Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
A4GXA9 | EME2_HUMAN | MARVGPGRAGVSCQGRGRGRGGSGQRRPPTWEISDSDAEDSAGSEAAARARDPAGERRAAAEALRLLRPEQVLKRLAVCVDTAILEDAGADVLMEALEALGCECRIEPQRPARSLRWTRASPDPCPRSLPPEVWAAGEQELLLLLEPEEFLQGVATLTQISGPTHWVPWISPETTARPHLAVIGLDAYLWSRQHVSRGTQQPESPKVAGAEVAVSWPEVEEALVLLQLWANLDVLLVASWQELSRHVCAVTKALAQYPLKQYRESQAFSFCTAGRWAAGEPVARDGAGLQAAWRRQIRQFSRVSPAVADAVVTAFPSPRL... | 3.1.22.- | null | double-strand break repair [GO:0006302]; mitotic intra-S DNA damage checkpoint signaling [GO:0031573]; replication fork processing [GO:0031297]; resolution of meiotic recombination intermediates [GO:0000712] | endodeoxyribonuclease complex [GO:1905347]; Holliday junction resolvase complex [GO:0048476]; nuclear replication fork [GO:0043596] | crossover junction DNA endonuclease activity [GO:0008821]; DNA binding [GO:0003677] | PF21292;PF02732; | 3.40.50.10130;1.10.150.670; | EME1/MMS4 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Interacts with MUS81 to form a DNA structure-specific endonuclease which cleaves substrates such as 3'-flap structures. {ECO:0000269|PubMed:17289582}. | Homo sapiens (Human) |
A4IFH6 | PPLA_BOVIN | MDKVQYLTRSAIRRASTIEMPQQARQNLQNLFINFCLISICLLLICIIVMLL | null | null | acrosome assembly [GO:0001675]; intracellular calcium ion homeostasis [GO:0006874]; negative regulation of ATPase-coupled calcium transmembrane transporter activity [GO:1901895]; negative regulation of calcium ion import into sarcoplasmic reticulum [GO:1902081]; negative regulation of heart rate [GO:0010459] | endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum membrane [GO:0033017] | ATPase inhibitor activity [GO:0042030]; protein homodimerization activity [GO:0042803] | PF04272; | 1.20.5.290; | Phospholamban family | PTM: Phosphorylation by PKA abolishes the inhibition of ATP2A2-mediated calcium uptake. Phosphorylated at Thr-17 by CaMK2, and in response to beta-adrenergic stimulation. Phosphorylation by DMPK may stimulate sarcoplasmic reticulum calcium uptake in cardiomyocytes (By similarity). {ECO:0000250|UniProtKB:P26678}.; PTM: ... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26678}; Single-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26678}; Single-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:17060615}; Single-pass membrane protein ... | null | null | null | null | null | FUNCTION: Reversibly inhibits the activity of ATP2A2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulates calcium re-uptake during muscle relaxation and pl... | Bos taurus (Bovine) |
A4IFJ5 | PA24A_BOVIN | MSFIDPYQHIIVEHHYSHKFTVVVLRATKVTKGTFGDMLDTPDPYVELFISSTPDSRKRTRHFNNDINPVWNETFEFILDPNQENILEITLMDANYVMDETLGTTTFPISSMKVGEKKQVPFIFNQVTEMILEMSLEVCSSPDLRFSMALCDQEKAFRQQRKENIKENMKKLLGPKNSEGLHSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYIAGLSGSTWYMSTLYSHPDFPEKGPEEINKELMKNVSHNPLLLLTPQKIKRYVESLWRKKSSGQPVTFTDIFGMLIGETLIHNRMNTTLSSLKEKVN... | 3.1.1.4; 3.1.1.5 | null | arachidonic acid metabolic process [GO:0019369]; glycerol metabolic process [GO:0006071]; glycerophospholipid catabolic process [GO:0046475]; leukotriene biosynthetic process [GO:0019370]; monoacylglycerol biosynthetic process [GO:0006640]; phosphatidylcholine acyl-chain remodeling [GO:0036151]; phosphatidylcholine cat... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nuclear envelope [GO:0005635]; nucleus [GO:0005634] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; calcium-dependent phospholipid binding [GO:0005544]; calcium-independent phospholipase A2 activity [GO:0047499]; ceramide 1-phosphate binding [GO:1902387]; lysophospholipase activity [GO:0004622]; O-acyltransferase activity [GO:... | PF00168;PF01735; | 2.60.40.150;3.40.1090.10; | null | PTM: Phosphorylated at both Ser-505 and Ser-727 in response to mitogenic stimuli. {ECO:0000250|UniProtKB:P47712}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P47712}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P47712}. Nucleus envelope {ECO:0000250|UniProtKB:P47712}. Note=Translocates to intracellular membranes in a calcium-dependent way. {ECO:0000250|UniProtKB:P47712}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:P47712}; Physiologica... | null | PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism. {ECO:0000250|UniProtKB:P47713}.; PATHWAY: Lipid metabolism; arachidonate metabolism. {ECO:0000250|UniProtKB:P47712}.; PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000250|UniProtKB:P47712}.; PATHWAY: Lipid metabolism; leukotriene B4 bios... | null | null | FUNCTION: Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (By similarity). Plays an important role in embryo implantation and parturition through its ability to trigger prostan... | Bos taurus (Bovine) |
A4IG62 | SUV3_DANRE | MSVNRCIYLLSRSHIRYRVCASTNLSTVSTLSTTQHSTRRTFDKLSTRHSSSGSSRPLDTSLFIPLPVKTDEDAEGSVGAELTKPLDKNELLKVLNRFYKRKEMQKLASDQGLDARLFHQAFVSFRKYVLEMNSLNADLHIILNDICCGAGHIDDIFPYFMRHAKQIFPMLDCIDDLRKISDLRVPANWYPEARAIQRKIVFHAGPTNSGKTYHAIKRYLEAKSGVYCGPLKLLAHEIYEKSNAAGVPCDLVTGEERIFVDPEGKPSGHIASTIEMCSVTTPYEVAVIDEIQMIKDPARGWAWTRALLGLCAEEIHVCGE... | 3.6.4.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; | DNA duplex unwinding [GO:0032508]; DNA recombination [GO:0006310]; liver development [GO:0001889]; mitochondrial mRNA catabolic process [GO:0000958]; mitochondrial mRNA surveillance [GO:0035946]; mitochondrial ncRNA surveillance [GO:0035945]; mitochondrial RNA 3'-end processing [GO:0000965]; mitochondrial RNA surveilla... | mitochondrial degradosome [GO:0045025]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | 3'-5' RNA helicase activity [GO:0034458]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; double-stranded RNA binding [GO:0003725]; RNA helicase activity [GO:0003724] | PF00271;PF12513;PF18147;PF18114; | 1.10.1740.140;1.20.272.40;1.20.58.1080;3.40.50.300; | Helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; | null | null | null | null | FUNCTION: Major helicase player in mitochondrial RNA metabolism. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. ATPase and ATP-dependent multisubstrate helicase, able to unwind double-stranded (ds) DNA ... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A4IGL7 | PXDN_XENTR | MAGAGSWLYLTAGLLVVALPQLSHSCPSRCLCFRTTVRCMHLMLESVPAVPPHTTILDLRFNRIKDIQTGAFKHLKNLNTLLLNNNQIKRIPSEAFKDLENLKYLYLYKNEIQSIDRQAFKGLASLEQLYLHFNQIETLEPESFNYLPKLERLFLHNNRITHLVPGTFSQLESMKRLRLDSNALHCDCEILWLADLLKIYSESGNAQAAATCEYPRRLQGRSVSTITPSELNCERPRITSEPQDVDVTFGNTVYFTCRAEGNPKPEIIWLRNNNELSMKDDSRLNLLNDGTLMIQNTKETDQGIYQCMAKNVAGEVKTHE... | 1.11.2.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00298}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:A5JUY8, ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 heme b (... | angiogenesis [GO:0001525]; basement membrane assembly [GO:0070831]; basement membrane organization [GO:0071711]; cell adhesion [GO:0007155]; hydrogen peroxide catabolic process [GO:0042744]; protein homooligomerization [GO:0051260]; protein homotrimerization [GO:0070207]; response to oxidative stress [GO:0006979] | basement membrane [GO:0005604]; cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on peroxide as acceptor [GO:0016684] | PF03098;PF07679;PF00560;PF13855;PF01463;PF00093; | 6.20.200.20;1.10.640.10;2.60.40.10;3.80.10.10; | Peroxidase family, XPO subfamily | PTM: Glycosylated. {ECO:0000250|UniProtKB:Q92626}.; PTM: Processed by FURIN and the proteolytic processing largely depends on the peroxidase activity of PXDN (By similarity). The proteolytic cleavage occurs after intracellular homotrimerization and releases into the extracellular matrix a large, catalytically active fr... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q92626}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q92626}. Cell surface {ECO:0000250|UniProtKB:Q92626}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q3UQ28}. Note=Enriche... | CATALYTIC ACTIVITY: Reaction=H2O2 + L-lysyl-[collagen] + L-methionyl-[collagen] = [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + H(+) + 2 H2O; Xref=Rhea:RHEA:66020, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949, Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16044, ChEBI:CHEBI:16240, ChEBI:CHEBI:... | null | null | null | null | FUNCTION: Catalyzes the two-electron oxidation of bromide by hydrogen peroxide and generates hypobromite as a reactive intermediate which mediates the formation of sulfilimine cross-links between methionine and hydroxylysine residues within an uncross-linked collagen IV/COL4A1 NC1 hexamer and participates to the baseme... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A4IGM9 | AURKB_XENTR | MSYKENLNPSSYTSKFATPSSATAAQRVLRKEPYVSTFTTPSDNLLAQRAQLARITPSASSSVPGRVAVSMDASSQNTALAELPKRKFTIDDFDIGRPLGKGKFGNVYLARDKQNKFIMALKVLFKSQLEKEGVEHQLRREIEIQSHLRHPNILRMYNYFHDRKRIYLMLEFAPRGELYKELQKHGRFDEQRSATFMEELADALQYCHERKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLRRRTMCGTLDYLPPEMIEGKTHDEKVDLWCAGVLCFEFLVGMPPFDSPSHTETHRRIVNVDLKFPPFLSDGSKDLI... | 2.7.11.1 | null | abscission [GO:0009838]; cellular response to UV [GO:0034644]; cleavage furrow formation [GO:0036089]; mitotic cytokinesis checkpoint signaling [GO:0044878]; mitotic spindle midzone assembly [GO:0051256]; negative regulation of B cell apoptotic process [GO:0002903]; negative regulation of cytokinesis [GO:0032466]; nega... | chromatin [GO:0000785]; chromosome [GO:0005694]; chromosome passenger complex [GO:0032133]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; midbody [GO:0030496]; nucleus [GO:0005634]; spindle microtubule [GO:0005876]; spindle midzone [GO:0051233]; spindle pole centrosome [... | ATP binding [GO:0005524]; histone H3S10 kinase activity [GO:0035175]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, Aurora subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96GD4}. Chromosome {ECO:0000250|UniProtKB:Q96GD4}. Chromosome, centromere {ECO:0000250|UniProtKB:Q96GD4}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q96GD4}. Midbody {ECO:0000250|UniProtKB:Q96GD4}. Note=Localizes on chromosome arms and inner centromeres... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q96GD4}; CATALYTI... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabiliz... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A4IGY6 | S39AE_XENTR | MPLLLLSALLPFSLMAGPTPSTGKELSAASFLQDILQRYGENESLSMPQLQSLLENLEVGKGGGNQRNMSQCLSSSTLFAAHNLTSGSVVDAEGFQSFCPTILQQLETRACQESPAFQNETTPGAEGRPSPGEVWGYGFLCVTVISLCSLFGAGVVPFMKKACYKRLLLFCIALAIGTLFSNALFQLIPEAFGFNPLEDSYVFTSSVIFGGFYLFFFTEKVLKMMLKQKHEHGHSHYSADTSKRDAEEGVTEKLQNGDLDHMIPPPHGSESDLRGDEKAVQQQDLPGQQSSCYWLKGIRYSDIGTLAWMITLSDGLHNFI... | null | null | cellular response to glucose stimulus [GO:0071333]; cellular response to insulin stimulus [GO:0032869]; import across plasma membrane [GO:0098739]; inorganic cation transmembrane transport [GO:0098662]; intracellular zinc ion homeostasis [GO:0006882]; iron import into cell [GO:0033212]; iron ion transmembrane transport... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; early endosome membrane [GO:0031901]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886] | cadmium ion transmembrane transporter activity [GO:0015086]; iron ion transmembrane transporter activity [GO:0005381]; manganese ion transmembrane transporter activity [GO:0005384]; monoatomic anion:monoatomic cation symporter activity [GO:0015296]; monoatomic cation:bicarbonate symporter activity [GO:0140410]; zinc io... | PF02535; | null | ZIP transporter (TC 2.A.5) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Early endoso... | CATALYTIC ACTIVITY: Reaction=2 hydrogencarbonate(out) + Zn(2+)(out) = 2 hydrogencarbonate(in) + Zn(2+)(in); Xref=Rhea:RHEA:62252, ChEBI:CHEBI:17544, ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q75N73}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62253; Evidence={ECO:0000250|UniProtKB:Q75N73}; CATALYTIC ... | null | null | null | null | FUNCTION: Electroneutral transporter of the plasma membrane mediating the cellular uptake of the divalent metal cations zinc, manganese and iron that are important for tissue homeostasis, metabolism, development and immunity (By similarity). Functions as an energy-dependent symporter, transporting through the membranes... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A4IH17 | BAG6_XENTR | MEVTVKTLDSQTRTFTVDAEITVKEFKTHISSDVGISPEKQRLIYQGRVLQEDKKLKEYNVDGKVIHLVERAPPQTQPSTGGPSTSSSTSPSSSNAANVPGAGAPERNGNSYVMVGTFNLPHVMSGLGEASRGPRVSTVSGNDGSTLDVHINLDQQLPVQSEPRVRLVLAQQILQDIQRILDRLEGQPVNEQTAEPMDTAVSEGEASSRETLPQTTQNTDGQSNTAPTSHPSPSEYVEVLQSLSRVEERLAPFMQRYREILSSATSDAYENQEEREQSQRIINLVGESLRLLGNALVAVSDLRCNLSSASPRHLHVVRPM... | null | null | brain development [GO:0007420]; chromatin organization [GO:0006325]; endoplasmic reticulum stress-induced pre-emptive quality control [GO:0061857]; ERAD pathway [GO:0036503]; internal peptidyl-lysine acetylation [GO:0018393]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042... | BAT3 complex [GO:0071818]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleus [GO:0005634] | misfolded protein binding [GO:0051787]; polyubiquitin modification-dependent protein binding [GO:0031593]; proteasome binding [GO:0070628]; ribosome binding [GO:0043022] | PF12057;PF20960;PF00240; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P46379}. Nucleus {ECO:0000250|UniProtKB:P46379}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P46379}. | null | null | null | null | null | FUNCTION: ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins. Functions as part of a cytosolic protein quality control complex, the bag6/bat3 complex, which maintains these client proteins in a soluble state and participates in their proper delivery t... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A4IHB9 | SL9B2_XENTR | MEDSLFSVDKAGPGKDASAASADCNHMVAEDGIITEQHKEIPLVALKVPDGHAPIDECELLNSDDQLPKGSQNQTNICMRIRAFACPPQGCFSLAITNVTMVILIWAVVWSITGPECLPGGNLFGILALLFSAALGGKLISLIKIPSLPPLPPLLGMLLAGFLIRNIPVITDQVQIHHKWSAALRNIALAIILVRAGLGLDPKALRKLKAVCLRLSFGPCVVESCTAAVVSHFIMGFPLTWGFMLGFVLGAVSPAVVVPSMLILQKEGFGVDKGIPTLLMAAGSFDDVLAITGFNTCLGMAFSSGSTLNTIVRGVLEVVV... | null | null | proton transmembrane transport [GO:1902600]; sodium ion homeostasis [GO:0055078]; sodium ion transport [GO:0006814] | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; mitochondrial membrane [GO:0031966]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; synaptic vesicle membrane [GO:0030672] | antiporter activity [GO:0015297]; metal ion binding [GO:0046872] | PF00999; | 1.20.1530.20; | Monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Endosome membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane... | CATALYTIC ACTIVITY: Reaction=H(+)(in) + Li(+)(out) = H(+)(out) + Li(+)(in); Xref=Rhea:RHEA:72407, ChEBI:CHEBI:15378, ChEBI:CHEBI:49713; Evidence={ECO:0000250|UniProtKB:Q86UD5}; CATALYTIC ACTIVITY: Reaction=Li(+)(in) + Na(+)(out) = Li(+)(out) + Na(+)(in); Xref=Rhea:RHEA:72415, ChEBI:CHEBI:29101, ChEBI:CHEBI:49713; Evide... | null | null | null | null | FUNCTION: Electroneutral Na(+) Li(+)/H(+) antiporter that extrudes Na(+) or Li(+) in exchange for external protons across the membrane (By similarity). Uses the proton gradient/membrane potential to extrude sodium (By similarity). Contributes to the regulation of intracellular pH and sodium homeostasis (By similarity).... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A4IHS0 | TM10C_XENTR | MAFVNTLLRTIRCSAVHTLVQEGRSLSLLKASHQLTQSRKIMLSNHVRKEEAKSEPNETLDLEEWKSILKSDIGNAEMVKTETQEDSSLNEMQELVEMWRLAGRAVPQSITTEQLQVLMELPTKTARKKYLKYLSVREVMKTNRKEKKKELKESKSKIESLDQLETKEDTPEKKNTFLLHVWDKSIDTMQRWKCVQAMKFGQPLVFDMVYEKNMSRYELENTVCQLMESEGWNRRSTDPFHIYFCSLQPYSMYHKELVKRYIGAWDNVFVTATDKSHVEMFPKEQLVYLTADSPNELKHFDHTKIYIIGSLVDRCQQTGL... | 2.1.1.-; 2.1.1.218; 2.1.1.221 | null | mitochondrial tRNA 5'-end processing [GO:0097745]; mitochondrial tRNA processing [GO:0090646]; mRNA methylation [GO:0080009]; positive regulation of mitochondrial translation [GO:0070131] | mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654] | tRNA (adenine(9)-N1)-methyltransferase activity [GO:0160106]; tRNA (guanosine(9)-N1)-methyltransferase activity [GO:0052905]; tRNA binding [GO:0000049] | PF01746; | 3.40.1280.30; | Class IV-like SAM-binding methyltransferase superfamily, TRM10 family | null | SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q7L0Y3}. | CATALYTIC ACTIVITY: Reaction=adenosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(9) in tRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43148, Rhea:RHEA-COMP:10363, Rhea:RHEA-COMP:10364, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.218;... | null | null | null | null | FUNCTION: Mitochondrial tRNA N(1)-methyltransferase involved in mitochondrial tRNA maturation. Component of mitochondrial ribonuclease P, which cleaves tRNA molecules in their 5'-ends. Together with hsd17b10/mrpp2, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays func... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A4II96 | CNOT7_XENTR | MPAATVDLSQRICEVWACNLDDQMKRIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQLGLTFVNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTSSGIQFKKHEEEGIETQYFAELFMTSGVVLCEGVKWLSFHSGYDFGYLIKILTNSNLPEVELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELKRIGPQHQAGSDSLLTGMAFFKMREMFFEDHIDDAKYCGHLYGLGSGSSYVQNGTGNAYEEEANKQS | 3.1.13.4 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9UIV1}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9UIV1}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250|UniProtKB:Q9UIV1}; Note=Binds 2 divalent metal cations per subunit with RNAase activity being h... | exonucleolytic catabolism of deadenylated mRNA [GO:0043928]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900153]; positive regul... | CCR4-NOT complex [GO:0030014]; CCR4-NOT core complex [GO:0030015]; nucleus [GO:0005634]; P-body [GO:0000932] | 3'-5'-RNA exonuclease activity [GO:0000175]; metal ion binding [GO:0046872]; poly(A)-specific ribonuclease activity [GO:0004535]; RNA binding [GO:0003723]; RNA exonuclease activity [GO:0004532] | PF04857; | 3.30.420.10; | CAF1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; | null | null | null | null | FUNCTION: Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. Catalytic component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression duri... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A4IID1 | MGT4A_XENTR | MRLRNGTVATALVFITTFLSLSWYTAWQNGKEKLMAYQREFHALKERLRIAEHRTLQRSSELHAILDHFRRMIKEANGSRDALNHFSDETQKLIKDLTNRKALQVPNIYYHMPHLLNHDGSLQPAVQVGLGRTGVSVVMGIPTVKRRVKSYLKETLHSLIDKLSPEEKLDCVIIVFVGETDLEYVNSVVASLQKEFATEISSGLVEVISPPATYYPDLNNLKETFGDSKERVRWRTKQNLDYCFLMMYAQRKGIYYIQLEDDIVAKQNYFSTIKNFALQLSSEDWMILEFSQLGFIGKMFQAPDITLIVEFILMFYKEKP... | 2.4.1.145 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:O77836}; | glyoxylate metabolic process [GO:0046487]; N-glycan processing [GO:0006491]; protein N-linked glycosylation [GO:0006487] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular region [GO:0005576]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; peroxisome [GO:0005777] | alanine-glyoxylate transaminase activity [GO:0008453]; alpha-1,3-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity [GO:0008454]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803] | PF04666; | null | Glycosyltransferase 54 family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:O77836}. | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9D4R2}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9D4R2}.; SUBCELLULAR LOCATION: [Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form]: Secreted {ECO:0000250|UniProtKB:O77836}. | CATALYTIC ACTIVITY: Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcN... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:O77836}. | null | null | FUNCTION: Glycosyltransferase that catalyze the transfer of GlcNAc from UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans through a beta1-4 linkage and participates in the production of tri- and tetra-antennary N-linked sugar chains (By similarity). Involved in glucose transport b... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A4IIN5 | TISD_XENTR | MSTTLLSAFYDIDLLYKNEKVLNNLALSTMLDKKAVGSPVSSTNSNLFPGFLRRHSASNLQALSGNTNPAKFCPNNNQLKEPAAGSTALLNRENKFRDRSFSENGERSQHLLHLQQQQQQKAGAQVNSTRYKTELCRPFEESGACKYGEKCQFAHGFHELRSLTRHPKYKTELCRTFHTIGFCPYGPRCHFIHNAEERRQAPGAGERPKLHHSLSFSGFPNHSLDSPLLESPTSRTPPPQSSSSLYCQELLQLNNNNNPCANNAFTFSGQELGLIAPLAIHTQNPPYCRQPSSSPPLSFQPLRRVSESPVFDAPPSPPDS... | null | null | 3'-UTR-mediated mRNA destabilization [GO:0061158]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to granulocyte macrophage colony-stimulating factor sti... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904] | metal ion binding [GO:0046872]; mRNA 3'-UTR AU-rich region binding [GO:0035925] | PF04553;PF00642; | 4.10.1000.10; | null | PTM: Phosphorylated (By similarity). {ECO:0000250|UniProtKB:P23949, ECO:0000250|UniProtKB:P47974}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P23949}. Cytoplasm {ECO:0000250|UniProtKB:P23949}. Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner. {ECO:0000250|UniProtKB:P23949}. | null | null | null | null | null | FUNCTION: Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis (By similarity). Acts as a 3'-untranslated region (UTR) ARE mRNA-bin... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A4IU28 | LADA_GEOTN | MTKKIHINAFEMNCVGHIAHGLWRHPENQRHRYTDLNYWTELAQLLEKGKFDALFLADVVGIYDVYRQSRDTAVREAVQIPVNDPLMLISAMAYVTKHLAFAVTFSTTYEHPYGHARRMSTLDHLTKGRIAWNVVTSHLPSADKNFGIKKILEHDERYDLADEYLEVCYKLWEGSWEDNAVIRDIENNIYTDPSKVHEINHSGKYFEVPGPHLCEPSPQRTPVIYQAGMSERGREFAAKHAECVFLGGKDVETLKFFVDDIRKRAKKYGRNPDHIKMFAGICVIVGKTHDEAMEKLNSFQKYWSLEGHLAHYGGGTGYDL... | 1.14.14.28 | null | null | extracellular region [GO:0005576] | monooxygenase activity [GO:0004497]; nucleotide binding [GO:0000166]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF00296; | 3.20.20.30; | NtaA/SnaA/DszA monooxygenase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17372208}. | CATALYTIC ACTIVITY: Reaction=a long-chain alkane + FMNH2 + O2 = a long chain fatty alcohol + FMN + H(+) + H2O; Xref=Rhea:RHEA:49060, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17135, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:83563; EC=1.14.14.28; Evidence={ECO:0000269|PubMed:17372208, ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.1 mM for hexadecane {ECO:0000269|PubMed:22526792}; Note=kcat is 1.3 min(-1) with hexadecane as substrate. {ECO:0000269|PubMed:22526792}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:22526792}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:22526792}; | FUNCTION: Involved in the degradation of long-chain alkanes (PubMed:17372208, PubMed:22526792). Converts alkanes ranging from C(15) to C(36) into their corresponding primary alcohols (PubMed:17372208). {ECO:0000269|PubMed:17372208, ECO:0000269|PubMed:22526792}. | Geobacillus thermodenitrificans (strain NG80-2) |
A4K144 | M2_I54A2 | MSLLTEVETPIRNEWGCRCNDSSDPLIIAASVVGILHLILWILDRLFFKCIYRLFKHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVNIELE | null | null | protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078] | PF00599; | 6.10.250.1640; | Influenza viruses matrix protein M2 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximit... | null | null | null | null | null | FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is... | Influenza A virus (strain A/Malaysia:Malaya/302/1954 H1N1) |
A4K2M3 | STK4_PAPAN | METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQESQQREVDQDDEENS... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; hippo signaling [GO:0035329]; phosphorylation [GO:0016310]; protein tetramerization [GO:0051262]; regulation of MAPK cascade [GO:0043408] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF11629;PF00069; | 1.10.287.4270;4.10.170.10;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | PTM: Autophosphorylated on serine and threonine residues. Phosphorylation at Thr-387 by PKB/AKT1, leads to inhibition of its: kinase activity, nuclear translocation and autophosphorylation at Thr-183. It also diminishes its cleavage by caspases and its ability to phosphorylate FOXO3 (By similarity). {ECO:0000250|UniPro... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The caspase-cleaved form cycles between the nucleus and cytoplasm. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13043}; Physiolo... | null | null | null | null | FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting pro... | Papio anubis (Olive baboon) |
A4K2P5 | STK4_COLGU | METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATVLQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQESQQREVDQDDEENS... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; hippo signaling [GO:0035329]; phosphorylation [GO:0016310]; protein tetramerization [GO:0051262]; regulation of MAPK cascade [GO:0043408] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF11629;PF00069; | 1.10.287.4270;4.10.170.10;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | PTM: Autophosphorylated on serine and threonine residues. Phosphorylation at Thr-387 by PKB/AKT1, leads to inhibition of its: kinase activity, nuclear translocation and autophosphorylation at Thr-183. It also diminishes its cleavage by caspases and its ability to phosphorylate FOXO3 (By similarity). {ECO:0000250|UniPro... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The caspase-cleaved form cycles between the nucleus and cytoplasm. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13043}; Physiolo... | null | null | null | null | FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting pro... | Colobus guereza (Mantled guereza) (Eastern black-and-white colobus monkey) |
A4K2Q5 | STK4_OTOGA | METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVRQCLVKSPDQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQEAQQREVDQDDEENS... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; hippo signaling [GO:0035329]; phosphorylation [GO:0016310]; protein tetramerization [GO:0051262]; regulation of MAPK cascade [GO:0043408] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF11629;PF00069; | 1.10.287.4270;4.10.170.10;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | PTM: Autophosphorylated on serine and threonine residues. Phosphorylation at Thr-387 by PKB/AKT1, leads to inhibition of its: kinase activity, nuclear translocation and autophosphorylation at Thr-183. It also diminishes its cleavage by caspases and its ability to phosphorylate FOXO3 (By similarity). {ECO:0000250|UniPro... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The caspase-cleaved form cycles between the nucleus and cytoplasm. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13043}; Physiolo... | null | null | null | null | FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting pro... | Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby) |
A4K2S1 | STK4_LEMCA | METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFMDFVRQCLVKSPDQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQEAQQREVDQDDEENS... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; hippo signaling [GO:0035329]; phosphorylation [GO:0016310]; protein tetramerization [GO:0051262]; regulation of MAPK cascade [GO:0043408] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF11629;PF00069; | 1.10.287.4270;4.10.170.10;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | PTM: Autophosphorylated on serine and threonine residues. Phosphorylation at Thr-387 by PKB/AKT1, leads to inhibition of its: kinase activity, nuclear translocation and autophosphorylation at Thr-183. It also diminishes its cleavage by caspases and its ability to phosphorylate FOXO3 (By similarity). {ECO:0000250|UniPro... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The caspase-cleaved form cycles between the nucleus and cytoplasm. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13043}; Physiolo... | null | null | null | null | FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting pro... | Lemur catta (Ring-tailed lemur) |
A4K2T0 | STK4_MACMU | METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQESQQREVDQDDEENS... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; hippo signaling [GO:0035329]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; protein tetramerization [GO:0051262]; regulation of MAPK cascade [GO:0043408] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF11629;PF00069; | 1.10.287.4270;4.10.170.10;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | PTM: Autophosphorylated on serine and threonine residues. Phosphorylation at Thr-387 by PKB/AKT1, leads to inhibition of its: kinase activity, nuclear translocation and autophosphorylation at Thr-183. It also diminishes its cleavage by caspases and its ability to phosphorylate FOXO3 (By similarity). {ECO:0000250|UniPro... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The caspase-cleaved form cycles between the nucleus and cytoplasm. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13043}; Physiolo... | null | null | null | null | FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting pro... | Macaca mulatta (Rhesus macaque) |
A4K2W5 | STK4_AOTNA | METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSHHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQESQQREVDQDDEENS... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; protein tetramerization [GO:0051262]; regulation of MAPK cascade [GO:0043408] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF11629;PF00069; | 1.10.287.4270;4.10.170.10;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | PTM: Autophosphorylated on serine and threonine residues. Phosphorylation at Thr-387 by PKB/AKT1, leads to inhibition of its: kinase activity, nuclear translocation and autophosphorylation at Thr-183. It also diminishes its cleavage by caspases and its ability to phosphorylate FOXO3 (By similarity). {ECO:0000250|UniPro... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The caspase-cleaved form cycles between the nucleus and cytoplasm. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13043}; Physiolo... | null | null | null | null | FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting pro... | Aotus nancymaae (Ma's night monkey) |
A4K2Y1 | STK4_CHLAE | METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQESQQREVDQDDEENS... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; hippo signaling [GO:0035329]; phosphorylation [GO:0016310]; protein tetramerization [GO:0051262]; regulation of MAPK cascade [GO:0043408] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF11629;PF00069; | 1.10.287.4270;4.10.170.10;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | PTM: Autophosphorylated on serine and threonine residues. Phosphorylation at Thr-387 by PKB/AKT1, leads to inhibition of its: kinase activity, nuclear translocation and autophosphorylation at Thr-183. It also diminishes its cleavage by caspases and its ability to phosphorylate FOXO3 (By similarity). {ECO:0000250|UniPro... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The caspase-cleaved form cycles between the nucleus and cytoplasm. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13043}; Physiolo... | null | null | null | null | FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting pro... | Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops) |
A4K436 | RTEL1_BOVIN | MPKITLKGVTVDFPFQPYKCQEEYMSKVLECLQEKVNGILESPTGTGKTLCLLCSTLAWREHLRDAVSARRIAERASGELFPDRTLASWGNAIPEGDVPACYTDIPKIIYASRTHSQLTQVISELRNTSYRPRVCVLGSREQLCIHPEVKKQESNHMQVHLCRRKVASRSCHFYNNVEEKSLEQELATPILDIEDLVRSGTKHKLCPYYLSRNLKQQADIIFMPYNYLLDAKSRRAHGIDLKGTVVIFDEAHNVEKMCEEAASFDLTPHDVASELDVIDRVLEERTKVAQQAELHPEFSADSARSGLNLEPEDLAKLKMI... | 3.6.4.12 | null | DNA duplex unwinding [GO:0032508]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; negative regulation of DNA recombination [GO:0045910]; negative regulation of t-circle formation [GO:1904430]; regulation of double-strand break repair via homologous recombination [GO:0010569]; tel... | nucleus [GO:0005634] | 4 iron, 4 sulfur cluster binding [GO:0051539]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; DNA polymerase binding [GO:0070182]; metal ion binding [GO:0046872] | PF06733;PF13307; | 1.20.1160.20;3.40.50.300; | Helicase family, RAD3/XPD subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03065}. Note=Colocalizes with PCNA within the replication foci in S-phase cells. {ECO:0000255|HAMAP-Rule:MF_03065}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000255|HAMAP-Rule:MF_03065}; | null | null | null | null | FUNCTION: ATP-dependent DNA helicase implicated in telomere-length regulation, DNA repair and the maintenance of genomic stability. Acts as an anti-recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic recombination and crossover homeostasis by physically dissociating stran... | Bos taurus (Bovine) |
A4KZ49 | POLG_TRMVU | MSSKKMMWVPKSAHKAPVVSREPVIRKKEWVARQIPKYIPVSNPSDCRDEISQTLLHFDSEEAVYDFVWRFPMGSIFWDTNGRIKPVVNCLLRATRMNLDYDVAADVYVCRDCLSCASSYMYFSNYHYDCRELRENHEAVVSCKYEQHIVSTFDVFPRYCTQEIEQNVVNWMTETLERYDNEPLRIEKQLQFYNHKTEQMESRVQEVQVTTAEYAVSDTYVPQQLSRKGSVSAKLTQRRANKIIMRTHEVENLIRETIDLCDERQIPITFVDVKHKRCLPRIPLRHMQAKPDISEIVEQGDMYNEVGQFIEQYQNLAEPF... | 2.7.7.48; 3.4.-.-; 3.4.22.44; 3.4.22.45; 3.6.4.- | null | DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral RNA genome replication [GO:0039694]; virus-mediated perturbation of host defense response [GO:0019049] | helical viral capsid [GO:0019029]; host cell cytoplasmic vesicle [GO:0044161] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; helicase activity [GO:0004386]; hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides [GO:0016818]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type peptidase activity [GO:0... | PF00270;PF00271;PF00863;PF00851;PF13611;PF00767;PF08440;PF00680; | 3.30.70.270;3.90.70.150;3.40.50.300;2.40.10.10; | Potyviridae genome polyprotein family | PTM: [Viral genome-linked protein]: VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250|UniProtKB:P09814}.; PTM: [Genome polyprotein]: Genome polyprotein of potyviru... | SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle. Note=Probably colocalizes with 6K2-induced vesicles associated with host chloroplasts. {ECO:0000250|UniProtKB:P13529}.; SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate ... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=Hydrolyz... | null | null | null | null | FUNCTION: [Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a m... | Triticum mosaic virus (isolate Triticum aestivum/United States/U06-123/2006) (TriMV) |
A4L691 | PINX1_RAT | MSMLAERRRKQKWAVDPRNTAWSNDDSKFGQKMLEKMGWSKGKGLGAQEQGATEHIKVKVKNNHLGLGATNNNEDNWIAHQDDFNQLLAALNTCHGQETADSSDNKEKKSFSLEEKSKISKNRVHYMKFTKGKDLSSRSETDLDCIFGKRRNKKLAQDGCSNSTADEADTSLTTTTTTTSAFTIQEYFAKRMAQLKSKSQAAAPGSDLSETPIEWKKGKKKTKEAAGTDIENSPQHKAKRHKKKKRVEAERGPAAKKRDQVELQPGGPSGDECSDASVEAAEDRVQTPDTQDDVPKPRKRRAKKTLQRPGGVAVDTAPDS... | null | null | mitotic metaphase chromosome alignment [GO:0007080]; negative regulation of G2/M transition of mitotic cell cycle [GO:0010972]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of telomere maintenance via telomerase [GO:0032211]; positive regulation of protein localization to nucleolus [G... | chromosome, telomeric region [GO:0000781]; kinetochore [GO:0000776]; nuclear chromosome [GO:0000228]; nucleolus [GO:0005730]; spindle [GO:0005819] | protein-containing complex binding [GO:0044877]; telomerase inhibitor activity [GO:0010521]; telomerase RNA binding [GO:0070034] | PF01585; | null | PINX1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96BK5}. Nucleus, nucleolus {ECO:0000269|PubMed:17624691}. Chromosome, telomere {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes in nucleoli, at telomere speckles and to the outer plate of kinetochores. Localization to the kinetochore ... | null | null | null | null | null | FUNCTION: Microtubule-binding protein essential for faithful chromosome segregation. Mediates TRF1 and TERT accumulation in nucleolus and enhances TRF1 binding to telomeres. Inhibits telomerase activity. May inhibit cell proliferation and act as tumor suppressor (By similarity). {ECO:0000250, ECO:0000269|PubMed:1762469... | Rattus norvegicus (Rat) |
A4L7N3 | FOXO1_PIG | MAEAPQVVEIDPDFEPLPRPRSCTWPLPRPEFSQSNSATSSPAPSGGAAANPDAAAGLPSASAAAVNADFMSNLSLLEESEDFPQAPGSVAAAAAAAAAVAAAAAAAATGGLCGDFQGPEAGCLHPAPPQQPPPPGPLSQHPPVPPAAAGSLAGQPRKSSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRGRAAKKKASLQSGQEGAGDSPGSQFSKWPASPGSHSNDDFDNWSTF... | null | null | apoptotic process [GO:0006915]; autophagy [GO:0006914]; cell differentiation [GO:0030154]; cellular response to hyperoxia [GO:0071455]; cellular response to insulin stimulus [GO:0032869]; cellular response to nitric oxide [GO:0071732]; cellular response to oxidative stress [GO:0034599]; cellular response to starvation ... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein phosphatase 2A binding [GO:0051721]; RNA polymerase II cis-regulatory region sequence... | PF00250;PF16676;PF16675; | 1.10.10.10; | null | PTM: Phosphorylation by NLK promotes nuclear export and inhibits the transcriptional activity. In response to growth factors, phosphorylation on Thr-24, Ser-263 and Ser-326 by PKB/AKT1 promotes nuclear export and inactivation of transactivational activity. Phosphorylation on Thr-24 is required for binding 14-3-3 protei... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9R1E0}. Nucleus {ECO:0000250|UniProtKB:Q9R1E0}. Note=Shuttles between the cytoplasm and nucleus (By similarity). Largely nuclear in unstimulated cells (By similarity). In osteoblasts, colocalizes with ATF4 and RUNX2 in the nucleus. Serum deprivation increases loca... | null | null | null | null | null | FUNCTION: Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress (PubMed:18293098). Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus seq... | Sus scrofa (Pig) |
A4L9P5 | HIPK1_RAT | MASQLQVFSPPSVSSSAFCSAKKLKIEPSGWDVSGQSSNDKYYTHSKTLPATQGQASSSHQVANFNIPAYDQGLLLQAPAVEHIVVTAADSSGSAATATFQSSQTLTHRSNVSLLEPYQKCGLKRKSEEVDSNGSVQIIEEHPPLMLQNRTVVGAAATTTTVTTKSSSSSGEGDYQLVQHEILCSMTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENADEYNFVRSYECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPEN... | 2.7.11.1 | null | adherens junction assembly [GO:0034333]; anterior/posterior pattern specification [GO:0009952]; cell population proliferation [GO:0008283]; embryonic camera-type eye morphogenesis [GO:0048596]; embryonic retina morphogenesis in camera-type eye [GO:0060059]; endothelial cell apoptotic process [GO:0072577]; extrinsic apo... | cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; PML body [GO:0016605] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, HIPK subfamily | PTM: Phosphorylated and activated by JNK1. Autophosphorylated (By similarity). {ECO:0000250|UniProtKB:Q86Z02}.; PTM: Sumoylated. When conjugated it is directed to nuclear speckles. SENP1-mediated desumoylation is mediated by TNF in response to stress stimuli, triggering transient translocation from nucleus to cytoplasm... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O88904}. Cytoplasm {ECO:0000250|UniProtKB:O88904}. Nucleus speckle {ECO:0000250|UniProtKB:O88904}. Note=Predominantly nuclear. Translocates from nucleus to cytoplasm in response to stress stimuli via SENP1-mediated desumoylation (By similarity). {ECO:0000250|UniProtK... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:O88904}; CATALYTI... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase involved in transcription regulation and TNF-mediated cellular apoptosis. Plays a role as a corepressor for homeodomain transcription factors. Phosphorylates DAXX and MYB. Phosphorylates DAXX in response to stress, and mediates its translocation from the nucleus to the cytoplas... | Rattus norvegicus (Rat) |
A4PBQ9 | VM3VA_CROAT | MIQVLLVTICLAAFPYQGSSIILESGNVNDYEIVYPRKVTALPKGAVQPKYEDAMQYELKVNGEPVVLHLEKNKQLFSKDYSETHYSPDGREITTYPLVEDHCYYHGRIENDADSTASISACNGLKGHFKLQGEMYLIEPLKLSDSEAHAVYKYENVEKEDEAPKMCGVTQNWKSYEPIKKASQLVVTAEHQKYNPFRFVELVLVVDKAMVTKNNGDLDKIKTRMYELANTVNDIYRYMYIHVALVGLEIWSNEDKITVKPEADYTLNAFGEWRKTDLLTRKKHDNAQLLTAIDLDRVIGLAYVGSMCHPKRSTGIIQDY... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | envenomation resulting in damage of muscle extracellular matrix in another organism [GO:0044523]; envenomation resulting in hemorrhagic damage in another organism [GO:0044358]; envenomation resulting in negative regulation of platelet aggregation in another organism [GO:0044477]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; toxin activity [GO:0090729] | PF08516;PF00200;PF01562;PF01421; | 3.40.390.10;4.10.70.10; | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIc sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17497365, ECO:0000269|PubMed:9578458}. | null | null | null | null | null | FUNCTION: Is implied in permanent muscle damage by attacking the collagen scaffold and other important basement membrane proteins of muscle, and by preventing muscle regeneration through disrupting the functions of satellite cells (PubMed:30695027). Displays collagenolytic activity, fibrinogenolytic activity (on both A... | Crotalus atrox (Western diamondback rattlesnake) |
A4PES0 | WEE2_PIG | MGDNGDNKELKQKLNFSYSEEEQEDEGQKEAQESKKVQYHTPERCGHQDSEAKFTPPRTPLNHVCELSTPQVKDRASPDQGLRTPVSRPHTRPETPAPPDKSKPPPHCESPFTPRGHSSQSVISTGKLPSRGSKHLRLTPGPLTDEMTSLALVNINPFTPESYRRQFLKSNGKRKTRRDLEEAGPEEGKVEKGLPAKRCVLRETNMACRYEKEFLEVEKIGVGEFGTVYKCIKRLDGCVYAIKRSTKPVSGLSDENLAMHEVYAHSVLGHHPHVVRYYSSWAEDDHMMIQNEYCNGGSLQAAISENAKSGNHFQEPKLKD... | 2.7.10.2 | null | female meiotic nuclear division [GO:0007143]; mitotic cell cycle [GO:0000278]; negative regulation of G2/MI transition of meiotic cell cycle [GO:0110031]; negative regulation of meiotic cell cycle process involved in oocyte maturation [GO:1904145]; negative regulation of oocyte development [GO:0060283]; phosphorylation... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, WEE1 subfamily | PTM: Phosphorylation leads to increase its activity. {ECO:0000269|PubMed:21123961}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21123961}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Oocyte-specific protein tyrosine kinase that phosphorylates and inhibits CDK1 and acts as a key regulator of meiosis during both prophase I and metaphase II. Required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, by phosphoryl... | Sus scrofa (Pig) |
A4Q998 | PNPH_ANOGA | MSKFSYLQNGKASTNGVPHANGHHQQHQNGHSNGVARNGGTATDTLPVAYQQKAATSGPFHMPRTEHVGYTYDTLQEIATYLLERTELRPKVGIICGSGLGTLAEQLTDVDSFDYETIPHFPVSTVAGHVGRLVFGYLAGVPVMCMQGRFHHYEGYPLAKCAMPVRVMHLIGCTHLIATNAAGGANPKYRVGDIMLIKDHINLMGFAGNNPLQGPNDERFGPRFFGMANTYDPKLNQQAKVIARQIGIENELREGVYTCLGGPNFETVAEVKMLSMLGVDAIGMSTVHEIITARHCGMTCFAFSLITNMCTMSYEEEEEH... | 2.4.2.1 | null | purine ribonucleoside salvage [GO:0006166] | cytoplasm [GO:0005737] | purine-nucleoside phosphorylase activity [GO:0004731] | PF01048; | 3.40.50.1580; | PNP/MTAP phosphorylase family | null | null | CATALYTIC ACTIVITY: Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; Evidence={ECO:0000269|PubMed:17918964}; CATALYTIC ACTIVITY: Reaction=guanosine + phosphate = alpha-D-ribose 1-phosph... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=585 uM for inosine (at 25 degrees Celsius and pH 7.4) {ECO:0000269|PubMed:17918964}; KM=187 uM for guanosine (at 25 degrees Celsius and pH 7.4) {ECO:0000269|PubMed:17918964}; KM=190 uM for 2-deoxyinosine (at 25 degrees Celsius and pH 7.4) {ECO:0000269|PubMed:179189... | PATHWAY: Purine metabolism; purine nucleoside salvage. {ECO:0000269|PubMed:17918964}. | null | null | FUNCTION: As part of the purine salvage pathway, catalyzes the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate (PubMed:17918964). Preferentially acts on 2'-deoxyinosine and inosine, and to a ... | Anopheles gambiae (African malaria mosquito) |
A4Q9E5 | TTLL3_MOUSE | MQGVSSALLLSAGQLGPGAAWYRQEGSSECSWLRRSQPSELRTNFSSRWPWPRNSESRRSERLQWPGPASAKPEVASCGDSRRDYSSLPARHLSSARESSMPGALGTVNPQPVRTLVPPTLDEPLPDALRPPDDSLLLWRGLTKGPNHMGRLRNAKIHVERAVKQKKIFMIHGRYPVIRCLLRQRGWVEKKMVHPPGTALPAPQKDLDSSMLGDSDATEDEDEEENEMFRESQLLDLDGFLEFDDLDGIHALMSRMVRNETPYLIWTTRRDVLDCRFLSKDQMINHYARAGSFTTKVGLCLNLRNLPWFDEADADSFFPR... | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; | axoneme assembly [GO:0035082]; cilium assembly [GO:0060271]; cilium movement [GO:0003341]; flagellated sperm motility [GO:0030317]; protein polyglycylation [GO:0018094] | axoneme [GO:0005930]; cilium [GO:0005929]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; sperm flagellum [GO:0036126] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein-glycine ligase activity [GO:0070735]; protein-glycine ligase activity, initiating [GO:0070736] | PF03133; | 3.30.470.20; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19524510}. Cell projection, cilium {ECO:0000305|PubMed:19524510}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305|PubMed:19524510}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000305|PubMed:33414192}. | CATALYTIC ACTIVITY: Reaction=ATP + glycine + L-glutamyl-[protein] = ADP + glycyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:67180, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:17207, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:167890, ChEBI:CHEBI:45621... | null | null | null | null | FUNCTION: Monoglycylase which modifies alpha- and beta-tubulin, adding a single glycine on the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of tubulin (PubMed:19524510). Not involved in elongation step of the polyglycylation reaction (PubMed:1952451... | Mus musculus (Mouse) |
A4Q9E8 | TTLL6_MOUSE | MLQCLTSESEEGAEEREESSTEDLEELKEFVTLAFVRENTQKRLQNAQQHGKKKRKKKRLVINLSNCRYDSVRRAAQQYGLREAGDNDDWTLYWTDYSVSLERVMEMKSYQKINHFPGMSEICRKDLLARNMSRMLKLFPKDFHFFPRTWCLPADWGDLQTYSRTRKNKTYICKPDSGCQGRGIFITRSVKEIKPGEDMICQLYISKPFIIDGFKFDLRVYVLVTSCDPLRVFVYNEGLARFATTSYSHPNLDNLDEICMHLTNYSINKHSSNFVQDAFSGSKRKLSTFNSYMKTHGYDVEQIWRGIEDVIIKTLISAHP... | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32747782}; | microtubule bundle formation [GO:0001578]; microtubule cytoskeleton organization [GO:0000226]; microtubule severing [GO:0051013]; positive regulation of cilium movement [GO:0003353]; protein polyglutamylation [GO:0018095]; regulation of cilium beat frequency involved in ciliary motility [GO:0060296] | 9+0 non-motile cilium [GO:0097731]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; microtubule [GO:0005874] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein-glutamic acid ligase activity [GO:0070739]; tubulin binding [GO:0015631]; tubulin-glutamic acid ligase activity [GO:0070740] | PF03133; | 3.30.470.20; | Tubulin--tyrosine ligase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26829768}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:20530212}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17499049}. Note=CEP41 is required for its transport between the basa... | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-glutamyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622, ChE... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.22 uM for glutamylated tubulin {ECO:0000269|PubMed:32747782}; KM=1.92 uM for non-glutamylated tubulin {ECO:0000269|PubMed:32747782}; Note=kcat is 0.73 min(-1) with glutamylated tubulin as substrate (PubMed:32747782). kcat is 0.04 min(-1) with non-glutamylated tub... | null | null | null | FUNCTION: Polyglutamylase which modifies both tubulin and non-tubulin proteins, generating alpha-linked polyglutamate side chains on the gamma-carboxyl group of specific glutamate residues of target proteins (PubMed:17499049, PubMed:20530212, PubMed:21074048, PubMed:26829768, PubMed:32747782). Preferentially mediates A... | Mus musculus (Mouse) |
A4Q9F0 | TTLL7_MOUSE | MPSLPQDGVIQGSSPVDLGTELPYQCTMKRKVRKKKKKGIITANVAGTKFEIVRLVIDEMGFMKTPDEDETSNLIWCDAAVQQEKITDLQNYQRINHFPGMGEICRKDFLARNMTKMIKSRPMDYTFVPRTWIFPSEYTQFQNYVKELKKKRKQKTFIVKPANGAMGHGISLIRNGDKVPSQDHLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPNESNLTQLYMHLTNYSVNKHNERFERNETEDKGSKRSIKWFTEFLQANQHDVTKFWSDISELVVKTLIVAEPHVLHAYRMCRPG... | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; | cell differentiation [GO:0030154]; microtubule cytoskeleton organization [GO:0000226]; nervous system development [GO:0007399]; protein polyglutamylation [GO:0018095] | 9+0 non-motile cilium [GO:0097731]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; microtubule [GO:0005874]; perikaryon [GO:0043204] | alpha-tubulin binding [GO:0043014]; ATP binding [GO:0005524]; beta-tubulin binding [GO:0048487]; metal ion binding [GO:0046872]; tubulin binding [GO:0015631]; tubulin-glutamic acid ligase activity [GO:0070740] | PF03133; | 3.30.470.20; | Tubulin--tyrosine ligase family | null | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. Cell projection, dendrite {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. Perikaryon {ECO:0000269|P... | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-glutamyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622, ChE... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20.2 uM for Glu (with 17 uM of tubulin for adult mouse) {ECO:0000269|PubMed:19152315}; KM=19.1 uM for ATP (with 17 uM of tubulin for adult mouse) {ECO:0000269|PubMed:19152315}; KM=19.6 uM for Glu (with 17 uM of tubulin for newborn mouse) {ECO:0000269|PubMed:1915231... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:19152315}; | null | FUNCTION: Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin (PubMed:16901895, PubMed:17499049, PubMed:19152315). Mediates both ATP-dependent initiation and elongation steps of ... | Mus musculus (Mouse) |
A4Q9F1 | TTLL8_MOUSE | MSCPPTPNPPFRPPSHTRVLRTPPLPPWVCLNSKSLSTGVGGQKNQLREASMENGERKKLSSTLSDGDHKEENKLKQGIPQDLSSSPKLDRYKIARQLTEKAIKERKIFSIYGHYPVIRATLRRKGWVEKKFNFFPKALQNLGSEDKSAETKENQEIALERFDDIHDVMSRLVKNEIPYLLWTIKRDVVDYHSLTCDQMLNHYGKTASFTTKIGLCLNMRSLPWYVQANPNTFFPRCYGLCTESEKQEFLDDFRRTVAASILKWVVLHQNYCSKVKGKSKKEEAKNSDPSPKKDPENPDLKLPSLSGQVVDTACKVCQAY... | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; | cilium assembly [GO:0060271]; cilium movement [GO:0003341]; flagellated sperm motility [GO:0030317]; protein polyglycylation [GO:0018094] | axoneme [GO:0005930]; cilium [GO:0005929]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; sperm flagellum [GO:0036126] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein-glycine ligase activity [GO:0070735]; protein-glycine ligase activity, initiating [GO:0070736] | PF03133; | 3.30.470.20; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19427864, ECO:0000269|PubMed:19524510, ECO:0000269|PubMed:33414192}. Cell projection, cilium {ECO:0000305|PubMed:19524510}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305|PubMed:19524510}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|Pub... | CATALYTIC ACTIVITY: Reaction=ATP + glycine + L-glutamyl-[protein] = ADP + glycyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:67180, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:17207, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:167890, ChEBI:CHEBI:45621... | null | null | null | null | FUNCTION: Monoglycylase which modifies both tubulin and non-tubulin proteins, adding a single glycine on the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of target proteins (PubMed:19524510, PubMed:28576883). Not involved in elongation step of the p... | Mus musculus (Mouse) |
A4Q9F3 | TTL10_MOUSE | MALHPQAGRPHRDGSEAQAEAAAQDLGRLPSPSKVGAAVCRIQGLGHRAARRPRRGIGTTSASRVPRPGALMPATRNRPRFIHCRGQPPRTRVSSKRSKRSRIHPCHTEVPGWTHEKQMGSSVKERLRPELSQLDQDADDLEEEEAARLPVTSPDGLLMEGDKQPSPGQGPFFYIGGTNGASIISNYCESKGWQRTQDSHCEDYKLKWCEIKCRDNYCSFREGQQLLFQLPNNKLLTTKIGLLSALREHARTLSKARMLPSTQTKVLKMEEFFPETYRLDIRDERQAFFALFDETQMWICKPTASNQGKGIFLIRSQEEA... | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; | protein polyglycylation [GO:0018094] | axoneme [GO:0005930]; cilium [GO:0005929]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein-glycine ligase activity [GO:0070735]; protein-glycine ligase activity, elongating [GO:0070737] | PF03133; | 3.30.470.20; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19427864, ECO:0000269|PubMed:19524510}. Cell projection, cilium {ECO:0000305}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305}. | CATALYTIC ACTIVITY: [Protein polyglycylase TTLL10]: Reaction=(glycyl)(n)-glycyl-L-glutamyl-[protein] + ATP + glycine = (glycyl)(n+1)-glycyl-L-glutamyl-[protein] + ADP + H(+) + phosphate; Xref=Rhea:RHEA:67184, Rhea:RHEA-COMP:17208, Rhea:RHEA-COMP:17209, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEB... | null | null | null | null | FUNCTION: Polyglycylase which modifies both tubulin and non-tubulin proteins, generating polyglycine side chains of variable lengths on the gamma-carboxyl groups of specific glutamate residues of target proteins (PubMed:18331838, PubMed:19427864, PubMed:19524510). Involved in the elongation step rather than the initiat... | Mus musculus (Mouse) |
A4Q9F4 | TTL11_MOUSE | MRRSSPEKKPEAEWEADAAAAAAATAAATESLPAETEKQQGVDAGAAGDPERLELEEQPKDVGRIPTPTRRHAPEEGEARVVRRLPPALPLAQPRPAARALSQLVKARGRSRSRVYRRSAGSMRPVTVDSSKARTSLDALKISLRQLRWKEFPFGRRLPCDIYWHGVSFRDSDILSGQVNKFPGMTEMVRKVTLSRALRIMQNLFPEEYNFYPRSWILPEEFQLFVSQVQTVKEGDPSWKPTFIVKPDSGCQGDGIYLIKDPCDGRLTGTLHNRPAVVQEYIRKPLLIDKLKFDIRLYVLLKSLDPLEIYIAKDGLSRFC... | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; | microtubule cytoskeleton organization [GO:0000226]; microtubule severing [GO:0051013]; protein modification process [GO:0036211] | ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; microtubule [GO:0005874] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; tubulin binding [GO:0015631]; tubulin-glutamic acid ligase activity [GO:0070740] | PF03133; | 3.30.470.20; | Tubulin--tyrosine ligase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:20530212}. | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-glutamyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622, ChE... | null | null | null | null | FUNCTION: Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin (PubMed:17499049, PubMed:20530212). Preferentially mediates ATP-dependent polyglutamate long side-chain elongation o... | Mus musculus (Mouse) |
A4QB65 | AROE_CORGB | MNDSILLGLIGQGLDLSRTPAMHEAEGLAQGRATVYRRIDTLGSRASGQDLKTLLDAALYLGFNGLNITHPYKQAVLPLLDEVSEQATQLGAVNTVVIDANGHTTGHNTDVSGFGRGMEEGLPNAKLDSVVQVGAGGVGNAVAYALVTHGVQKLQVADLDTSRAQALADVINNAVGREAVVGVDARGIEDVIAAADGVVNATPMGMPAHPGTAFDVSCLTKDHWVGDVVYMPIETELLKAARALGCETLDGTRMAIHQAVDAFRLFTGLEPDVSRMRETFLSL | 1.1.1.-; 1.1.1.24 | null | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; shikimate metabolic process [GO:0019632] | cytosol [GO:0005829] | NAD+ binding [GO:0070403]; NADP binding [GO:0050661]; quinate 3-dehydrogenase (NAD+) activity [GO:0030266]; shikimate 3-dehydrogenase (NAD+) activity [GO:0052734]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764] | PF18317;PF08501; | 3.40.50.10860;3.40.50.720; | Shikimate dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=L-quinate + NAD(+) = 3-dehydroquinate + H(+) + NADH; Xref=Rhea:RHEA:22364, ChEBI:CHEBI:15378, ChEBI:CHEBI:29751, ChEBI:CHEBI:32364, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.24; Evidence={ECO:0000250|UniProtKB:Q9X5C9}; CATALYTIC ACTIVITY: Reaction=NAD(+) + shikimate = 3-dehydroshikimat... | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000303|PubMed:19376919}.; PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate biosynthesis; 3-dehydroquinate from D-quinate (NAD(+) route). {ECO:0000303|PubMed... | null | null | FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids, and plays a key role in the quinate degradation pathway. Catalyzes the NAD(+)-dependent oxidation of both quinate and shikimate to 3-dehydroquinate and 3-dehydroshikimate, respectively. {ECO:0000269|PubMed... | Corynebacterium glutamicum (strain R) |
A4QPC6 | BT2A2_MOUSE | MEPTTSLRSCPIASLLFFLVLSLFVLVSAQFTVIGPAEPILAMVGENTTLHCHLSPERNAEEMEVRWFRWRFFPAVLVYRGHQERPEEQMVAYRGRTTFMRTDISKGRVALIIHNVTAYDNGIYCCYFQEGRSYDQATMKLMVASLGSEPLIKMKTLEDGSILLECTSEGWYPEPRAVWRDPYDEVVPALEEEYTADREGLFTVTMTIIIRDCSVRNMTCSVNNTLLSQEVESVILIPESFVPSLPLWMVAVAVTLPVVMLILLTSGSICLVKKHRRKKSILSAEKEAEYEEKEAARQLQEELRWRRTLLHAADVVLDPD... | null | null | ERK1 and ERK2 cascade [GO:0070371]; G1/S transition of mitotic cell cycle [GO:0000082]; negative regulation of activated T cell proliferation [GO:0046007]; negative regulation of cytokine production [GO:0001818]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of G1/S transition of mitoti... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897] | signaling receptor binding [GO:0005102] | PF13765;PF00622;PF07686; | 2.60.120.920;2.60.40.10; | Immunoglobulin superfamily, BTN/MOG family | PTM: N-glycosylated. {ECO:0000269|PubMed:20208008}. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Inhibits the proliferation of CD4 and CD8 T-cells activated by anti-CD3 antibodies, T-cell metabolism and IL2 and IFNG secretion. {ECO:0000269|PubMed:20208008}. | Mus musculus (Mouse) |
A4QUT2 | KATG2_PYRO7 | MHASLSSWLLAASLLTQPISVSGQGCPFAKRDGTVDSSLPQKRADAPETTTFGRCAVKSNQAGGGTRSHDWWPCQLRLDVLRQFQPSQNPLGGDFDYAEAFQSLDYEAVKKDIAALMTESQDWWPADFGNYGGLFVRMAWHSAGTYRAMDGRGGGGMGQQRFAPLNSWPDNQNLDKARRLIWPIKQKYGNKISWADLMLLTGNVALENMGFKTLGFGGGRADTWQSDEAVYWGAETTFVPQGNDVRYNNSVDINARADKLEKPLAATHMGLIYVNPEGPNGTPDPAASAKDIREAFGRMGMNDTETVALIAGGHAFGKTH... | 1.11.1.21 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:22822072}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer. {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:22822072}; | cellular response to hydrogen peroxide [GO:0070301]; hydrogen peroxide catabolic process [GO:0042744] | cytosol [GO:0005829]; extracellular region [GO:0005576] | catalase activity [GO:0004096]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00141; | 1.10.520.10;1.10.420.10; | Peroxidase family, Peroxidase/catalase subfamily | PTM: Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme. {ECO:0000255|HAMAP-Rule:MF_03108}. | SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:21043575}. | CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_03108}; CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.84 mM for H(2)O(2) for the catalase reaction (at pH 5.25) {ECO:0000269|PubMed:21971530, ECO:0000269|PubMed:22822072}; KM=2.77 mM for H(2)O(2) for the catalase reaction (at pH 7.0) {ECO:0000269|PubMed:21971530, ECO:0000269|PubMed:22822072}; Note=kcat is 6446 sec(-... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.25 for the catalase reaction. Stable from pH 5.5 to pH 11. {ECO:0000269|PubMed:21971530, ECO:0000269|PubMed:22822072}; | null | FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Confers resistance to H(2)O(2) in hyphae. May play an antioxidative role in fungal defense against the host-produced H(2)O(2) (oxidative burst) at the early stage of plant infection. {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|Pu... | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
A4QXX4 | SSN3_PYRO7 | MSHSNPPTGASGGPGSASASAAPARGYYSLKRSIQTAFNDPLDRGLGPPAYQSKVRVMDKYQVIGFISSGTYGRVYKARGRQGQPGEFAIKKFKPDKEGEQITYTGISQSAIREMALCSELRHPNVIRLVETILEDKAIFMVFEYAEHDLLQIIHHHTQQPKHPIPPQTIKSIMFQLLNGCQYLHTNWVLHRDLKPANIMVTSSGEVKVGDLGLARIFWKPVRTLMQGDKVVVTIWYRAPELLMGSHHYTPAVDMWAVGCIFAELLSLRPIFKGEEAKMDNTKKGGSRDMPFQRHQMQKIVDIMGMPTKERWPLLTSMPD... | 2.7.11.22; 2.7.11.23 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | negative regulation of filamentous growth [GO:0060258]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nuclear-transcribed mRNA catabolic process, non-stop decay [GO:0070481]; phosphorylation [GO:0016310]; positive regulation of developmental process [GO:0051094]; positive regulation of transcr... | CKM complex [GO:1990508]; mediator complex [GO:0016592] | ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by ... | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
A4R5S9 | KATG1_PYRO7 | MGECPLRTANVAGGGTRNRDWWPNTLKLNILRQHTEATNPYDPNFDYAEAFKSLDYEGLKKDLRALMTDSQEYWPADFGHYGGLFVRMAWHSAGTYRVMDGRGGGGQGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGNKISWADLMLLTGNVALEDMGFKTFGFAGGRPDTWEADESTYWGGETTWLGNEVRYSSGNEGHKESGVIDGSESKKGHKDIHTRDLEKPVSAAHMGLIYVNPEGPDGIPDPVAAARDIRTTFSRMAMNDEETVALIAGGHTVGKTHGAAPSDNVGPEPEAAPIENQGLGWSNKHGSGKGPD... | 1.11.1.21 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:19000033}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer. {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:19000033}; | cellular response to hydrogen peroxide [GO:0070301]; hydrogen peroxide catabolic process [GO:0042744] | cytosol [GO:0005829] | catalase activity [GO:0004096]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00141; | 1.10.520.10;1.10.420.10; | Peroxidase family, Peroxidase/catalase subfamily | PTM: Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme. {ECO:0000255|HAMAP-Rule:MF_03108}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03108}. | CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:19000033}; CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEB... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.8 mM for H(2)O(2) for the catalase reaction {ECO:0000269|PubMed:19000033}; Note=kcat is 7010 sec(-1) with H(2)O(2) as substrate.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0 for the catalase reaction. {ECO:0000269|PubMed:19000033}; | null | FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:19000033}. | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
A4RD09 | ARO1_PYRO7 | MSTANGSSPTRISILGEESIIVDYGLWLNYVTHDLLNNIPSSTYVLITDTNLHSLYVPQFETAFTSASAAATSNSSATPPPPRAPRLLTYAIPPGEGSKSRDTKAEIEDWLLEQQCTRDTVIIALGGGVIGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPMGKNLVGAFWQPRRIYIDLAFLNTLPAREFINGMAEVIKTAAIWDAEEFSALEQNAPAILSAVRTPASAAADPNARLLPISDILKRIVLGSARVKAHIVSADEKEGGLRNLLNFGHSIGHAFEAILTPQVLHGEAVAVGMVKEAELARH... | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:000476... | PF01761;PF01487;PF00275;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
A4RPM5 | UBA4_PYRO7 | MEEADKRAEELRAQIAECEATLQSLKEQLAAAEAAKTPPYSDSTETDRGSSSSTWKWPLAEAEYERYGRQLILPSVGIQGQLRLKAASVLIVGAGGLGCPASAYFAGAGVGTIGLVDGDTVEASNLHRQVAHGTSRVGMLKVDSAISYLRELNPLVKYNAHQSHLTPENAESIVSGYDLVLDCTDHPTSRYLISDVCVLLRKPLVSASALRTDGQLIVLNTPAAPQADLSGGPCYRCVFPKPPPPDAVTSCGEGGILGPVVGVMGVLQALEGIRLLAAGRHLSPSPEQQQTAISPSLLLFSAPPDGSPAGFRSVRMRGRR... | 2.7.7.80; 2.8.1.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049}; | cell budding [GO:0007114]; cellular response to oxidative stress [GO:0034599]; invasive growth in response to glucose limitation [GO:0001403]; Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; protein urmylation [GO:0032447]; regulation of pseudohyphal growth [GO:2000220]; tRNA wobble position uridine thiola... | cytosol [GO:0005829] | AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; molybdopterin-synthase sulfurtransferase activity [GO:0061604]; sulfotransferase activity [GO:0008146]; thiosulfate sulfurtr... | PF00581;PF00899; | 3.40.50.720;3.40.250.10; | HesA/MoeB/ThiF family, UBA4 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}. | CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ... | null | PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}. | null | null | FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates urm... | Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae) |
A4STF2 | FADB_AERS4 | MIYQGETLSVSYLENGIAELRFDAPGSVNKLDRATLLSLSEAIAALQQQADLKGLILTSGKDAFIVGADITEFLELFDLPQEDLLGWLKKANDIFSAIEDLPVPTLSAIKGHALGGGCETILSTDFRLADTSAKIGLPETKLGIMPGFGGTVRLPRVIGADNALEWITTGKDYRADDALKVGAIDAVVAPDALHSAAVQMMKDAIAGKLNWQSRRAAKKAPLRLSKLEAMMSFSTAAGMVAAVAGKHYPAPMTAVKTVEAAAGMSRDEALVVEAQGFIKLAKTDVAKALVGIFLNDQHIKALAKKAAKQAAKATRHAAVL... | 1.1.1.35; 4.2.1.17; 5.1.2.3; 5.3.3.8 | null | fatty acid beta-oxidation [GO:0006635] | fatty acid beta-oxidation multienzyme complex [GO:0036125] | 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 3-hydroxybutyryl-CoA epimerase activity [GO:0008692]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; NAD+ binding [GO:0070403] | PF00725;PF02737;PF00378; | 1.10.1040.50;3.40.50.720; | Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-... | null | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000255|HAMAP-Rule:MF_01621}. | null | null | FUNCTION: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. | Aeromonas salmonicida (strain A449) |
A4U6V3 | M2_I45A0 | MSLLTEVETPIRNEWGCRCNDSSDPLVVAANIIGILHLILWILDRLFFKCIYRLFKHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVNIELE | null | null | protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078] | PF00599; | 6.10.250.1640; | Influenza viruses matrix protein M2 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximit... | null | null | null | null | null | FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is... | Influenza A virus (strain A/USA:Huston/AA/1945 H1N1) |
A4U7A7 | M2_I51A0 | MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRLFKHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVNIELE | null | null | protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078] | PF00599; | 6.10.250.1640; | Influenza viruses matrix protein M2 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximit... | null | null | null | null | null | FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is... | Influenza A virus (strain A/USA:Albany/12/1951 H1N1) |
A4UGR9 | XIRP2_HUMAN | MSPESGHSRIFEATAGPNKPESGFAEDSAARGEGVSDLHEVVSLKERMARYQAAVSRGDCRSFSANMMEESEMCAVPGGLAKVKKQFEDEITSSRNTFAQYQYQHQNRSEQEAIHSSQVGTSRSSQEMARNEQEGSKVQKIDVHGTEMVSHLEKHTEEVNQASQFHQYVQETVIDTPEDEEIPKVSTKLLKEQFEKSAQEKILYSDKEMTTPAKQIKTESEYEETFKPSSVVSTSSTSCVSTSQRKETSTTRYSDHSVTSSTLAQINATSSGMTEEFPPPPPDVLQTSVDVTAFSQSPELPSPPRRLPVPKDVYSKQRNL... | null | null | actin filament organization [GO:0007015]; cardiac muscle tissue morphogenesis [GO:0055008]; cell-cell junction organization [GO:0045216]; ventricular septum development [GO:0003281] | focal adhesion [GO:0005925]; stress fiber [GO:0001725]; Z disc [GO:0030018] | actin filament binding [GO:0051015]; alpha-actinin binding [GO:0051393] | PF08043; | null | Xin family | null | SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:15454575}. Note=Colocalizes with actin stress fibers. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Protects actin filaments from depolymerization. {ECO:0000269|PubMed:15454575}. | Homo sapiens (Human) |
A4UHT7 | SALR_PAPBR | MPETCPNTVTKMRCAVVTGGNKGIGFEICKQLSSSGIMVVLTCRDVTRGLEAVEKLKNSNHENVVFHQLDVTDPITTMSSLADFIKARFGKLDILVNNAGVAGFSVDADRFKAMISDIGEDSEEVVKIYEKPEAQELMSETYELAEECLKINYYGVKSVTEVLLPLLQLSDSPRIVNVSSSTGSLKYVSNETALEILGDGDALTEERIDMVVNMLLKDFKENLIETNGWPSFGAAYTTSKACLNAYTRVLAKKIPKFQVNCVCPGLVKTEMNYGIGNYTADEGAKHVVRIALFPDDGPSGFFYDCSELSAF | 1.1.1.248 | null | alkaloid metabolic process [GO:0009820] | membrane [GO:0016020] | salutaridine reductase (NADPH) activity [GO:0047037] | PF00106;PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=(7S)-salutaridinol + NADP(+) = H(+) + NADPH + salutaridine; Xref=Rhea:RHEA:10108, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58061, ChEBI:CHEBI:58349, ChEBI:CHEBI:58463; EC=1.1.1.248; Evidence={ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.9 uM for salutaridine (Termination and extraction with NaHCO(3) and ethylacetate, respectively) {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114}; KM=2.1 uM for salutaridine (Termination with methanol without extraction) {ECO:0000269|PubMed:17337529, ECO... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6 for the reverse reaction (reduction) with activity decreasing sharply towards pH 4.5 and pH 7.5. Optimum pH is 9.5 for the forward reaction (oxidation) with greatly reduced activity at pH 6. {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114}; | FUNCTION: Involved in biosynthesis of morphinan-type benzylisoquinoline alkaloids. Catalyzes the stereospecific conversion of salutaridine to salutaridinol. {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114}. | Papaver bracteatum (Great scarlet poppy) |
A4UTP7 | MEF2C_PIG | MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVEALNKKENKGCESPDPDSSYALTPRTEEKYKKINEEFDNMIKSHKIPAVPPPNFEMPVSIPVSSHNSLVYSNPVSSLGNPNFLPLAHPSLQRNSMSPGVTHRPPSAGNTGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNMQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVSQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYGTEYSLSSADL... | null | null | B cell homeostasis [GO:0001782]; B cell proliferation [GO:0042100]; B cell receptor signaling pathway [GO:0050853]; blood vessel development [GO:0001568]; blood vessel remodeling [GO:0001974]; cardiac ventricle formation [GO:0003211]; cardiocyte differentiation [GO:0035051]; cellular response to calcium ion [GO:0071277... | cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; sarcoplasm [GO:0016528] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; histone deacetylase binding [GO:0042826]; protein dimerization acti... | PF12347;PF00319; | 3.40.1810.10; | null | PTM: Phosphorylated on Ser-59; which enhances DNA binding activity. Phosphorylated on Ser-386; which is required for Lys-381 sumoylation and inhibits transcriptional activity. {ECO:0000250}.; PTM: Acetylated by p300 on several sites in diffentiating myocytes. Acetylation on Lys-4 increases DNA binding and transactivati... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0A096MJY4}. Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:A0A096MJY4}. | null | null | null | null | null | FUNCTION: Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes. Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. Enhances transcriptional activation mediated by SOX18. Plays an essential role in h... | Sus scrofa (Pig) |
A4UUI3 | GBP4_MOUSE | MTQPQMAPICLVENHNEQLSVNQEAIEILDKISQPVVVVAIVGWSHTGKSYLMNCLAGQNHVSGTLPTSQRFPSGLHRAVSDQGHLDVVHAPPHQARALVLLDTEGLGDVEKGDPKNDLWIFALSVLLSSTFVYNSMNTINHQALEQLHYVTELTELIRAKSSPNPHGIKNSTEFVSFFPDFVWTVRDFMLELKLNGEDITSDEYLENALKLIPGNNPRIQASNSARECIRRFFPNRKCFVFEWPTHDIELIKQLETISEDQLDPTFKESAMAFASYIFTYAKIKTLREGIKVTGNGLGTLVTTYVDAINSGAVPCLDDA... | 3.6.5.- | null | cellular response to type II interferon [GO:0071346]; defense response to Gram-positive bacterium [GO:0050830]; defense response to protozoan [GO:0042832]; negative regulation of interferon-alpha production [GO:0032687]; negative regulation of protein import into nucleus [GO:0042308]; negative regulation of protein pho... | cytoplasmic vesicle [GO:0031410]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; ubiquitin-protein transferase inhibitor activity [GO:0055105] | PF02263;PF02841; | 1.20.1000.10;3.40.50.300; | TRAFAC class dynamin-like GTPase superfamily, GB1/RHD3 GTPase family, GB1 subfamily | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q96PP9}. Cytoplasm {ECO:0000250|UniProtKB:Q96PP9}. Nucleus {ECO:0000250|UniProtKB:Q96PP9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96PP9}. Note=Heterodimers with GBP1, GBP2 and GBP5 localize in the compartment of the prenylated GBPs: wi... | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P32455}; | null | null | null | null | FUNCTION: Interferon (IFN)-inducible GTPase that plays important roles in innate immunity against a diverse range of bacterial, viral and protozoan pathogens (PubMed:18025219). Negatively regulates the antiviral response by inhibiting activation of IRF7 transcription factor (PubMed:22095711). {ECO:0000269|PubMed:180252... | Mus musculus (Mouse) |
A4UVI1 | FADS1_PAPAN | MAPDPVAAKTPVQGPTPRYFTWDEVAQRSGCEERWLVIDRKVYDISEFTRRHPGGSRVISHYAGQDATDPFVAFHSNKGLVKKYMNSLLIGELSPEQPSFEPTKNKELTDEFRELRATVEQMGLMKANHVFFLLYLLHILLLDGAAWLTLWIFGTSFLPFLLCAVLLTAAQIQAGWLQHDLGHLSVFSTSKWNHLVHHFVIGHLKGVPASWWNHMHFQHHAKPNCFGKDPDINMHPFFFALGKILSVELGKQKKKYMPYNHQHKYFFLIGPPALVPFFFQWYVFYFVIQRKKWVDLAWMITFYIRLLLTYVPLLGLKAFL... | 1.14.19.44 | null | unsaturated fatty acid biosynthetic process [GO:0006636] | endoplasmic reticulum membrane [GO:0005789]; mitochondrion [GO:0005739] | acyl-CoA delta5-desaturase activity [GO:0062076] | PF00173;PF00487; | 3.10.120.10; | Fatty acid desaturase type 1 family | null | SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22619218}; Multi-pass membrane protein {ECO:0000269|PubMed:22619218}. Mitochondrion {ECO:0000269|PubMed:22619218}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22619218}; Multi-pass membrane p... | CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46424, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ... | null | PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. | null | null | FUNCTION: [Isoform 1]: Acts as a front-end fatty acyl-coenzyme A (CoA) desaturase that introduces a cis double bond at carbon 5 located between a preexisting double bond and the carboxyl end of the fatty acyl chain. Involved in biosynthesis of highly unsaturated fatty acids (HUFA) from the essential polyunsaturated fat... | Papio anubis (Olive baboon) |
A4VBF0 | PA2H_VIPBN | MRTLWIVAVCLIGVEGNLFQFGDMILQKTGKEAVHSYAIYGCYCGWGGQGRAQDATDRCCFAQDCCYGRVNDCNPKTATYTYSFENGDIVCGDNDLCLRAVCECDRAAAICLGENVNTYDKNYEYYSISHCTEESEQC | null | null | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 inhibitor activity [GO:0019834]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Heterodimer: slightly affects neuromuscular transmission acting presynaptically. It has a low catalytic activity, a low anticoagulant activity and weakly inhibits ADP-induced platelet aggregation. {ECO:0000269|PubMed:18083205}.; FUNCTION: Monomer: has no activity (neurotoxic, catalytic, anticoagulant and a AD... | Vipera berus nikolskii (Nikolsky's adder) (Vipera nikolskii) |
A4VCL2 | FA20C_DROME | MAVLRTMKLKERLVISLGATLVLLTLLLIVDVQMDFGVANRHLLQQQHQKIRLGNDYDGGTGGGGMLHEFKRKFLQKSNASGSKEASTQAGASQSGGATSGQDAAAGASGGAAGPGTSRSTSTRKPTPHDRYADLQKHLLSDEYSHVIVDNAPDVSRDNPTLAEMLHRKASANASNLERFQLRITKKELYGEQDTLVDAVLRDMIKLPIQHVVQKEGGTQLKLIIEYPNDIKALMKPMRFPREQQTLPNHFYFTDYERHNAEIAAFHLDRILGFRRAMPVAGRTLNITTEIYQLAEENLLKTFFVSPSLNLCFHGKCSYY... | 2.7.11.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9XTW2}; | protein phosphorylation [GO:0006468] | extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF06702; | null | FAM20 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:22900076}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8IXL6}. Secreted {ECO:0000250|UniProtKB:Q8IXL6}. Note=Resides in the Golgi apparatus membrane and is secreted following propeptide cleavage. {ECO:0000250|UniProtKB:Q8IXL6}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000303|PubMed:22900076}; CATALYTIC... | null | null | null | null | FUNCTION: Golgi serine/threonine protein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs. {ECO:0000250|UniProtKB:Q8IXL6, ECO:0000250|UniProtKB:Q9XTW2, ECO:0000303|PubMed:22900076}. | Drosophila melanogaster (Fruit fly) |
A4VFY3 | AKECT_STUS1 | MHTVEKIGGTSMSRFEEVLDNIFIGRREGAALYQRIFVVSAYSGMTNLLLEHKKTGEPGVYQRFADAQSEGAWREALEGVRQRMLAKNAELFSSEYELHAANQFINSRIDDASECMHSLQKLCAYGHFQLSEHLMKVREMLASLGEAHSAFNSVLALKQRGVNARLADLTGWQQEAPLPFEEMISSHFAGFDFSRELVVATGYTHCAEGLMNTFDRGYSEITFAQIAAATGAREAIIHKEFHLSSADPNLVGADKVVTIGRTNYDVADQLSNLGMEAIHPRAAKTLRRAGVELRIKNAFEPEHGGTLISQDYKSEKPCVE... | 2.7.2.4 | null | ectoine biosynthetic process [GO:0019491]; homoserine biosynthetic process [GO:0009090]; lysine biosynthetic process via diaminopimelate [GO:0009089]; phosphorylation [GO:0016310] | cytosol [GO:0005829] | aspartate kinase activity [GO:0004072]; ATP binding [GO:0005524] | PF00696;PF13840; | 3.40.1160.10;3.30.2130.10; | Aspartokinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP; Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4; Evidence={ECO:0000269|PubMed:21725014}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.3 mM for ATP {ECO:0000269|PubMed:21725014}; KM=29.7 mM for L-aspartate {ECO:0000269|PubMed:21725014}; Vmax=6.9 umol/min/mg enzyme {ECO:0000269|PubMed:21725014}; | PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis. | null | null | FUNCTION: Involved in the biosynthesis of L-aspartate-beta-semialdehyde, which is an intermediate in the biosynthesis of ectoine, a highly soluble organic osmolyte, called compatible solute. Ectoine is used to avoid excessive water efflux, plasmolysis, molecular crowding of the cytoplasm, and cessation of growth in hig... | Stutzerimonas stutzeri (strain A1501) (Pseudomonas stutzeri) |
A4VGK4 | D2HDH_STUS1 | MTDPALIDELKTLVEPGKVLTDADSLNAYGKDWTKHFAPAPSAIVFPKSIEQVQAIVRWANAHKVALVPSGGRTGLSAAAVAANGEVVVSFDYMNQILEFNEMDRTAVCQPGVVTAQLQQFAEDKGLYYPVDFASAGSSQIGGNIGTNAGGIKVIRYGMTRNWVAGMKVVTGKGDLLELNKDLIKNATGYDLRQLFIGAEGTLGFVVEATMRLERQPTNLTALVLGTPDFDSIMPVLHAFQDKLDLTAFEFFSDKALAKVLGRGDVPAPFETDCPFYALLEFEATTEERAEQALATFEHCVEQGWVLDGVMSQSEQQLQN... | 1.1.99.-; 1.1.99.39 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:28827360, ECO:0000269|PubMed:30131334}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:28827360}; | lactate oxidation [GO:0019516]; respiratory electron transport chain [GO:0022904] | null | FAD binding [GO:0071949]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491] | PF02913;PF01565; | 3.30.465.10;3.30.70.2190;3.30.70.2740; | FAD-binding oxidoreductase/transferase type 4 family | null | null | CATALYTIC ACTIVITY: Reaction=(R)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2; Xref=Rhea:RHEA:38295, ChEBI:CHEBI:13193, ChEBI:CHEBI:15801, ChEBI:CHEBI:16810, ChEBI:CHEBI:17499; EC=1.1.99.39; Evidence={ECO:0000269|PubMed:28827360, ECO:0000269|PubMed:30131334}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38296;... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.17 mM for D-2-hydroxyglutarate (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:28827360}; KM=7.71 uM for electron transfer flavoprotein (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:28827360}; KM=210 uM for cytochrome c (at pH 7.4 and 37 degrees C... | null | null | null | FUNCTION: Catalyzes the dehydrogenation of (R)-2-hydroxyglutarate (D-2-hydroxyglutarate or D-2-HG) to 2-oxoglutarate and of (R)-malate (D-malate) to oxaloacetate. Is functionally tied to L-serine biosynthesis, via its coupling with the D-3-phosphoglycerate dehydrogenase SerA, encoded by the adjacent gene in the locus. ... | Stutzerimonas stutzeri (strain A1501) (Pseudomonas stutzeri) |
A4VJB4 | AKLYS_STUS1 | MALIVQKFGGTSVGTVERIEQVAEKVKKFRDGGDDIVVVVSAMSGETNRLIDLAKQISEQPVPRELDVMVSTGEQVTIALLAMALIKRGVPAVSYTGNQVRILTDSAHTKARILQIDAQRIQRDIKAGRVVVVAGFQGVDEKGNITTLGRGGSDTTGVALAAALKADECQIYTDVDGVYTTDPRVVAKAQRLDKITFEEMLEMASLGSKVLQIRAVEFAGKYSVPLRVLHSFQEGPGTLITLDEEESMEQPIISGIAFNRDEAKLTIRGVPDTPGVAFKILGPISAANVEVDMIVQNVAHDNTTDFTFTVHRNDYNNALQ... | 2.7.2.4 | null | diaminopimelate biosynthetic process [GO:0019877]; homoserine biosynthetic process [GO:0009090]; lysine biosynthetic process via diaminopimelate [GO:0009089]; methionine biosynthetic process [GO:0009086]; phosphorylation [GO:0016310]; threonine biosynthetic process [GO:0009088] | cytosol [GO:0005829] | aspartate kinase activity [GO:0004072]; ATP binding [GO:0005524] | PF00696;PF01842;PF13840; | 3.40.1160.10;3.30.2130.10; | Aspartokinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP; Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4; Evidence={ECO:0000269|PubMed:21725014}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.8 mM for ATP {ECO:0000269|PubMed:21725014}; KM=21.6 mM for L-aspartate {ECO:0000269|PubMed:21725014}; Vmax=5.1 umol/min/mg enzyme {ECO:0000269|PubMed:21725014}; | PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.; PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threon... | null | null | FUNCTION: Involved in the biosynthesis of L-aspartate-beta-semialdehyde which is a central intermediate in the biosynthesis of different amino acids (L-lysine, L-methionine, L-threonine). Catalyzes the phosphorylation of the beta-carboxyl group of L-aspartate to yield 4-phospho-L-aspartate. {ECO:0000269|PubMed:21725014... | Stutzerimonas stutzeri (strain A1501) (Pseudomonas stutzeri) |
A4WFX4 | FADB_ENT38 | MLYKGDTLYVDWLEDGIAELVFDAPGSVNKLDTATVASLGHALDVLEKQSDLKGLLLRSEKAAFIVGADITEFLSLFQVPEEQLSQWLHFANSVFNRLEDLPVPTISAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLIDGIVKAEKLRDGAISILRQAINGDLDWKAKRQRKLEPLKLSKIEATMSFTIAKGMVMQTAGKHYPAPITAVKTIEAAARLGREEALKLENQSFVPLAHTNEARALVGIFLNDQFVKGKAKQLTKNVEMPKQAAVLG... | 1.1.1.35; 4.2.1.17; 5.1.2.3; 5.3.3.8 | null | fatty acid beta-oxidation [GO:0006635] | fatty acid beta-oxidation multienzyme complex [GO:0036125] | 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 3-hydroxybutyryl-CoA epimerase activity [GO:0008692]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; NAD+ binding [GO:0070403] | PF00725;PF02737;PF00378; | 1.10.1040.50;3.40.50.720; | Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-... | null | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000255|HAMAP-Rule:MF_01621}. | null | null | FUNCTION: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. | Enterobacter sp. (strain 638) |
A4WYU7 | AGO_CERS5 | MAPVQAADEMYDSNPHPDRRQLVSNGFEVNLPDQVEVIVRDLPDPSKVKEERTRLMGYWFVHWFDGKLFHLRIKAGGPNVDGEHRAIRTAEHPWLLRARLDDALEEALPKYAAVKKRPFTFLAQKDELIDAAATAAGLSHRLLNSFKVIPRFALSPKIYEPVDGTTRVGVFVTIGMRYDIEASLRDLLEAGIDLRGMYVVRRKRQPGERGLLGRVRAISDDMVQLFEETDLASVNVNDAKLEGSKENFTRCLSALLGHNYKKLLNALDDQEAGYRTGPRFDDAVRRMGEFLAKKPIRLADNINAQVGDRIVFSNEGQARN... | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:27325485}; Note=Mg(2+) contributes to binding the 5'-end of the gRNA. {ECO:0000269|PubMed:27325485}; | clearance of foreign intracellular DNA [GO:0044355] | null | DNA binding [GO:0003677]; metal ion binding [GO:0046872]; RNA binding [GO:0003723] | PF02171; | 3.40.50.2300;3.30.420.10; | Argonaute family, Long pAgo subfamily | null | null | null | null | null | null | null | FUNCTION: A catalytically inactive argonaute protein. Binds 5'-phosphorylated RNA as the guide (gRNA) and short DNA as target DNA (tDNA); does not bind other nucleic acid combinations, does not bind tDNA alone (PubMed:27325485, PubMed:29996105, PubMed:33333714). Has highest affinity for gRNA that begins with 5'-phospho... | Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter sphaeroides) |
A4X3Q0 | SALL_SALTO | MQHNLIAFLSDVGSADEAHALCKGVMYGVAPAATIVDITHDVAPFDVREGALFLADVPHSFPAHTVICAYVYPETGTATHTIAVRNEKGQLLVGPNNGLLSFALDASPAVECHEVLSPDVMNQPVTPTWYGKDIVAACAAHLAAGTDLAAVGPRIDPKQIVRLPYASASEVEGGIRGEVVRIDRAFGNVWTNIPTHLIGSMLQDGERLEVKIEALSDTVLELPFCKTFGEVDEGQPLLYLNSRGRLALGLNQSNFIEKWPVVPGDSITVSPRVPDSNLGPVLG | 2.5.1.94 | null | null | null | transferase activity, transferring alkyl or aryl (other than methyl) groups [GO:0016765] | PF20257;PF01887; | 2.40.30.90;3.40.50.10790; | SAM hydrolase / SAM-dependent halogenase family | null | null | CATALYTIC ACTIVITY: Reaction=chloride + S-adenosyl-L-methionine = 5'-chloro-5'-deoxyadenosine + L-methionine; Xref=Rhea:RHEA:28110, ChEBI:CHEBI:17996, ChEBI:CHEBI:47133, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.94; Evidence={ECO:0000269|PubMed:18059261}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 uM for SAM (at pH 7.9 and 37 degrees Celsius) {ECO:0000269|PubMed:18059261}; KM=45 mM for chloride (at pH 7.9 and 37 degrees Celsius) {ECO:0000269|PubMed:18059261}; KM=150 mM for bromide (at pH 7.9 and 37 degrees Celsius) {ECO:0000269|PubMed:18059261}; KM=260 mM ... | null | null | null | FUNCTION: Involved in the biosynthesis of the proteosome inhibitor salinosporamide A (SalA). Catalyzes the halogenation of S-adenosyl-L-methionine (SAM) with chloride to generate 5'-chloro-5'-deoxyadenosine (5'-CIDA) and L-methionine. It can also use bromide and iodide, producing halogenated 5'-deoxyadenosine (5'-XDA) ... | Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / JCM 13857 / NBRC 105044 / CNB-440) |
A4XF23 | MAND_NOVAD | MKITAARVIITCPGRNFVTLKIETDQGVYGIGDATLNGRELSVVAYLQEHVAPCLIGMDPRRIEDIWQYVYRGAYWRRGPVTMRAIAAVDMALWDIKAKMAGMPLYQLLGGRSRDGIMVYGHANGSDIAETVEAVGHYIDMGYKAIRAQTGVPGIKDAYGVGRGKLYYEPADASLPSVTGWDTRKALNYVPKLFEELRKTYGFDHHLLHDGHHRYTPQEAANLGKMLEPYQLFWLEDCTPAENQEAFRLVRQHTVTPLAVGEIFNTIWDAKDLIQNQLIDYIRATVVGAGGLTHLRRIADLASLYQVRTGCHGATDLSPV... | 4.2.1.8 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17944491, ECO:0000269|PubMed:24697546}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:17944491, ECO:0000269|PubMed:24697546}; | amino acid catabolic process [GO:0009063]; carbohydrate catabolic process [GO:0016052] | null | magnesium ion binding [GO:0000287]; mannonate dehydratase activity [GO:0008927] | PF13378;PF02746; | 3.20.20.120;3.30.390.10; | Mandelate racemase/muconate lactonizing enzyme family, GalD subfamily | null | null | CATALYTIC ACTIVITY: Reaction=D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O; Xref=Rhea:RHEA:20097, ChEBI:CHEBI:15377, ChEBI:CHEBI:17767, ChEBI:CHEBI:57990; EC=4.2.1.8; Evidence={ECO:0000269|PubMed:17944491, ECO:0000269|PubMed:24697546}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat is 1.3 sec(-1) with D-mannonate. {ECO:0000269|PubMed:17944491, ECO:0000269|PubMed:24697546}; | PATHWAY: Carbohydrate metabolism; pentose and glucuronate interconversion. | null | null | FUNCTION: Catalyzes the dehydration of D-mannonate. Has no detectable activity with a panel of 70 other acid sugars (in vitro). {ECO:0000269|PubMed:17944491, ECO:0000269|PubMed:24697546}. | Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084 / F199) |
A4YDR9 | HBCL2_METS5 | MGGFKIPNYEGVDPTGSWYSVLTPLLFLERAGKYFKDKTAVVYRDSRYTYSTFYDNVMVQASALMRRGFSREDKLSFISRNRPEFLESFFGVPYAGGVLVPINFRLSPKEMAYIINHSDSKFVVVDEPYLNSLLEVKDQIKAEIILLEDPDNPSASETARKEVRMTYRELVKGGSRDPLPIPAKEEYSMITLYYTSGTTGLPKGVMHHHRGAFLNAMAEVLEHQMDLNSVYLWTLPMFHAASWGFSWATVAVGATNVCLDKVDYPLIYRLVEKERVTHMCAAPTVYVNLADYMKRNNLKFSNRVHMLVAGAAPAPATLKA... | 6.2.1.1; 6.2.1.17; 6.2.1.2; 6.2.1.40 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q08AH3}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q08AH3}; | fatty acid metabolic process [GO:0006631] | null | acetate-CoA ligase activity [GO:0003987]; ATP binding [GO:0005524]; butyrate-CoA ligase activity [GO:0047760]; medium-chain fatty acid-CoA ligase activity [GO:0031956]; propionate-CoA ligase activity [GO:0050218] | PF00501;PF13193; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=4-hydroxybutanoate + ATP + CoA = 4-hydroxybutanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:23128, ChEBI:CHEBI:16724, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:58574, ChEBI:CHEBI:456215; EC=6.2.1.40; Evidence={ECO:0000269|PubMed:23258541}; CATALYTIC ACTIVITY: React... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=60 uM for butyrate {ECO:0000269|PubMed:23258541}; KM=120 uM for valerate {ECO:0000269|PubMed:23258541}; KM=540 uM for propionate {ECO:0000269|PubMed:23258541}; KM=680 uM for acetate {ECO:0000269|PubMed:23258541}; KM=1540 uM for 4HB {ECO:0000269|PubMed:23258541}; KM... | null | null | null | FUNCTION: Catalyzes the ligation of coenzyme A (CoA) to 4-hydroxybutyrate (4HB). It can also use butyrate, valerate, propionate, acetate and 3-hydroxybutyrate (3HB) as substrates. {ECO:0000269|PubMed:23258541}. | Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2) |
A4YDT1 | HBCL1_METS5 | MVTVQDFFRKFIEFQNSPNEKSLQEIVKLVGQLDLRRFNWVRDVFEDIHVKERGSKTALIWRDINTGEEAKLSYHELSLMSNRVLSTLRKHGLKKGDVVYLMTKVHPMHWAVFLAVIKGGFVMVPSATNLTVAEMKYRFSDLKPSAIISDSLRASVMEEALGSLKVEKFLIDGKRETWNSLEDESSNAEPEDTRGEDVIINYFTSGTTGMPKRVIHTAVSYPVGSITTASIVGVRESDLHLNLSATGWAKFAWSSFFSPLLVGATVVGINYEGKLDTRRYLGEVENLGVTSFCAPPTAWRQFITLDLDQFRFERLRSVVS... | 6.2.1.1; 6.2.1.17; 6.2.1.2; 6.2.1.40 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q08AH3}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q08AH3}; | acyl-CoA metabolic process [GO:0006637]; fatty acid biosynthetic process [GO:0006633] | membrane [GO:0016020] | acetate-CoA ligase activity [GO:0003987]; ATP binding [GO:0005524]; butyrate-CoA ligase activity [GO:0047760]; fatty-acyl-CoA synthase activity [GO:0004321]; medium-chain fatty acid-CoA ligase activity [GO:0031956]; propionate-CoA ligase activity [GO:0050218] | PF00501;PF13193; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=4-hydroxybutanoate + ATP + CoA = 4-hydroxybutanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:23128, ChEBI:CHEBI:16724, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:58574, ChEBI:CHEBI:456215; EC=6.2.1.40; Evidence={ECO:0000269|PubMed:23258541}; CATALYTIC ACTIVITY: React... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=320 uM for butyrate {ECO:0000269|PubMed:23258541}; KM=380 uM for propionate {ECO:0000269|PubMed:23258541}; KM=740 uM for valerate {ECO:0000269|PubMed:23258541}; KM=810 uM for 3HB {ECO:0000269|PubMed:23258541}; KM=2000 uM for 4HB {ECO:0000269|PubMed:23258541}; KM=20... | null | null | null | FUNCTION: Involved in the 3-hydroxypropionate/4-hydroxybutyrate cycle which incorporates carbon dioxide into cellular carbon. Catalyzes the ligation of coenzyme A (CoA) to 4-hydroxybutyrate (4HB). It can also use butyrate, valerate, propionate, acetate and 3-hydroxybutyrate (3HB) as substrates. {ECO:0000269|PubMed:2325... | Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2) |
A4ZDL6 | GNK2_GINBI | MKTMRMNSAFILAFALAAAMLILTEAANTAFVSSACNTQKIPSGSPFNRNLRAMLADLRQNTAFSGYDYKTSRAGSGGAPTAYGRATCKQSISQSDCTACLSNLVNRIFSICNNAIGARVQLVDCFIQYEQRSF | null | null | defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; induction of programmed cell death [GO:0012502]; killing of cells of another organism [GO:0031640] | extracellular space [GO:0005615]; plasmodesma [GO:0009506] | actin binding [GO:0003779]; aspartic-type endopeptidase inhibitor activity [GO:0019828]; mannose binding [GO:0005537] | PF01657; | 3.30.430.20; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26315821}. | null | null | null | null | null | FUNCTION: Possesses antifungal activity against F.oxysporum, T.reesei and C.albicans. Weakly inhibits the aspartic acid protease pepsin activity (PubMed:17338634). Exerts antifungal activity against S.cerevisiae and F.culmorum through its carbohydrate-binding specificity. Acts as a lectin that stricly recognizes alpha-... | Ginkgo biloba (Ginkgo) (Maidenhair tree) |
A4ZFB2 | SCAF_BP80A | MEENKLKFNLQFFADQSDDPDEPGGDGKKGNPDKKENDEGTEITFTPEQQKKVDEILERRVAHEKKKADEYAKEKAAEAAKEAAKLAKMNKDQKDEYEREQMEKELEQLRSEKQLNEMRSEARKMLSEAEVDSSDEVVNLVVTDTAEQTKSNVEAFSNAVKKAVNEAVKVNARQSPLTGGDSFNHSTKNKPQNLAEIARQKRIIKN | null | null | virus-mediated perturbation of host defense response [GO:0019049] | viral scaffold [GO:0046806] | null | PF14265; | null | null | PTM: The N-terminus is cleaved by ribosomal processing protease Prp (PubMed:25388641). {ECO:0000269|PubMed:25388641}. | SUBCELLULAR LOCATION: Note=Found in provirions but not in mature virions. {ECO:0000269|PubMed:17693489, ECO:0000269|PubMed:18565341, ECO:0000269|PubMed:28984245}. | null | null | null | null | null | FUNCTION: Scaffolding protein involved in icosahedric procapsid assembly. Coassembles with capsid protein(s) to form the procapsid (PubMed:28984245). The scaffolding protein is found within the capsid as a series of concentric shells. During DNA packaging, the scaffolding protein molecules are released from the procaps... | Staphylococcus phage 80alpha |
A5A3E0 | POTEF_HUMAN | MVVEVDSMPAASSVKKPFGLRSKMGKWCCRCFPCCRESGKSNVGTSGDHDDSAMKTLRSKMGKWCRHCFPCCRGSGKSNVGASGDHDDSAMKTLRNKMGKWCCHCFPCCRGSSKSKVGAWGDYDDSAFMEPRYHVRGEDLDKLHRAAWWGKVPRKDLIVMLRDTDVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASI... | null | null | axonogenesis [GO:0007409]; cell motility [GO:0048870] | actin filament [GO:0005884]; axon [GO:0030424]; blood microparticle [GO:0072562]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; NuA4 histone acetyltransferase complex [GO:0035267]; synapse [GO:0045202] | protein kinase binding [GO:0019901]; structural constituent of postsynaptic actin cytoskeleton [GO:0098973] | PF00022;PF12796;PF14915; | 3.30.420.40;1.25.40.20; | POTE family; Actin family | null | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:17101985}. Note=Colocalizes with actin filaments. | null | null | null | null | null | null | Homo sapiens (Human) |
A5A616 | MGTS_ECOLI | MLGNMNVFMAVLGIILFSGFLAAYFSHKWDD | null | null | cellular response to magnesium starvation [GO:0010350] | plasma membrane [GO:0005886] | null | null | null | null | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:21778229, ECO:0000305|PubMed:19121005}; Single-pass membrane protein {ECO:0000269|PubMed:21778229}. | null | null | null | null | null | FUNCTION: Modulates intracellular Mg(2+) levels to maintain cellular integrity upon Mg(2+) limitation. Acts by binding and stabilizing the Mg(2+) transporter MgtA, thereby leading to increased intracellular level of Mg(2+). May inhibit FtsH proteolysis of MgtA. {ECO:0000269|PubMed:28512220}. | Escherichia coli (strain K12) |
A5A6H8 | ITM2B_PANTR | MVKVTFNSALAQKEAKKDEPKSGEEALIIPPDAVAVDCKDPDDVVPVGQRRAWCWCMCFGLAFMLAGVILGGAYLYKYFALQPDDVYYCGIKYIKDDVILNEPSADAPAALYQTIEENIKIFEEEEVEFISVPVPEFADSDPANIVHDFNKKLTAYLDLNLDKCYVIPLNTSIVMPPRNLLELLINIKAGTYLPQSYLIHEHMVITDRIENIDHLGFFIYRLCHDKETYKLQRRETIKGIQKREASNCFAIRHFENKFAVETLICS | null | null | negative regulation of amyloid precursor protein biosynthetic process [GO:0042985] | endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi-associated vesicle membrane [GO:0030660]; organelle membrane [GO:0031090]; plasma membrane [GO:0005886] | amyloid-beta binding [GO:0001540]; ATP binding [GO:0005524] | PF04089; | null | ITM2 family | PTM: The ectodomain C-terminal part of the imBRI2 is processed by furin producing a secreted Bri23 peptide and a mature BRI2, membrane form (mBRI2). The remaining part of the ectodomain of mBRI2 containing the BRICHOS domain is cleaved by ADAM10 and is secreted (BRI2C, soluble form). The membrane-bound N-terminal fragm... | SUBCELLULAR LOCATION: [Integral membrane protein 2B]: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Y287}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9Y287}. Note=Immature BRI2 (imBRI2) is cleaved by furin in the Golgi into mBRI2 and a Bri23 peptide. mBRI2 is transported to the plasma membrane and... | null | null | null | null | null | FUNCTION: Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleava... | Pan troglodytes (Chimpanzee) |
A5A6J1 | TBA1A_PANTR | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278] | cytoplasm [GO:0005737]; microtubule [GO:0005874] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Bo... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6836... | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Pan troglodytes (Chimpanzee) |
A5A6J2 | DDX5_PANTR | MSGYSSDRDRGRDRGFGAPRFGGSRAGPLSGKKFGNPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVETYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVENCIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSANHNILQIVDVC... | 3.6.4.13 | null | alternative mRNA splicing, via spliceosome [GO:0000380]; androgen receptor signaling pathway [GO:0030521]; epithelial to mesenchymal transition [GO:0001837]; intracellular estrogen receptor signaling pathway [GO:0030520]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; miRNA transcription [GO:... | cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]; spliceosomal complex [GO:0005681] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; mRNA 3'-UTR binding [GO:0003730]; nuclear androgen receptor binding [GO:0050681]; promoter-specific chromatin binding [GO:1990841]; ribonucleoprotein complex binding [GO:0043021]; RNA helicase activity [GO:0003724] | PF00270;PF00271;PF08061; | 3.40.50.300; | DEAD box helicase family, DDX5/DBP2 subfamily | PTM: Sumoylated; sumoylation, promoted by PIAS1, promotes interaction with HDAC1 and transcriptional repression activity. Sumoylation also significantly increases stability, and reduces polyubiquitination (By similarity). {ECO:0000250|UniProtKB:P17844}.; PTM: Polyubiquitinated, leading to proteasomal degradation. {ECO:... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P17844}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P17844}. Cytoplasm {ECO:0000250|UniProtKB:P17844}. Note=During the G0 phase, predominantly located in the nucleus. Cytoplasmic levels increase during the G1/S phase. During the M phase, located at the vicinity of the... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; | null | null | null | null | FUNCTION: Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-str... | Pan troglodytes (Chimpanzee) |
A5A6J7 | RAP1B_PANTR | MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDAQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWNNCAFLESSAKSKINVNEIFYDLVRQINRKTPVPGKARKKSSCQLL | 3.6.5.2 | null | calcium-ion regulated exocytosis [GO:0017156]; cell population proliferation [GO:0008283]; cellular response to cAMP [GO:0071320]; establishment of endothelial barrier [GO:0061028]; establishment of localization in cell [GO:0051649]; modification of postsynaptic structure [GO:0099010]; negative regulation of calcium io... | cell-cell junction [GO:0005911]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; lipid droplet [GO:0005811]; plasma membrane [GO:0005886] | G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein-containing complex binding [GO:0044877] | PF00071; | 3.40.50.300; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P61224}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61224}. Cell junction {ECO:0000250|UniProtKB:P61224}. Note=May shuttle between plasma membrane and cytosol (By similarity). Presence of KRIT1 and CDH5 is required for its localization to the cell junction (By ... | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P61224}; | null | null | null | null | FUNCTION: GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Play... | Pan troglodytes (Chimpanzee) |
A5A6K9 | HS90A_PANTR | MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVIPHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKEDKEEEKEKEEKESEDKPEIEDVGSDEEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTND... | null | null | cellular response to heat [GO:0034605]; protein folding [GO:0006457]; protein stabilization [GO:0050821]; response to antibiotic [GO:0046677]; response to cold [GO:0009409]; response to heat [GO:0009408] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; melanosome [GO:0042470]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; disordered domain specific binding [GO:0097718]; unfolded protein binding [GO:0051082] | PF13589;PF00183; | 3.30.230.80;3.40.50.11260;1.20.120.790;3.30.565.10; | Heat shock protein 90 family | PTM: ISGylated. {ECO:0000250|UniProtKB:P07900}.; PTM: S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1. {ECO:0000250|UniProtKB:P07900}.; PTM: Ubiquitinated via 'Lys-63'-linked polyubiquitination by HECTD1. Ubiquitination promotes translocation into the cytoplasm away from ... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm {ECO:0000250|UniProtKB:P07901}. Melanosome {ECO:0000250|UniProtKB:P07900}. Cell membrane {ECO:0000250|UniProtKB:P07900}. | null | null | null | null | null | FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This... | Pan troglodytes (Chimpanzee) |
A5A6M2 | ANXA1_PANTR | MAMVSEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTRRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDADELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYTKYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMVSRSEIDMNDIKAFYQKMYG... | null | null | actin cytoskeleton organization [GO:0030036]; adaptive immune response [GO:0002250]; alpha-beta T cell differentiation [GO:0046632]; arachidonic acid secretion [GO:0050482]; cell surface receptor signaling pathway [GO:0007166]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to hydrogen per... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; lateral plasma membrane [GO:0016328]; motile cilium [GO:0031514]; nucleus [GO:0005634]; phagocytic cup [GO:00... | cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; phosphatidylserine binding [GO:0001786]; phospholipase A2 inhibitor activity [GO:0019834] | PF00191; | 1.10.220.10; | Annexin family | PTM: Phosphorylated by protein kinase C, EGFR and TRPM7. Phosphorylated in response to EGF treatment. {ECO:0000250|UniProtKB:P04083}.; PTM: Sumoylated. {ECO:0000250|UniProtKB:P10107}.; PTM: Proteolytically cleaved by cathepsin CTSG to release the active N-terminal peptide Ac2-26. {ECO:0000250|UniProtKB:P04083}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07150}. Cytoplasm {ECO:0000250|UniProtKB:P10107}. Cell projection, cilium {ECO:0000250|UniProtKB:P10107}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51662}. Lateral cell membrane {ECO:0000250|UniProtKB:P10107}. Cell membrane {ECO:0000250|UniProtKB:P10107}; Pe... | null | null | null | null | null | FUNCTION: Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity. Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response. Contributes to the adaptive i... | Pan troglodytes (Chimpanzee) |
A5A6M3 | RBMX_PANTR | MVEADRPGKLFIGGLNTETNEKALEAVFGKYGRIVEVLLMKDRETNKSRGFAFVTFESPADAKDAARDMNGKSLDGKAIKVEQATKPSFESGRRGPPPPPRSRGPPRGLRGGRGGSGGTRGPPSRGGHMDDGGYSMNFNMSSSRGPLPVKRGPPPRSGGPPPKRSAPSGPVRSSSGMGGRAPVSRGRDSYGGPPRREPLPSRRDVYLSPRDDGYSTKDSYSSRDYPSSRDTRDYAPPPRDYTYRDYGHSSSRDDYPSRGYSDRDGYGRDRDYSDHPSGGSYRDSYESYGNSRSAPPTRGPPPSYGGSSRYDDYSSSRDGY... | null | null | cellular response to interleukin-1 [GO:0071347]; membrane protein ectodomain proteolysis [GO:0006509]; mRNA processing [GO:0006397]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; positive regulation of transcription by RNA polymer... | catalytic step 2 spliceosome [GO:0071013]; euchromatin [GO:0000791]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; supraspliceosomal complex [GO:0044530] | chromatin binding [GO:0003682]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF08081;PF00076; | 3.30.70.330; | null | PTM: O-glycosylated. {ECO:0000250}.; PTM: Arg-185 is dimethylated, probably to asymmetric dimethylarginine. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus. Note=Localizes in numerous small granules in the nucleus. Component of ribonucleosomes (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus ... | Pan troglodytes (Chimpanzee) |
A5A6N6 | EMP2_PANTR | MLVLLAFIIAFHITSAALLFIATIDNAWWVGDEFFADVWRICTNNTNCTVINDSFQEYSTLQAVQATMILSTILCCIAFFIFVLQLFRLKQGERFVLTSIIQLMSCLCVMIAASIYTDRREDIHHKNAKFYPVTREGSYGYSYILAWVAFACTFISGMMYLILRKRK | null | null | actin filament organization [GO:0007015]; actin-mediated cell contraction [GO:0070252]; activation of protein kinase activity [GO:0032147]; apoptotic process [GO:0006915]; bleb assembly [GO:0032060]; blood vessel endothelial cell migration [GO:0043534]; cell adhesion [GO:0007155]; cell migration [GO:0016477]; cell-matr... | apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane raft [GO:0045121]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | protein kinase binding [GO:0019901] | PF00822; | 1.20.140.150; | PMP-22/EMP/MP20 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O88662}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}. Apical cell membrane {ECO:0000250|UniProtKB:O88662}. Membrane raft {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P5... | null | null | null | null | null | FUNCTION: Functions as a key regulator of cell membrane composition by regulating protein surface expression. Also, plays a role in regulation of processes including cell migration, cell proliferation, cell contraction and cell adhesion. Regulates transepithelial migration of neutrophils into the alveolar lumen, potent... | Pan troglodytes (Chimpanzee) |
A5A6P2 | ASAH1_PANTR | MPGRSRVALVLLAAAVSCAVAQHAPPWTEDCRKSTYPPSGPTYRGPVPWYTINLDLPPYKRWHELMLDKAPMLKVIVNSLKNMINTFVPSGKIVQVVDEKLPGLLGNFPGPFEEEMKGIAAVTDIPLGEIISFNIFYELFTICTSIVAEDKKGHLIHGRNMDFGVFLGWNINNDTWVITEQLKPLTVNLDFQRNNKTVFKASSFAGYVGMLTGFKPGLFSLSLNERFSINGGYLGILEWILGKKDAMWIGFLTRTVLENSTSYEEAKNLLTKTKILAPAYFILGGNQSGEGCVITRDRKESLDVYELDAKQGRWYVVQTN... | 3.5.1.-; 3.5.1.23 | null | cellular response to tumor necrosis factor [GO:0071356]; ceramide biosynthetic process [GO:0046513]; ceramide catabolic process [GO:0046514]; fatty acid metabolic process [GO:0006631]; keratinocyte differentiation [GO:0030216]; regulation of programmed necrotic cell death [GO:0062098]; regulation of steroid biosyntheti... | extracellular space [GO:0005615]; lysosome [GO:0005764] | ceramidase activity [GO:0102121]; fatty acid amide hydrolase activity [GO:0017064]; N-acylsphingosine amidohydrolase activity [GO:0017040] | PF02275;PF15508; | null | Acid ceramidase family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q13510}.; PTM: Proteolytically cleaved into two chains alpha and beta that remain associated via a disulfide bond. Cleavage gives rise to a conformation change that activates the enzyme. The same catalytic Cys residue mediates the autoproteolytic cleavage and subsequent hydro... | SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q13510}. Secreted {ECO:0000250|UniProtKB:Q13510}. Note=Secretion is extremely low and localization to lysosomes is mannose-6-phosphate receptor-dependent. {ECO:0000250|UniProtKB:Q13510}. | CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine; Xref=Rhea:RHEA:20856, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868, ChEBI:CHEBI:52639, ChEBI:CHEBI:57756; EC=3.5.1.23; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-dodecanoylsphing-4-enine = dodecanoate ... | null | PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000250|UniProtKB:Q13510}. | null | null | FUNCTION: Lysosomal ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at acidic pH (By similarity). Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes incl... | Pan troglodytes (Chimpanzee) |
A5A6P7 | GPC3_PANTR | MAGTVRTACLVVAMLLSLDFPGQAQPPPPPPDATCHQVRSFFQRLQPGLKWVPETPVPGSDLQVCLPKGPTCCSRKMEEKYQLTARLNMEQLLQSASKELKFLIIQNAAVFQEAFEIVVRHAKNYTNAMFKNNYPSLTPQAFEFVGEFFTDVSLYILGSDINVDDMVNELFDSLFPVIYTQLMNPGLPDSALDINECLRGARRDLKVFGNFPKLIMTQVSKSLQVTRIFLQALNLGIEVINTTDHLKFSKDCGRMLTRMWYCSYCQGLMMVKPCGGYCNVVMQGCMAGVVEIDKYWREYILSLEELVNGMYRIYDMENVL... | null | null | cell migration [GO:0016477]; cell migration involved in gastrulation [GO:0042074]; cell proliferation involved in kidney development [GO:0072111]; coronary vasculature development [GO:0060976]; mesonephric duct morphogenesis [GO:0072180]; negative regulation of smoothened signaling pathway [GO:0045879]; positive regula... | cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; lysosomal lumen [GO:0043202]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | peptidyl-dipeptidase inhibitor activity [GO:0060422] | PF01153; | null | Glypican family | PTM: O-glycosylated; contains heparan sulfate and/or chondroitin sulfate. {ECO:0000250|UniProtKB:P51654}.; PTM: Cleaved intracellularly by a furin-like convertase to generate 2 subunits, alpha and beta, which remain associated through disulfide bonds and are associated with the cell surface via the GPI-anchor. This pro... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P13265}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P13265}; Extracellular side {ECO:0000250|UniProtKB:P13265}. | null | null | null | null | null | FUNCTION: Cell surface proteoglycan (By similarity). Negatively regulates the hedgehog signaling pathway when attached via the GPI-anchor to the cell surface by competing with the hedgehog receptor PTC1 for binding to hedgehog proteins (By similarity). Binding to the hedgehog protein SHH triggers internalization of the... | Pan troglodytes (Chimpanzee) |
A5A7I8 | CDPK5_SOLTU | MGNACRGSFGGKTFQGYPQPQDHSESNSNPKHNSDSPKPKKEQQPLVTMNRTSTNQSYYVLGHKTPNIRDLYTLGRKLGQGQFGTTYLCTELSSGIDYACKSIAKRKLISKEDVEDVRREIQIMHHLAGHKNIVSIKGAYEDPLYVHIVMELCGGGELFDRIIQRGHYTERKAADLTKIIVGVVEACHSLGVMHRDLKPENFLLVNKDDDFSLKAIDFGLSVFFKPGQIFTDVVGSPYYVAPEVLLKHYGPEADVWTAGVILYILLSGVPPFWAETQQGIFDAVLKGHIDFDSDPWPLLSESAKDLIRKMLCMRPSERLT... | 2.7.11.1 | null | intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; protein serine kinase activity [GO:0106310] | PF13499;PF00069; | 1.10.238.10;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CDPK subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17400895}; Lipid-anchor {ECO:0000305|PubMed:17400895}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Regulates the production of reactive oxygen species (ROS) by NADPH oxidase. {ECO:0000269|PubMed:17400895}. | Solanum tuberosum (Potato) |
A5ABG0 | PYNA_ASPNC | MDTPLSSSEISPRFSNTVPSSVSSMTPNADPSVIVGLACRVPGATNPSQLWENIVAQKDLQRKMPADRFNVDAFYHPDGTNKGTTNAKFGYFLDQDIGMFDAGFFRISGKEAEAMDPQQRLLLEVVYEALEDAGITLDEVNGSNTAVFCGSFTNDYNAMVTKDLEYYPKYTVTGTGNAILSNRISYFYNLHGPSVTIDTACSSSLNESDIAIVVGSALHFDPNVFITMTDLGMLSSDGRCRTFDSMGSGYVRGEGICAAVLKRRRDAVYNGDNIRAVVRASGVNHDGIKQGITLPNTNAQEKLIRRTYDLAGLDPNDTQY... | 2.3.1.-; 6.3.2.- | null | fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; secondary metabolic process [GO:0019748]; secondary metabolite biosynthetic process [GO:0044550] | null | fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF13602;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.30.70.3290;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.90.180.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110; | NRP synthetase family | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:24106156, ECO:0000269|PubMed:26414728}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds (PubMed:24106156, PubMed:26414728). The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an ace... | Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513) |
A5CAL1 | 2KGR_VITVI | MESIGVLLTCPMNPYLEQELDKRFKLFRFWDFPSANDLFREHSNSIRAVVGNSFIGADAQMIEALPKMEIVSSFSVGLDKIDLVRCKEKGIRVTNTPDVLTEDVADLALALILATLRRICESDRYVRSGSWKKGDFKLTTKFTGKSVGIIGLGRIGSAIAKRAEGFSCPISYHSRTEKPGTNYKYYPSVVELASNCQILVVACALTPETRHIINREVINALGPKGVVINIGRGLHVDEPELVSALVEGRLGGAGLDVFENEPNVPEELLAMDNVVLLPHVGSGTVETRKDMADLVLGNLEAHFLNKPLLTPVV | 1.1.1.-; 1.1.1.26; 1.1.1.28; 1.1.1.79 | null | null | cytosol [GO:0005829] | D-lactate dehydrogenase activity [GO:0008720]; glyoxylate reductase (NAD+) activity [GO:0047964]; glyoxylate reductase (NADP+) activity [GO:0030267]; hydroxypyruvate reductase activity [GO:0016618]; NAD binding [GO:0051287] | PF00389;PF02826; | 3.40.50.720; | D-isomer specific 2-hydroxyacid dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=L-idonate + NADP(+) = 2-dehydro-L-idonate + H(+) + NADPH; Xref=Rhea:RHEA:29839, ChEBI:CHEBI:15378, ChEBI:CHEBI:17796, ChEBI:CHEBI:36602, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:31488549}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29840; Evidence={ECO:00... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.7 mM for 2-keto-L-gulonate (in presence of NADPH) {ECO:0000269|PubMed:31488549}; KM=1.56 mM for 2-keto-L-gulonate (in presence of NADH) {ECO:0000269|PubMed:31488549}; KM=0.096 mM for hydroxypyruvate (in presence of NADPH) {ECO:0000269|PubMed:31488549}; KM=0.044 m... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:31488549}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:31488549}; | FUNCTION: Involved in the biosynthesis of L-tartarate from L-ascorbate (PubMed:31488549). Catalyzes the NAD(P)H-dependent reduction of 2-dehydro-L-idonate (2-keto-L-gulonate) to L-idonate (PubMed:31488549). Can also reduce hydroxypyruvate to glycerate, glyoxylate to glycolate and pyruvate to D-lactate (PubMed:31488549)... | Vitis vinifera (Grape) |
A5D7B7 | SEPR_BOVIN | MKTWLKIVFGVATSAVLALLVMCIVLRPSRVHNSEESTTRALTLKDILNGTFSYKTFFPNWISGQEYLHQSTDNNVVFYNIETGESYTILSNTTMKSVNASNYGLSPDRQFAYLESDYSKLWRYSYTATYHIYDLTNGEFIRRNELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPEDPPFQITYNGKENKIFNGIPDWVYEEEMLATKYALWWSPNGKFLAYAEFNDTEIPVIAYSYYGDEQYPRTINIPYPKAGAKNPVVRIFIIDATYPEHIGPREVPVPAMIASSDYYFSWLTWVTDDRICLQWLKRIQNVSVLST... | 3.4.14.5; 3.4.21.-; 3.4.21.26 | null | angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cell adhesion [GO:0007155]; proteolysis [GO:0006508] | anchoring junction [GO:0070161]; cell surface [GO:0009986]; extracellular region [GO:0005576]; lamellipodium membrane [GO:0031258]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587] | dipeptidyl-peptidase activity [GO:0008239]; serine-type endopeptidase activity [GO:0004252] | PF00930;PF00326; | 3.40.50.1820;2.140.10.30; | Peptidase S9B family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q12884}.; PTM: The N-terminus may be blocked. {ECO:0000250|UniProtKB:Q12884}. | SUBCELLULAR LOCATION: [Prolyl endopeptidase FAP]: Cell surface {ECO:0000250|UniProtKB:Q12884}. Cell membrane {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein {ECO:0000255}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein {ECO:0000255}. Cel... | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.; EC=3.4.14.5; Evidence={ECO:0000250|UniProtKB:Q12884, ECO:0000255|PROSITE-ProRule:PRU10084}; CATALYTIC ACTIVITY: Reaction=Hydrolysis of Pro... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.27 mM for Gly-Pro (Prolyl endopeptidase activity) {ECO:0000269|PubMed:15313476}; KM=0.206 mM for Gly-Pro-Phe-His (Prolyl endopeptidase activity) {ECO:0000269|PubMed:15313476}; | null | null | null | FUNCTION: Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activi... | Bos taurus (Bovine) |
A5D7D1 | ACTN4_BOVIN | MVDYHAANQSYQYGPSSGSNGAGGGGTMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYERLASDLLEWIRRTIPWLEDRV... | null | null | actin cytoskeleton organization [GO:0030036]; muscle cell development [GO:0055001]; peroxisome proliferator activated receptor signaling pathway [GO:0035357]; protein transport [GO:0015031]; retinoic acid receptor signaling pathway [GO:0048384] | anchoring junction [GO:0070161]; cell junction [GO:0030054]; cell projection [GO:0042995]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ribonucleoprotein complex [GO:1990904]; stress fiber [GO:0001725]... | actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; nuclear receptor coactivator activity [GO:0030374] | PF00307;PF08726;PF00435; | 1.20.58.60;1.10.418.10;1.10.238.10; | Alpha-actinin family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43707}. Cytoplasm {ECO:0000250|UniProtKB:O43707}. Cell junction {ECO:0000250|UniProtKB:P57780}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O43707}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P57780}. Note=Localized in cytoplasmic mRNP gra... | null | null | null | null | null | FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR... | Bos taurus (Bovine) |
A5D7F8 | SH3R1_BOVIN | MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVEQLPSNILLVRLLDGIKQRPWKPGPVGGSGTNGTSALRAQSSAVVTCSPKDGPSSQGGPQPRAQAWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDIIVLRRQVDENWYHGEVGGVHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEGMLADKIGIFPISYVEFNSAAKQLIEWDQPPGPGVAAGEGALATTPSSTTTKQPDGKKNTKKRHSFTSLSMASKASQAAQQ... | 2.3.2.27 | null | negative regulation of apoptotic process [GO:0043066]; neuron migration [GO:0001764]; positive regulation of JNK cascade [GO:0046330]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein autoubiquitination [GO:0051865]; protein ubiquitination [GO:0016567]; regulation o... | cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; lamellipodium [GO:0030027]; perinuclear region of cytoplasm [GO:0048471] | MAP-kinase scaffold activity [GO:0005078]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630] | PF00018;PF07653;PF14604;PF13923; | 2.30.30.40;3.30.40.10; | SH3RF family | PTM: Phosphorylated at Ser-304 by AKT1 and AKT2. When phosphorylated, it has reduced ability to bind Rac. {ECO:0000250|UniProtKB:Q7Z6J0}.; PTM: Autoubiquitinated. Ubiquitinated by SH3RF2, leading to proteasome-mediated degradation. {ECO:0000250|UniProtKB:Q71F54}. | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q69ZI1}. Note=Colocalizes, with AKT2, in lamellipodia. Colocalizes, with HERP1, in trans-Golgi network. {ECO:0000... | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q7Z6J0}; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin-dependent and clathrin-independent endocytosis. Acts as a scaffold protein that coordinates with MAPK8IP1/JIP1 in... | Bos taurus (Bovine) |
A5D7L5 | S39AE_BOVIN | MELLRPALPSYFLLTLLSIWTAASEARAVSTGMPTISAASFLQNLMHRYGEGDSLTLQQLKALLNHLDVGVGRGNISQPVQGPRNLSTCFSSGELFAAHNLSHQSQIGEREFQEFCPTILQQLDSRACSSENQENEENEQTEEGRPSSVEVWGYGLLCVTVISLCSLLGASVVPFMKKTFYKRLLLYFIALAIGTLYSNALFQLIPEAFGFNPMEDYYVSKSAVVFGGFYLFFFTEKILKMLLKQKNEHHHGHSHYTSETLPSQKDQEEGVTEKLQNGDLDHMIPQHCSGELDGKTPVVDEKVIVGSLSVQDLQASQSAC... | null | null | cellular response to glucose stimulus [GO:0071333]; cellular response to insulin stimulus [GO:0032869]; import across plasma membrane [GO:0098739]; inorganic cation transmembrane transport [GO:0098662]; intracellular zinc ion homeostasis [GO:0006882]; iron import into cell [GO:0033212]; iron ion transmembrane transport... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; early endosome membrane [GO:0031901]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886] | cadmium ion transmembrane transporter activity [GO:0015086]; iron ion transmembrane transporter activity [GO:0005381]; manganese ion transmembrane transporter activity [GO:0005384]; monoatomic anion:monoatomic cation symporter activity [GO:0015296]; monoatomic cation:bicarbonate symporter activity [GO:0140410]; zinc io... | PF02535; | null | ZIP transporter (TC 2.A.5) family | PTM: Ubiquitinated. Ubiquitination occurs upon iron depletion. The ubiquitinated form undergoes proteasomal degradation. {ECO:0000250|UniProtKB:Q15043}.; PTM: N-glycosylated. N-glycosylation at Asn-100 is required for iron-regulated extraction of the transporter from membranes and subsequent proteasomal degradation. {E... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Early endoso... | CATALYTIC ACTIVITY: Reaction=2 hydrogencarbonate(out) + Zn(2+)(out) = 2 hydrogencarbonate(in) + Zn(2+)(in); Xref=Rhea:RHEA:62252, ChEBI:CHEBI:17544, ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q75N73}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62253; Evidence={ECO:0000250|UniProtKB:Q75N73}; CATALYTIC ... | null | null | null | null | FUNCTION: Electroneutral transporter of the plasma membrane mediating the cellular uptake of the divalent metal cations zinc, manganese and iron that are important for tissue homeostasis, metabolism, development and immunity (By similarity). Functions as an energy-dependent symporter, transporting through the membranes... | Bos taurus (Bovine) |
A5D8Q0 | XIAP_XENLA | MEPQIVKFVFKEEMTCQCPKMSDSACDVDTDQNYFEEEVRLASFANFSSSYPVSAPALARAGFYYTGDGDRVKCFSCMAMVEDWQHGDTAIGKHRKISPNCKFINGFNNFRSDCIQTQAPVMQNSHANGFPNSAEDPGEKSSSEIMADYMLRTGRVVDMSKPKYPRHMAMCSEEARLQTFQNWPGYSPLMPKELANAGLFYTGINDQVKCFCCGGKLMNWEPSDRAWTEHKKHFPECYFVLGRDVGNVTRDASVQGSTYMNSYNARLETFSSWPFPIDKETLAKAGFYRIGDEDATKCFSCGGMLNCWAANDDPWEEHAK... | 2.3.2.27 | null | apoptotic process [GO:0006915]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of proteolysis [GO:0045861]; nucleotide-binding oligomerization domain containing 2 signaling pathway [GO:007... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | cysteine-type endopeptidase inhibitor activity [GO:0004869]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF00653;PF21290;PF13920; | 1.10.8.10;3.30.40.10; | IAP family | PTM: Degraded in a 2-step mechanism; a caspase-independent first step and a caspase-dependent second step (PubMed:15853809). Stabilized indirectly by MAPK, which acts to delay caspase activation, rather than directly phosphorylating xiap (PubMed:15853809). {ECO:0000269|PubMed:15853809}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P98170}. Nucleus {ECO:0000250|UniProtKB:P98170}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:P98170}; | null | null | null | null | FUNCTION: Multi-functional protein which regulates not only caspases and apoptosis, but also acts as an E3 ubiquitin-protein ligase mediating ubiquitination and subsequent proteasomal degradation of its target proteins (By similarity). Acts as a direct caspase inhibitor (By similarity). E3 ubiquitin-protein ligase that... | Xenopus laevis (African clawed frog) |
A5D8S5 | SH3R1_DANRE | MDESALLDLLECPVCLERLDATAKVLPCQHTFCRRCLLGIVGSRGELRCPECRTLVESGVDELPSNILLVRLLDGIKQRPRRTGSVHGTCANGSAVAGVRAQGAGGSQRDPGPTGGQSQRVQAKSTPVRGVPQLPCAKALYNYDGKEPGDLKFSKGDIIILRRQVDENWYHGEMGGVHGFFPTNFVQVIKPLPQPPPQCKALYDFELKDKEADKDCLPFSKDDILTVIRRVDENWAEGMLGDKIGIFPISYVEFNSAARQLIELDKPSEGGGDSSEGPSSSSSGPQANGSQKAPGEKKNSKKRHSFTSLTMSHKPCLAPP... | 2.3.2.27 | null | negative regulation of apoptotic process [GO:0043066]; neuron migration [GO:0001764]; positive regulation of JNK cascade [GO:0046330]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein autoubiquitination [GO:0051865]; protein ubiquitination [GO:0016567]; regulation o... | Golgi apparatus [GO:0005794]; lamellipodium [GO:0030027]; perinuclear region of cytoplasm [GO:0048471] | MAP-kinase scaffold activity [GO:0005078]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630] | PF00018;PF14604;PF13445; | 2.30.30.40;3.30.40.10; | SH3RF family | PTM: Autoubiquitinated. Ubiquitinated by SH3RF2, leading to proteasome-mediated degradation. {ECO:0000250|UniProtKB:Q71F54}. | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q69ZI1}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q7Z6J0}; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Acts as a scaffold protein that contributes to the effective activation of the JNK signaling pathway. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A5D8T8 | CL18A_HUMAN | MLHPETSPGRGHLLAVLLALLGTAWAEVWPPQLQEQAPMAGALNRKESFLLLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALCGTPTPSLASGLWRTLQVGWNMQLLPAGLVSFVEVVSLWFAEGQRYSHAAGECARNATCTHYTQLVWATSSQLGCGRHLCSAGQAAIEAFVCAYSPRGNWEVNGKTIVPYKKGAWCSLCTASVSGCFKAWDHAGGLCEVPRNPCRMSCQNHGRLNISTCHCHCPPGYTGRYCQVRCSLQCVHGRFREEECSCVCDIGYGGAQCATKVHFPFHTCDLRIDGDCFMVSSEADTY... | null | null | null | endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794] | polysaccharide binding [GO:0030247] | PF00188;PF00059; | 3.40.33.10;2.10.25.10;3.10.100.10; | null | PTM: N-glycosylated. {ECO:0000269|PubMed:26170455}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26170455}. Endoplasmic reticulum {ECO:0000305|PubMed:26170455}. Golgi apparatus {ECO:0000305|PubMed:26170455}. Endosome {ECO:0000305|PubMed:26170455}. | null | null | null | null | null | FUNCTION: Binds polysaccharides in a Ca(2+)-independent manner with a preferentially binding to fucoidan, beta-glucans and galactans (PubMed:26170455). {ECO:0000269|PubMed:26170455}. | Homo sapiens (Human) |
A5D8V6 | VP37C_HUMAN | METLKDKTLQELEELQNDSEAIDQLALESPEVQDLQLEREMALATNRSLAERNLEFQGPLEISRSNLSDRYQELRKLVERCQEQKAKLEKFSSALQPGTLLDLLQVEGMKIEEESEAMAEKFLEGEVPLETFLENFSSMRMLSHLRRVRVEKLQEVVRKPRASQELAGDAPPPRPPPPVRPVPQGTPPVVEEQPQPPLAMPPYPLPYSPSPSLPVGPTAHGALPPAPFPVVSQPSFYSGPLGPTYPAAQLGPRGAAGYSWSPQRSMPPRPGYPGTPMGASGPGYPLRGGRAPSPGYPQQSPYPATGGKPPYPIQPQLPSF... | null | null | macroautophagy [GO:0016236]; membrane fission [GO:0090148]; multivesicular body assembly [GO:0036258]; protein targeting to membrane [GO:0006612]; protein targeting to vacuole [GO:0006623]; protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway... | endosome membrane [GO:0010008]; ESCRT I complex [GO:0000813]; extracellular exosome [GO:0070062]; late endosome membrane [GO:0031902] | calcium-dependent protein binding [GO:0048306] | PF07200; | 1.10.287.660; | VPS37 family | PTM: Phosphorylated by TBK1. {ECO:0000269|PubMed:21270402}. | SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000305|PubMed:15509564}; Peripheral membrane protein {ECO:0000305|PubMed:15509564}. Note=Probably associates with membranes. Recruited to the plasma membrane by HIV-1. | null | null | null | null | null | FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation. {ECO:0000269|PubMed:15509564}. | Homo sapiens (Human) |
A5D8V7 | ODAD3_HUMAN | MTSPLCRAASANALPPQDQASTPSSRVKGREASGKPSHLRGKGTAQAWTPGRSKGGSFHRGAGKPSVHSQVAELHKKIQLLEGDRKAFFESSQWNIKKNQETISQLRKETKALELKLLDLLKGDEKVVQAVIREWKWEKPYLKNRTGQALEHLDHRLREKVKQQNALRHQVVLRQRRLEELQLQHSLRLLEMAEAQNRHTEVAKTMRNLENRLEKAQMKAQEAEHITSVYLQLKAYLMDESLNLENRLDSMEAEVVRTKHELEALHVVNQEALNARDIAKNQLQYLEETLVRERKKRERYISECKKRAEEKKLENERMER... | null | null | brain development [GO:0007420]; cerebrospinal fluid circulation [GO:0090660]; cilium movement [GO:0003341]; determination of heart left/right asymmetry [GO:0061371]; determination of left/right symmetry [GO:0007368]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287]; flagellated ... | axoneme [GO:0005930]; centriole [GO:0005814]; ciliary basal body [GO:0036064]; ciliary rootlet [GO:0035253]; ciliary tip [GO:0097542]; cilium [GO:0005929]; extracellular region [GO:0005576]; outer dynein arm docking complex [GO:0120228] | null | null | null | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8BSN3}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8BSN3}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:25192045}. | null | null | null | null | null | FUNCTION: Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule (PubMed:25192045). Involved in mediating assembly of both ODAs and their axonemal docking complex onto ciliary microtubules (PubMed:25192045). {ECO:0000269|PubMed:25192045}. | Homo sapiens (Human) |
A5D8W1 | CFA69_HUMAN | MWTEEAGATAEAQESGIRNKSSSSSQIPVVGVVTEDDEAQDVFKPMDLNRVIKLLEETDKDGLEEKQLKFVKKLVQCYQNGLPLRDLAQIFKILNLCSGKIKNQPRFIESAYDIIKLCGLPFLKKKVSDEITYAEDTANSIALLGDLMKIPSSELRIQICKCIVDFYHAEPPKKHIPGYQQASSSYKIQMAEVGGLAKTMVQSMTLLENQLVEKLWVLKVLQHLSTSEVNCTIMMKAQAASGICTHLNDPDPSGQLLFRSSEILWNLLEKSSKEEVIQQLSNLECLLALKEVFKNLFMRGFSHYDRQLRNDILVITTIIA... | null | null | flagellated sperm motility [GO:0030317]; olfactory behavior [GO:0042048]; positive regulation of fertilization [GO:1905516]; positive regulation of flagellated sperm motility [GO:1902093]; response to odorant [GO:1990834]; sensory perception of smell [GO:0007608]; sperm axoneme assembly [GO:0007288] | cytoplasm [GO:0005737]; non-motile cilium [GO:0097730]; sperm midpiece [GO:0097225] | null | PF21049; | 1.25.10.10; | null | null | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:Q8BH53}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:29606301}. Note=Localizes to the midpiece of the sperm flagellum. {ECO:0000269|PubMed:29606301}. | null | null | null | null | null | FUNCTION: Cilium- and flagellum-associated protein (PubMed:29606301). In the olfactory epithelium, regulates the speed of activation and termination of the odor response and thus contributes to the robustness of olfactory transduction pathways (By similarity). Required for sperm flagellum assembly and stability (PubMed... | Homo sapiens (Human) |
A5D979 | SPRTN_BOVIN | MDEDLVLALQLQEEWNLQVSEREPAQEPLSLVDASWELVDPTPDLQGLFVLFNDRFFWGQLEAVEVKWSVRMTLCAGICSYEGRGGMCSIRLSEPLLKLRPRKDLVETLLHEMIHAYLFVTNNDKDREGHGPEFCKHMHRINRLTGANITVYHTFHDEVDEYRRHWWRCNGPCQNSKPYYGYVKRATNRAPSAHDYWWAEHQKTCGGTYIKIKEPENYSKKGKGKTKLRKQPVSEAENKDKPNRGEKQLLIPFTGKGYVLGETSNFSSGKCITSHAINESQEPLSQDHSANALRPHSKTEVKFEQNGPSKKTSVASPVLS... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9H040}; | DNA damage response [GO:0006974]; positive regulation of protein ubiquitination [GO:0031398]; protein autoprocessing [GO:0016540]; protein-DNA covalent cross-linking repair [GO:0106300]; proteolysis [GO:0006508]; response to UV [GO:0009411]; S-adenosylmethionine biosynthetic process [GO:0006556]; translesion synthesis ... | chromatin [GO:0000785]; nucleus [GO:0005634] | double-stranded DNA binding [GO:0003690]; K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; methionine adenosyltransferase activity [GO:0004478]; polyubiquitin modification-dependent protein binding [GO:0031593]; sin... | PF10263; | 3.30.160.60; | Spartan family | PTM: Autocatalytically cleaved in response to double-stranded DNA-binding: autocatalytic cleavage takes place in trans and leads to inactivation. {ECO:0000250|UniProtKB:Q9H040}.; PTM: Monoubiquitinated; monoubiquitination promotes exclusion from chromatin. Deubiquitinated by VCPIP1: deubiquitination is required for sub... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H040}. Chromosome {ECO:0000250|UniProtKB:Q9H040}. Note=Localizes to sites of UV damage via the PIP-box. Recruited to stalled replication forks at sites of replication stress following deubiquitination. CHEK1 stimulates recruitment to chromatin. {ECO:0000250|UniProt... | null | null | null | null | null | FUNCTION: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication an... | Bos taurus (Bovine) |
A5D9M6 | BAG6_PIG | MEPNDSTSTTMEEPESLEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVGGKVIHLVERAPPQTQLPSGASSGTGSASATHGGGPPPGTRGPGASVHDRNANSYVMVGTFNLPSDGSAVDVHINMEQAPIQSEPRVRLVMAQHMIRDIQTLLSRMECRGGSQAQHSQPPSQMPTVAPEPVALSSQTSESVESEVPPREPMAAEEVEERASAQSPGLSPSGPAPAGPTPAPETNAPNHPSPAEYVEVLQELQRLESRLQPFLQRYYEVLGAAATTDYNNNQEGREEDQRLINL... | null | null | apoptotic process [GO:0006915]; brain development [GO:0007420]; cell differentiation [GO:0030154]; chromatin organization [GO:0006325]; endoplasmic reticulum stress-induced pre-emptive quality control [GO:0061857]; ERAD pathway [GO:0036503]; immune system process [GO:0002376]; internal peptidyl-lysine acetylation [GO:0... | BAT3 complex [GO:0071818]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleus [GO:0005634] | misfolded protein binding [GO:0051787]; polyubiquitin modification-dependent protein binding [GO:0031593]; proteasome binding [GO:0070628]; ribosome binding [GO:0043022] | PF12057;PF20960;PF00240; | null | null | PTM: Ricin can induce a cleavage by the caspase CASP3. The released C-terminal peptide induces apoptosis. {ECO:0000250|UniProtKB:P46379}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P46379}. Nucleus {ECO:0000250|UniProtKB:P46379}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P46379}. Note=Normally localized in cytosol and nucleus, it can also be released extracellularly, in exosomes, by tumor and myeloid dendritic cells. {EC... | null | null | null | null | null | FUNCTION: ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins. Functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates in their proper delivery t... | Sus scrofa (Pig) |
A5F120 | NHAD_VIBC3 | MTGRIALLSLTLFSPLSLASTPDGQALDFTHSTIGYAALLIFAIAYTLVMLEEYLQLRKSKPVLLAAGLIWAMIGYVYQQTGSTEVARQALEHNLLEYAELLLFLLVAMTYISAMEERRLFDALKAWMINRGFNFHTLFWITGWLAFFISPIADNLTTALLMCAVVMKVGGENPKFVSLACINIVIAANAGGAFSPFGDITTLMVWQAGHVSFLEFMDLFLPSLANYLVPALVMSLFVPHQTPSSIQEVVELKRGAKRIVVLFLFTILSAIGFHAFFHFPPVIGMMMGLAYLQFFGYFLRKTLARSLAKKTAIAMAKNDE... | null | null | sodium ion transport [GO:0006814] | plasma membrane [GO:0005886] | antiporter activity [GO:0015297] | PF03600; | null | NhaD Na(+)/H(+) (TC 2.A.62) antiporter family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11936836, ECO:0000269|PubMed:16186100}; Multi-pass membrane protein {ECO:0000269|PubMed:11936836, ECO:0000269|PubMed:16186100}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. Totally inactive at pH 9.0. {ECO:0000269|PubMed:11936836}; | null | FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. Can also transport lithium. {ECO:0000269|PubMed:11936836, ECO:0000269|PubMed:12101001, ECO:0000269|PubMed:16186100}. | Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) |
A5F465 | FADB_VIBC3 | MIYQAKTLQVKQLANGIAELSFCAPASVNKLDLHTLESLDKALDALAADSSVKGLLLSSDKEAFIVGADITEFLGLFAKPEAELDEWLQFANRIFNKLEDLPFPTLSALKGHTLGGGCECVLATDFRIGDATTSIGLPETKLGIMPGFGGTVRLPRLIGADSAMEIITQGKACRAEEALKVGLLDAIVDSDKLIDSAITTLTQAIEEKLDWQKRRQQKTSALTLSKLEAMMSFTMAKGMVAQVAGKHYPAPMTSVVTIEEAARLPRDAALDIERKHFIKLAKSTEAQALVGIFLNDQYIKGLAKQSAKAASQDTQHAAVL... | 1.1.1.35; 4.2.1.17; 5.1.2.3; 5.3.3.8 | null | fatty acid beta-oxidation [GO:0006635] | fatty acid beta-oxidation multienzyme complex [GO:0036125] | 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 3-hydroxybutyryl-CoA epimerase activity [GO:0008692]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; NAD+ binding [GO:0070403] | PF00725;PF02737;PF00378; | 1.10.1040.50;3.40.50.720; | Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-... | null | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000255|HAMAP-Rule:MF_01621}. | null | null | FUNCTION: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. | Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) |
A5F5X0 | NQRB_VIBC3 | MGLKKFLEDIEHHFEPGGKHEKWFALYEAAATLFYTPGLVTKRSSHVRDSVDLKRIMIMVWLAVFPAMFWGMYNAGGQAIAALNHLYSGDQLAAIVAGNWHYWLTEMLGGTMSSDAGWGSKMLLGATYFLPIYATVFIVGGFWEVLFCMVRKHEVNEGFFVTSILFALIVPPTLPLWQAALGITFGVVVAKEVFGGTGRNFLNPALAGRAFLFFAYPAQISGDLVWTAADGYSGATALSQWAQGGAGALINNATGQTITWMDAFIGNIPGSIGEVSTLALMIGAAFIVYMGIASWRIIGGVMIGMILLSTLFNVIGSDTN... | 7.2.1.1 | COFACTOR: Name=riboflavin; Xref=ChEBI:CHEBI:57986; Evidence={ECO:0000269|PubMed:20558724}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-Rule:MF_00426, ECO:0000269|PubMed:11888296, ECO:0000269|PubMed:20558724, ECO:0000269|PubMed:22366169}; | respiratory electron transport chain [GO:0022904]; sodium ion transport [GO:0006814]; transmembrane transport [GO:0055085] | plasma membrane [GO:0005886] | FMN binding [GO:0010181]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor [GO:0016655]; riboflavin binding [GO:1902444] | PF03116; | null | NqrB/RnfD family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00426, ECO:0000305}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00426}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+); Xref=Rhea:RHEA:47748, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:29101, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.2.1.1; Evidence={ECO:0000255... | null | null | null | null | FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00426}. | Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) |
A5F5Y4 | NQRF_VIBC3 | MSTIIFGVVMFTLIILALVLVILFAKSKLVPTGDITISINGDPEKAIVTQPGGKLLTALAGAGVFVSSACGGGGSCGQCRVKIKSGGGDILPTELDHISKGEAREGERLACQVAVKADMDLELPEEIFGVKKWECTVISNDNKATFIKELKLAIPDGESVPFRAGGYIQIEAPAHHVKYADFDVPEKYRGDWDKFNLFRYESKVDEPIIRAYSMANYPEEFGIIMLNVRIATPPPNNPNVPPGQMSSYIWSLKAGDKCTISGPFGEFFAKDTDAEMVFIGGGAGMAPMRSHIFDQLKRLKSKRKMSYWYGARSKREMFYV... | 7.2.1.1 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|HAMAP-Rule:MF_00430, ECO:0000269|PubMed:15379571}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|HAMAP-Rule:MF_00430, ECO:0000269|PubMed:15379571}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_00430, ECO:000... | sodium ion transport [GO:0006814] | plasma membrane [GO:0005886] | 2 iron, 2 sulfur cluster binding [GO:0051537]; electron transfer activity [GO:0009055]; FAD binding [GO:0071949]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor [GO:0016655] | PF00970;PF00111;PF00175; | 3.10.20.30;3.40.50.80;2.40.30.10; | NqrF family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00430, ECO:0000305}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00430}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+); Xref=Rhea:RHEA:47748, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:29101, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.2.1.1; Evidence={ECO:0000255... | null | null | null | null | FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NqrF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one-electron transf... | Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) |
A5F7A4 | NANH_VIBC3 | MRFKNVKKTALMLAMFGMATSSNAALFDYNATGDTEFDSPAKQGWMQDNTNNGSGVLTNADGMPAWLVQGIGGRAQWTYSLSTNQHAQASSFGWRMTTEMKVLSGGMITNYYANGTQRVLPIISLDSSGNLVVEFEGQTGRTVLATGTAATEYHKFELVFLPGSNPSASFYFDGKLIRDNIQPTASKQNMIVWGNGSSNTDGVAAYRDIKFEIQGDVIFRGPDRIPSIVASSVTPGVVTAFAEKRVGGGDPGALSNTNDIITRTSRDGGITWDTELNLTEQINVSDEFDFSDPRPIYDPSSNTVLVSYARWPTDAAQNGD... | 3.2.1.18 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | ganglioside catabolic process [GO:0006689]; oligosaccharide catabolic process [GO:0009313] | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020] | exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; sialic acid binding [GO:0033691] | PF13088;PF09264; | 2.120.10.10;2.60.120.200; | Glycosyl hydrolase 33 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; | null | null | null | null | FUNCTION: Cleaves the terminal sialic acid (N-acetyl neuraminic acid) from carbohydrate chains in glycoproteins providing free sialic acid which can be used as carbon and energy sources. Sialidases have been suggested to be pathogenic factors in microbial infections. Facilitates cholera toxin binding to host intestinal... | Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) |
A5FB63 | CHIA_FLAJ1 | MKHYYRLLFLLLFPLLASAQPAHGKKVVGYYAQWSIYARDFNVPKIDGSKLTHLNYSFYGTTYDPAHPENTKLKCLDTYADFEHMEGGIPWDAPVKGNFYDLMKLKQKYPHLKILISVGGWTKGQDLSPIAASPVARAALAADMANFIVTYPFIDGFDIDWEYPLSGGTDGTEIVNGMPVPPQKYSPDDNKNLVLLLKAMRQAMPNKLVTIAAGNNVRNVSKQYLGPNNRAQYGMTEDISTYCDYITYFGYDFGGNWYDKTCYNAPLYASGNPNDPLYGATQSESLDELTNQYLNVIGFPANKLIMGLPFYGKKFDNVAA... | 3.2.1.14 | null | chitin catabolic process [GO:0006032]; polysaccharide catabolic process [GO:0000272] | extracellular region [GO:0005576] | carbohydrate binding [GO:0030246]; chitin binding [GO:0008061]; chitinase activity [GO:0004568] | PF17957;PF13620;PF00704; | 3.10.50.10;2.60.40.1120;3.20.20.80;2.60.40.10; | Glycosyl hydrolase 18 family, Chitinase class II subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24363341}. Note=Translocated across the cytoplasmic membrane via the Sec system, and across the outer membrane via the type IX secretion system (T9SS). | CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; Evidence={ECO:0000269|PubMed:24363341}; | null | null | null | null | FUNCTION: Major extracellular chitinase, which is essential for chitin utilization. {ECO:0000269|PubMed:24363341}. | Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae) |
A5GFS8 | VAPB_PIG | MAKVEQVLSLEPQHELKFRGPFTDVVTTNLKLGNPTDRNVCFKVKTTAPRRYCVRPNSGIIDAGASINVSVMLQPFDYDPNEKSKHKFMVQSMFAPADTSDMEAAWKEAKPEDLMDSKLRCVFELPAENDKPHDVEINKIISTTASKTETPVVSKALSSALDDTEVKKVMEECKRLQSEVQRLREENKQLKEEDGLRMRKPVLSNSPAPAPATPGKEEGLSTRLLALVVLFFIVGVIIGKIAL | null | null | endoplasmic reticulum membrane organization [GO:0090158]; endoplasmic reticulum unfolded protein response [GO:0030968]; endoplasmic reticulum-plasma membrane tethering [GO:0061817]; intracellular calcium ion homeostasis [GO:0006874]; IRE1-mediated unfolded protein response [GO:0036498]; positive regulation of viral gen... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886] | beta-tubulin binding [GO:0048487]; enzyme binding [GO:0019899]; FFAT motif binding [GO:0033149]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803] | PF00635; | 2.60.40.10; | VAMP-associated protein (VAP) (TC 9.B.17) family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O95292}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9P0L0}. Note=Present in mitochondria-associated membranes that are endoplasmic reticulum membrane regions closely apposed to the outer mitochondrial membrane. {ECO:0000250|Un... | null | null | null | null | null | FUNCTION: Endoplasmic reticulum (ER)-anchored protein that mediates the formation of contact sites between the ER and endosomes via interaction with FFAT motif-containing proteins such as STARD3 or WDR44. Interacts with STARD3 in a FFAT motif phosphorylation dependent manner. Via interaction with WDR44 participates in ... | Sus scrofa (Pig) |
A5GFW1 | AURKA_PIG | MDKCKENCISGLKTTVPPGDGPKRVPVTQHFPAQHLPSANSGQAQRVLCPSNSSQRLPSHTQKLVSSHKPVQNLKQKQSQATSGPRPVSRPLSNTQQSEQPQPAAPGNNPEKEAASKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKTQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGAVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCY... | 2.7.11.1 | null | cell division [GO:0051301]; cilium disassembly [GO:0061523]; meiotic spindle organization [GO:0000212]; mitotic centrosome separation [GO:0007100]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of meiotic cell cycle process involved in oocyte maturation [GO:1904146]; posit... | basolateral plasma membrane [GO:0016323]; centriole [GO:0005814]; centrosome [GO:0005813]; chromosome passenger complex [GO:0032133]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; mitotic spindle pole [GO:0097431]; neuron projection [GO:0043005]; spindle microtubule [GO:0005876]; sp... | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, Aurora subfamily | PTM: Activated by phosphorylation at Thr-288; this brings about a change in the conformation of the activation segment (By similarity). Phosphorylation at Thr-288 varies during the cell cycle and is highest during M phase (By similarity). Autophosphorylated at Thr-288 upon TPX2 binding (By similarity). Thr-288 can be p... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O14965}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:O14965}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P97477}. Cell projection, ne... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:O14965}; CATALYTI... | null | null | null | null | FUNCTION: Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression (By similarity). Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, c... | Sus scrofa (Pig) |
A5GFZ6 | MOCS3_PIG | MAAREEVLALQAEVARREEELSSLKHRLAAALLAEQESERLLPVSPLPPKAALSQDEILRYSRQLVLPELGVQGQLRLATASVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEVSNLARQVLHGEALAGQAKVFSAAASLRRLNSAVECVPYAQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVYHYGGGPCYRCVFPQPPPAETVTNCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDALRGLFRRIQLRRRRPDCAACGERPTVTELQDYEGFCGSSATD... | 2.7.7.80; 2.8.1.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049}; | Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; protein urmylation [GO:0032447]; tRNA thio-modification [GO:0034227]; tRNA wobble position uridine thiolation [GO:0002143]; tRNA wobble uridine modification [GO:0002098] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; molybdopterin-synthase sulfurtransferase activity [GO:0061604]; nucleotidyltransferase activity [GO:0016779]; sulfotransferase activity [GO:0008146]; sulfurtransferase activity [GO:0016783]; thios... | PF00581;PF00899; | 3.40.50.720;3.40.250.10; | HesA/MoeB/ThiF family, UBA4 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}. | CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ... | null | PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.; PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}. | null | null | FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM... | Sus scrofa (Pig) |
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