FUNCTION: Translation initiation factor that is able to deliver tRNA to the P-site of the eukaryotic ribosome in a GTP-independent manner. The binding of Met-tRNA(I) occurs after the AUG codon finds its position in the P-site of 40S ribosomes, the situation that takes place during initiation complex formation on some specific RNAs. Its activity in tRNA binding with 40S subunits does not require the presence of the aminoacyl moiety. Possesses the unique ability to deliver non-Met (elongator) tRNAs into the P-site of the 40S subunit. In addition to its role in initiation, can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF2D family.


FUNCTION: Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection. The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel. Binds to the terminase subunits to form the packaging machine. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the phage portal family. PBSX subfamily.


FUNCTION: Cytochrome c oxidase subunit which plays a role in assembly of respiratory supercomplexes. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the RCF1 family.


FUNCTION: Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TtcA family.


FUNCTION: [Isoform a]: G-protein coupled receptor which is activated by neuropeptides PDF-1 and PDF-2 (PubMed:18390545). Probably acts through the G-alpha(s) type of G proteins to elevate cAMP levels (PubMed:18390545). FUNCTION: G-protein coupled receptor for PDF neuropeptides (PubMed:18390545). Plays a role in responses to environmental signals, including chemicals and touch, and in modulating locomotory behaviors (PubMed:30024377, PubMed:18390545, PubMed:14551910, PubMed:22579613, PubMed:23143519, PubMed:23972393, PubMed:26113231). Capable of transducing signals via an adenylate cyclase acy-1 cAMP-dependent pathway (PubMed:23972393, PubMed:30024377). Required to regulate the sex-specific expression of TGFbeta-like daf-7 in the ASJ chemosensory neurons, perhaps acting via acy-1 (PubMed:30024377). Involved in modulating mate searching behavior independent of nutritional status (PubMed:18390545, PubMed:22579613, PubMed:23143519, PubMed:14551910). In the presence of food, plays a role in initiating and extending exploratory roaming behavior, perhaps acting in AIY, RIM, RIA, and other neurons, in opposition to 5-hydroxytryptamine (serotonin) signaling (PubMed:23972393). Involved in mediating arousal from the sleep-like state called lethargus, which occurs during molting between larval and adult stages, in part by regulating touch sensitivity (PubMed:18390545, PubMed:23764289). May play a role in circadian rhythms of locomotor activity (PubMed:26113231). FUNCTION: [Isoform b]: G-protein coupled receptor which is activated by neuropeptides PDF-1 and PDF-2 (PubMed:18390545). Probably acts through the G-alpha(s) type of G proteins to elevate cAMP levels (PubMed:18390545). FUNCTION: [Isoform c]: G-protein coupled receptor which is activated by neuropeptides PDF-1 and PDF-2; however, activation is lower compared to isoforms a and b (PubMed:18390545). Probably inhibits cAMP levels through the G-alpha(i/o) type of G proteins (PubMed:18390545). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 2 family.


FUNCTION: Catalyzes the transfer of an acetyl group from acetyl-CoA to tetrahydrodipicolinate. SIMILARITY: Belongs to the transferase hexapeptide repeat family. DapH subfamily.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase gamma chain family.


FUNCTION: [Surface protein]: The surface protein (SU) attaches the virus to the host cell entry receptor TVC (PubMed:16051833). This interaction triggers the refolding of the transmembrane protein (TM) thereby unmasking its fusion peptide and the formation of a reactive thiolate on Cys-100 to activate its fusogenic potential. Fusion occurs at the host cell plasma membrane (By similarity). FUNCTION: [Transmembrane protein]: The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre- hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm. SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein Host cell membrane; Peripheral membrane protein Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. Both proteins are thought to be concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N- terminus of Gag (By similarity). SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the Alpharetroviruses envelope glycoprotein family.


SIMILARITY: In the C-terminal section; belongs to the HAD-like hydrolase superfamily. MasA/MtnC family. SIMILARITY: In the N-terminal section; belongs to the aldolase class II family. MtnB subfamily.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the GcvT family. CAF17 subfamily.


FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the extracellular potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the KdpA family.


FUNCTION: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. Required for normal plant growth. May be required for rapid internodal elongation in deepwater rice during submergence. SUBCELLULAR LOCATION: Secreted, cell wall Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the expansin family. Expansin A subfamily.


FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prokaryotic pantothenate kinase family.


FUNCTION: Acts as a transcriptional activator. Stimulates the promoter of the alpha-glycoprotein gene. Transcriptional regulatory protein involved in the control of cell differentiation in developing lymphoid and neural cell types (By similarity). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DapA family. NanA subfamily.


FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.


FUNCTION: Converts farnesyl diphosphate to alpha-bisabolene (PubMed:28096378). Involved in defensive oleoresin formation in conifers in response to insect attack or other injury (By similarity). Involved in sesquiterpene (C15) olefins biosynthesis (By similarity). SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.


FUNCTION: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit SdhB of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the complex I LYR family. SDHAF3 subfamily.


FUNCTION: Non-receptor type tyrosine-specific phosphatase that dephosphorylates receptor protein tyrosine kinases including INSR, EGFR, CSF1R, PDGFR. Also dephosphorylates non-receptor protein tyrosine kinases like JAK1, JAK2, JAK3, Src family kinases, STAT1, STAT3 and STAT6 either in the nucleus or the cytoplasm. Negatively regulates numerous signaling pathways and biological processes like hematopoiesis, inflammatory response, cell proliferation and differentiation, and glucose homeostasis. Plays a multifaceted and important role in the development of the immune system. Functions in T- cell receptor signaling through dephosphorylation of FYN and LCK to control T-cells differentiation and activation. Dephosphorylates CSF1R, negatively regulating its downstream signaling and macrophage differentiation. Negatively regulates cytokine (IL2/interleukin-2 and interferon)-mediated signaling through dephosphorylation of the cytoplasmic kinases JAK1, JAK3 and their substrate STAT1, that propagate signaling downstream of the cytokine receptors. Also regulates the IL6/interleukin-6 and IL4/interleukin-4 cytokine signaling through dephosphorylation of STAT3 and STAT6 respectively. In addition to the immune system, it is involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth. Activated by the integrin ITGA1/ITGB1, it dephosphorylates EGFR and negatively regulates EGF signaling. Dephosphorylates PDGFRB and negatively regulates platelet-derived growth factor receptor-beta signaling pathway and therefore cell proliferation. Negatively regulates tumor necrosis factor-mediated signaling downstream via MAPK through SRC dephosphorylation. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of the hepatocyte growth factor receptor MET. Also plays an important role in glucose homeostasis. For instance, negatively regulates the insulin receptor signaling pathway through the dephosphorylation of INSR and control gluconeogenesis and liver glucose production through negative regulation of the IL6 signaling pathways. May also bind DNA (By similarity). SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum Nucleus membrane. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus Cytoplasm Cell membrane Note=Predominantly localizes to chromatin. Able to shuttle between the nucleus and the cytoplasm and to dephosphorylate plasma membrane receptors. Recruited by activated ITGA1 at the plasma membrane (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum-Golgi intermediate compartment Note=Targeted to the endoplasmic reticulum by its C-terminal hydrophobic region. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class 1 subfamily.


FUNCTION: Central component of a redox-sensitive mitochondrial intermembrane space import machinery which is required for the biogenesis of respiratory chain complexes. Functions as chaperone and catalyzes the formation of disulfide bonds in substrate proteins, such as COX17, COX19, MICU1 and COA7. Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Required for the import of COA7 in the IMS. Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria. The oxidized form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with the reduced precursor protein, resulting in oxidation of the precursor protein that now contains an intramolecular disulfide bond and is able to undergo folding in the IMS. Reduced CHCHD4/MIA40 is then reoxidized by GFER/ERV1 via a disulfide relay system. Mediates formation of disulfide bond in MICU1 in the IMS, promoting formation of the MICU1- MICU2 heterodimer that regulates mitochondrial calcium uptake. SUBCELLULAR LOCATION: Mitochondrion intermembrane space.


FUNCTION: High-affinity potassium transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HAK/KUP transporter (TC 2.A.72.3) family.


FUNCTION: Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uS15 family.


FUNCTION: Hydrolyzes 1,4-beta-glycosyl linkages of 1,4-beta-glucans and 1,3-1,4-beta-glucans. Possesses broad substrate specificity for hemicelluloses of type II cell walls. Substrate preference is carboxymethyl-cellulose > 1,3-1,4-beta-glucan > lichenan > arabinoxylan > phospho-swollen cellulose > xylan > glucomannan. May participate in lateral root development. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.


FUNCTION: General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation (By similarity). SIMILARITY: Belongs to the TBP family.


FUNCTION: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family.


FUNCTION: Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 20 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Binds to erythroid progenitor cells expressing high levels of P antigen and uses host ITGA5-ITGB1 and XRCC5/Ku80 autoantigen as coreceptors on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region. The additional N- terminal region of isoform Minor capsid protein VP1, called VP1u, may serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus. SUBCELLULAR LOCATION: [Isoform Minor capsid protein VP1]: Virion Host nucleus Host cytoplasm. SUBCELLULAR LOCATION: [Isoform Major capsid protein VP2]: Virion Host nucleus Host cytoplasm. SIMILARITY: Belongs to the parvoviridae capsid protein family.


FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PTH2 family.


FUNCTION: May help in the organization of the PsaL subunit. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsaI family.


FUNCTION: Inactive GDP-bound Rho GTPases reside in the cytosol, are found in a complex with Rho GDP-dissociation inhibitors (Rho GDIs), and are released from the GDI protein in order to translocate to membranes upon activation. SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein Note=Associated with the membrane when activated. SIMILARITY: Belongs to the small GTPase superfamily. Rho family.


FUNCTION: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. SIMILARITY: Belongs to the eIF-2-alpha family.


FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. May indirectly enhance GAP-43 expression by binding to the NGF- regulatory region of its mRNA (By similarity). FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. May indirectly enhance GAP-43 expression. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the endosulfine family.


FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N- acyltransferase subfamily.


FUNCTION: Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opiod activity, it is 700 times more potent than Leu-enkephalin (By similarity). FUNCTION: Leumorphin has a typical opiod activity and may have anti- apoptotic effect. FUNCTION: Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the opioid neuropeptide precursor family.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eS4 family.


FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as the reductant. SIMILARITY: Belongs to the thymidylate synthase ThyX family.


FUNCTION: Hydrolyzes linear guanidino acids to form urea and the corresponding amines. Displays specificity for substrates having a negatively charged head group and short chains including taurocyamine, guanidino propanoic and butanoic acids. May protect cells by detoxifying potentially harmful amounts of guanidino acids. Metabolizes L-arginine with low efficiency. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.


FUNCTION: Involved in the export of arginine. Important to control the intracellular level of arginine and the correct balance between arginine and lysine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the LysE/ArgO transporter (TC 2.A.75) family.


FUNCTION: Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. SIMILARITY: Belongs to the universal ribosomal protein uS13 family.


FUNCTION: Translation initiation regulator which may repress non-AUG initiated translation and repeat-associated non-AUG (RAN) initiated translation by acting as a competitive inhibitor of eukaryotic translation initiation factor 5 (EIF5) function. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the BZW family.


FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0391 family.


FUNCTION: Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine- Dalgarno cleft in the 70S ribosome. SIMILARITY: Belongs to the universal ribosomal protein uS11 family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SprT family.


FUNCTION: Regulatory subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Necessary for cell cycle progression through the S-M checkpoint. Overexpression of NAE1 causes apoptosis through deregulation of NEDD8 conjugation (By similarity). The covalent attachment of NEDD8 to target proteins is known as 'neddylation' and the process is involved in the regulation of cell growth, viability and development. SUBCELLULAR LOCATION: Cell membrane Note=Colocalizes with APP in lipid rafts. SIMILARITY: Belongs to the ubiquitin-activating E1 family. ULA1 subfamily.


FUNCTION: Monoheme c-type cytochrome. Probable electron donor to membrane cytochrome oxidase and to periplasmic nitrite reductase. SUBCELLULAR LOCATION: Periplasm.


FUNCTION: Has an important role in stress fiber formation induced by active diaphanous protein homolog 1 (DRF1). Induces microspike formation, in vivo (By similarity). In vitro, stimulates N-WASP-induced ARP2/3 complex activation in the absence of CDC42 (By similarity). May play an important role in the maintenance of sarcomeres and/or in the assembly of myofibrils into sarcomeres. Implicated in regulation of actin polymerization and cell adhesion. Plays a role in angiogenesis. SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with DRF1 at membrane ruffles, and with Nck at Z-disks in mature cardiac myocytes.


FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln). SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.


FUNCTION: Necessary for the splicing of pre-mRNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the splicing factor SR family.


FUNCTION: Involved in the biosynthesis of BC325, a rapamycin analog containing a 3-hydroxybenzoate starter unit. Catalyzes the hydrolysis of chorismate via an intramolecular mechanism to yield 3- hydroxybenzoate (3HBA). SIMILARITY: Belongs to the FkbO/Hyg5 family.


SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily.


FUNCTION: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CheZ family.


FUNCTION: May be a lipoprotein-borne regulator of either the coagulation or the complement cascades. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.


FUNCTION: Xylosyltransferase specific to UDP-D-xylose that accepts both cellopentaose and cellohexaose as substrates, with a better use of cellohexaose, to produce xyloglucan. Adds preferentially the first xylosyl residue to the fourth glucosyl residue from the reducing end of both acceptors. Transfer one xylose mainly to the second glucose residue from the non-reducing end. The acceptor should have a minimum of four glucose residues (PubMed:16982611, PubMed:18544630). Associates with other xyloglucan-synthesizing enzymes to form multiprotein complexes for xyloglucan synthesis in the Golgi (PubMed:25392066). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 34 family.


FUNCTION: Regulates protein folding in the endoplasmic reticulum (ER) lumen. Forms a complex in the ER with SDF2 and MED37A/BIP1 which is required for the proper accumulation and function of the surface- exposed leucine-rich repeat receptor kinases EFR involved in pathogen- associated molecular pattern (PAMP) triggered immunity. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.


FUNCTION: Required for the function of many mechanoreceptors. Modulate mechanotransduction channels and acid-sensing ion channels (ASIC) proteins. Potentiates PIEZO1 and PIEZO2 function by increasing their sensitivity to mechanical stimulations. SUBCELLULAR LOCATION: Cell membrane; Single-pass type III membrane protein Note=Detected in lipid rafts, in apical dendrites and in olfactory cilia. SIMILARITY: Belongs to the band 7/mec-2 family.


FUNCTION: Transcription activator that binds DNA on 5'-ACTCTAC-3' and promotes auxin homeostasis-regulating gene expression (e.g. YUC genes), as well as genes affecting stamen development, cell expansion and timing of flowering. Synergistically with other SHI-related proteins, regulates gynoecium, stamen and leaf development in a dose-dependent manner, controlling apical-basal patterning. Promotes style and stigma formation, and influences vascular development during gynoecium development. May also have a role in the formation and/or maintenance of the shoot apical meristem (SAM). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SHI protein family.


FUNCTION: Promotes megakaryocyte differentiation by enhancing ERK and JNK signaling as well as up-regulating RUNX1 and FLI1 expression (PubMed:24681962). Represses NF-kappa-B transcriptional activity by inhibiting phosphorylation of RELA at 'Ser-536' (PubMed:24681962). May be involved in early neuronal development (By similarity). FUNCTION: Promotes megakaryocyte differentiation by enhancing ERK and JNK signaling as well as up-regulating RUNX1 and FLI1 expression (By similarity). Represses NF-kappa-B transcriptional activity by inhibiting phosphorylation of RELA at 'Ser- 536' (By similarity). May be involved in early neuronal development (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MTURN family.


FUNCTION: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones. FUNCTION: Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines. SIMILARITY: Belongs to the azoreductase type 1 family.


FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the bacterial CoaD family.


FUNCTION: Converts 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol) into 3-(2,3- dihydroxylphenyl)propanoic acid (DHPP) and 2,3-dihydroxicinnamic acid (DHCI), respectively. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. SIMILARITY: Belongs to the universal ribosomal protein uS8 family.


FUNCTION: Required to stabilize the cell wall in the absence of multiple GPI-anchored mannoproteins. SUBCELLULAR LOCATION: Secreted, cell wall. Cell surface.


FUNCTION: Specifically methylates the guanine in position 1835 (m2G1835) of 23S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RlmG family.


FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.


FUNCTION: Catalyzes the oxidation 4-aminobutanal (gamma- aminobutyraldehyde) to 4-aminobutanoate (gamma-aminobutyrate or GABA). This is the second step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate via 4- aminobutanal. Also functions as a 5-aminopentanal dehydrogenase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. SIMILARITY: Belongs to the aldehyde dehydrogenase family. Gamma- aminobutyraldehyde dehydrogenase subfamily.


FUNCTION: Interferes with one step of hemostasis (modulation of platelet aggregation, or coagulation cascade, for example). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snaclec family.


FUNCTION: Involved in resistance toward heavy metals. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CutA family.


FUNCTION: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Involved in K(+) homeostasis under low-K(+) stress. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Targeted to the tonoplast when interacting with CBL2 or CBL3. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.


FUNCTION: Involved in restoring normal CheY-P levels by dephosphorylating CheY-P. Inhibits CheD by incorporating in its fold a structural motif that mimics a CheD substrate recognition site to bait and inactivate it. SIMILARITY: Belongs to the CheC family.


FUNCTION: This phospholipase A2 inhibitor binds directly phospholipase A2 in the presence or absence of calcium. SUBCELLULAR LOCATION: Secreted Note=Secreted in plasma. SIMILARITY: Belongs to the alpha-type phospholipase A2 inhibitor family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase family.


FUNCTION: Transcriptional repressor which functions as a downstream effector of Notch signaling. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HEY family.


FUNCTION: Purine salvage pathway enzyme which catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1- diphosphate (PRPP) to the N9 position of hypoxanthine to yield IMP (inosine 5'-monophosphate). To a lesser extent, can also act on guanine leading to GMP, but shows a highly less efficient activity with xanthine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family.


FUNCTION: May be involved in chemotaxis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CheB family.


SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein.


FUNCTION: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Note=In myofibrils with sarcomeric structure, localizes to the pointed end of actin thin filaments (PubMed:25250574). SIMILARITY: Belongs to the tropomodulin family.


FUNCTION: Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as histone chaperone that facilitates deposition of histone H3.3. Acts as targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Plays a role as a positive regulator of the heat shock transcription factor HSF1 activity during the stress protein response (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleoplasm Nucleus, PML body Nucleus, nucleolus Chromosome, centromere Note=Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli. Colocalizes with histone H3.3, ATRX, HIRA and ASF1A at PML-nuclear bodies. Colocalizes with a subset of interphase centromeres, but is absent from mitotic centromeres. Detected in cytoplasmic punctate structures. Translocates from the nucleus to the cytoplasm upon glucose deprivation or oxidative stress. Colocalizes with RASSF1 in the nucleus. Colocalizes with USP7 in nucleoplasma with accumulation in speckled structures. SIMILARITY: Belongs to the DAXX family.


FUNCTION: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HAK/KUP transporter (TC 2.A.72) family.


FUNCTION: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. SUBCELLULAR LOCATION: Virion Host cytoplasm, host perinuclear region Host cell membrane; Lipid-anchor; Cytoplasmic side Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. SIMILARITY: Belongs to the arenaviridae Z protein family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the uridine kinase family.


FUNCTION: Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. SUBCELLULAR LOCATION: Cytoplasm Note=Localizes at mid-cell. SIMILARITY: Belongs to the ZapA family. Type 1 subfamily.


FUNCTION: Probably involved in the biosynthesis of germacrene-derived sesquiterpene lactones. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peptidase S41A family.


FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).


FUNCTION: Specifically methylates the adenine in position 1618 of 23S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. METTL16/RlmF family.


FUNCTION: Thiol protease inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cystatin family.


FUNCTION: Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans (PubMed:21961565, PubMed:21502315, PubMed:23106432, PubMed:22123821, PubMed:25478983, PubMed:27966912, PubMed:30420606, PubMed:30457329). Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans (By similarity). Required for proper brain and neuronal development (PubMed:32001716). SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.


FUNCTION: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 43 family.


FUNCTION: Transcription factor that can function as an activator or repressor depending on its binding partners, and by targeting negative regulators of cell cycle progression. Has been shown to bind to the promoters of adenovirus major late protein and cyclin D1 and activate transcription. Required for early embryonic development during gastrulation. Plays a critical role in early lymphocyte development, where it is essential to prevent apoptosis in lymphoid precursors, allowing them to survive in response to IL7 and undergo proper lineage commitment. Represses RB1 transcription; this repression can be blocked by interaction with ZBTB49 (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family.


FUNCTION: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm. SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily.


FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A. SIMILARITY: Belongs to the protein prenyltransferase subunit alpha family.


FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.


FUNCTION: Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism.


FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase HII family. RnhC subfamily.


FUNCTION: Probable lipolytic acyl hydrolase (LAH), an activity which is thought to be involved in the response of tubers to pathogens. SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the patatin family.


FUNCTION: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thioester dehydratase family. FabZ subfamily.


FUNCTION: Calcium- and diacylglycerol-independent serine/threonine- protein kinase that functions in phosphatidylinositol 3-kinase (PI3K) pathway and mitogen-activated protein (MAP) kinase cascade, and is involved in NF-kappa-B activation, mitogenic signaling, cell proliferation, cell polarity, inflammatory response and maintenance of long-term potentiation (LTP). Upon lipopolysaccharide (LPS) treatment in macrophages, or following mitogenic stimuli, functions downstream of PI3K to activate MAP2K1/MEK1-MAPK1/ERK2 signaling cascade independently of RAF1 activation. Required for insulin-dependent activation of AKT3, but may function as an adapter rather than a direct activator. Upon insulin treatment may act as a downstream effector of PI3K and contribute to the activation of translocation of the glucose transporter SLC2A4/GLUT4 and subsequent glucose transport in adipocytes. In EGF-induced cells, binds and activates MAP2K5/MEK5- MAPK7/ERK5 independently of its kinase activity and can activate JUN promoter through MEF2C. Through binding with SQSTM1/p62, functions in interleukin-1 signaling and activation of NF-kappa-B with the specific adapters RIPK1 and TRAF6. Participates in TNF-dependent transactivation of NF-kappa-B by phosphorylating and activating IKBKB kinase, which in turn leads to the degradation of NF-kappa-B inhibitors. In migrating astrocytes, forms a cytoplasmic complex with PARD6A and is recruited by CDC42 to function in the establishment of cell polarity along with the microtubule motor and dynein. In association with FEZ1, stimulates neuronal differentiation in PC12 cells. In the inflammatory response, is required for the T-helper 2 (Th2) differentiation process, including interleukin production, efficient activation of JAK1 and the subsequent phosphorylation and nuclear translocation of STAT6. May be involved in development of allergic airway inflammation (asthma), a process dependent on Th2 immune response. In the NF-kappa-B-mediated inflammatory response, can relieve SETD6-dependent repression of NF- kappa-B target genes by phosphorylating the RELA subunit at 'Ser-311'. Phosphorylates VAMP2 in vitro (By similarity). SUBCELLULAR LOCATION: Cytoplasm Endosome Cell junction Membrane; Peripheral membrane protein Note=In the retina, localizes in the terminals of the rod bipolar cells (By similarity). Associated with endosomes (By similarity). Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction (By similarity). Colocalizes with VAMP2 and WDFY2 in intracellular vesicles (By similarity). Transiently translocates to the membrane of CA1 hippocampal cells in response to the induction of long term potentiation (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.


FUNCTION: Radical SAM enzyme involved in the synthesis of archaeosine, a modified nucleoside present in the dihydrouridine loop (D-loop) of archaeal tRNAs. Catalyzes the cleavage of the C(epsilon)-N bond of the lysine moiety of q0kN15-tRNA, leading to the formation of archaeosine at position 15 in tRNAs. SIMILARITY: Belongs to the radical SAM superfamily. RaSEA family.


FUNCTION: Transfers the UMP unit from UDP-glucose (UDP-Glc) to Gal1P. Can also transfer the UMP unit to GlcNAc1P and GalNAc1P. Involved in the general galactose metabolism, and also involved in the lacto-N- biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase type 2 family.


FUNCTION: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). SIMILARITY: Belongs to the HPrK/P family.


FUNCTION: Major structural component of PMF fimbriae. SUBCELLULAR LOCATION: Fimbrium. SIMILARITY: Belongs to the fimbrial protein family.


FUNCTION: Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.


FUNCTION: Probable non-functional open reading frame (ORF) of V region of the variable domain of T cell receptor (TR) beta chain (PubMed:24600447). Non-functional ORF generally cannot participate in the synthesis of a productive T cell receptor (TR) chain due to altered V-(D)-J or switch recombination and/or splicing site (at mRNA level) and/or conserved amino acid change (protein level) (PubMed:9619395). Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens (PubMed:25493333). Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation (PubMed:23524462). The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity (PubMed:15040585). SUBCELLULAR LOCATION: Cell membrane.


FUNCTION: May play a role in cardiomyocyte proliferation through paracrine signaling and activation of the PPI3K-AKT-CDK7 signaling cascade. SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPI-coated vesicle. Golgi apparatus. Secreted. SIMILARITY: Belongs to the DIPK family.


FUNCTION: Involved in the activation of the plasma membrane proton- ATPase (PMA1) by glucose.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-lactamase family.


FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA. SIMILARITY: Belongs to the alanine racemase family.


FUNCTION: Probable GTP-binding protein that possesses GTPase activity. May play a role in endothelial cell polarity and endothelial barrier function (By similarity). SUBCELLULAR LOCATION: Cell membrane Cytoplasm, cytosol Cell junction Note=May shuttle between plasma membrane and cytosol. SIMILARITY: Belongs to the small GTPase superfamily. Ras family.


FUNCTION: One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL3 family.


FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PanD family.


FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. Is the predominant 6-P-gluconate dehydrogenase isoenzyme in B.subtilis during growth on glucose and gluconate. SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.


FUNCTION: ATP-binding RNA helicase involved in transcription elongation and required for the export of mRNA out of the nucleus. SUB2 also plays a role in pre-mRNA splicing and spliceosome assembly. May be involved in rDNA and telomeric silencing, and maintenance of genome integrity (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DEAD box helicase family. DECD subfamily.


FUNCTION: Component of the intraflagellar transport (IFT) complex B: together with IFT74, forms a tubulin-binding module that specifically mediates transport of tubulin within the cilium. Binds tubulin via its CH (calponin-homology)-like region (PubMed:23990561). Required for ciliogenesis (PubMed:27666822, PubMed:23990561). Required for proper regulation of SHH signaling (PubMed:27666822). Plays an important role during spermatogenesis by modulating the assembly and elongation of the sperm flagella (By similarity). SUBCELLULAR LOCATION: Cell projection, cilium Cytoplasm. SIMILARITY: Belongs to the IFT81 family.


FUNCTION: Serine protease. SIMILARITY: Belongs to the peptidase S8 family.


FUNCTION: Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily.


FUNCTION: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TatA/E family.


FUNCTION: Gas vesicles are hollow, gas filled proteinaceous nanostructures found in some microorganisms. During planktonic growth they allow positioning of the organism at a favorable depth for light or nutrient acquisition. GvpA forms the protein shell. SUBCELLULAR LOCATION: Gas vesicle shell. SIMILARITY: Belongs to the gas vesicle protein type A family.


FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AdoMet synthase family.


FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 16 family.


FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine. SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.


SIMILARITY: Belongs to the FrhG family.


FUNCTION: Hydrolyzes specifically phosphatidic acid (PA) to produce 2- acyl lysophosphatidic acid (LPA; a potent bioactive lipid mediator) and fatty acid. Does not hydrolyze other phospholipids, like phosphatidylserine (PS), phosphatidylcholine (PC) and phosphatidylethanolamine (PE) or triacylglycerol (TG). SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane Secreted Note=May associate with lipid draft. SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane Secreted Note=May associate with lipid draft. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.


FUNCTION: 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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. SIMILARITY: Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.


FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the complex I 23 kDa subunit family.


FUNCTION: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8- phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate. SIMILARITY: Belongs to the KdsC family.


FUNCTION: Putative O-acetyltransferase; part of the satratoxin SC2 cluster involved in the biosynthesis of satratoxins, trichothecene mycotoxins that are associated with human food poisonings (PubMed:25015739). Satratoxins are suggested to be made by products of multiple gene clusters (SC1, SC2 and SC3) that encode 21 proteins in all, including polyketide synthases, acetyltransferases, and other enzymes expected to modify the trichothecene skeleton (PubMed:25015739). SC1 encodes 10 proteins, SAT1 to SAT10 (PubMed:25015739). The largest are SAT8, which encodes a putative polyketide synthase (PKS) with a conventional non-reducing architecture, and SAT10, a putative protein containing four ankyrin repeats and thus may be involved in protein scaffolding (PubMed:25015739). The putative short-chain reductase SAT3 may assist the PKS in some capacity (PubMed:25015739). SAT6 contains a secretory lipase domain and acts probably as a trichothecene esterase (PubMed:25015739). SAT5 encodes a putative acetyltransferase, and so, with SAT6, may affect endogenous protection from toxicity (PubMed:25015739). The probable transcription factor SAT9 may regulate the expression of the SC1 cluster (PubMed:25015739). SC2 encodes proteins SAT11 to SAT16, the largest of which encodes the putative reducing PKS SAT13 (PubMed:25015739). SAT11 is a cytochrome P450 monooxygenase, while SAT14 and SAT16 are probable acetyltransferases (PubMed:25015739). The SC2 cluster may be regulated by the transcription factor SAT15 (PubMed:25015739). SC3 is a small cluster that encodes 5 proteins, SAT17 to SAT21 (PubMed:25015739). SAT21 is a putative MFS-type transporter which may have a role in exporting secondary metabolites (PubMed:25015739). The four other proteins putatively encoded in SC3 include the taurine hydroxylase-like protein SAT17, the O-methyltransferase SAT18, the acetyltransferase SAT19, and the Cys6-type zinc finger SAT20, the latter being probably involved in regulation of SC3 expression (PubMed:25015739). SIMILARITY: Belongs to the lysine N-acyltransferase MbtK family.


FUNCTION: 3'-5' exonuclease that prefers single-stranded DNA and RNA. May play a role in the H(2)O(2)-induced DNA damage repair. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. TatD-type hydrolase family. TatD subfamily.


FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. SIMILARITY: Belongs to the CTP synthase family.


FUNCTION: Catalyzes the deesterification of methyl-esterified D- galactosiduronic acid units in pectic compounds. It participates in modulating cell wall during fruit ripening, cell wall extension during pollen germination, and in defense mechanisms against pathogens. SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: Belongs to the pectinesterase family.


SIMILARITY: Belongs to the glutaminase family.


FUNCTION: Catalyzes the biosynthesis of agmatine from arginine. SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.


FUNCTION: May act as a receptor in regulating T-cell proliferation. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.


FUNCTION: Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation. SIMILARITY: Belongs to the ClpS family.


FUNCTION: Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. SIMILARITY: Belongs to the arginine N-succinyltransferase family.


SIMILARITY: Belongs to the yippee family.


FUNCTION: Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Controls the expression of genes associated with innate immunity in the absence of pathogens or elicitors. Involved in brassinosteroid (BR) signal transduction. Phosphorylates BRI1. May be involved in changing the equilibrium between plasma membrane-located BRI1 homodimers and endocytosed BRI1- BAK1 heterodimers. Interaction with MSBP1 stimulates the endocytosis of BAK1 and suppresses brassinosteroid signaling. Acts in pathogen- associated molecular pattern (PAMP)-triggered immunity (PTI) via its interactions with FLS2 and EFR, and the phosphorylation of BIK1. Involved in programmed cell death (PCD) control. Positively regulates the BR-dependent plant growth pathway and negatively regulates the BR- independent cell-death pathway (PubMed:17583510, PubMed:17600708, PubMed:18667726, PubMed:18694562, PubMed:19124768, PubMed:20018402, PubMed:20404519, PubMed:21693696). Phosphorylates BIR2 and thus promotes interaction with BIR2 (PubMed:24388849, PubMed:24556575). This interaction prevents interaction with FLS2 in the absence of pathogen- associated molecular patterns (PAMP) (PubMed:24388849, PubMed:24556575). Component of the RLP23-SOBIR1-BAK1 complex that mediates NLP-triggered immunity (PubMed:27251392). Required for PSK promotion of seedling growth and protoplast expansion (PubMed:26071421). CNGC17 and AHAs form a functional cation- translocating unit that is activated by PSKR1/BAK1 and possibly other BAK1/RLK complexes (PubMed:26071421). Required during SCOOP small peptides (e.g. RGF1, SCOOP10 and SCOOP12) perception and signaling; associates with MIK2 as a coreceptor upon MIK2 perception of SCOOP peptides, and relays the signaling through the activation of receptor- like cytosolic kinases (RLCKs) BIK1 and PBL1 (Probable) (PubMed:30715439, PubMed:34535661). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Endosome membrane; Single- pass type I membrane protein Note=Endocytosis enhanced upon interaction with MSBP1. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


FUNCTION: Essential peptidyl-tRNA hydrolase component of the mitochondrial large ribosomal subunit (PubMed:20869366). Acts as a codon-independent translation release factor that has lost all stop codon specificity and directs the termination of translation in mitochondrion, possibly in case of abortive elongation. May be involved in the hydrolysis of peptidyl-tRNAs that have been prematurely terminated and thus in the recycling of stalled mitochondrial ribosomes (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor family. Mitochondrion-specific ribosomal protein mL62 subfamily.


FUNCTION: Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1 (By similarity). Essential for embryonic development (By similarity). SUBCELLULAR LOCATION: Cytoplasm, P-body Nucleus Note=Co-localizes with NANOS3 in the processing bodies (By similarity). Predominantly cytoplasmic, in processing bodies (PB). Nuclear, after TGFB1 treatment. Translocation to the nucleus depends on interaction with SMAD4 (By similarity). SIMILARITY: Belongs to the DCP1 family.


FUNCTION: Binds specifically to voltage-gated sodium channels (Nav) (site 3), thereby delaying their inactivation during signal transduction (PubMed:19609479). Has a strong effect on crustaceans and insects and a weaker effect on mammals (By similarity). It strongly inhibits D.melanogaster sodium channel (DmNav1) (PubMed:19609479). It strongly affects the heart sodium channels (Nav1.5/SCN5A) and weakly inhibits the brain sodium channel Nav1.2/SCN2A (By similarity). In vivo, when released into the medium, this recombinant toxin induces impaired swimming, paralysis and death of the crustacean A.nauplii within several hours (PubMed:22048953). Its effect on zebrafish (D.rerio) larvae is much faster, since it induces paralysis or strong convulsion and impaired swimming, within 10 minutes (PubMed:22048953). SUBCELLULAR LOCATION: Secreted Nematocyst Note=In nematocyst, is associated with the tubule prior to discharge. SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin family. Type I subfamily.


FUNCTION: Scaffold protein that participates in the c-ring assembly of mitochondrial ATP synthase (F(1)F(0) ATP synthase or complex V) by facilitating the membrane insertion and oligomer formation of the subunit c/ATP5MC3. Participates in the incorporation of the c-ring into vestigial complexes. Additionally influences the incorporation of subunits MT-ATP6, MT-ATP8, ATP5MJ, and ATP5MK in the ATP synthase. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM242 family.


FUNCTION: Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2 homeostasis at the plasma membrane. Heme-binding protein that may play a role in organic oxidant-induced stress responses. SUBCELLULAR LOCATION: Cytoplasm Endoplasmic reticulum membrane; Peripheral membrane protein Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the SFH5 family.


FUNCTION: Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome. The capsid contains also 1 copy of the A2 maturation protein. FUNCTION: Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site. SUBCELLULAR LOCATION: Virion Note=The shell is composed of 178 copies of the capsid protein and 1 copy of the maturation protein. SIMILARITY: Belongs to the Leviviricetes capsid protein family.


FUNCTION: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The mdm12-mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta- barrel proteins, and acts in a late step after the SAM complex. The mdm10-mdm12-mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the mdm12-mmm1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids. SIMILARITY: Belongs to the MMM1 family.


FUNCTION: May be involved in the transport of PQQ or its precursor to the periplasm. SIMILARITY: Belongs to the PqqB family.


FUNCTION: Essential for recycling GMP and indirectly, cGMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the guanylate kinase family.


SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family. SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family.


FUNCTION: Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins. SUBCELLULAR LOCATION: Virion membrane; Multi-pass membrane protein Host Golgi apparatus membrane; Multi-pass membrane protein Note=Largely embedded in the lipid bilayer. SIMILARITY: Belongs to the betacoronaviruses M protein family.


FUNCTION: As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an antioxidant, has antibacterial activity, and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidly cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation pathway. FUNCTION: The uncleaved form of allele alpha-2 (2-2), known as zonulin, plays a role in intestinal permeability, allowing intercellular tight junction disassembly, and controlling the equilibrium between tolerance and immunity to non-self antigens. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mS23 family.


FUNCTION: PUMPS are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation. This leads to a decrease in the efficiency of oxidative phosphorylation and an increase in heat production. May be involved in protecting plant cells against oxidative stress damage (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.


SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the MG439/MG440 family.


FUNCTION: Defense against chitin-containing fungal pathogens. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily.


FUNCTION: Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily.


FUNCTION: Part of an ATP-driven transport system CT_067/CT_068/CT_069/CT_070 for a metal. Probably responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily.


FUNCTION: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor Bacterial flagellum basal body. SIMILARITY: Belongs to the FlgH family.


FUNCTION: Bifunctional oxidoreductase ables to act both on prenyl naphthoquinones and on prenyl benzoquinones (PubMed:21844348, PubMed:26023160). May serve a respiratory function (PubMed:12972666). Involved in an electron flow toward the plastoglobule plastoquinone pool (PubMed:21844348, PubMed:25018761). Required for plastochromanol-8 accumulation and for phylloquinone (vitamin K1) production (PubMed:21844348, PubMed:25018761). Probably not directly involved in cyclic or chlororespiratory electron flows under standard growth conditions, but participates in the redox metabolism of plastoquinone-9 and the tocophrol recycling-intermediate alpha-tocopherol quinone (PubMed:21844348, PubMed:25018761). Catalyzes the penultimate step in the biosynthesis of vitamin K1 (PubMed:26023160). SUBCELLULAR LOCATION: Mitochondrion Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Plastid, chloroplast Plastid, chloroplast, plastoglobule. SIMILARITY: Belongs to the NADH dehydrogenase family.


FUNCTION: Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of conidiogenone, a diterpene known to induce the conidiation (PubMed:30343633). The bifunctional terpene synthase PchDS converts isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into deoxyconidiogenol (PubMed:30343633). The C- terminal prenyltransferase (PT) domain of PchDS catalyzes formation of GGPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of GGPP into deoxyconidiogenol (PubMed:30343633). The cytochrome P450 monooxygenase PchP450 then catalyzes two rounds of oxidation to furnish conidiogenone (PubMed:30343633). SIMILARITY: In the N-terminal section; belongs to the terpene synthase family. SIMILARITY: In the C-terminal section; belongs to the FPP/GGPP synthase family.


FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4L family.


FUNCTION: Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the LptD family.


FUNCTION: 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. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily. UNG family.


SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL27 family.


FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long subfamily. SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long subfamily.


FUNCTION: Cytochrome b5 is a membrane-bound hemoprotein functioning as an electron carrier for several membrane-bound oxygenases. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side. Microsome membrane; Single-pass membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the cytochrome b5 family.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the PPR family. PCMP-E subfamily.


FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in N-acetylgalactosamine transport. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome. SIMILARITY: Belongs to the archaeal DnaG primase family.


FUNCTION: Has exonuclease activity on both single-stranded and duplex templates bearing overhangs, but not blunt ended duplex DNA, and cleaves in a 3'-5' direction. Essential for the formation of DNA replication focal centers. Has an important role in maintaining genome stability. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WRNexo family.


SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.


FUNCTION: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N- acetylglucosamine of the oligosaccharide chains in glycoproteins. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 22 family.


FUNCTION: Structural protein of a layer within the wall of the spermatophore produced probably by cell type 4 of the bean-shaped gland (BAG). Fixation in the spermatophore seems to require covalent cross- linking of spermatophorins. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Has NADP-dependent alcohol dehydrogenase activity. SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase family.


FUNCTION: Involved in cytoplasm to vacuole transport (Cvt) and autophagic vesicle formation. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy). Also required for mitophagy, which eliminates defective or superfluous mitochondria in order to fulfill cellular energy requirements and prevent excess ROS production. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1- like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes (By similarity). SUBCELLULAR LOCATION: Preautophagosomal structure membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATG5 family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. TPMT family.


SIMILARITY: Belongs to the FAM13 family.


FUNCTION: Involved in the biosynthesis of rosmarinic acid, a compound with antiviral, antimicrobial and anti-inflammatory activities. Can use 4-coumaroyl- and caffeoyl-CoA as hydroxycinnamoyl donors and 4- Hydroxyphenyllactate and 3.4-Dihydroxyphenyllactate, but not shikimate or quinate, as hydroxycinnamoyl acceptors. Can also putatively catalyze amide formation with D-amino acids as acceptors. SIMILARITY: Belongs to the plant acyltransferase family.


FUNCTION: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex. SUBCELLULAR LOCATION: Nucleus. Chromosome. SIMILARITY: Belongs to the protamine P1 family.


SUBCELLULAR LOCATION: Mitochondrion.


FUNCTION: Part of the gene cluster that mediates the biosynthesis of imizoquins A to D, tripeptide-derived alkaloids that serve a protective role against oxidative stress that are essential for normal germination (PubMed:29182847). ImqB is a canonical three-module NRPS that assembles the tripeptide backbone of the imizoquins via condensation of Trp, Tyr, and Leu-derived precursors (PubMed:29182847). N-methylation by imqF and phenol oxidation by imqC, followed by cyclization via the FAD-dependent oxidase imqH carry out the three-step transformation of L-tyrosine into tetrahydroisoquinoline (PubMed:29182847). Importantly, this sequence requires the presence of a free amine in the tyrosine moiety, indicating that isoquinoline formation occurs prior to peptide bond formation (PubMed:29182847). The imidazolidin-4-one ring of imizoquins could form following additional oxidation of the methyl-derived bridgehead carbon by imqH (PubMed:29182847). Lastly, O-methylation by imqG and leucine hydroxylation by imqE complete biosynthesis of the imizoquins (PubMed:29182847).


FUNCTION: Involved in lipid metabolism and lipid droplet (LD) morphology, number, and size. Facilitates the formation of large-sized LDs and modulates triacylglycerol accumulation. Induces probably a reorganization of the endoplasmic reticulum into LD-forming domains. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Localized to the lipid droplet-forming sites. SIMILARITY: Belongs to the seipin family.


FUNCTION: Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage. SIMILARITY: Belongs to the Nudix hydrolase family. RppH subfamily.


FUNCTION: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. SIMILARITY: Belongs to the peptidase S24 family.


FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. SUBCELLULAR LOCATION: Membrane; Lipid-anchor. SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.


FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. SIMILARITY: Belongs to the ThiC family.


FUNCTION: Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn- glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1- phosphate (DGGGP) and CTP. This reaction is the third ether-bond- formation step in the biosynthesis of archaeal membrane lipids. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CDP-archaeol synthase family.


SIMILARITY: Belongs to the bacterial ribosomal protein bL36 family.


FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is responsible for the expression of sporulation specific genes in the mother cell. SIMILARITY: Belongs to the sigma-70 factor family.


FUNCTION: Functions as response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Type-A response regulators seem to act as negative regulators of the cytokinin signaling. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ARR family. Type-A subfamily.


FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's. May acquire specificity through interaction with a cleavage and polyadenylation factor (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the poly(A) polymerase family.


FUNCTION: May act as an effector of RAP2A in neuronal cells. SIMILARITY: Belongs to the RUNDC3 family.


FUNCTION: Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q). Is required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly. In vitro, can also catalyze the release of the q base directly from Q as substrate; however, it was shown that Q is not the biologically relevant substrate. Shows a very low activity on queuosine 3',5'-diphosphate, and cannot release q from queuosine 3'-phosphate and from the 5'-nucleotides AMP, UMP, CMP or GMP, indicating specificity for the queuine base (PubMed:36610787). Can complement the yeast mutant SPAC589.05c, restoring Q incorporation into tRNA (PubMed:24911101). SIMILARITY: Belongs to the QNG1 protein family.


FUNCTION: Lignin degradation and detoxification of lignin-derived products. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the multicopper oxidase family.


FUNCTION: GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut. FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GST superfamily. Mu family.


FUNCTION: Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc2-PP-Dol. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 58 family.


FUNCTION: Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS19 family.


FUNCTION: One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the IF-1 family.


FUNCTION: Transcriptional regulator involved in developmental processes. Can activate POMC gene expression and repress the alpha glycoprotein subunit and thyroid-stimulating hormone beta promoters (By similarity). SUBCELLULAR LOCATION: Nucleus.


SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: Belongs to the fungal hydrophobin family.


FUNCTION: Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. vinblastine, catharanthine, tabersonine, vincadifformine, vindoline, vincristine, quinine and strychnine) biosynthesis pathway. Converts precondylocarpine acetate to dihydroprecondylocarpine acetate. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.


SIMILARITY: Belongs to the bacterial ribosomal protein bL31 family. Type B subfamily.


FUNCTION: Extracellular lectin functioning as a pattern-recognition receptor in innate immunity. Binds the sugar moieties of pathogen- associated molecular patterns (PAMPs) displayed on microbes and activates the lectin pathway of the complement system. May also activate monocytes through a G protein-coupled receptor, FFAR2, inducing the secretion of interleukin-8/IL-8. Binds preferentially to 9-O-acetylated 2-6-linked sialic acid derivatives and to various glycans containing sialic acid engaged in a 2-3 linkage (By similarity). SUBCELLULAR LOCATION: Secreted Cell membrane; Peripheral membrane protein; Extracellular side Note=Found on the monocyte and granulocyte surface. SIMILARITY: Belongs to the ficolin lectin family.


FUNCTION: Catalytic subunit in the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis. SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.


FUNCTION: Binds long-chain acyl-coenzyme A molecules with a strong preference for unsaturated C18:1-CoA, lower affinity for unsaturated C20:4-CoA, and very weak affinity for saturated C16:0-CoA. Does not bind fatty acids (By similarity). SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second half-reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components (By similarity). SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. SIMILARITY: Belongs to the universal ribosomal protein uS17 family.


FUNCTION: Its primary physiological function is unclear. Has cytoprotective activity against internal or environmental stresses. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Golgi apparatus Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis. SIMILARITY: Belongs to the prion family.


SIMILARITY: Belongs to the cysteine synthase/cystathionine beta- synthase family.


SIMILARITY: Belongs to the MTFR1 family.


FUNCTION: Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.


FUNCTION: Involved in cell adhesion. Contributes to integrin activation. When coexpressed with talin, potentiates activation of ITGA2B. Required for normal keratinocyte proliferation. Required for normal polarization of basal keratinocytes in skin, and for normal cell shape. Required for normal adhesion of keratinocytes to fibronectin and laminin, and for normal keratinocyte migration to wound sites (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell junction, focal adhesion Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side Note=Colocalizes with filamentous actin. Constituent of focal adhesions (By similarity). Localized at the basal aspect of skin keratinocytes, close to the cell membrane (By similarity). Upon TGFB1 treatment, it localizes to membrane ruffles (By similarity). SIMILARITY: Belongs to the kindlin family.


FUNCTION: Chaperone protein that cooperates with UL148 to regulate the abundance of gH complexes in virion (PubMed:33889136, PubMed:26937030). First interactor of gH in the host endoplasmic reticulum, regulates the early folding steps of virion assembly. Then, UL148 is recruited and favors the binding of gL (PubMed:34011552). SUBCELLULAR LOCATION: Virion Host endoplasmic reticulum Note=First localizes to the cellular site of virus assembly and then inserts into the virion envelope. SIMILARITY: Belongs to the HHV-5 UL116 protein family.


FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.


SIMILARITY: Belongs to the RimK family.


FUNCTION: Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. SUBCELLULAR LOCATION: Cytoplasm Nucleus.


FUNCTION: Seems to function as a Vpr-like protein, since it mediates host cell cycle arrest in G2 phase. Cell cycle arrest creates a favorable environment for maximizing viral expression and production (By similarity). SUBCELLULAR LOCATION: Virion Host nucleus.


FUNCTION: The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid. FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assures fusion between virion membrane and endosomal membrane. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein. SUBCELLULAR LOCATION: Virion membrane. SIMILARITY: Belongs to the orthohepadnavirus major surface antigen family.


FUNCTION: Involved in initiation control of chromosome replication. SIMILARITY: Belongs to the YabA family.


FUNCTION: Seems to bind zinc and copper. Could play a special role in regulating zinc metabolism during the differentiation of stratified epithelia. SIMILARITY: Belongs to the metallothionein superfamily. Type 1 family.


FUNCTION: Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate. SIMILARITY: Belongs to the PurK/PurT family.


FUNCTION: Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the BCD1 family.


FUNCTION: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. It also functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Nucleus, nuclear pore complex. SIMILARITY: Belongs to the WD repeat SEC13 family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin I1 superfamily.


FUNCTION: Required for chromosome condensation and partitioning. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SMC family.


FUNCTION: Regulates the export of target proteins, such as DRD1, from the endoplasmic reticulum to the cell surface. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein.


FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NqrDE/RnfAE family.


FUNCTION: LEA proteins are late embryonic proteins abundant in higher plant seed embryos. The function of those proteins is not known. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the LEA type SMP family.


FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family.


FUNCTION: Catalyzes the GTP-dependent phosphorylation of the 3'- hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA). SIMILARITY: Belongs to the GTP-dependent DPCK family.


SIMILARITY: Belongs to the CTNNBIP1 family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin T superfamily.


FUNCTION: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein Note=Localizes to the division septum. SIMILARITY: Belongs to the FtsB family.


FUNCTION: Has antimicrobial activity against E.coli, E.faecalis, P.aeruginosa, and S.aureus. Has insecticidal and hemolytic activities. Probably acts by disturbing membrane function with its amphipathic structure. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cationic peptide 04 (cupiennin) family. 01 subfamily.


FUNCTION: Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Rho GDI family.


FUNCTION: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.


FUNCTION: Hydrolyzes with equal efficiency cytidine or uridine to ribose and cytosine or uracil, respectively. SIMILARITY: Belongs to the IUNH family. RihA subfamily.


FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein. SIMILARITY: Belongs to the GcvP family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.


FUNCTION: Cytoskeletal protein that is involved in cell-shape control through regulation of the length of the long axis. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein Note=Forms helical filaments along the long axis of the cell. SIMILARITY: Belongs to the RodZ family.


FUNCTION: Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ferredoxin thioredoxin reductase beta subunit family.


FUNCTION: Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. UreG subfamily.