FUNCTION: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT (By similarity). SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Has antifungal activity. Inhibits Candida albicans and Trichoderma reesei; marginal inhibition observed against Alternaria solani and Neurospora crassa. SIMILARITY: Belongs to the thaumatin family.


FUNCTION: Could play a direct role in the oxidation or reduction of the quenching species formed in the chlorosome. SUBCELLULAR LOCATION: Chlorosome.


FUNCTION: Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FdhD family.


FUNCTION: May have an olfactory function associated with the identification of pathogens or of pathogenic states. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Transporter for the divalent cation Zn(2+). Mediates the influx of Zn(2+) into cells from extracellular space (PubMed:11301334, PubMed:12888280, PubMed:16844077). Functions as the major importer of zinc from circulating blood plasma into prostate cells (PubMed:12888280). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Shows a vesicular localization corresponding partially to the endoplasmic reticulum in several epithelial cell lines. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.


SIMILARITY: To R.meliloti RA0936 and y4aO.


FUNCTION: Functions as a ribosomal silencing factor. Addition to isolated ribosomal subunits partially inhibits their association, preventing translation. Interacts with ribosomal protein uL14 (rplN), blocking formation of intersubunit bridge B8, preventing association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation. FUNCTION: Functions as a ribosomal silencing factor. Interacts with ribosomal protein uL14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm Note=Comigrates with the 50S ribosomal subunit in sucrose gradients, specifically with ribosomal protein uL14 (rplN). SIMILARITY: Belongs to the Iojap/RsfS family. SIMILARITY: Belongs to the Iojap/RsfS family.


FUNCTION: Possesses xyloglucan endotransglucosylase (XET) activity in vitro. Does not possess xyloglucan endohydrolysis (XEH) activity (PubMed:20732879). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues (PubMed:23585673). Involved in cell proliferation in the tissue reunion process of wounded inflorescence stems. Maybe a downstream target of NAC071 as a consequence of auxin action in wounded stems (PubMed:25182467). SUBCELLULAR LOCATION: Secreted, cell wall Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 2 subfamily.


FUNCTION: Has a broad substrate specificity. Can use synthetic substrates such as pyridylaminated chitotriose, pyridylaminated chitobiose, p-nitrophenyl-beta-N-acetylglucosaminide, p-nitrophenyl-2- acetamido-2-deoxy-beta-D-glucopyranoside (pNP-GlcNAc), p-nitrophenyl-2- acetamido-2-deoxy-beta-D-galactopyranoside (pNP-GalNAc), 4- methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU- GlcNAc), and 4-methylumbelliferyl-6-sulfo-2-acetamido-2-deoxy-beta-D- glucopyranoside (MU-GlcNAc-6SO(4)) as substrates. Removes terminal GlcNAc residues from alpha1,3- and alpha1,6-mannosyl branches of biantennary N-glycans without any strict branch preference. Required for the presence of paucimannosidic N-glycans in glycoproteins of roots and, to a lower extent, of leaves. SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the glycosyl hydrolase 20 family.


FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the MHC class I family.


FUNCTION: Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at lysine 16 which is implicated in the formation of higher-order chromatin structure (By similarity). Acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. This activity is greatly enhanced by heterodimerization with MSL1. H2B ubiquitination in turn stimulates histone H3 methylation at 'Lys-5' (H3K4me) and 'Lys-80' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1 (By similarity). SIMILARITY: Belongs to the MSL2 family.


FUNCTION: Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the kappa-casein family.


FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 2 subfamily.


FUNCTION: DNA repair enzyme that cleaves apurinic/apyrimidinic (AP) sites and removes 3'-blocking groups present at single strand breaks of damaged DNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.


SIMILARITY: Belongs to the SH3YL1 family.


FUNCTION: Histone-binding protein that binds to histones H2A/H2B, H3/H4 and cellular chromatin to overcome the host DNA damage response triggered by the viral genome ends. Interferes with histone ubiquitination and recruitment of repair proteins. SUBCELLULAR LOCATION: Virion tegument Host nucleus Host cytoplasm, host perinuclear region. SIMILARITY: Belongs to the lymphocryptovirus BKRF4 family.


FUNCTION: Together with movement protein P3a, facilitates long-distance movement of virions in host (Probable). Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding (Probable). The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier (Probable). Binds ssRNA (By similarity). SUBCELLULAR LOCATION: Host cell junction, host plasmodesma Host chloroplast envelope Host Golgi apparatus Host mitochondrion outer membrane Note=Localizes to secondary branched plasmodesmata in source organs. Targeted to plasmodesmata in an actin- and endoplasmic reticulum-Golgi-dependent manner (By similarity). P3a directs P17 to the mitochondrial outer membrane while P17 regulates the localization of the P3a-P17 heterodimer to plastids (By similarity). SIMILARITY: Belongs to the polerovirus movement protein family.


FUNCTION: Has bactericidal activity. May act as a ligand for C-C chemokine receptor CCR6. Positively regulates the sperm motility and bactericidal activity in a CCR6-dependent manner. Binds to CCR6 and triggers Ca2+ mobilization in the sperm which is important for its motility. SUBCELLULAR LOCATION: Secreted Membrane Note=Associates with tumor cell membrane-derived microvesicles. SIMILARITY: Belongs to the beta-defensin family.


FUNCTION: Purine nucleoside phosphorylase which is highly specific for 6-oxopurine nucleosides. Cleaves guanosine or inosine to respective bases and sugar-1-phosphate molecules. Involved in purine salvage. SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.


FUNCTION: Member of the two-component regulatory system DctS/DctR. Essential for expression of DctP (By similarity). SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Cytoplasmic and mitochondrial threonylcarbamoyl-AMP synthase required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine (PubMed:29760464, PubMed:31481669, PubMed:34545459). Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate (PubMed:29760464). Participates in t(6)A37 formation in cytoplasmic and mitochondrial tRNAs (PubMed:29760464). May regulate the activity of some transporters (By similarity). SUBCELLULAR LOCATION: Cytoplasm Mitochondrion Cell membrane; Peripheral membrane protein Note=A large fraction localizes in the cytoplasm, whereas a smaller fraction is imported to mitochondria. SIMILARITY: Belongs to the SUA5 family.


FUNCTION: The subtype gamma methyltransferase (M) subunit of a type I restriction enzyme. The M and S subunits together form a methyltransferase (MTase) that methylates A-2 on the top strand and A-3 on the bottom strand of the sequence 5'-AACN(6)GTRC-3'. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated (PubMed:3025838, PubMed:12654995). After locating a non- methylated recognition site, the enzyme complex serves as a molecular motor that translocates DNA in an ATP-dependent manner until a collision occurs that triggers cleavage (By similarity). SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.


FUNCTION: May play a key role in the control of gene expression during oogenesis and early embryogenesis, presumably through the perturbation of chromatin structure. Essential for meiotic maturation of germinal vesicle-stage oocytes. The somatic type linker histone H1c is rapidly replaced by H1oo in a donor nucleus transplanted into an oocyte. The greater mobility of H1oo as compared to H1c may contribute to this rapid replacement and increased instability of the embryonic chromatin structure. The rapid replacement of H1c with H1oo may play an important role in nuclear remodeling (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Chromosome. SIMILARITY: Belongs to the histone H1/H5 family.


FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of malbrancheamide, a dichlorinated fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core (PubMed:23213353, PubMed:31548667, PubMed:28777910). The first step of malbrancheamide biosynthesis involves coupling of L-proline and L-tryptophan by malG, a bimodular NRPS, to produce L-Pro-L-Trp aldehyde through reductive offloading (PubMed:23213353, PubMed:31548667). This compound undergoes spontaneous cyclization and dehydration to give a dienamine which is reverse prenylated at C-2 by malE (PubMed:31548667). The other prenyltransferase present in the cluster, malB, displays modest activity, suggesting that may be a redundant gene in the pathway (PubMed:31548667). Subsequently, a [4+2] Diels-Alder cyclo-addition catalyzed by the bifunctional enzyme malC forms the characteristic bicyclo[2.2.2]diazaoctane ring of premalbrancheamid (PubMed:31548667). Finally, the flavin-dependent halogenase malA catalyzes the iterative dichlorination of the indole ring of premalbrancheamide to yield C-9 monochlorinated malbrancheamide B, C-8 monochlorinated isomalbrancheamide B, and dichlorinated malbrancheamide (PubMed:31548667, PubMed:28777910). MalA is also able to brominate premalbrancheamide at C-9 to yield malbrancheamide C, and, to a lesser extend, at C-8 to yield isomalbrancheamide C (PubMed:28777910). Finally, malA can brominate C-9 monochlorinated malbrancheamide B at C- 8 to yield malbrancheamide D, or C-8 monochlorinated isomalbrancheamide B at C-9 to produce isomalbrancheamide D (PubMed:28777910). SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family.


FUNCTION: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (PubMed:11991638, PubMed:18984161, PubMed:19325628, PubMed:25555158, PubMed:26912367, PubMed:28502770, PubMed:28781166, PubMed:28076346). Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes (PubMed:11991638, PubMed:28502770, PubMed:28781166, PubMed:28076346). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077). As part of the U7 snRNP it is involved in histone pre-mRNA 3'-end processing (PubMed:12975319). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Note=SMN- mediated assembly into core snRNPs occurs in the cytosol before SMN- mediated transport to the nucleus to be included in spliceosomes. SIMILARITY: Belongs to the snRNP SmB/SmN family.


FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses (PubMed:15240257, PubMed:16820452). The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha- ionylideneethane performed by the alpha-ionylideneethane synthase aba3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene (PubMed:30226766). The cytochrome P450 monooxygenase aba1 might then be involved in the conversion of alpha- ionylideneethane to alpha-ionylideneacetic acid (Probable). Alpha- ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase aba2 and the short-chain dehydrogenase/reductase aba4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (Probable). Aba2 is responsible for the hydroxylation of carbon atom C-1' and aba4 might be involved in the oxidation of the C-4' carbon atom (PubMed:16820452). SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs. SIMILARITY: Belongs to the archaeosine tRNA-ribosyltransferase family.


FUNCTION: Purine nucleoside phosphorylase involved in purine salvage. SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.


FUNCTION: Plays a central role in chromosome cohesion during cell division by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere. SIMILARITY: Belongs to the shugoshin 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 6 packaging RNA molecules (pRNA) forming a double-ring structure which in turn binds to the ATPase gp16 hexamer, forming the active DNA-translocating motor. This complex is essential for the specificity of packaging from the left DNA end. SUBCELLULAR LOCATION: Virion Note=Present in 12 copies in the virion. SIMILARITY: Belongs to the phi29likevirus portal protein family.


SIMILARITY: Belongs to the WXG100 family. sagEsxA-like subfamily.


FUNCTION: Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in a peroxiredoxin. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the sulfiredoxin family.


FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of paraherquonin, a meroterpenoid with a unique, highly congested hexacyclic molecular architecture (PubMed:27602587). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase prhL (By similarity). Synthesis of DMOA is followed by farnesylation by the prenyltransferase prhE, methylesterification by the methyl-transferase prhM, epoxidation of the prenyl chain by the flavin-dependent monooxygenase prhF, and cyclization of the farnesyl moiety by the terpene cyclase prhH, to yield the tetracyclic intermediate, protoaustinoid A (By similarity). The short chain dehydrogenase prhI then oxidizes the C-3 alcohol group of the terpene cyclase product to transform protoaustinoid A into protoaustinoid B (PubMed:27602587). The FAD-binding monooxygenase prhJ catalyzes the oxidation of protoaustinoid B into preaustinoid A which is further oxidized into preaustinoid A1 by FAD-binding monooxygenase phrK (PubMed:27602587). Finally, prhA leads to berkeleydione via the berkeleyone B intermediate (PubMed:27602587, PubMed:29317628). PrhA is a multifunctional dioxygenase that first desaturates at C5-C6 to form berkeleyone B, followed by rearrangement of the A/B-ring to form the cycloheptadiene moiety in berkeleydione (PubMed:27602587, PubMed:29317628). Berkeleydione serves as the key intermediate for the biosynthesis of paraherquonin as well as many other meroterpenoids (Probable). The cytochrome P450 monooxygenases prhB, prhD, and prhN, as well as the isomerase prhC, are probably involved in the late stage of paraherquonin biosynthesis, after the production of berkeleydione (Probable). Especially prhC might be a multifunctional enzyme that catalyzes the D-ring expansion via intramolecular methoxy rearrangement, as well as the hydrolysis of the expanded D-ring (Probable). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of D6 and A7, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase. SUBCELLULAR LOCATION: Virion Note=All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with the DNA genome. This is necessary because viral early mRNAs are synthesized within minutes after virus entry into the cell and are extruded through pores in the core particle. SIMILARITY: Belongs to the poxviridae DNA-directed RNA polymerase 35 kDa subunit family.


FUNCTION: Low-potential electron donor to a number of redox enzymes. SIMILARITY: Belongs to the flavodoxin family.


FUNCTION: Catalyzes the proton-dependent uptake of 2-keto-3- deoxygluconate (KDG) into the cell. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the KdgT transporter family.


FUNCTION: Involved in the regulation of sporulation (PubMed:1624431, PubMed:8001132, PubMed:11923303, PubMed:22267516). Acts as a phosphatase that specifically dephosphorylates the sporulation initiation phosphotransferase Spo0F and inhibits its activity (PubMed:8001132, PubMed:11923303, PubMed:22267516). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Rap family.


FUNCTION: Confers reduced sensitivity to the fluoroquinolone antibiotic ciprofloxacin (five-fold increase in minimum inhibitory concentration) when expressed in E.coli. SIMILARITY: Belongs to the pentapeptide repeat protein family.


FUNCTION: Serine/threonine-protein kinase involved in cell cycle regulation, response to stress and Golgi disassembly. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates ATF2, BCL2L1, CDC25A, CDC25C, CHEK2, HIF1A, JUN, p53/TP53, p73/TP73, PTEN, TOP2A and VRK1. Involved in cell cycle regulation: required for entry into S phase and cytokinesis. Phosphorylates BCL2L1, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Plays a key role in response to stress: rapidly activated upon stress stimulation, such as ionizing radiation, reactive oxygen species (ROS), hyperosmotic stress, UV irradiation and hypoxia. Involved in DNA damage response and G1/S transition checkpoint by phosphorylating CDC25A, p53/TP53 and p73/TP73. Phosphorylates p53/TP53 in response to reactive oxygen species (ROS), thereby promoting p53/TP53-mediated apoptosis. Phosphorylates CHEK2 in response to DNA damage, promoting the G2/M transition checkpoint. Phosphorylates the transcription factor p73/TP73 in response to DNA damage, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates HIF1A and JUN is response to hypoxia. Phosphorylates ATF2 following hyperosmotic stress in corneal epithelium. Also involved in Golgi disassembly during the cell cycle: part of a MEK1/MAP2K1-dependent pathway that induces Golgi fragmentation during mitosis by mediating phosphorylation of VRK1. May participate in endomitotic cell cycle, a form of mitosis in which both karyokinesis and cytokinesis are interrupted and is a hallmark of megakaryocyte differentiation, via its interaction with CIB1. SUBCELLULAR LOCATION: Cytoplasm Nucleus Nucleus, nucleolus Golgi apparatus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Translocates to the nucleus upon cisplatin treatment. Localizes to the Golgi apparatus during interphase (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.


FUNCTION: Acts as an electrogenic sodium (Na(+)) and chloride (Cl-)- dependent sodium-coupled solute transporter, including transport of monocarboxylates (short-chain fatty acids including L-lactate, D- lactate, pyruvate, acetate, propionate, valerate and butyrate), mocarboxylate drugs (nicotinate, benzoate, salicylate and 5- aminosalicylate) and ketone bodies (beta-D-hydroxybutyrate, acetoacetate and alpha-ketoisocaproate), with a Na(+):substrate stoichiometry of between 4:1 and 2:1 (By similarity). Catalyzes passive carrier mediated diffusion of iodide. Mediates iodide transport from the thyrocyte into the colloid lumen through the apical membrane (By similarity). Mediates sodium-coupled electrogenic transport of pyroglutamate (5-oxo-L-proline) (By similarity). Can mediate the transport of chloride, bromide, iodide and nitrate ions when external concentration of sodium ions is reduced (By similarity). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.


FUNCTION: Putative defense peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Tryptophillin subfamily.


FUNCTION: Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as isobutyryl-CoA, propionyl-CoA and butyryl-CoA, but not indoleacetyl- CoA, phenylacetyl-CoA or succinyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetate CoA ligase beta subunit family.


FUNCTION: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria (By similarity). FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single- pass membrane protein. SIMILARITY: Belongs to the ATPase B chain family.


FUNCTION: Component of the mitochondrial ribosome large subunit. Also involved in apoptosis and cell cycle. Enhances p53/TP53 stability, thereby contributing to p53/TP53-induced apoptosis in response to growth-inhibitory condition. Enhances p53/TP53 translocation to the mitochondria. Has the ability to arrest the cell cycle at the G1 phase, possibly by stabilizing the CDKN1A and CDKN1B (p27Kip1) proteins. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mL41 family.


FUNCTION: Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-dependent steps (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Tim17/Tim22/Tim23 family.


SIMILARITY: Belongs to the poxviridae A49 protein family.


FUNCTION: Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. Flotillins are thought to be important factors in membrane fluidity. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Membrane raft; Multi-pass membrane protein. SIMILARITY: Belongs to the flotillin-like FloA family.


FUNCTION: Xylanase exhibiting endo- and exo-xylanase activity (PubMed:31110561). Shows the highest activity toward beechwood glucuronoxylan, which consists of a beta-1,4-linked xylose backbone decorated with the methylated form of D-glucuronic acid (MeGlcA) attached directly to the main chain at xylose C2 (PubMed:31110561). Acts also against wheat arabinoxylan, a xylan without MeGlcA substituents along the main chain, but the xylanase activity is about two orders of magnitude lower than that achieved in the case of beechwood xylan (PubMed:31110561). Shows no activity against carob galactomannan, konjac glucomannan, or barley beta-glucan (PubMed:31110561). The recombinant xylanase also exhibits an exo- activity by releasing processively disaccharide units from the non- reducing end of linear and decorated xylooligosaccharides (XOS) (PubMed:31110561). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 30 family.


FUNCTION: Modulates the competence to flowering of apical meristems. Involved in a GA-dependent response in apical meristems during the transition to flowering. SIMILARITY: Belongs to the FPF1 family.


FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). FUNCTION: 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 (By similarity). SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein. 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: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 03 subfamily.


FUNCTION: Antimicrobial peptide active against S.aureus (MIC=8 uM) but inactive against E.coli (PubMed:17561225). Shows also fungicide activity (By similarity). Also inhibits growth of B.dendrobatidis zoospores at high concentrations (above 25 uM) (PubMed:17561225). Shows anticancer activities since it is cytolytic against HepG2 human hepatoma-derived cells (LC(50)=35 uM) (PubMed:17561225). Is strongly hemolytic on human erythrocytes (LC(50)=40 uM) (PubMed:17561225). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Medusin subfamily.


FUNCTION: Putative regulator of protein phosphatase 1 (PP1) activity. May play a role in the endosomal sorting process or in endosome maturation pathway. SUBCELLULAR LOCATION: Early endosome.


FUNCTION: Involved in regulation of intracellular signaling pathways during development. Specifically thought to play a role in canonical and/or non-canonical Wnt signaling pathways through interaction with DSH (Dishevelled) family proteins. Binds to dvl2 and may regulate the degradation of ctnnb1/beta-catenin, thereby modulating the transcriptional activation of target genes of the Wnt signaling pathway. Seems to activate the canonical Wnt signaling pathway. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the dapper family.


FUNCTION: Converts adenosine-3',5'-bisphosphate (PAP) to AMP. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the inositol monophosphatase superfamily. CysQ family.


FUNCTION: A positive regulator of the alternate pathway of complement (PubMed:28264884). It binds to and stabilizes the C3- and C5-convertase enzyme complexes (By similarity). Inhibits CFI-CFH mediated degradation of Inhibits CFI-CFH mediated degradation of Complement C3 beta chain (C3b) (By similarity). SUBCELLULAR LOCATION: Secreted.


FUNCTION: Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond- formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales. SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group I subfamily.


FUNCTION: Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited proteolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade. SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: [Isoform 2]: Secreted. SIMILARITY: Belongs to the tissue factor family.


FUNCTION: RNA-binding protein that binds to misfolded non-coding RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y RNAs (PubMed:18056422, PubMed:26382853). Binds to endogenous Alu retroelements which are induced by type I interferon and stimulate porinflammatory cytokine secretion (PubMed:26382853). Regulates the expression of Alu retroelements as well as inflammatory genes (PubMed:26382853). May play roles in cilia formation and/or maintenance (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. SIMILARITY: Belongs to the Ro 60 kDa family.


FUNCTION: Probable transcription factor (By similarity). Involved in spikelet transition (Probable). Together with SNB, controls synergistically inflorescence architecture and floral meristem establishment via the regulation of spatio-temporal expression of B- and E-function floral organ identity genes in the lodicules and of spikelet meristem genes (PubMed:22003982). Prevents lemma and palea elongation as well as grain growth (PubMed:28066457). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the AP2/ERF transcription factor family. AP2 subfamily.


FUNCTION: Transcriptional repressor (PubMed:25578968). Histone demethylase that demethylates 'Lys-4' (H3K4me) of histone H3 with a higher activity for H3K4me3 and H3K4me2 than H3K4me1 (PubMed:29233856). No activity on H3K9me3/2, H3K36me3/2 and H3K27me3/2 (PubMed:29233856). Function as a nocturne 'eraser' to counteract the diurnal 'writer' methylase activity of ATXR3/SDG2 thus orchestrating the circadian rythm of histone modifications (e.g. H3K4me3) and modulating the rythmic expression of diurnal target genes; this mechanism relies also on the circadian clock oscillators CCA1 and LHY (PubMed:31429787). Involved in a negative regulation of root meristem growth upon suboptimal root growth conditions (PubMed:31826870). Represses FT and TSF expression to inhibit the floral transition. Binds around the transcription start site of the FT locus. Involved in the DRM2-mediated maintenance of DNA methylation, but not required for the de novo DNA methylation. Required for demethylating histone H3K4me3 at the target of RNA silencing. Counteracts the DNA methylation of expressed transgenes; specific attenuation of transgene DNA methylation enhances the production of aberrant RNAs (e.g. uncapped and antisense) that readily induce systemic RDR6-dependent post-transcriptional transgene silencing (PTGS) spreading (PubMed:33986281). Together with NAC051/NAC052 and NAC050, regulates gene expression and flowering time, probably by the promotion of RNA-mediated gene silencing (PubMed:25578968). Together with JMJ16 and JMJ17, required for plant growth and development (PubMed:31038749). Promotes local and systemic immunity (especially toward the bacterial pathogen Pseudomonas syringae Pst DC3000 avrRpt2) by regulating positively pathogen-induced H3K4me3 enrichment and expression of defense genes involved in salicylic acid (SA)- and pipecolic acid (Pip)-mediated defense pathways (e.g. PR1, FMO1, ALD1 and SARD4) (PubMed:31622519). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Nucleus Note=Not detected in the nucleolus and the chromocenters. SIMILARITY: Belongs to the JARID1 histone demethylase family.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eS28 family.


FUNCTION: Catalyzes the initial reaction in intramitochondrial fatty acid synthesis, by activating malonate and methylmalonate, but not acetate, into their respective CoA thioester. May have some preference toward very-long-chain substrates. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.


FUNCTION: [Obestatin]: Obestatin may be the ligand for GPR39. May have an appetite-reducing effect resulting in decreased food intake. May reduce gastric emptying activity and jejunal motility (By similarity). FUNCTION: [Ghrelin]: Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the motilin family.


SIMILARITY: Belongs to the AIM32 family.


FUNCTION: Acts as a chaperone. FUNCTION: Acts as a chaperone. SIMILARITY: Belongs to the heat shock protein 70 family. SIMILARITY: Belongs to the heat shock protein 70 family.


FUNCTION: Regulatory light chain of myosin. Does not bind calcium.


FUNCTION: Putative phospholipase. SUBCELLULAR LOCATION: Lysosome lumen. SIMILARITY: Belongs to the phospholipase B-like family.


SUBCELLULAR LOCATION: Glyoxysome. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.


FUNCTION: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Responsible for energy coupling to the transport system (Probable). FUNCTION: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Galactose/methyl galactoside importer (TC 3.A.1.2.3) family.


FUNCTION: This peptide both inhibits the activity of the angiotensin- converting enzyme (ACE) and enhances the action of bradykinin by inhibiting the peptidases that inactivate it. It acts as an indirect hypotensive agent (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bradykinin-potentiating peptide family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis (By similarity). Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). Plays a role in microtubule polymerization (PubMed:16054029). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TCP-1 chaperonin family.


FUNCTION: Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Promotes the dissociation of GDP-bound Rab proteins from the membrane and inhibits their activation. Promotes the dissociation of RAB1A, RAB3A, RAB5A and RAB10 from membranes. SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus, trans- Golgi network. SIMILARITY: Belongs to the Rab GDI family.


FUNCTION: Required for type IV pilus biogenesis and competence. Could function as a pore for exit of the pilus but also as a channel for entry of heme and antimicrobial agents and uptake of transforming DNA. SUBCELLULAR LOCATION: Cell outer membrane. Note=Associated with the membrane through its C-terminus. SIMILARITY: Belongs to the bacterial secretin family. PilQ subfamily.


FUNCTION: May be involved in specific transport of UDP-Gal from the cytosol to the Golgi lumen. Involved in the maintenance of optimal conditions for the folding of secretory pathway proteins in the endoplasmic reticulum (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35B subfamily.


FUNCTION: Key regulator of mitochondrial calcium uniporter (MCU) that senses calcium level via its EF-hand domains (PubMed:24560927). MICU1 and MICU2 form a disulfide-linked heterodimer that stimulates and inhibits MCU activity, depending on the concentration of calcium (PubMed:24560927). MICU1 acts both as an activator or inhibitor of mitochondrial calcium uptake (By similarity). Acts as a gatekeeper of MCU at low concentration of calcium, preventing channel opening (By similarity). Enhances MCU opening at high calcium concentration, allowing a rapid response of mitochondria to calcium signals generated in the cytoplasm (PubMed:24560927). Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake (By similarity). Induces T-helper 1-mediated autoreactivity, which is accompanied by the release of IFNG (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein Mitochondrion intermembrane space Note=The topology is subject to debate. SIMILARITY: Belongs to the MICU1 family. MICU1 subfamily.


SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GDT1 family.


FUNCTION: Mediates the nuclear localization of RNR2 and RNR4, 2 subunits of the ribonucleotide reductase. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the DIF1/spd1 family.


FUNCTION: Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation. SIMILARITY: Belongs to the DNA photolyase class-1 family.


FUNCTION: Methyltransferase that adds a 2'-O-methyl group at the 3'-end of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. This probably protects the 3'-end of piRNAs from uridylation activity and subsequent degradation. Stabilization of piRNAs is essential for gametogenesis. SUBCELLULAR LOCATION: Cytoplasm Note=Component of the meiotic nuage, also named P granule, a germ-cell- specific organelle required to repress transposon activity during meiosis. SIMILARITY: Belongs to the methyltransferase superfamily. HEN1 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 7 family.


FUNCTION: The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. FUNCTION: The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. SIMILARITY: Belongs to the TrpB family. SIMILARITY: Belongs to the TrpB family.


FUNCTION: Acts probably as a methyl group carrier between MttB and either MtbA or MtaA. SIMILARITY: Belongs to the methylamine corrinoid protein family.


FUNCTION: Zinc phosphodiesterase, which displays tRNA 3'-processing endonuclease activity. Involved in tRNA maturation, by removing a 3'- trailer from precursor tRNA. Can process the mitochondrial tRNA-like structures (t-elements). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the RNase Z family.


FUNCTION: Participates in the assembly of the infectious particles by decorating the outer surface of the capsid shell and thus forming a layer between the capsid and the tegument. Complexes composed of the capsid protein VP5 and UL48A assemble together in the host cytoplasm and are translocated to the nucleus, where they accumulate and participate in capsid assembly. FUNCTION: Participates in the assembly of the infectious particles by decorating the outer surface of the capsid shell and thus forming a layer between the capsid and the tegument. Complexes composed of the major capsid protein and small capsomere-interacting protein/SCP assemble together in the host cytoplasm and are translocated to the nucleus, where they accumulate and participate in capsid assembly. SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the herpesviridae small capsomere-interacting protein family.


FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. FUNCTION: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase B chain family.


FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:25759169). F-type ATP synthases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:27791192). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). Part of the complex F(0) domain (PubMed:27791192). Minor subunit located with subunit a/ATP6 in the membrane (PubMed:27791192). SUBCELLULAR LOCATION: Mitochondrion inner membrane Note=The F-type ATP synthase complex is anchored in the mitochondrial inner membrane via the F(0) domain with the F(1) domain and the peripheral stalk extending into the mitochondrial matrix. SIMILARITY: Belongs to the ATPase F chain family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0750 family.


FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex.


FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell junction, desmosome Cytoplasm Nucleus.


FUNCTION: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+) and Co(2+) but to a much less extent than Mg(2+) (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Early endosome Note=Recruited to the cell membrane in response to low extracellular magnesium. SIMILARITY: Belongs to the NIPA (TC 2.A.7) family.


FUNCTION: Putative sodium-dependent amino acid/proton antiporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.


FUNCTION: Involved in the Preiss-Handler pathway, which is a recycling route that permits the salvage of free nicotinamide (NM) and nicotinic acid (Na) involved in the NAD biosynthesis. Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP. It is not able to use nicotinamide. PncB1 contributes to basal NAD level (By similarity). SIMILARITY: Belongs to the NAPRTase family.


FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family.


FUNCTION: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport pathways (PubMed:26783301). Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the rab-5-to-rab-7 endosome conversion probably implicating sand-1, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion (By similarity). The HOPS complex is proposed to be recruited to rab-7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes (By similarity). Within the HOPS complex, contributes to the normal development of gut granules in the adult intestine (PubMed:15843430, PubMed:24501423, PubMed:25273556). The CORVET complex is proposed to function as a rab-5 effector to mediate early endosome fusion probably in specific endosome subpopulations (By similarity). Required for recruitment of vps-33.1 to the HOPS complex (By similarity). Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with vps-33.1 but not vps-33.2 (By similarity). SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane protein; Cytoplasmic side Lysosome membrane; Peripheral membrane protein; Cytoplasmic side Note=Cytoplasmic, peripheral membrane protein associated with late endosomes/lysosomes. SIMILARITY: Belongs to the VPS16 family.


FUNCTION: Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. Plays a role in the regulation of cell proliferation. May act as a tumor suppressor. Inhibits tumor cell growth. FUNCTION: Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. Plays a role in the regulation of cell proliferation. May act as a tumor suppressor (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion. Note=Detected along actin stress fibers. SUBCELLULAR LOCATION: Cytoplasm Cell junction, focal adhesion Note=Detected along actin stress fibers. SIMILARITY: Belongs to the prickle / espinas / testin family.


FUNCTION: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes. May be involved in transport from the vacuolar compartment to the cytoplasm (By similarity). SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Note=Tonoplast. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. TIP (TC 1.A.8.10) subfamily.


SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.


FUNCTION: E3 ubiquitin-protein ligase involved in the positive regulation of abscisic acid-dependent drought stress responses (PubMed:22405823). Involved in the positive regulation of responses to salt and osmotic stresses during seed germination and early seedling development (PubMed:23951086). Possesses E3 ubiquitin ligase activity in vitro (PubMed:22405823, PubMed:23951086). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus.


FUNCTION: Probable component of a ligand-gated anion channel. Negatively regulates synaptic transmission and synaptic vesicle release in response to acetylcholine in cholinergic motor neurons. Role in synaptic vesicle release kinetics may be in association with the ligand-gated ion channel protein acc-4. SUBCELLULAR LOCATION: Presynaptic cell membrane; Multi-pass membrane protein Cell projection, axon Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.


FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mS42 family.


FUNCTION: Binds to the G-box-like motif (5'-ACGTGGC-3') of the chalcone synthase (CHS) gene promoter. G-box and G-box-like motifs are defined in promoters of certain plant genes which are regulated by such diverse stimuli as light-induction or hormone control. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family.


FUNCTION: Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. Does not constitute the major arsenate reductase in cells: essential only in the absence of ArsC (AC P74313). SIMILARITY: Belongs to the ArsC family.


FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, perinuclear region Cell projection, growth cone Cell projection Note=Binds lipids with phosphatidylinositol 3,4,5-trisphosphate groups (By similarity). Perinuclear in undifferentiated PC12 cells. Redistributes to growing neurites and growth cones during NGF-induced neuronal differentiation (By similarity). Localizes at the leading edge of migrating cells (By similarity). SIMILARITY: Belongs to the EXO84 family.


FUNCTION: Recombinant C-type lectin BML-1 is able to agglutinate erythrocytes. May be a calcium-dependent lectin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the true venom lectin family.


FUNCTION: Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. When antigen presenting cells (APC) activate T-cell receptor (TCR), a series of phosphorylation lead to the recruitment of ITK to the cell membrane, in the vicinity of the stimulated TCR receptor, where it is phosphorylated by LCK. Phosphorylation leads to ITK autophosphorylation and full activation. Once activated, phosphorylates PLCG1, leading to the activation of this lipase and subsequent cleavage of its substrates. In turn, the endoplasmic reticulum releases calcium in the cytoplasm and the nuclear activator of activated T-cells (NFAT) translocates into the nucleus to perform its transcriptional duty. Phosphorylates 2 essential adapter proteins: the linker for activation of T-cells/LAT protein and LCP2. Then, a large number of signaling molecules such as VAV1 are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation (PubMed:12186560, PubMed:12682224, PubMed:21725281). Required for TCR-mediated calcium response in gamma-delta T-cells, may also be involved in the modulation of the transcriptomic signature in the Vgamma2-positive subset of immature gamma-delta T-cells (By similarity). Phosphorylates TBX21 at 'Tyr-530' and mediates its interaction with GATA3 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes in the vicinity of cell surface receptors in the plasma membrane after receptor stimulation. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. TEC subfamily.


FUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine) (By similarity). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation (By similarity). Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2) (By similarity). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription (By similarity). LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency (By similarity). Involved in epithelial to mesenchymal transition (EMT) and participates in repression of E-cadherin, probably by mediating deamination of histone H3 (By similarity). When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (By similarity). Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding (PubMed:21835952). Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation (By similarity). Required with loxl2a for correct expression of Sox2 and for neural differentiation (PubMed:25959397). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane Nucleus Chromosome Endoplasmic reticulum Note=Associated with chromatin. It is unclear how LOXL2 is nuclear as it contains a signal sequence and has been shown to be secreted. However, a number of reports confirm its intracellular location and its key role in transcription regulation. SIMILARITY: Belongs to the lysyl oxidase family.


FUNCTION: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNA methyltransferase RsmE family.


FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the RuBisCO small chain family.


FUNCTION: May be involved in the regulation of cell differentiation. FUNCTION: Promotes intracellular multiplication of tobamoviruses, probably being a component of the replication complex. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tetraspanin (TM4SF) family.


FUNCTION: May form complexes with phosphorylated ligands by interfering with kinases and their effectors. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein family.


FUNCTION: Component of the cap-binding complex (CBC), which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5'-end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2 and is required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP1/CBP80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a high affinity cap-binding state with the cap structure. Associates with NCBP3 to form an alternative cap-binding complex (CBC) which plays a key role in mRNA export and is particularly important in cellular stress situations such as virus infections. The conventional CBC with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus whereas the alternative CBC with NCBP3 does not bind snRNA and associates only with mRNA thereby playing a role only in mRNA export. NCBP1/CBP80 is required for cell growth and viability (PubMed:26382858). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. SIMILARITY: Belongs to the NCBP1 family.


SIMILARITY: Belongs to the UPF0276 family.


FUNCTION: Adapter protein for the cul3 E3 ubiquitin-protein ligase complex. Promotes the export of zbtb16/plzf from the nucleus to the cytoplasm and targets zbtb16/plzf for ubiquitination and degradation. Up-regulates neurog1 expression and antagonizes zbtb16/plzf, to promote neurogenesis. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Present mainly, but not excusively in the cytoplasm.


FUNCTION: Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding to specific cellular receptor. Once attached, the virion is endocytosed. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm. SIMILARITY: Belongs to the caliciviridae capsid protein family.


FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution (By similarity). SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the beta type-B retroviral envelope protein family. HERV class-II K(HML-8) env subfamily.


FUNCTION: Water channel required to facilitate the transport of water across membranes (Probable). Involved in conidiation (PubMed:26527167). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.


FUNCTION: Participates in receptor endocytosis during interphase, is also involved in mitotic processes when endocytosis is switched off.


FUNCTION: Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes (PubMed:24790029, PubMed:26824658, PubMed:28193731). The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine (PubMed:24790029, PubMed:26824658). Mediates efflux of amino acids, such as aspartate, in response to osmotic stress (PubMed:28193731). The VRAC channel also mediates transport of immunoreactive cyclic dinucleotide GMP-AMP (2'- 3'-cGAMP), an immune messenger produced in response to DNA virus in the cytosol (PubMed:33171122). Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition (PubMed:24790029, PubMed:26824658, PubMed:28193731). Also plays a role in lysosome homeostasis by forming functional lysosomal VRAC channels in response to low cytoplasmic ionic strength condition: lysosomal VRAC channels are necessary for the formation of large lysosome-derived vacuoles, which store and then expel excess water to maintain cytosolic water homeostasis (PubMed:33139539). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endoplasmic reticulum membrane Lysosome membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=In the absence of LRRC8A, resides primarily in the endoplasmic reticulum (PubMed:24790029, PubMed:33139539). Requires LRRC8A for localization at the cell membrane or lysosome membrane (PubMed:24790029, PubMed:33139539). SIMILARITY: Belongs to the LRRC8 family.


FUNCTION: Catalyzes the addition of a second glycerol phosphate unit from CDP-glycerol to the prenolpyrophosphate-linked disaccharide, to complete the linkage unit. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the CDP-glycerol glycerophosphotransferase family.


FUNCTION: May play a role in epithelial cell-cell contacts. May play a role in tumor invasiveness and metastasis formation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type III membrane protein Cytoplasmic vesicle membrane; Single-pass type III membrane protein Note=Predominantly on lateral parts of the membrane, at cell-cell epithelial junctions. Detected on cytoplasmic membranes in undifferentiated tumors. SIMILARITY: Belongs to the SMAGP family.


FUNCTION: May mediate protein transfer from the SecYEG translocon to the periplasmic chaperone network via its periplasmic C-terminal region. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein; Periplasmic side. SIMILARITY: Belongs to the YfgM family.


FUNCTION: Protein-disulfide reductase of the endoplasmic reticulum that promotes disulfide bond formation in client proteins through its thiol- disulfide oxidase activity. May function as an important antioxidant, and may be involved in the responses to viral infection. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.


FUNCTION: Is lethal to drosophila larvae. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the turripeptide family.


FUNCTION: May be involved in the unfolded protein response (UPR) during ER stress. SUBCELLULAR LOCATION: Secreted Endoplasmic reticulum lumen.


FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit F family.


FUNCTION: Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across the endoplasmic reticulum (ER). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypeptides (By similarity). The SEC61 channel is also involved in ER membrane insertion of transmembrane proteins: it mediates membrane insertion of the first few transmembrane segments of proteins, while insertion of subsequent transmembrane regions of multi-pass membrane proteins is mediated by the multi-pass translocon (MPT) complex (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SecE/SEC61-gamma family.


FUNCTION: [Isoform 3]: Sequesters MAD2L1 in the cytoplasm preventing its function as an activator of the mitotic spindle assembly checkpoint (SAC) resulting in SAC impairment and chromosomal instability in hepatocellular carcinomas. FUNCTION: Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate (PubMed:10049595, PubMed:20133940, PubMed:29162720). Forms a heterotetrameric complex with the closed conformation form of MAD2L1 (C-MAD2) at unattached kinetochores during prometaphase, recruits an open conformation of MAD2L1 (O-MAD2) and promotes the conversion of O-MAD2 to C-MAD2, which ensures mitotic checkpoint signaling (PubMed:29162720). SUBCELLULAR LOCATION: Nucleus Chromosome, centromere, kinetochore Nucleus envelope Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, spindle pole Note=Co- localizes with TPR at the nucleus envelope during interphase and throughout the cell cycle (PubMed:22351768, PubMed:18981471). From the beginning to the end of mitosis, it is seen to move from a diffusely nuclear distribution to the centrosome, to the spindle midzone and finally to the midbody (PubMed:9546394). Localizes to kinetochores during prometaphase (PubMed:22351768, PubMed:29162720). Does not localize to kinetochores during metaphase (PubMed:29162720). Colocalizes with NEK2 at the kinetochore (PubMed:14978040). Colocalizes with IK at spindle poles during metaphase and anaphase (PubMed:22351768). SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. SIMILARITY: Belongs to the MAD1 family.


SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WNK subfamily.


FUNCTION: Recruits and activates the Arp2/3 complex, which in turn leads to actin polymerization, promoting Rickettsia motility during infection. SUBCELLULAR LOCATION: Cell surface.


SIMILARITY: Belongs to the UDPGP type 1 family.


FUNCTION: Catalyzes the cyclization of 2-methylgeranyl diphosphate (2- MeGPP) to 2-methylisoborneol (2-MIB), which likely involves the intermediacy of 2-methyllinalyl diphosphate. Is also able to catalyze the cyclization of geranyl diphosphate (GPP), albeit with much lower efficiency, leading to the formation of a complex mixture of cyclic monoterpenes, consisting of alpha-pinene (6%), beta-pinene (23%), limonene (32%), gamma-terpinene (29%), and delta-terpinene (10%). SIMILARITY: Belongs to the terpene synthase family. 2-methylisoborneol synthase subfamily.


FUNCTION: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain (PubMed:30905148). IccB collaborates with the hybrid PKS-NRPS synthetase iccA to assemble the backbone of ilicicolin H (PubMed:30905148). The PKS portion of iccA and trans- acting enoyl reductase iccB work together to construct an octaketide, and two methyl groups are introduced by the MT domain of iccA during the chain assembly (PubMed:30905148). The nascent chain is then condensed with tyrosine, catalyzed by the iliA C domain, and the resulting PKS-NRPS hybrid is offloaded by the iliA RED domain to form an advanced tetramic acid intermediate (PubMed:30905148). The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iccA with the partnering trans-enoyl reductase iccB since iccA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iccC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iccD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. Finally, the epimerase iccE converts 8-epi-ilicicolin H into ilicicolin H via epimerization. IccA to iccE are sufficient for ilicicolin H biosynthesis and the roles of the remaining enzymes, iccF, iccG and iccH within the pathway have still to be determined (PubMed:30905148) (Probable). SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.


FUNCTION: Required for correct processing of both the 5' and 3' ends of 5S rRNA precursor. Cleaves both sides of a double-stranded region yielding mature 5S rRNA in one step. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ribonuclease M5 family.


FUNCTION: Receptor for prostaglandin F2-alpha (PGF2-alpha). The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. Initiates luteolysis in the corpus luteum. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Metamorphosin A may be part of an internal signaling system involved in control of metamorphosis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the LWamide neuropeptide family.


SIMILARITY: Belongs to the complex I NDUFA4 subunit family.


FUNCTION: Catalyzes the depolymerization of alginate by cleaving the beta-1,4 glycosidic bond between two adjacent sugar residues via a beta-elimination mechanism. May serve to degrade mislocalized alginate that is trapped in the periplasmic space. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the polysaccharide lyase 5 family.


FUNCTION: Mitochondrial E3 ubiquitin-protein ligase that plays a crucial role in the control of mitochondrial morphology by acting as a positive regulator of mitochondrial fission. May play a role in the prevention of cell senescence acting as a regulator of mitochondrial quality control. Promotes ubiquitination of FIS1, DNM1L and MFN1. FUNCTION: Mitochondrial E3 ubiquitin-protein ligase that plays a crucial role in the control of mitochondrial morphology by acting as a positive regulator of mitochondrial fission. May play a role in the prevention of cell senescence acting as a regulator of mitochondrial quality control. Promotes ubiquitination of FIS1, DNM1L and MFN1. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Authors show that the protein can be detected in endoplasmic reticulum (PubMed:14722266). Authors (PubMed:16874301) show its presence only in mitochondria (PubMed:16874301). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein.


FUNCTION: Transcription factor involved in the control of strigolactone biosynthesis in roots through the activation of the beta-carotene isomerase D27, which participates in a pathway leading to biosynthesis of strigolactones. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GRAS family.


FUNCTION: [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. FUNCTION: [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway. FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. FUNCTION: [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). FUNCTION: [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic GolGi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side Note=Located in RE-derived vesicles hosting the replication complex. SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane; Multi-pass membrane protein Host endoplasmic reticulum membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane; Multi-pass membrane protein Host endoplasmic reticulum membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: [Peptide pr]: Secreted. SUBCELLULAR LOCATION: [Capsid protein C]: Virion Host nucleus Host cytoplasm Host cytoplasm, host perinuclear region.


SUBCELLULAR LOCATION: Note=Starch granule. SIMILARITY: Belongs to the Poa p IX/Phl p VI allergen family.


FUNCTION: Calcium- and diacylglycerol-independent serine/ threonine- protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI(3)K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis. Involved in early synaptic long term potentiation phase in CA1 hippocampal cells and short term memory formation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Membrane Endosome Nucleus Note=Transported into the endosome through interaction with SQSTM1/p62. After phosphorylation by SRC, transported into the nucleus through interaction with KPNB1. Colocalizes with CDK7 in the cytoplasm and nucleus. Transported to vesicular tubular clusters (VTCs) through interaction with RAB2A. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.


FUNCTION: Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, pVIII, and pX) inside newly assembled particles giving rise to mature virions. Protease complexed to its cofactor slides along the viral DNA to specifically locate and cleave the viral precursors. Mature virions have a weakened organization compared to the unmature virions, thereby facilitating subsequent uncoating. Without maturation, the particle lacks infectivity and is unable to uncoat. Late in adenovirus infection, in the cytoplasm, may participate in the cytoskeleton destruction. Cleaves host cell cytoskeletal keratins K7 and K18. SUBCELLULAR LOCATION: Virion Host nucleus Note=Present in about 10 copies per virion. SIMILARITY: Belongs to the peptidase C5 family.


SIMILARITY: Belongs to the IIV-6 329R family.


FUNCTION: Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins. Required for the translocation of pullulanase. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the GSP C family.


FUNCTION: Binds specifically to the neurotoxin saxitoxin. Its physiological role may be to transport or sequester an endogenous organic molecule other than Fe(3+). It may participate in a detoxification mechanism for neutralizing a microbial toxin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the transferrin family.


FUNCTION: Hydrolyzes nucleotides into nucleosides (By similarity). Snake venom 5'-nucleotidases are widely distributed among venomous snake taxa, but there is a lack of information about their biological activities. They have been shown to inhibit platelet aggregation. This effect may be due to the liberation of inhibitory AMP or adenosine by its action on ADP released upon initiation of aggregation. Venom 5'- nucleotidases are also known to synergistically act in vivo with other toxins like ADPases, phospholipases, and disintegrins to exert a more pronounced anti-coagulant effect. SUBCELLULAR LOCATION: Membrane; Lipid- anchor, GPI-anchor. SIMILARITY: Belongs to the 5'-nucleotidase family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DP1 family.


FUNCTION: Transcription factor that regulates specifically the 4'- methoxyviridicatin/aspoquinolone biosynthesis cluster (PubMed:25251934). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Probable transcription factor involved in somatic embryogenesis. Acts as positive regulator of BHLH109. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Functions as sphingoid long-chain base phosphate (LCBP) phosphatase. May play a role in the regulation of LCBP levels and be involved in stomatal responses through LCBP-mediated ABA signaling. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the type 2 lipid phosphate phosphatase family.


FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine 5'- monophosphate (dUMP) to thymidine 5'-monophosphate (dTMP), using the cosubstrate, 5,10- methylenetetrahydrofolate (CH2H4folate) as a 1- carbon donor and reductant and contributes to the de novo mitochondrial thymidylate biosynthesis pathway. SUBCELLULAR LOCATION: Nucleus Cytoplasm Mitochondrion Mitochondrion matrix Mitochondrion inner membrane. SIMILARITY: Belongs to the thymidylate synthase family.


FUNCTION: Plays a role in primary cilia formation (By similarity). May act as a downstream effector of HOXC8 possibly by transducing or transmitting extracellular information required for axial skeletal patterning during development (By similarity). May be involved in cartilage and bone development (By similarity). May play a role in the differentiation of cranial neural crest cells (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, cilium basal body Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TAPT1 family.


FUNCTION: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism. SIMILARITY: Belongs to the GlnD family.


SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DMRT family.


FUNCTION: Probable component of the salicylic acid (SA) defense signaling pathway and pathogen-induced systemic acquired resistance (SAR) (Probable). May be involved in disease resistance against fungal pathogens (Probable). May be involved in tolerance to salt and osmotic stresses (PubMed:24407603).


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 eL37 family.


FUNCTION: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus. Membrane; Lipid- anchor. SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion. SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.


FUNCTION: Component of the ribosomal small subunit processome for the biogenesis of ribosomes, functions in pre-ribosomal RNA (pre-rRNA) processing (By similarity). Essential for embryonic development in part through the regulation of p53 pathway. Controls the expansion growth of digestive organs and liver (PubMed:29262616, PubMed:32303961). Also involved in the sympathetic neuronal development (By similarity). Mediates, with CAPN3, the proteasome-independent degradation of p53/TP53 (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the UTP25 family.


FUNCTION: Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein, possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)- alpha-GDP complex. Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Colocalizes with RIC8A in CA2 hippocampal neurons. Colocalizes with GNAI1 and RGS14 at the plasma membrane (By similarity). SIMILARITY: Belongs to the synembryn family.


FUNCTION: Catalyzes the two steps reaction converting geranylgeranyl diphosphate to phytoene via prephytoene diphosphate. SUBCELLULAR LOCATION: Plastid, chromoplast stroma. SIMILARITY: Belongs to the phytoene/squalene synthase family.


FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Probably involved in the regulatory network controlling carbon source utilization. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RSP5/NEDD4 family.


FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the histidinol dehydrogenase family.


FUNCTION: Induces local and distal defense responses (incompatible hypersensitive reaction) in plants from the solanaceae and cruciferae families. Elicits leaf necrosis and causes the accumulation of pathogenesis-related proteins. Might interact with the lipidic molecules of the plasma membrane. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the elicitin family.


FUNCTION: Asymmetrically hydrolyzes Ap4p to yield AMP and ATP. SIMILARITY: Belongs to the PrpE family.


FUNCTION: Catalyzes the depolymerization of both polygalacturonate and pectins with low (20-34%) and high (90%) levels of methyl esterification, with an endo mode of action. In contrast to the majority of pectate lyases, displays high activity on highly methylated pectins. Does not show xylanase and cellulase activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the polysaccharide lyase 3 family.


FUNCTION: Inhibits BMP signaling. Acts as a transcriptional corepressor of LBX1 (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SKI family.


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


FUNCTION: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the COQ4 family.


FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2. Metabolizes cholesterol toward 25- hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. May act as a major enzyme for all-trans retinoic acid biosynthesis in the liver. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. Primarily catalyzes stereoselective epoxidation of the last double bond of polyunsaturated fatty acids (PUFA), displaying a strong preference for the (R,S) stereoisomer. Catalyzes bisallylic hydroxylation and omega-1 hydroxylation of PUFA. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase- like reaction, NADPH-independent). Plays a role in the oxidative metabolism of xenobiotics. Catalyzes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin. Metabolizes caffeine via N3-demethylation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


SIMILARITY: Belongs to the MST(3)CGP family.


FUNCTION: Might be involved in Fe(2+) ion uptake (By similarity). SIMILARITY: Belongs to the FeoA family.


FUNCTION: Involved in light signaling, mainly phyA-mediated photomorphogenesis and in the integration of various phytohormone signals to modulate various aspects of plant development by affecting glutathione pools. In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the GST superfamily. Tau family.


FUNCTION: Beta-D-xylosidase showing an optimal efficiency with the natural substrate xylobiose. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 3 family.


FUNCTION: Regulator of protein export for NES-containing proteins. Also plays a role in mRNA nuclear export (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between the nucleus and the cytoplasm.


FUNCTION: Aminopeptidase with broad substrate specificity. Has lower activity with substrates that have Asp or Glu in the P2' position, or Pro in the P3' position. Lacks activity with substrates that have both Pro in the P3' position and Asp or Glu in the P2' position (PubMed:25752612). Lacks carboxypeptidase activity. Lacks dipeptidyl- peptidase IV type activity (PubMed:25752612). SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II membrane protein Note=Ileal brush border membrane. SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.


FUNCTION: Involved in regulating membrane fusion at the tonoplast and the prevacuolar compartment. SUBCELLULAR LOCATION: Vacuole membrane; Peripheral membrane protein Prevacuolar compartment membrane; Peripheral membrane protein. SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family.


FUNCTION: Probably acts synergistically with sop-2 to maintain the transcriptionally repressive state of homeotic genes in order to regulate various neurogenic identities. Specification of some neuronal identities also involves expression of non-Hox genes. Specifies dopaminergic and serotonergic neuronal cell fate, and regulates neurotransmitter choice and axon pathfinding. SUBCELLULAR LOCATION: Cytoplasm Nucleus.


FUNCTION: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein component 1 family.


FUNCTION: Plays a role in innate immunity (PubMed:35938871). Mechanistically, promotes alphaviruses RNA degradation by interacting with the viral polymerase nsP4 and the mRNA-capping enzyme nsP1 and thereby interfering with the interaction between viral RNA and nsP1.(PubMed:35938871). SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein Lysosome membrane; Multi-pass membrane protein Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM45 family.


FUNCTION: Dehydrogenase; part of the gene cluster that mediates the biosynthesis of the selective antifungal agent ascochitine, an o- quinone methide that plays a possible protective role against other microbial competitors in nature and is considered to be important for pathogenicity of legume-associated Didymella species (PubMed:31554725). The pathway probably begins with the synthesis of a keto-aldehyde intermediate by the ascochitine non-reducing polyketide synthase pksAC from successive condensations of 4 malonyl-CoA units, presumably with a simple acetyl-CoA starter unit (Probable). Release of the keto-aldehyde intermediate is consistent with the presence of the C-terminal reductive release domain (Probable). The HR-PKS (orf7) probably makes a diketide starter unit which is passed to the non-reducing polyketide synthase pksAC for further extension, producing ascochital and ascochitine (Probable). The aldehyde dehydrogenase (orf1), the 2- oxoglutarate-dependent dioxygenase (orf3) and the dehydrogenase (orf9) are probably involved in subsequent oxidations of methyl groups to the carboxylic acid of the heterocyclic ring (Probable). The ascochitine gene cluster also includes a gene encoding a short peptide with a cupin domain (orf2) that is often found in secondary metabolite gene clusters and which function has still to be determined (Probable). SIMILARITY: Belongs to the GMC oxidoreductase family.


FUNCTION: F-actin regulator involved in anterograde Golgi to endosome transport: upon ubiquitination via 'Lys-33'-linked ubiquitin chains by the BCR(KLHL20) E3 ubiquitin ligase complex, interacts with EPS15 and localizes to the trans-Golgi network, where it promotes actin polymerization, thereby facilitating post-Golgi trafficking. May play a role in the maintenance of the Golgi apparatus morphology (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane Golgi apparatus, trans-Golgi network Cytoplasmic vesicle Cytoplasm, cytosol Note=Predominantly cytosolic. Detected on vesicle-like cytoplasmic structures and on the cis-Golgi. Not associated with actin filaments. SIMILARITY: Belongs to the WD repeat coronin family.


FUNCTION: Bifunctional nuclease with both RNase and DNase activities. Involved in basal defense response. Participates in abscisic acid- derived callose deposition following infection by a necrotrophic pathogen (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bifunctional nuclease family.