation of the enzyme (PubMed:22529389). Proteolytic cleavage is required for catalytic activity towards large protein substrates (PubMed:28089596).
Auto-proteolytic cleavage of the propeptide after Lys-55 and between the large and small subunits after Lys-268 is required for catalytic activity towards large protein substrates but is dispensable towards small oligopeptide substrates (PubMed:18005666, PubMed:28089596, PubMed:22529389). After processing, the propeptide and the large and small subunits remain associated by non-covalent bonds (PubMed:18005666). In vivo, the unprocessed enzyme appears to be the predominant form (By similarity).
Cysteine protease that cleaves specifically after arginine or lysine residues.
There are 2 calcium binding sites with high and low affinity, respectively.
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
Belongs to the universal ribosomal protein uS8 family.
Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN).
Component of the Golgi-associated retrograde protein (GARP) complex.
Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase VP55 that creates mRNA's poly(A) tail. In the presence of VP39, VP55 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.
Methyltransferase activity: Monomer, poly(A) polymerase activity: Heterodimer composed of a catalytic component, VP55, and a processivity factor, VP39. Interacts with Rap94 and NPH-I; these interactions might help linking transcription to capping and polyadenylation.
Common component of the spliceosome and rRNA processing machinery.
Belongs to the eukaryotic ribosomal protein eS6 family.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.
Belongs to the universal ribosomal protein uL4 family.
Involved in ribosomal large subunit assembly.
Belongs to the DODA-type extradiol aromatic ring-opening dioxygenase family.
Belongs to the RNA polymerase beta' chain family.
Belongs to the bacterial ribosomal protein bL21 family.
Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.
Ubiquitin-protein ligase which is mainly involved pre-mRNA splicing and DNA repair. Required for pre-mRNA splicing as component of the spliceosome.
Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Belongs to the actin family. ARP6 subfamily.
Belongs to the pseudouridine synthase TruB family.
Component of the conserved oligomeric Golgi complex.
Belongs to the RNA 3'-terminal cyclase family. Type 2 subfamily.
Belongs to the TTC30/dfy-1/fleer family.
Belongs to the MINDY deubiquitinase family. FAM188 subfamily.
Belongs to the eukaryotic ribosomal protein eL31 family.
Belongs to the eukaryotic release factor 1 family. Pelota subfamily.
May function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs.
Belongs to the V-ATPase D subunit family.
Belongs to the SMC family. SMC3 subfamily.
Belongs to the DNA mismatch repair MutL/HexB family.
Belongs to the steroid 5-alpha reductase family.
Required for 60S pre-ribosomal subunits export to the cytoplasm.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily.
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.
Belongs to the methyltransferase superfamily. HEN1 family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family.
Belongs to the eukaryotic ribosomal protein eL15 family.
Component of the RNA editing complex, a 1600 kDa complex composed of at least 20 proteins.
RNA editing in kinetoplastid mitochondria inserts and deletes uridylates at multiple sites in pre-mRNAs as directed by guide RNAs.
Belongs to the nucleoporin interacting component (NIC) family.
Belongs to the SRP receptor beta subunit family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. UbiG/COQ3 family.
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Belongs to the ANT/ATPSC lysine N-methyltransferase family.
Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family.
Pyridoxal 5'-phosphate (PLP)-binding protein, which may be involved in intracellular homeostatic regulation of pyridoxal 5'-phosphate (PLP), the active form of vitamin B6.
Belongs to the CND1 (condensin subunit 1) family.
Belongs to the protein prenyltransferase subunit alpha family.
Belongs to the methyltransferase superfamily. LCMT family.
Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Belongs to the PpiC/parvulin rotamase family. PIN4 subfamily.
Belongs to the universal ribosomal protein uS11 family.
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Belongs to the universal ribosomal protein uL2 family.
Belongs to the gamma-glutamylcyclotransferase family.
Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
Belongs to the class VI-like SAM-binding methyltransferase superfamily. Isoprenylcysteine carboxyl methyltransferase family.
Belongs to the universal ribosomal protein uL23 family.
Belongs to the universal ribosomal protein uL29 family.
Belongs to the protein kinase superfamily. RIO-type Ser/Thr kinase family.
Belongs to the methylthiotransferase family. CDKAL1 subfamily.
Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine.
Belongs to the class-II aminoacyl-tRNA synthetase family. Alax-L subfamily.
Belongs to the dolichyldiphosphatase family.
Required for efficient N-glycosylation. Necessary for maintaining optimal levels of dolichol-linked oligosaccharides. Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl monophosphate at a much lower rate. Does not act on phosphatidate.
Belongs to the ubiquitin-conjugating enzyme family. UFC1 subfamily.
E1-like enzyme which specifically catalyzes the second step in ufmylation. Ufmylation is involved in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress.
Component of the REH2-associated complex (REH2C) composed of helicase REH2, associated factors H2F1 and H2F2, and mRNAs at various editing stages; the formation of the complex is RNA-independent (PubMed:26769962, PubMed:31034523). Within the complex, interacts with REH2; the interaction is direct (PubMed:26769962). Interacts with various editing complexes including the RNA editing core (RECC) complex, the gRNA-binding (GRBC) complex (also known as the MRB1 complex) and the RNA editing mediator (REMC) complex (PubMed:26769962, PubMed:31034523).
Plays an important role in mitochondrial mRNA editing by promoting the assembly of the mRNA editosome (PubMed:26769962, PubMed:31034523). Facilitates the recruitment of mRNA to the REH2C complex and promotes the interaction between various editing complexes including REH2C, GRBC, REMC and RECC complexes (PubMed:26769962, PubMed:31034523).
RNAi-mediated knockdown at the procyclic stage causes a reduction in mitochondrial mRNA editing (PubMed:26769962). Formation of the REH2C complex is not affected but REH2C complex association with the GRBC, REMC, RECC complexes and with and pre-mRNA is impaired (PubMed:26769962). Integrity of the GRBC complex is not affected but GRBC complex association with the RECC complex and pre-mRNA is reduced (PubMed:26769962). Causes a slight decrease in REH2 protein levels (PubMed:26769962, PubMed:31034523). Does not affect the RNA unwinding activity of the REH2C complex (PubMed:26769962).
Component of the intraflagellar transport (IFT) complex required for transport of proteins in the motile cilium.
Belongs to the DZIP C2H2-type zinc-finger protein family.
Belongs to the glycosyl hydrolase 31 family.
Belongs to the acyl carrier protein (ACP) family.
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Belongs to the AB hydrolase superfamily. LDAH family.
Has a role in transport between endoplasmic reticulum and Golgi.
Arginine methyltransferase that specifically catalyzes the formation of omega-N monomethylarginine (MMA). Has activity toward multiple substrates in vitro. Able to mediate the arginine methylation of histones and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily.
Compared to PRMT7 orthologs in other metazoans, it is shorter and lacks the C-terminal part.
Expressed during both bloodstream (BF) and procyclic insect (PF) life cycle stages.
Present in large multiprotein complexes.
Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Arp2/3 complex plays a critical role in the control of cell morphogenesis via the modulation of cell polarity development.
Belongs to the universal ribosomal protein uS4 family.
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.
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 type IA topoisomerase family.
Belongs to the eukaryotic-type primase large subunit family.
DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.
Component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs).
Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ("psi") residues may serve to stabilize the conformation of rRNAs.
Belongs to the endoribonuclease YbeY family.
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.
Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs.
Component of the endosomal sorting complex required for transport II (ESCRT-II).
Belongs to the thymidylate kinase family.
Associates with the pre-60S ribosomal particle.
Belongs to the universal ribosomal protein uL10 family.
Component of the ribosome assembly machinery. Nuclear paralog of the ribosomal protein P0, it binds pre-60S subunits at an early stage of assembly in the nucleolus, and is replaced by P0 in cytoplasmic pre-60S subunits and mature 80S ribosomes.
Belongs to the ubiquitin-activating E1 family. UBA3 subfamily.
Catalytic subunit of the dimeric E1 enzyme, which activates NEDD8.
Belongs to the small heat shock protein (HSP20) family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family.
Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone.
In contrast to other lysine histone methyltransferases, it does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones.
Nuclear chaperone required for maturation and nuclear export of pre-60S ribosome subunits.
Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain vtc4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation. The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen. PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase. VTC1 contributes only 3 transmembrane domains to the complex. The VTC complex also plays a role in vacuolar membrane fusion.
Causes an abnormal morphology of acidocalcisomes, a significant decrease in the amount of polyP and a deficient response to hyposmotic stress.
The VTC core complex is an integral membrane heterooligomer composed of at least the catalytic subunit vtc4 and the accessory subunits vtc1 and vtc2. vtc1 is a small membrane protein without hydrophilic domain. Vtc2 and vtc4 are related and have 2 hydrophilic domains that face the cytosol, an N-terminal SPX domain and the central core domain. The central core in vtc4 is the catalytic domain.
Small GTPase-like component of the intraflagellar transport (IFT) complex B required for both anterograde and retrograde intraflagellar transport. May be involved in cargo loading of the retrograde transport.
Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.
Required for N-linked oligosaccharide assembly.
Belongs to the WD repeat CDC20/Fizzy family.
Belongs to the deoxyhypusine synthase family.
Heterotetramer formed by a homodimer of the non-catalytic regulatory subunit DHSp and a homodimer of the catalytic subunit DHSc where DHSc appears to bind spermidine and DHSp appears to bind NAD(+).
Lacks the conserved active site Lys, and therefore lacks catalytic activity.
RNAi-mediated knockdown causes cell growth arrest followed by death, loss of DHSp expression and a failure to sustain infection in mice.
Required for the activation and stability of deoxyhypusine synthase DHSc. Required for cell growth and survival.
Belongs to the transaldolase family. Type 1 subfamily.
Catalyzes the rate-limiting step of the non-oxidative phase in the pentose phosphate pathway. Catalyzes the reversible conversion of sedheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into erythrose-4-phosphate and beta-D-fructose 6-phosphate.
Belongs to the 5'-AMP-activated protein kinase beta subunit family.
Belongs to the eukaryotic ribosomal protein eL14 family.
Belongs to the eukaryotic diacylglycerol kinase family.
Belongs to the AB hydrolase superfamily. AB hydrolase 4 family.
Belongs to the PDK/BCKDK protein kinase family.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. YchF/OLA1 subfamily.
Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP.
Belongs to the glycosyltransferase 22 family. PIGB subfamily.
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2-GlcN-acyl-PI during GPI precursor assembly (By similarity).
The protozoan parasite evades the immune response of mammalian hosts and digestion in the gut of the insect vector by means of its coat proteins tethered to the cell surface via GPI-anchors. GPI10 is essential for growth of mammalian stage bloodstream form, while procyclic form (insect stage parasites) are viable but grow slower, suggesting that inhibition of GPI synthesis may be an effective chemotherapy against African trypanosomiasis (By similarity).
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.
Belongs to the ubiquitin-activating E1 family. ULA1 subfamily.
Belongs to the BPG-independent phosphoglycerate mutase family.
Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
NAD(+)-dependent glutamate dehydrogenase which degrades glutamate to ammonia and alpha-ketoglutarate.
Belongs to the SEC23/SEC24 family. SEC23 subfamily.
Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Belongs to the DEAD box helicase family. DDX47/RRP3 subfamily.
Component of a complex composed of CBF5, GAR1, NHP2, MTR1, NOP10 and Tb11.01.8210.
S-adenosyl-L-methionine-dependent methyltransferase that mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of spliced leader and U1 small nuclear RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped RNA to produce m(7)GpppNmp (cap1). Cap1 modification is linked to higher levels of translation. Recognizes a guanosine cap on RNA independent of its N(7) methylation status.
Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. May methylate the carboxyl group of leucine residues to form alpha-leucine ester residues.
Belongs to the neutral sphingomyelinase family.
Belongs to the small GTPase superfamily. SAR1 family.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family.
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Belongs to the glucose-6-phosphate 1-epimerase family.
Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein.
Belongs to the TRAPP small subunits family.
Part of the multisubunit transport protein particle (TRAPP) complex.
Belongs to the peptidase M67A family. CSN5 subfamily.
Essential for the assembly of the distal half of centrioles, required for centriole elongation.
Belongs to the ubiquitin-activating E1 family.
Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins.
Belongs to the ATPase epsilon chain family.
Belongs to the universal ribosomal protein uL5 family.
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase (PubMed:25040552). Together with the diflavin oxidoreductase, 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 (By similarity).
The C-terminal domain binds 2 Fe-S clusters 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.
Essential component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. Required for the maturation of extramitochondrial Fe/S proteins.
Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase complex; essential for the ER localization.
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 actin-binding proteins ADF family.
Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins.
Belongs to the bacterial ribosomal protein bL33 family.
Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm.
Belongs to the UTP23/FCF1 family. FCF1 subfamily.
Belongs to the V-ATPase F subunit family.
Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase type II family.
Belongs to the queuosine salvage protein family.
Belongs to the eukaryotic RPC3/POLR3C RNA polymerase subunit family.
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.
Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.
In the C-terminal section; belongs to the thymidylate synthase family.
In the N-terminal section; belongs to the dihydrofolate reductase family.
Belongs to the queuine tRNA-ribosyltransferase family. QTRT2 subfamily.
Heterodimer of a catalytic subunit and an accessory subunit.
Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Belongs to the GMC oxidoreductase family.
Belongs to the DEAD box helicase family. DDX18/HAS1 subfamily.
Belongs to the glutamate--cysteine ligase type 3 family.
Belongs to the glycosyltransferase group 1 family.
Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate).
The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Belongs to the protein kinase superfamily. ADCK protein kinase family.
Belongs to the DNA repair enzymes AP/ExoA family.
Probably binds two magnesium or manganese ions 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. Likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity.
Component of the EKC/KEOPS complex; the whole complex dimerizes.
Belongs to the eukaryotic ribosomal protein eL21 family.
Belongs to the HMG-CoA reductase family.
Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.
Belongs to the CND3 (condensin subunit 3) family.
Belongs to the sirtuin family. Class II subfamily.
NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of acyl groups from lysine residues.
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Belongs to the complex I 51 kDa subunit family.
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Belongs to the replication factor A protein 2 family.
Belongs to the 6-phosphogluconate dehydrogenase family.
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.
Belongs to the complex I NDUFA12 subunit 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 ATP-dependent DNA ligase family.
Belongs to the ClpA/ClpB family. Torsin subfamily.
Belongs to the WD repeat PRL1/PRL2 family.
Belongs to the eukaryotic ribosomal protein eS19 family.
Belongs to the non-repetitive/WGA-negative nucleoporin family.
Belongs to the acetyltransferase family. ECO subfamily.
Belongs to the glycosyl hydrolase 85 family.
Belongs to the V-ATPase 116 kDa subunit family.
Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP1/NBP35 subfamily.
Belongs to the helicase family. RAD3/XPD subfamily.
Belongs to the MsrA Met sulfoxide reductase family.
Belongs to the spermidine/spermine synthase family.
Belongs to the ubiquitin-activating E1 family. UBA5 subfamily.
Belongs to the WD repeat coronin family.
Belongs to the eukaryotic-type primase small subunit family.
Belongs to the type IB topoisomerase family.
Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
The glycine cleavage system catalyzes the degradation of glycine.
Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Belongs to the eukaryotic ribosomal protein eL42 family.
Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.
Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Belongs to the eukaryotic ribosomal protein eL33 family.
Belongs to the eukaryotic RPC34/RPC39 RNA polymerase subunit family.
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 a tRNA-binding adapter protein for full tRNA acetyltransferase activity but not for 18S rRNA acetylation.
Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport (By similarity).
The vault ribonucleoprotein particle is a huge (400 A x 670 A) cage structure of 12.9 MDa. It consists of a dimer of half-vaults, with each half-vault comprising 39 identical major vault protein (MVP) chains, PARP4 and one or more vault RNAs (vRNAs) (By similarity).
Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle.
Although it belongs to the XPG/RAD2 endonuclease family, only two of the seven Asp residues involved in Mg(2+) binding are conserved suggesting that it has no nuclease activity.
Forms a complex composed of at least MKT1, PBP1, XAC1 and LSM12 (PubMed:32532821). Within the complex, interacts (via C-terminus) with PBP1; the interaction is direct (PubMed:32532821, PubMed:24470144). Interacts with RNA-binding protein ZC3H11 (via MKT1-binding motif); the interaction is direct (PubMed:32532821, PubMed:24470144). May interact with RNA-binding proteins CFB1 and CFB2 (PubMed:32532821). Interacts with the EIF4E6-EIF4G5 translation initiation complex via EIF4G5; the interaction with EIF4G5 is direct (PubMed:32532821).
Involved in post-transcriptional regulation of gene expression (PubMed:24470144). Promotes mRNA stabilization by recruiting a complex containing PBP1, LSM12 and XAC1 to mRNAs (PubMed:24470144, PubMed:32532821). Recruited to mRNAs by sequence-specific RNA binding proteins (PubMed:24470144). May regulate translation through interactions with the EIF4E6-EIF4G5 translation initiation complex (PubMed:32532821).
RNAI-mediated knockdown in the bloodstream form is lethal (PubMed:24470144). RNAi-mediated knockdown in the procyclic form has no effect on viability (PubMed:24470144).
Belongs to the complex I NDUFB11 subunit family.
Belongs to the complex I NDUFA5 subunit family.
Gene knockout results in significant reduction of flagellar beating and cell swimming, and absence of outer dynein arms in the distal region of flagellum axoneme. Cell motility is characterized by an erratic swimming pattern with altered propagation of the tip-to-base wave, increased frequency of base-to-tip waves, and frequent tumbling typical of outer dynein arm mutants.
Required for the assembly of dynein arms in the distal portion of flagellum axoneme.
Belongs to the phosphoenolpyruvate carboxykinase (ATP) family.
Belongs to the pyrroline-5-carboxylate reductase family.
Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. May also be involved in ribosome biogenesis.
Monomer. Associates with the 60S ribosomal subunit.
Expressed in the bloodstream form (at protein level).
Forms a complex composed of at least MKT1, PBP1, XAC1 and LSM12 (PubMed:32532821). Forms a complex composed of at least MKT1L, PBP1, XAC1 and LSM12 (PubMed:32532821).
RNAi-mediated knockdown in the bloodstream form abolishes cell population growth.
Belongs to the histone deacetylase family. HD Type 1 subfamily.
Belongs to the amino acid-polyamine-organocation (APC) superfamily. Polyamine:cation symporter (PHS) (TC 2.A.3.12) family.
Belongs to the PI3/PI4-kinase family. ATM subfamily.
Belongs to the poly(ADP-ribose) glycohydrolase family.
Belongs to the acetyltransferase ATAT1 family.
Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released.
Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.
Belongs to the vitamin-B12 independent methionine synthase family.
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment.
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 diacylglycerol acyltransferase family.
Belongs to the ERCC1/RAD10/SWI10 family.
Allosterically activated by DHSp. Inhibited by spermididine analog N1-guanyl-1,7-diamineoheptane (GC7).
In association with the non-catalytic regulatory subunit DHSp, 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 eIF5A precursor protein to form the intermediate deoxyhypusine residue. Regulates protein levels of its regulatory subunit DHSp. Required for cell growth and survival.
The binding sites for NAD(+) are contained in the regulatory subunit DHSp.
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 CDP-alcohol phosphatidyltransferase class-II family.
Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Belongs to the clathrin light chain family.