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 |
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A7GBG3 | BXF_CLOBL | MPVVINSFNYNDPVNDDTILYMQIPYEEKSKKYYKAFEIMRNVWIIPERNTIGTDPSDFDPPASLENGSSAYYDPNYLTTDAEKDRYLKTTIKLFKRINSNPAGEVLLQEISYAKPYLGNEHTPINEFHPVTRTTSVNIKSSTNVKSSIILNLLVLGAGPDIFENSSYPVRKLMDSGGVYDPSNDGFGSINIVTFSPEYEYTFNDISGGYNSSTESFIADPAISLAHELIHALHGLYGARGVTYKETIKVKQAPLMIAEKPIRLEEFLTFGGQDLNIITSAMKEKIYNNLLANYEKIATRLSRVNSAPPEYDINEYKDYF... | 3.4.24.69 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:19543288}; Note=Binds 1 zinc ion per subunit (PubMed:19543288). {ECO:0000269|PubMed:19543288}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; host cell cytoplasmic vesicle [GO:0044161]; host cell cytosol [GO:0044164]; host cell plasma membrane [GO:0020002]; host cell presynaptic membrane [GO:0044231]; membrane [GO:0016020] | lipid binding [GO:0008289]; metalloendopeptidase activity [GO:0004222]; protein transmembrane transporter activity [GO:0008320]; toxin activity [GO:0090729]; zinc ion binding [GO:0008270] | PF01742;PF07951;PF07953;PF07952; | 2.60.120.200;2.80.10.50;1.20.1120.10;3.90.1240.10; | Peptidase M27 family | null | SUBCELLULAR LOCATION: [Botulinum neurotoxin type F]: Secreted {ECO:0000250|UniProtKB:P0DPI0}.; SUBCELLULAR LOCATION: [Botulinum neurotoxin F light chain]: Secreted {ECO:0000250|UniProtKB:P0DPI0}. Host cytoplasm, host cytosol {ECO:0000305|PubMed:19476346, ECO:0000305|PubMed:19543288}.; SUBCELLULAR LOCATION: [Botulinum n... | CATALYTIC ACTIVITY: Reaction=Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.; EC=3.4.24.69; Evidence={ECO:0000305|PubMed:19476346}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=19 uM for over-expressed human VAMP1 {ECO:0000269|PubMed:22289120}; KM=24.5 uM for over-expressed human VAMP2 {ECO:0000269|PubMed:22289120}; KM=15 uM for over-expressed human VAMP3 {ECO:0000269|PubMed:22289120}; Note=kcat is 16.12, 34.37 and 28.57 sec(-1) for over-... | null | null | null | FUNCTION: [Botulinum neurotoxin type F]: Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of the eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure (PubMed:14423425). Precursor... | Clostridium botulinum (strain Langeland / NCTC 10281 / Type F) |
A7HD43 | GCHK_ANADF | MTGVPETVFEELKRYVGWGDGDERALRSLHGAAAPHFPRLAEEFYDRILGHEGARTALVGGESQVGHLKVTMIAWLDELLGGPWDEAYWDRRYRIGRVHVRIGLPQHYMFGAMNVHRTGLARLAYERFHGDPPELERVRNALGKVLDLELAVMLHTYREDLLAQQARVERLSTFGQLVGSIGHDLRNPLGVIETSLYILRTRTGEDERARKHLDRIGEQLGVANGIITNLLDMIRDRPLAREPVELAAVVGGAAESVRRPTGVSLALEGLDALPPVEGDPGQLRQVFVNLLENAVFAASPEGVVAVRASRADGLVALDVE... | 2.7.13.3 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:21852234}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000269|PubMed:21852234}; | peptidyl-histidine phosphorylation [GO:0018106]; phosphorelay signal transduction system [GO:0000160] | null | ATP binding [GO:0005524]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxygen binding [GO:0019825]; phosphorelay sensor kinase activity [GO:0000155]; protein homodimerization activity [GO:0042803] | PF02518;PF00512;PF11563; | 1.10.287.130;1.10.490.10;3.30.565.10; | null | PTM: Autophosphorylated. {ECO:0000269|PubMed:21852234, ECO:0000269|PubMed:26212354}. | null | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:21852234, ECO:0000269|PubMed:26212354}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18.9 uM for ATP (with the Fe(III)-OH(-) bound form of the enzyme) {ECO:0000269|PubMed:26212354}; KM=35.4 uM for ATP (with the Fe(III)-CN(-) bound form of the enzyme) {ECO:0000269|PubMed:26212354}; KM=23.8 uM for ATP (with the Fe(III)-imidazole bound form of the enz... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 11.0 for the autophosphorylation reaction with the Fe(III)-OH(-) bound form of the enzyme. At pH 8.0, displays 75% of the optimal rate. Is inactive below pH 5.5 and above pH 12.7. {ECO:0000269|PubMed:26212354}; | null | FUNCTION: Member of the two-component regulatory system GcHK/Anae109_2439. Autophosphorylates in response to oxygen availability, and then transfers the phosphate group to a conserved Asp residue in the receiver domains of the cognate response regulator Anae109_2439, resulting in its activation. {ECO:0000269|PubMed:218... | Anaeromyxobacter sp. (strain Fw109-5) |
A7IQH5 | HCDS3_XANP2 | MSNRLKNEVIAITGGGAGIGLAIASAALREGAKVALIDLDQGLAERSAAMLSTGGAVAKGFGADVTKAADITAAITSAEQTIGSLTGLVNNAGIAGFGSVHDADAAAWDRIMAVNVTGTFLASKAALAGMLERHKGTIVNFGSVAGLVGIPTMAAYCAAKGAIVNLTRQMAADYSGRGVRVNAVCPGTVTSTGMGQQLLGSDTSPEVQARRLAKYPIGRFGTPEDIAEAVIFLLSDQAAFVTGAAFAVDGGMTAI | 1.1.1.269 | null | null | null | nucleotide binding [GO:0000166]; oxidoreductase activity [GO:0016491] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-2-hydroxypropyl-coenzyme M + NAD(+) = 2-oxopropyl-coenzyme M + H(+) + NADH; Xref=Rhea:RHEA:21052, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57552, ChEBI:CHEBI:57945, ChEBI:CHEBI:58430; EC=1.1.1.269; Evidence={ECO:0000269|PubMed:20302306}; PhysiologicalDirection=left-to-right; Xr... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=31 uM for S-HPC {ECO:0000269|PubMed:20302306}; KM=270 uM for 2-KPC {ECO:0000269|PubMed:20302306}; KM=9100 uM for R-HPC {ECO:0000269|PubMed:20302306}; KM=120 mM for 2-butanone {ECO:0000269|PubMed:20302306}; KM=1400 mM for 2-propanol {ECO:0000269|PubMed:20302306}; KM... | null | null | null | FUNCTION: Involved in aliphatic epoxide carboxylation (PubMed:20302306). Catalyzes the reversible oxidation of (2S)-2-hydroxypropyl-coenzyme M (S-HPC) to 2-oxopropyl-coenzyme M (2-KPC) (PubMed:20302306). The enzyme is highly specific for the S enantiomers (PubMed:20302306). In vitro can also use the aliphatic ketone 2-... | Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) |
A7IZE9 | ALL21_BLOTA | MKFIIALAALIAVACALPVSNDNFRHEFDHMIVNTATQRFHEIEKFLLHITHEVDDLEKTGNKDEKARLLRELTVSEAFIEGSRGYFQRELKRTDLDLLEKFNFEAALATGDLLLKDLKALQKRVQDSE | null | null | null | null | IgE binding [GO:0019863]; protein homodimerization activity [GO:0042803] | PF11642; | 1.20.58.970; | Mite group 5 allergen family | null | null | null | null | null | null | null | null | Blomia tropicalis (Mite) |
A7KAL2 | ATG1_PENRW | MASQHSRRSREAPRPEMSIGRYTRLDEIGRGSFATVYQGVHTKSKTYVAIKSVNLSKLNKKLKENLSSEIDILKGLHHPHIVALIDCHESTSHIHLVMEYCALGDLSLFIKRRDTLGSHKYTRDMIAKYPNPPGGSLNEVVTRHFLKQLSSALKFLRDRNLIHRDIKPQNLLLCPSPSSYRSGHAQVMPYKGSDDSYEPTTGLESLPMLKIADFGFARSLPATSLAETLCGSPLYMAPEILRYEKYDAKADLWSVGTVLYEMVVGRPPFRATNHVELLRKIEKGEDRIRFPEDNPASDDIKKLIRGLLKRNPVERLNFPE... | 2.7.11.1 | null | autophagosome assembly [GO:0000045]; axon extension [GO:0048675]; negative regulation of collateral sprouting [GO:0048671]; phosphorylation [GO:0016310]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of autophagy [GO:0010508]; protein transport [GO:0015031]; response to starvation [GO:004259... | autophagosome [GO:0005776]; cytosol [GO:0005829]; phagophore assembly site membrane [GO:0034045] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF12063;PF21127;PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}. | 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:P53104}; CATALYTI... | null | null | null | null | FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes (PubMed:17204848). Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Requir... | Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum) |
A7KAU2 | S47A1_RABIT | MEAPVELGPGGRQASPERRHWLRCLVLSDFREELRALLVLACPAFLAQLMVFLISFVSSVFCGHLSKLELNAVTLAIAVINVMGVSVGFGLSSACDTLISQTYGSRNLKHVGVILQRGSLILLLCCLPCWALFLNTQHILLLFRQDPAVSRLTQTYVTIFIPALPATFLYTLQVKYLLNQGIVLPQVVTGVAANLVNALANYLFVYQLHLGVMGSALANTVAQFTLALLLFLYILRSKVYQATWGGWSLECLQDWASFFRLAIPSMLMLCMEWWAYEIGSFLSGILGMVELGAQSVTYELAVIVYMIPMGLSVAVNVRVG... | null | null | organic cation transport [GO:0015695]; putrescine transport [GO:0015847]; xenobiotic detoxification by transmembrane export across the plasma membrane [GO:1990961] | apical plasma membrane [GO:0016324]; plasma membrane [GO:0005886] | antiporter activity [GO:0015297]; organic cation transmembrane transporter activity [GO:0015101]; polyspecific organic cation:proton antiporter activity [GO:0140968]; putrescine transmembrane transporter activity [GO:0015489]; thiamine transmembrane transporter activity [GO:0015234]; xenobiotic transmembrane transporte... | PF01554; | null | Multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17442726}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q96FL8}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the plasma membrane; at the brush border membranes of the proximal tubules (kidney) and at the b... | CATALYTIC ACTIVITY: Reaction=H(+)(in) + thiamine(out) = H(+)(out) + thiamine(in); Xref=Rhea:RHEA:71271, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385; Evidence={ECO:0000250|UniProtKB:Q96FL8}; CATALYTIC ACTIVITY: Reaction=estrone 3-sulfate(in) + H(+)(out) = estrone 3-sulfate(out) + H(+)(in); Xref=Rhea:RHEA:72139, ChEBI:CHEBI:153... | null | null | null | null | FUNCTION: Multidrug efflux pump that functions as a H(+)/organic cation antiporter (PubMed:17442726). Plays a physiological role in the excretion of cationic compounds including endogenous metabolites, drugs, toxins through the kidney and liver, into urine and bile respectively. Mediates the efflux of endogenous compou... | Oryctolagus cuniculus (Rabbit) |
A7KAX9 | RHG32_HUMAN | METESESSTLGDDSVFWLESEVIIQVTDCEEEEREEKFRKMKSSVHSEEDDFVPELHRNVHPRERPDWEETLSAMARGADVPEIPGDLTLKTCGSTASMKVKHVKKLPFTKGHFPKMAECAHFHYENVEFGSIQLSLSEEQNEVMKNGCESKELVYLVQIACQGKSWIVKRSYEDFRVLDKHLHLCIYDRRFSQLSELPRSDTLKDSPESVTQMLMAYLSRLSAIAGNKINCGPALTWMEIDNKGNHLLVHEESSINTPAVGAAHVIKRYTARAPDELTLEVGDIVSVIDMPPKVLSTWWRGKHGFQVGLFPGHCVELIN... | null | null | regulation of small GTPase mediated signal transduction [GO:0051056]; small GTPase-mediated signal transduction [GO:0007264] | actin cytoskeleton [GO:0015629]; cell cortex [GO:0005938]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; fibrillar center [GO:0001650]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleoplasm [GO:0005654]; postsynaptic den... | GTPase activator activity [GO:0005096]; phosphatidylinositol phosphate binding [GO:1901981] | PF00620;PF14604; | 3.30.1520.10;1.10.555.10;2.30.30.40; | PX domain-containing GAP family | PTM: Isoform 2 is phosphorylated on multiple tyrosine residues by FYN. Phosphorylated tyrosine residues undergo dephosphorylation after stimulation of NMDA receptors (By similarity). Phosphorylated in vitro by CaMK2 in the presence of calmodulin and calcium; which inhibits GAP activity (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Postsynaptic density {ECO:0000250|UniProtKB:Q811P8}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q811P8}. Cytoplasm, cell cortex {ECO:0000269|PubMed:12446789}. Endosome membrane {ECO:0000269|PubMed:17663722}. Golgi apparatus membrane {ECO:0000269|PubMed:17663722}. Endoplasmic reticulum... | null | null | null | null | null | FUNCTION: GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks be... | Homo sapiens (Human) |
A7L9Z8 | AT2C2_MOUSE | MGRRLKFLQKLAFLGQNHRYKALERDEVETLIDEQCELKAIEREKTVAALPPGEACKCSREELARAFHVDLDSGLSEFAVAQRRLVHGWNEFVTDNAEPVWKKYLDQFRNPLILLLLGSSVVSVLTKEYEDAVSIALAVLIVVTVGFIQEYRSEKSLEELTKLVPPECNCLRDGKLRHMLARDLVPGDIVSLSMGDRIPADIRLTEVTDLLVDESSFTGEVEPCGKTDSPLADGGDLSTLSNVVFMGTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTIFSFGIIGLLMLVGWVQGKPFLS... | 7.2.2.10 | null | calcium ion transmembrane transport [GO:0070588]; intracellular calcium ion homeostasis [GO:0006874]; mammary gland epithelium development [GO:0061180]; manganese ion transport [GO:0006828]; positive regulation of calcium ion import [GO:0090280]; protein localization to plasma membrane [GO:0072659] | basolateral plasma membrane [GO:0016323]; cytoplasmic side of plasma membrane [GO:0009898]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; Golgi membrane [GO:0000139]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; trans-Golgi network membrane [GO:0032588] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type calcium transporter activity [GO:0005388]; P-type manganese transporter activity [GO:0140613] | PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIA subfamily | null | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:15677451}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O75185}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:23840669}; Multi-pass membrane protein {ECO... | CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000250|UniProtKB:O75185}; PhysiologicalDirection=left-to-right;... | null | null | null | null | FUNCTION: ATP-driven pump that supplies the Golgi apparatus with Ca(2+) and Mn(2+) ions, both essential cofactors for processing and trafficking of newly synthesized proteins in the secretory pathway. Within a catalytic cycle, acquires Ca(2+) or Mn(2+) ions on the cytoplasmic side of the membrane and delivers them to t... | Mus musculus (Mouse) |
A7LCJ3 | SN_PIG | MDFLLLLLLLASSALAGLASWTVSRPETVQGIKGSCLIIPCTFGFPANVEVPHGITAIWYYDYSGKRLVVSHSRNPKVVENHFQGRALLLGQAEQRTCSLLLKDLQPQDSGSYNFRFEISEGNRWSDVKGTVVTVTEVPSVPTIALPAKLHEGMEVDFNCSTPYVCPTEPVNLQWQGQDPTRSVTSHLQKLEPSGTSHMETLHMALSWQDHGRILSCQVSAAERRMQKEIHLQVQHAPKGVEILFSHSGRNVLPGDLVTLSCQVNSSNPQVSSVQWVKDGTKLKDQKRVLQLRRAAWADAGVYTCQAGNAVGSSVSPPVS... | null | null | cell adhesion [GO:0007155]; clathrin-dependent endocytosis [GO:0072583]; clathrin-dependent endocytosis of virus by host cell [GO:0075512]; negative regulation of phagocytosis [GO:0050765]; symbiont entry into host cell [GO:0046718] | early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; late endosome [GO:0005770]; plasma membrane [GO:0005886] | carbohydrate binding [GO:0030246]; virion binding [GO:0046790]; virus receptor activity [GO:0001618] | PF08205;PF07679;PF00047;PF13895;PF07686; | 2.60.40.10; | Immunoglobulin superfamily, SIGLEC (sialic acid binding Ig-like lectin) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32093750}; Single-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Macrophage-restricted adhesion molecule that mediates sialic-acid dependent binding to lymphocytes, including granulocytes, monocytes, natural killer cells, B-cells and CD8 T-cells. Plays a crucial role in limiting bacterial dissemination by engaging sialylated bacteria to promote effective phagocytosis and a... | Sus scrofa (Pig) |
A7LFZ6 | DCL4_ORYSJ | MGDAAAAAPAAAAAGPSSTRGEPKDPRTIARKYQLDLCKRAVEENIIVYLGTGCGKTHIAVLLIYELGHLIRKPSREVCIFLAPTIPLVRQQAVVIASSTDFKVQCYYGNGKNSRDHQEWENDMREFEVLVMTPQILLQSLRHCFIKMNSIALLILDECHHAQPQKRHPYAQIMKEFYNSNSVEKFPRVFGMTASPIIGKGVMPSHSFTEKGGRSPCQPLIFFLPKGGSNKLNYTKCINSLEELLHAKVCSVDNEELESVVASPDMEVYFYGPVNHSNLTTICIKELDSLKLQSERMLRASLCDFKDSQKKLKSLWRLHE... | 3.1.26.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; | DNA-templated transcription termination [GO:0006353]; lsiRNA processing [GO:0010599]; maintenance of shoot apical meristem identity [GO:0010492]; polarity specification of adaxial/abaxial axis [GO:0009944]; reproductive structure development [GO:0048608]; RNAi-mediated antiviral immunity against RNA virus [GO:0051214];... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; helicase activity [GO:0004386]; metal ion binding [GO:0046872]; ribonuclease III activity [GO:0004525]; RNA binding [GO:0003723] | PF00270;PF03368;PF14709;PF00271;PF02170;PF00636; | 3.30.160.20;3.30.160.380;3.40.50.300;2.170.260.10;1.10.1520.10; | Helicase family, Dicer subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Involved in the RNA silencing pathway. Cleaves double-stranded RNA to produce small interfering RNAs (siRNAs) which target the selective destruction of complementary RNAs. Required for the production of 21 nucleotide siRNAs. Regulates shoot apical meristem (SAM) initiation and maintenance, leaf polarization a... | Oryza sativa subsp. japonica (Rice) |
A7LXT0 | GH31A_BACO1 | MIMNMKNIFYCLLPGLLLGACSNKVYEKTGDSVIVKVQHKETGGPRLVRLQVMGDKLIHVSATADSKFADPQSLIVVPQKKQTSFAVVQNGDTITVSTEEVKASVLASTGEVWFTDKNGELILQENKGGGKTFTPIEVEGTKGYTVCQVFESPEDEAFYGLGQHQADEFNYKGKNEELFQYNTKVSVPFVVSNKNYGILLDSYSFCRFGNPNDYSQLNRIFKLYDKTGQEGALTGTYVPKKGETLVRREDSIYFENLKTIENLPKKLPLMGAKVTYEGEIEPAQTGEFKFILYYAGYVKVYLNNEPVVPERWRTAWNPNS... | 3.2.1.177 | null | symbiotic process benefiting host [GO:0085030]; xyloglucan catabolic process [GO:2000899] | plasma membrane [GO:0005886] | alpha-D-xyloside xylohydrolase [GO:0061634]; carbohydrate binding [GO:0030246]; hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553] | PF17137;PF13802;PF01055;PF21365; | 2.60.120.380;3.20.20.80;2.60.40.1760;2.60.40.1180; | Glycosyl hydrolase 31 family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. Note=Cell inner membrane localization is predicted by analogy with the archetypal sus locus. {ECO:0000269|PubMed:24463512}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing alpha-D-xylose residues with release of alpha-D-xylose.; EC=3.2.1.177; Evidence={ECO:0000269|PubMed:24463512}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.7 mM for Xyl-alpha-PNP {ECO:0000269|PubMed:24463512}; KM=31.8 mM for Glc-alpha-PNP {ECO:0000269|PubMed:24463512}; KM=0.223 mM for XXXG {ECO:0000269|PubMed:24463512}; KM=0.378 mM for XLLG {ECO:0000269|PubMed:24463512}; KM=38.1 mM for isoprimeverose {ECO:0000269|Pu... | PATHWAY: Glucan metabolism; xyloglucan degradation. {ECO:0000269|PubMed:24463512}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-7.0. {ECO:0000269|PubMed:24463512}; | null | FUNCTION: Catalyzes the liberation of alpha-xylose from the non-reducing terminal glucose of xyloglucan oligosaccharides in xyloglucan degradation, converting the 'X' to 'G' units. {ECO:0000269|PubMed:24463512}. | Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) |
A7LXT7 | BGH5A_BACO1 | MEKQSFSDGLFSPLGIKRVIFMLVLLTTSFISCSNSDEKGGSLEVAQEYRNLEFDARGSRQTIQIDGPAEWHISTSESWCKSSHTIGEGKQYVNITVEANDTQKERTATVTVSASGAPDIIINVKQSLYSVPAYDEYIAPDNTGMRDLTSMQLSALMKAGVNVGNTFEAVIVGNDGSLSGDETCWGNPTPNKVLFEGIKAAGFDVVRIPVAYSHQFEDAATYKIKSAWMDKVEAAVKAALDAGLYVIINIHWEGGWLNHPVDANKEALDERLEAMWKQIALRFRDYDDRLLFAGTNEVNNDDANGAQPTEENYRVQNGFN... | 3.2.1.151 | null | symbiotic process benefiting host [GO:0085030]; xyloglucan catabolic process [GO:2000899] | cell outer membrane [GO:0009279]; cell surface [GO:0009986]; extracellular region [GO:0005576] | beta-glucosidase activity [GO:0008422]; xyloglucan-specific endo-beta-1,4-glucanase activity [GO:0033946] | PF13004;PF00150; | 3.20.20.80;2.60.40.10; | Glycosyl hydrolase 5 (cellulase A) family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Cell outer membrane localization is predicted by analogy with the archetypal sus locus. {ECO:0000269|PubMed:24463512}. | CATALYTIC ACTIVITY: Reaction=xyloglucan + H2O = xyloglucan oligosaccharides.; EC=3.2.1.151; Evidence={ECO:0000269|PubMed:24463512}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.036 mM for XXXG-beta-CNP {ECO:0000269|PubMed:24463512}; KM=0.145 mM for XLLG-beta-CNP {ECO:0000269|PubMed:24463512}; KM=3.59 mM for GGGG-beta-CNP {ECO:0000269|PubMed:24463512}; Note=kcat is 10.5 sec(-1) for XXXG-beta-CNP. kcat is 11.1 sec(-1) for XLLG-beta-CNP. k... | PATHWAY: Glucan metabolism; xyloglucan degradation. {ECO:0000269|PubMed:24463512}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-7.0. {ECO:0000269|PubMed:24463512}; | null | FUNCTION: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues in xyloglucan degradation. Cleaves the backbone of the 3 major types of natural xyloglucans (seed galactoxyloglucan from tamarind kernel, dicot fucogalactoxyloglucan from ... | Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) |
A7M7C7 | SKOR2_MOUSE | MASSPLPGPNDILLASPSSAFQPDALSQPRPGHANLKPNQVGQVILYGIPIVSLVIDGQERLCLAQISNTLLKNFSYNEIHNRRVALGITCVQCTPVQLEILRRAGAMPISSRRCGMITKREAERLCKSFLGENRPPKLPDNFAFDVSHECAWGCRGSFIPARYNSSRAKCIKCSYCNMYFSPNKFIFHSHRTPDAKYTQPDAANFNSWRRHLKLTDKSPQDELVFAWEDVKAMFNGGSRKRALPQPSAHPACHPLSSVKAAAVAAAAAVAGGGGLLGPHLLGAPPPPPPPPPLAELAGAPHAHHKRPRFDDDDDSLQEA... | null | null | cell development [GO:0048468]; cerebellar Purkinje cell differentiation [GO:0021702]; cerebellum morphogenesis [GO:0021587]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of smoothened signaling pathway [GO:0045880]... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; histone deacetylase binding [GO:0042826]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; SMAD binding [GO:0046332] | PF08782;PF02437; | 3.10.390.10;3.10.260.20; | SKI family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18522874}. Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Acts as a TGF-beta antagonist in the nervous system (By similarity). Exhibits transcriptional repressor activity. {ECO:0000250, ECO:0000269|PubMed:18522874}. | Mus musculus (Mouse) |
A7MAQ2 | DIOA3_DIOJA | MSSSTLLHLLLLSSLLFSCLSCLTNVEDEFSYIEGNPNGPENWGNLKPEWETCGKGMEQSPIQLRDNRVIFDQTLGKLRRNYRAVDARLRNSGHDVLVDFKGNAGSLSINRVEYQLKRIHFHSPSEHEMNGERFDLEAQLVHESQDQKRAVVSILFRFGRADPFLSDLEDFIKQFSNSQKNEINAGVVDPNQLQIDDSAYYRYMGSFTAPPCTEGISWTVMRKVATVSPRQVLLLKQAVNENAINNARPLQPTNFRSVFYFEQLKSKLGVI | 1.6.5.4; 4.2.1.1 | null | carbon utilization [GO:0015976]; cellular oxidant detoxification [GO:0098869]; cellular response to carbon dioxide [GO:0071244]; negative regulation of endopeptidase activity [GO:0010951]; one-carbon metabolic process [GO:0006730]; positive regulation of gene expression [GO:0010628]; positive regulation of phagocytosis... | null | antioxidant activity [GO:0016209]; carbonate dehydratase activity [GO:0004089]; L-ascorbic acid binding [GO:0031418]; monodehydroascorbate reductase (NADH) activity [GO:0016656]; nutrient reservoir activity [GO:0045735]; protein homodimerization activity [GO:0042803]; serine-type endopeptidase inhibitor activity [GO:00... | PF00194; | 3.10.200.10; | Alpha-carbonic anhydrase family | PTM: Not glycosylated. {ECO:0000250|UniProtKB:Q75N34}. | null | CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000269|PubMed:22195572, ECO:0000269|PubMed:25747844}; CATALYTIC ACTIVITY: Reaction=H(+) + 2 monodehydro-L-ascorbate radical + NA... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.49 mM for dehydroascorbate (DHA) (at ph 7.0 and 30 degrees Celsius) {ECO:0000269|PubMed:25747844}; KM=10.2 mM for sodium bicarbonate (at ph 7.1 and 4 degrees Celsius) {ECO:0000269|PubMed:25747844}; Note=kcat is 0.0152 min(-1) for DHA. kcat is 30500 min(-1) for so... | null | null | null | FUNCTION: Storage protein of tuber. Involved in protection against oxidative stress (Probable). Has carbonate dehydratase, trypsin inhibitor, dehydroascorbate (DHA) reductase and monodehydroascorbate (MDA) reductase activities (PubMed:22195572). Catalyzes the reactions of carbonate dehydratase and DHA reductase indepen... | Dioscorea japonica (Japanese yam) |
A7MB74 | SGK1_BOVIN | MTVKTEAARDTLTYSRMRGMVAILIAFMKQRRMGLNDFIQKIANNSYACKHPEVQSILKISPPQEPELMNANPSPPPSPSQQINLGPSSNPHAKPSDFHFLKVIGKGSFGKVLLARHKAEEAFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTADKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEHNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNI... | 2.7.11.1 | null | apoptotic process [GO:0006915]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069;PF00433; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family | PTM: Regulated by phosphorylation. Activated by phosphorylation on Ser-422 by mTORC2, transforming it into a substrate for PDPK1 which phosphorylates it on Thr-256. Phosphorylation on Ser-397 and Ser-401 are also essential for its activity. Phosphorylation on Ser-78 by MAPK7 is required for growth factor-induced cell c... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Cell membrane {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=The subcellular localization is controlled by the cell cycle, as well as by exposure to specific hormones and environmental stress stimuli. I... | 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: Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cellular enzymes, transcription factors, neuronal excitability, cell growth, proliferation, survival, migration and apoptosis. Plays an important role in cellular stress response. Cont... | Bos taurus (Bovine) |
A7MBB4 | M3K13_BOVIN | MANPQEHLSCSSSPRLPLSENKTFNGLQDDLAPMGSHASPKLLKDQQEKGMVQTELAEGTNSPITTTVLTSISEDSRDQFENSVLQLREQDESEMAMSHGNSNTVDGEGTSGTEDIKIQFSRSGSGSGGFLEGLFGCLRPVWNIIGKAYSTDYKLQQQDTWEVPFEEISELQWLGSGAQGAVFLGKFRAEEVAIKKVREQNETDIKHLRKLKHPNIIAFKGVCTQAPCYCIIMEYCAHGQLYEVLRAGRKITPRLLVDWSTGIASGMNYLHLHKIIHRDLKSPNVLVTHTDAVKISDFGTSKELSDKSTKMSFAGTVAWM... | 2.7.11.25 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | JNK cascade [GO:0007254]; phosphorylation [GO:0016310]; signal transduction [GO:0007165] | cytoplasm [GO:0005737]; membrane [GO:0016020] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310] | PF07714; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated on serine and threonine residues. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250}; Peripheral membrane protein {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=2.7.11.25; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Activates the JUN N-terminal pathway through activation of the MAP kinase kinase MAP2K7. Acts synergistically with PRDX3 to regulate the activation of NF-kappa-B in the cytosol. This activation is kinase-dependent and involves activating the IKK complex, the IKBKB-containing complex that phosphorylates inhibi... | Bos taurus (Bovine) |
A7MBE0 | S22A1_BOVIN | MLTVDDVLEQVGEFGWFQKQTFLILCLLSAAFAPIYVGIVFLAFTPDHRCRSPGVAELSRRCGWSLAEELNYTVPGPGPESQCLRYEVDWNQSTLGCLDPLASLATNGSPLPLGPCEQGWVYDTPGSSIVTEFNLVCDDSWKVDLFQSCVNLGFFLGSLGVGYIADRFGRKVCLLATTLTCASLGVLTAVAPDYTSLLIFRLLQGLVSKGSWTAGYTLITEFVGLGYRRTVAILYQMAFTVGLVLLSGLAYILPHWRWLQLAVSLPIFLLLFRFWFVPESPRWLLSQKRNTEAIKIMDHIAQKNGKLPPADLKMLSLEED... | null | null | (R)-carnitine transmembrane transport [GO:1902270]; acetylcholine transport [GO:0015870]; acyl carnitine transmembrane transport [GO:1902616]; dopamine transport [GO:0015872]; monoamine transport [GO:0015844]; monoatomic ion transport [GO:0006811]; norepinephrine transport [GO:0015874]; organic cation transport [GO:001... | apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; lateral plasma membrane [GO:0016328] | (R)-carnitine transmembrane transporter activity [GO:1901235]; acetylcholine transmembrane transporter activity [GO:0005277]; monoamine transmembrane transporter activity [GO:0008504]; neurotransmitter transmembrane transporter activity [GO:0005326]; organic anion transmembrane transporter activity [GO:0008514]; organi... | PF00083; | 1.20.1250.20; | Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family | PTM: Phosphorylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250|UniProtKB:O15245}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:O15245}; Multi-pass membrane protein {ECO:0000305}. Lateral cell membrane {ECO:0000250|UniProtKB:O15245}; Multi-pass membrane protein {ECO:0000305}. Basa... | CATALYTIC ACTIVITY: Reaction=1-methylnicotinamide(out) = 1-methylnicotinamide(in); Xref=Rhea:RHEA:73859, ChEBI:CHEBI:16797; Evidence={ECO:0000250|UniProtKB:Q63089}; CATALYTIC ACTIVITY: Reaction=dopamine(out) = dopamine(in); Xref=Rhea:RHEA:73863, ChEBI:CHEBI:59905; Evidence={ECO:0000250|UniProtKB:O08966}; CATALYTIC ACTI... | null | null | null | null | FUNCTION: Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (By similarity). Functions as a pH- and Na(+)-independent, bidirectional transporter (By similarity). Cation cellular uptake or release is ... | Bos taurus (Bovine) |
A7MBI0 | PACN1_BOVIN | MSGSYDEASLAPEETTDSFWEVGNYKRTVKRIDDGHRLCNDLMSCVQERAKIEKAYAQQLTDWAKRWRQLLEKGPQYGSLERAWGAIMTEADKVSELHQEMKNSLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAVTREMNSKTEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLDDVGKTTPQYMEGMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNLAESSSYVQVYRELEQAIRGADAQDDLRWFRSTSGPGMPMNWPQFEEWNPDLPHTAAKKEKQP... | null | null | actin filament organization [GO:0007015]; cytoskeleton organization [GO:0007010]; negative regulation of endocytosis [GO:0045806]; neuron projection morphogenesis [GO:0048812]; plasma membrane tubulation [GO:0097320]; positive regulation of dendrite development [GO:1900006]; protein localization to membrane [GO:0072657... | axon terminus [GO:0043679]; COPI-coated vesicle [GO:0030137]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; endosome [GO:0005768]; photoreceptor ribbon synapse [GO:0098684]; plasma membrane [GO:0005886]; presynaptic endocytic zone [GO:0098833]; ruffle membrane [GO:0032587] | cytoskeletal protein binding [GO:0008092]; identical protein binding [GO:0042802]; phospholipid binding [GO:0005543] | PF00611;PF14604; | 1.20.1270.60;2.30.30.40; | PACSIN family | PTM: Phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC). {ECO:0000305}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Syna... | null | null | null | null | null | FUNCTION: Binds to membranes via its F-BAR domain and mediates membrane tubulation. Plays a role in the reorganization of the microtubule cytoskeleton via its interaction with MAPT; this decreases microtubule stability and inhibits MAPT-induced microtubule polymerization. Plays a role in cellular transport processes by... | Bos taurus (Bovine) |
A7MBI7 | COMT_BOVIN | MLEAPPLLLVAGGVGLALLALRWLATTDLQFFGRAFIVWNEFIMKPIRNLLMGSSKEQRILQHVLQHAVAGDPQSVVAAIDSYSLEKEWAMHVGEKKGQIVDRVLREQQPSVLLELGAYCGYSAVRMARLLLPGARLLTIEFNPDYAAITQRMVEFAGLQDKVTVVLGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDMLLLEECGLLREGTVLLADNVIYPGAPDFLEYVRGNSRFECSHFSSYLEYSKVVDGLEKVVYKGLSGPARP | 2.1.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P22734}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P22734}; | catecholamine catabolic process [GO:0042424]; developmental process [GO:0032502]; dopamine metabolic process [GO:0042417]; lipid metabolic process [GO:0006629]; methylation [GO:0032259] | axon [GO:0030424]; cytosol [GO:0005829]; dendrite [GO:0030425]; membrane [GO:0016020]; plasma membrane [GO:0005886] | catechol O-methyltransferase activity [GO:0016206]; L-dopa O-methyltransferase activity [GO:0102084]; magnesium ion binding [GO:0000287]; orcinol O-methyltransferase activity [GO:0102938] | PF01596; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Cation-dependent O-methyltransferase family | null | SUBCELLULAR LOCATION: [Isoform Soluble]: Cytoplasm {ECO:0000250|UniProtKB:P22734}.; SUBCELLULAR LOCATION: [Isoform Membrane-bound]: Cell membrane {ECO:0000250|UniProtKB:P22734}; Single-pass type II membrane protein {ECO:0000255}; Extracellular side {ECO:0000250|UniProtKB:P22734}. | CATALYTIC ACTIVITY: Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378, ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134251; EC=2.1.1.6; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-rig... | null | null | null | null | FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol. {ECO:0000250|UniProtKB:P21964}. | Bos taurus (Bovine) |
A7MBL8 | PKN2_DANRE | MAADSVQNDARGPMVSGRLDFDQNLDFSDTMVQKNLDEIKDQIKREIRKELKIKEGAENLRKVTTDKKSLAYVDNMLKKSNKKVEELHQELQELNAHIVVKDPEEVEEYPLTPDTPKSETRMSTNSNRLAALKKQADIELKVKQGAEDMIQMYSNGSSKDRKLLAAAQQMLQDSKTKIEFIRMQILKASQTSEINYENNDVTTSKPIISPLDLRIEELRHHYRIESAVADGAKNVMKLLGTGKVTEKKAHSEAQARLNESSQKLDLLKFSLEQRLSELPKNHPKGTLIMEELAMVASPPNSPRQSIMSTSNQYSTVAKPA... | 2.7.11.13 | null | cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell division [GO:0051301]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310] | anchoring junction [GO:0070161]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; lamellipodium [GO:0030027]; midbody [GO:0030496]; nucleus [GO:0005634] | ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; small GTPase binding [GO:0031267] | PF02185;PF00069;PF00433; | 1.10.287.160;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | PTM: Autophosphorylated. Phosphorylated. {ECO:0000250}.; PTM: Proteolytically cleaved. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Membrane {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Cell junction {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=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Pkc-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. May play a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion and transcription activation signaling proce... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A7MBS7 | THS7A_DANRE | MGLASRAPGKGGTSAGALASLFRVALLFFGLWDVQTQTVANTRPTYIWQTGPWGRCMGSECGPGGSQSRAVWCAHSEGWTTLHTNCQQSERPSNQQSCFRVCDWHKELYDWQLGAWNQCVPVSMRNAGVPRPAVCTRGEEGIQTREVGCVHKSDGVPAEDAICEYFEPKPRLEQACLIPCPRDCVVSEFSPWTSCSKSCGMGLQNRLRSVLAPPLFGGSACPNLTEFRTCQPGKCEGVESLHSLRVGPWGQCMASPIRQARDTGEARVPKAERKAKRDRQARQERQGKRRKNKEKKELRESKGERVRERVKEKKRMRDPE... | null | null | angiogenesis [GO:0001525]; axon extension [GO:0048675]; blood vessel endothelial cell migration [GO:0043534]; glomerular filtration [GO:0003094]; glomerulus development [GO:0032835]; podocyte development [GO:0072015]; regulation of Notch signaling pathway [GO:0008593]; sprouting angiogenesis [GO:0002040] | cell projection [GO:0042995]; plasma membrane [GO:0005886] | null | PF19030;PF19028;PF00090; | 2.20.100.10; | null | PTM: Extensively N-glycosylated. {ECO:0000250|UniProtKB:Q69ZU6}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q69ZU6}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q69ZU6}. Cell projection {ECO:0000250|UniProtKB:Q69ZU6}. Note=Detected on podocyte foot processes. {ECO:0000250|UniProtKB:Q69ZU6}. | null | null | null | null | null | FUNCTION: Required for normal sprouting angiogenesis and normal embryonic development of intersegmental vessels (ISV) (PubMed:21520329, PubMed:27484901). Required for normal function of the glomerular filtration barrier (PubMed:28814510). Required for normal axon outgrowth on embryonic motor neurons at the level of the... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A7MCT6 | EKI2_MOUSE | MAVPPSAPVPCSPFYLRRQEPCPQCSWSMEEKAVASAGCWEPPGPPRAAVPCFSVTVEQDDILPGALRLIRELRPHWKPEQVRTKRFKDGITNKLLACYVEEDMRDCVLVRVYGERTELLVDRENEVRNFQLLRAHGCAPKLYCTFQNGLCYEYVQGVALGPEHIREPQLFRLIALEMAKIHTIHANGSLPKPTLWHKMHRYFTLVKDEISPSLSADVPKVEVLEQELAWLKEHLSQLDSPVVFCHNDLLCKNIIYDSDKGRVCFIDYEYAGYNYQAFDIGNHFNEFAGVNVVDYSRYPARETQVQWLRYYLEAQKGTAA... | 2.7.1.82 | null | in utero embryonic development [GO:0001701]; multicellular organism growth [GO:0035264]; phosphatidylethanolamine biosynthetic process [GO:0006646]; phosphorylation [GO:0016310]; placenta development [GO:0001890]; post-embryonic development [GO:0009791] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; ethanolamine kinase activity [GO:0004305] | PF01633; | 3.90.1200.10; | Choline/ethanolamine kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + ethanolamine = ADP + H(+) + phosphoethanolamine; Xref=Rhea:RHEA:13069, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57603, ChEBI:CHEBI:58190, ChEBI:CHEBI:456216; EC=2.7.1.82; Evidence={ECO:0000269|PubMed:16861741}; | null | PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3. | null | null | FUNCTION: Highly specific for ethanolamine phosphorylation. Does not have choline kinase activity. {ECO:0000269|PubMed:16861741}. | Mus musculus (Mouse) |
A7MCY6 | TBKB1_HUMAN | MESMFEDDISILTQEALGPSEVWLDSPGDPSLGGDMCSASHFALITAYGDIKERLGGLERENATLRRRLKVYEIKYPLISDFGEEHGFSLYEIKDGSLLEVEKVSLQQRLNQFQHELQKNKEQEEQLGEMIQAYEKLCVEKSDLETELREMRALVETHLRQICGLEQQLRQQQGLQDAAFSNLSPPPAPAPPCTDLDLHYLALRGGSGLSHAGWPGSTPSVSDLERRRLEEALEAAQGEARGAQLREEQLQAECERLQGELKQLQETRAQDLASNQSERDMAWVKRVGDDQVNLALAYTELTEELGRLRELSSLQGRILR... | null | null | canonical NF-kappaB signal transduction [GO:0007249]; defense response to virus [GO:0051607]; type I interferon-mediated signaling pathway [GO:0060337] | cytoplasm [GO:0005737]; serine/threonine protein kinase complex [GO:1902554] | metal ion binding [GO:0046872] | PF12845; | null | null | null | null | null | null | null | null | null | FUNCTION: Adapter protein which constitutively binds TBK1 and IKBKE playing a role in antiviral innate immunity. {ECO:0000269|PubMed:21931631}. | Homo sapiens (Human) |
A7MD48 | SRRM4_HUMAN | MASVQQGEKQLFEKFWRGTFKAVATPRPESIIVASITARKPLPRTEPQNNPVVPAQDGPSEKLGQHLATEPLGTNSWERDKTCRELGATRGHSASHDKDLTPPPSSRGKKKKKKSTRKKRRRSSSYSPSPVKKKKKKSSKKHKRRRSFSKKRRHSSSSPKSKRRDEKRHKKQSRSRPRKSHRHRHHRCPSRSQSSESRPSSCESRHRGRSPEEGQKSRRRHSRRCSKTLCKDSPEAQSSRPPSQPLQMLGYLSARGVITGSGSAADLFTKTASPLTTSRGRSQEYDSGNDTSSPPSTQTSSARSRGQEKGSPSGGLSKSR... | null | null | cell differentiation [GO:0030154]; mRNA processing [GO:0006397]; nervous system development [GO:0007399]; neuron maturation [GO:0042551]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of RNA splicing [GO:0043484]; RNA splicing [GO:0008380]; sensory perception of sound [GO:0007605] | nucleus [GO:0005634] | identical protein binding [GO:0042802]; mRNA binding [GO:0003729] | PF15230; | null | NSR100 family | PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q8BKA3}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8BKA3}. | null | null | null | null | null | FUNCTION: Splicing factor specifically required for neural cell differentiation. Acts in conjunction with nPTB/PTBP2 by binding directly to its regulated target transcripts and promotes neural-specific exon inclusion in many genes that function in neural cell differentiation. Required to promote the inclusion of neural... | Homo sapiens (Human) |
A7MRY4 | LUXN_VIBC1 | MFDFSLEAIVYAKAITLLATVAVVMMWLFYYCYRLKQKNEVIFGTHHAAYIAYSVCIIAWISSNAYFHTDLLPELGASAGMFMAKFANLASFFAFAFAYYFSCQLAAEQRKGKVHRWQQGIFVSLTVYSLFINLRPGLTVEHVDIVGPSQFIIEFGPHTSYFFIGLVSFVVLTLVNLVAMRTNSSKLTLAKTNYMIAGILVFMLSTAVIHLGMTYFMGDFSLTWLPPALSISEMLFVGYALLTSRFYSVKYIAYLALSVLLVCAIFVLPLGAIFIPLTESNQWLIAIPICALIGITWQLLYKKTSRYASFLIYGDKKTPV... | 2.7.13.3; 3.1.3.- | null | null | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; histidine phosphotransfer kinase activity [GO:0009927]; phosphoprotein phosphatase activity [GO:0004721]; phosphorelay sensor kinase activity [GO:0000155] | PF02518;PF00072; | 1.10.287.130;3.40.50.2300;3.30.565.10; | null | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; | null | null | null | null | FUNCTION: At low cell density, in the absence of AI-1 (autoinducer 1), LuxN has a kinase activity and autophosphorylates on His-471. The phosphoryl group is then transferred on Asp-771 of the response regulator domain. The phosphoryl group is transferred to LuxU, and ultimately to LuxO. At high cell density, in the pre... | Vibrio campbellii (strain ATCC BAA-1116) |
A7N805 | MPAA_VIBC1 | MNRYYSNNQEITVSLIPRTERAAFLITPTSYGKSVLGAPLLYFPAQVESNSRGLILAGTHGDETASIAGLSCALRSLPAECLKHDVILSMNPDANQLGTRANANQVDLNRAFPTQNWTEHGTVYRWSSHTPVRDVKVKTGDKEQLEPEVDALISLIELRRPKFVVSFHEPLAFVDDPAHSDLAKWLGKQFNLPIVDDVDYETPGSFGTWCNERQLPCITVELPPISADLTIEKHLDAFIALLQHDPDL | 3.4.17.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000269|PubMed:22970852}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000269|PubMed:22970852}; | cell wall macromolecule catabolic process [GO:0016998]; cell wall organization [GO:0071555]; peptidoglycan catabolic process [GO:0009253]; proteolysis [GO:0006508] | cytoplasm [GO:0005737] | amidase activity [GO:0004040]; hydrolase activity, acting on ester bonds [GO:0016788]; murein tripeptide carboxypeptidase activity [GO:0061473]; zinc ion binding [GO:0008270] | PF04952; | 3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02211}. | CATALYTIC ACTIVITY: Reaction=H2O + L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate = L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate; Xref=Rhea:RHEA:28398, ChEBI:CHEBI:15377, ChEBI:CHEBI:57791, ChEBI:CHEBI:61395, ChEBI:CHEBI:61401; Evidence={ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000269|PubMed:22970852}; | null | PATHWAY: Cell wall degradation; peptidoglycan degradation. {ECO:0000255|HAMAP-Rule:MF_02211, ECO:0000305|PubMed:22970852}. | null | null | FUNCTION: Involved in muropeptide degradation. Catalyzes the hydrolysis of the gamma-D-glutamyl-diaminopimelic acid (gamma-D-Glu-Dap) amide bond in the murein tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid, leading to the formation of L-Ala-gamma-D-Glu and Dap. Has weak activity with L-Ala-gamma-D-Glu-L-... | Vibrio campbellii (strain ATCC BAA-1116) |
A7RDN6 | RNLS_MOUSE | MSRVLVVGAGLTGSLCAALLRKEITAPLYLGLWDKGGDIGGRMITASSPHNPRCTADLGAQYITCSPHYVKEHQNFYEELLAHGILKPLTSPIEGMKGKEGDCNFVAPQGFSSVIKYYLKKSGAEVSLKHCVTQIHLKDNKWEVSTDTGSAEQFDLVILTMPAPQILELQGDIVNLISERQREQLKSVSYSSRYALGLFYEVGMKIGVPWSCRYLSSHPCICFISIDNKKRNIESSECGPSVVIQTTVPFGVQHLEASEADVQKLMIQQLETILPGLPQPVATICHKWTYSQVTSSVSDRPGQMTLHLKPFLVCGGDGFT... | 1.6.3.5 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q5VYX0}; | cardiac left ventricle morphogenesis [GO:0003214]; dopamine metabolic process [GO:0042417]; epinephrine metabolic process [GO:0042414]; heart contraction [GO:0060047]; norepinephrine metabolic process [GO:0042415]; phosphate ion homeostasis [GO:0055062]; regulation of systemic arterial blood pressure [GO:0003073]; resp... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on NAD(P)H [GO:0016651] | PF01593;PF13450; | 3.90.660.10;3.50.50.60; | Renalase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17846919}. | CATALYTIC ACTIVITY: Reaction=1,2-dihydro-beta-NAD + H(+) + O2 = H2O2 + NAD(+); Xref=Rhea:RHEA:40395, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57540, ChEBI:CHEBI:88138; EC=1.6.3.5; Evidence={ECO:0000250|UniProtKB:Q5VYX0}; CATALYTIC ACTIVITY: Reaction=1,2-dihydro-beta-NADP + H(+) + O2 = H2O2 +... | null | null | null | null | FUNCTION: Catalyzes the oxidation of the less abundant 1,2-dihydro-beta-NAD(P) and 1,6-dihydro-beta-NAD(P) to form beta-NAD(P)(+). The enzyme hormone is secreted by the kidney, and circulates in blood and modulates cardiac function and systemic blood pressure. Lowers blood pressure in vivo by decreasing cardiac contrac... | Mus musculus (Mouse) |
A7T1N0 | TMP2L_NEMVE | MGKDSFTPLYDGGDSSHVHLNKFGSNQLSQSKKSWIARNFSRRECIRFVPKSHDVSRCKCGRPRERHSQQALESGQGSEEWNVASCTTKHPTNAYGEIDFEGYGGQKRAPYLRMSHDTDANLVITLMLKRWNLEIPNLVISVTGGAKSFVLKPRLREMFRRGLIKAAKTTGAWIITGGTNTGVMKHVGEAVKEQQLMFGSDTQVNVIGIATWGIVDKQSDLISEKNGKYPALYSMEPTPGHQGAMLDPNHSHFFLVDDGTEGKYGVEIGMRSRIEEAIMKVKTDSRSEAGSIGVPVVLLVLEGGPNTVATMYELIKKKVP... | null | null | calcium ion transmembrane transport [GO:0070588]; sodium ion transmembrane transport [GO:0035725] | plasma membrane [GO:0005886] | ADP-ribose diphosphatase activity [GO:0047631]; ligand-gated calcium channel activity [GO:0099604]; ligand-gated sodium channel activity [GO:0015280]; metal ion binding [GO:0046872] | PF00520;PF18139;PF00293; | 3.90.79.10; | Transient receptor (TC 1.A.4) family, LTrpC subfamily, TRPM2 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:27333281, ECO:0000305|PubMed:28775320}; Multi-pass membrane protein {ECO:0000269|PubMed:29745897}. | null | null | null | null | null | FUNCTION: Nonselective, voltage-independent cation channel that mediates Ca(2+) and to a lesser extent Na(+) influx, leading to increased cytoplasmic Ca(2+) levels (PubMed:25620041, PubMed:27333281, PubMed:28775320, PubMed:29745897). Functions as a ligand-gated ion channel (PubMed:25620041, PubMed:27333281, PubMed:2877... | Nematostella vectensis (Starlet sea anemone) |
A7TUE1 | CCLOP_MEDTR | MEGRGFSGLYKNSSEELFLKTVMESPIGMPVPTMEMLGFKTVSQSFRTDSEELFKRWLTNDQEGYNSSSMGLNSRLSKRISTEIANMSNQQHIGVASEGRNNDKSCLQNNFLANDVSSDFNFPIRDPVDRELQSSNLFLAKAWFITDQRMTRSRSSELRRRYTEMQNSQAPQGLDSMFMVPEHDTNTIKEELANFNGFDYLSMCELPSQKGTFMSPSNSSSSTFNTHQLVDVDKVSSCVSMLKGTLQRKKLECQVEKEAAEDGLNEIFCIREPLFQSAFNEEESWNQQKLVNVQGDFTDQVNDPGVMQTLEGTTNFVLDG... | null | null | arbuscular mycorrhizal association [GO:0036377]; nodulation [GO:0009877] | nucleus [GO:0005634] | protein homodimerization activity [GO:0042803]; sequence-specific DNA binding [GO:0043565] | null | null | CYCLOPS family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17722695, ECO:0000269|PubMed:21787150}. | null | null | null | null | null | FUNCTION: Involved symbiotic signaling. Required for root infection by symbiotic rhizobia, infection thread (IT) formation, and nodule development. Required for proper induction of early nodulin gene expression. Probably not involved in nodule organogenesis. Involved in arbuscular mycorrhizal (AM) symbiosis. Required f... | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
A7TZE6 | SKIT1_MOUSE | MGSTGLCFYGHCIVMFLLQMVTASSEPFIVNGLEGPVLASLGGNLELSCQLSPPQQAQHMEIRWFRNLYTEPVHLYRDGKDMFGEIISKYVERTELLKDGIGEGKVTLRIFNVTVDDDGSYHCVFKDGDFYEEHITEVKITAINLQVQIHVHPPNTKGVIVECHSGGWFPRPLMQWRDRRGEVIPAASKSHSQGRDKLFNMKISLLISESFFQKVICCLQNPLTGQEERTSVILSDAFFSWNRIWKMILGIILSMMVVSIFVFSCLLHHEHKVCKWKWDAPWIKGLLIMTSSMVTVVLVMVYLHMKQRVPVSDVHFELDT... | null | null | epithelial cell differentiation [GO:0030855]; gamma-delta T cell differentiation [GO:0042492]; positive regulation of epithelial cell differentiation [GO:0030858]; positive regulation of gamma-delta T cell differentiation [GO:0045588]; positive regulation of T cell differentiation [GO:0045582]; positive regulation of T... | cell periphery [GO:0071944]; external side of plasma membrane [GO:0009897]; membrane [GO:0016020] | signaling receptor binding [GO:0005102] | PF07686; | 2.60.40.10; | SKINT family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: May act by engaging a cell surface molecule on immature T-cells in the embryonic thymus. Plays a central role in mediating key epithelial-immune interactions by being involved in the selection of Vgamma5(+)Vdelta1(+) T-cells, which constitute 90% of epidermal gammadelta T-cells. {ECO:0000269|PubMed:18408721}. | Mus musculus (Mouse) |
A7UL74 | CTF7_ARATH | MQAKINSFFKPSSSSSIAASVTTDTDDGLAVWENNRNAIVNTYQRRSAITERSEVLKGCIEKTLKKGSSSVPKNHKKKRNYTQFHLELGQSDFLLRHCAECGAKYAPGDELDEKNHQSFHKDYMYGLPFKGWQNEKAFTSPLFIKNRIVMVSENDSPAHRNKVQEVVKMMEVELGEDWILHQHCKVYLFISSQRISGCLVAEPIKEAFKLIASPDDERQLQKESSSSPSTSIQFGNIVLQREVSKRCRTSDDRLDNGVIVCEEEAKPAVCGIRAIWVSPSNRRKGIATWLLDTTRESFCNNGCMLEKSQLAFSQPSSIGR... | 2.3.1.- | null | anther development [GO:0048653]; cell division [GO:0051301]; developmental vegetative growth [GO:0080186]; DNA repair [GO:0006281]; double-strand break repair via homologous recombination [GO:0000724]; embryo development ending in seed dormancy [GO:0009793]; embryo sac development [GO:0009553]; establishment of meiotic... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | acetyltransferase activity [GO:0016407]; metal ion binding [GO:0046872]; peptide-lysine-N-acetyltransferase activity [GO:0061733] | PF13880;PF13878; | null | Acetyltransferase family, ECO subfamily | PTM: Autoacetylated. {ECO:0000269|PubMed:20671110}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20671110}. Cytoplasm {ECO:0000269|PubMed:20671110}. | null | null | null | null | null | FUNCTION: Acetyltransferase required for the establishment of sister chromatid cohesion (PubMed:20671110). Involved in preservation of genome integrity and meiosis (PubMed:20671110, PubMed:23750584). Required for DNA repair and for the regulation of chromosome segregation during mitotic cell division (PubMed:20671110, ... | Arabidopsis thaliana (Mouse-ear cress) |
A7VJC2 | ROA2_RAT | MEKTLETVPLERKKREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIFLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGN... | null | null | G-quadruplex DNA unwinding [GO:0044806]; lung development [GO:0030324]; male gonad development [GO:0008584]; miRNA transport [GO:1990428]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; mRNA transport [GO:0051028]; negative regulation of mRNA splicing, ... | Cajal body [GO:0015030]; catalytic step 2 spliceosome [GO:0071013]; chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; neuronal ribonucleoprotein granule [GO:0071598]; nuclear... | DNA polymerase binding [GO:0070182]; G-rich strand telomeric DNA binding [GO:0098505]; miRNA binding [GO:0035198]; molecular condensate scaffold activity [GO:0140693]; mRNA 3'-UTR binding [GO:0003730]; mRNA CDS binding [GO:1990715]; N6-methyladenosine-containing RNA reader activity [GO:1990247]; pre-mRNA intronic bindi... | PF11627;PF00076; | 3.30.70.330; | null | PTM: Asymmetric dimethylation at Arg-266 constitutes the major methylation site (PubMed:24098712). According to a report, methylation affects subcellular location and promotes nuclear localization (PubMed:10772824). According to another report, methylation at Arg-266 does not influence nucleocytoplasmic shuttling (PubM... | SUBCELLULAR LOCATION: [Isoform B1]: Nucleus {ECO:0000269|PubMed:20406423}.; SUBCELLULAR LOCATION: [Isoform A2]: Nucleus {ECO:0000269|PubMed:20406423, ECO:0000269|PubMed:24098712}.; SUBCELLULAR LOCATION: [Isoform A2b]: Cytoplasm {ECO:0000269|PubMed:20406423}. Nucleus {ECO:0000269|PubMed:20406423}. Note=Mainly localizes ... | null | null | null | null | null | FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging p... | Rattus norvegicus (Rat) |
A7WLH8 | SUMO1_PIG | MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSTV | null | null | cellular response to cadmium ion [GO:0071276]; cellular response to heat [GO:0034605]; negative regulation of action potential [GO:0045759]; negative regulation of delayed rectifier potassium channel activity [GO:1902260]; protein sumoylation [GO:0016925]; roof of mouth development [GO:0060021] | nuclear membrane [GO:0031965]; nuclear speck [GO:0016607]; nuclear stress granule [GO:0097165]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; PML body [GO:0016605]; septin ring [GO:0005940] | potassium channel regulator activity [GO:0015459]; protein tag activity [GO:0031386]; transcription factor binding [GO:0008134]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-like protein ligase binding [GO:0044389] | PF11976; | null | Ubiquitin family, SUMO subfamily | PTM: Cleavage of precursor form by SENP1 or SENP2 is necessary for function. {ECO:0000250|UniProtKB:P63165}.; PTM: Polymeric SUMO1 chains undergo polyubiquitination by RNF4. {ECO:0000250|UniProtKB:P63165}. | SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}. Note=Recruited by BCL11... | null | null | null | null | null | FUNCTION: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, ... | Sus scrofa (Pig) |
A7WM73 | HEXO1_ARATH | MSTNLLRLILLFITLSITSSLSTPSPADSPPYLWPLPAEFSFGNETLSVDPTVTLIVAGNGGGSLIIRAAFDRYMGIIFKHASGRGSLLSRIRFLKMVEYDITSLKIVVHSDSEELQLGVDESYTLMVSKKNEQSIVGAATIEANTVYGALRGLETFSQLCAFDYITKSVQIYKAPWYIQDKPRFGYRGLLIDTSRHYLPIDVIKQIIESMSFAKLNVLHWHIVDEQSFPLETPTYPNLWKGAYSRWERYTVEDASEIVRFAKMRGINVMAEVDVPGHAESWGTGYPDLWPSLSCREPLDVTKNFTFDVISGILADMRKI... | 3.2.1.52 | null | carbohydrate metabolic process [GO:0005975]; glycosaminoglycan metabolic process [GO:0030203] | membrane [GO:0016020]; plant-type vacuole [GO:0000325]; secretory vesicle [GO:0099503]; vacuole [GO:0005773] | beta-N-acetylhexosaminidase activity [GO:0004563]; hexosaminidase activity [GO:0015929]; N-acetyl-beta-D-galactosaminidase activity [GO:0102148] | PF00728;PF14845; | 3.30.379.10;3.20.20.80; | Glycosyl hydrolase 20 family | PTM: N-glycosylated. {ECO:0000269|PubMed:17644627}. | SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:17644627, ECO:0000269|PubMed:21252225}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52; Evidence={ECO:0000269|PubMed:17644627}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.7 mM for pNP-GlcNAc (at pH 4.6 and 37 degrees Celsius) {ECO:0000269|PubMed:17636254, ECO:0000269|PubMed:17644627}; Vmax=151 umol/min/mg enzyme with pNP-GlcNAc as substrate (at pH 4.6 and 37 degrees Celsius) {ECO:0000269|PubMed:17636254, ECO:0000269|PubMed:1764462... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-5. {ECO:0000269|PubMed:17636254, ECO:0000269|PubMed:17644627}; | null | FUNCTION: Has a broad substrate specificity. Can use synthetic substrates such as pyridylaminated chitotriose, pyridylaminated chitobiose, p-nitrophenyl-beta-N-acetylglucosaminide, p-nitrophenyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (pNP-GlcNAc), p-nitrophenyl-2-acetamido-2-deoxy-beta-D-galactopyranoside (pNP-GalN... | Arabidopsis thaliana (Mouse-ear cress) |
A7WPL6 | BBLB_TOBAC | MFPLIILISFSLTSLSATATSGAGGGVANLYTCLIDHNVHNFSIYPTKNDQSSSNYFNLLDFSLQNLRFAASYMPKPTVIILPNSKEELVSTILCCRQASYEIRVRCGGHSYEGTSYVSFDGSPFVIVDLMKLDEVSVDLDSETAWAQGGATIGQIYYAIAKVSDVHAFSAGSGPTVGSGGHISGGGFGLLSRKFGLAADNVVDALLIDADGRLLDRKAMGEDVFWAIRGGGGGNWGIIYAWKIRLLKVPKIVTTCMIYRPGSKQYVAQLLQKWQIVTPNLVDDFTLGVLLRPADLPADMKYGNSTPIEIFPQFNALYLG... | 1.1.1.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:O64743}; | alkaloid biosynthetic process [GO:0009821]; nicotine biosynthetic process [GO:0042179]; response to jasmonic acid [GO:0009753] | plant-type vacuole [GO:0000325] | FAD binding [GO:0071949]; oxidoreductase activity [GO:0016491] | PF08031;PF01565; | 3.30.465.10;3.40.462.20;3.30.43.10; | Oxygen-dependent FAD-linked oxidoreductase family | null | SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:21343426}. | null | null | PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis. {ECO:0000269|PubMed:21343426}. | null | null | FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the... | Nicotiana tabacum (Common tobacco) |
A7WYY0 | HCHA_STAA1 | MSQDVNELSKQPTPDKAEDNAFFPSPYSLSQYTAPKTDFDGVEHKGAYKDGKWKVLMIAAEERYVLLENGKMFSTGNHPVEMLLPLHHLMEAGFDVDVATLSGYPVKLELWAMPTEDEAVISTYNKLKEKLKQPKKLADVIKNELGPDSDYLSVFIPGGHAAVVGISESEDVQQTLDWALDNDRFIVTLCHGPAALLSAGLNREKSPLEGYSVCVFPDSLDEGANIEIGYLPGRLKWLVADLLTKQGLKVVNDDMTGRTLKDRKLLTGDSPLASNELGKLAVNEMLNAIQNK | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790] | PF01965; | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Staphylococcus aureus (strain Mu3 / ATCC 700698) |
A7X5R6 | BAG6_ORNAN | MDPGGGGGGGGPGPGPDMEEPADLEVSVKTLDSQTRTFTVGAEMTVKEFKEHIAAAVSIPPDKQRLIYQGRVLQDDKKLQEYNVGGKVIHLVERAPPQTQGPSSGGASRAGSPSAPHAGAPPAGPRGPGAPVHDRNANSYVMVGTFNLPSDGSAVDVHINMEQAPIQSEPRVRLVMAQHMLRDIQALLARLEPQPGQQGQQGQQQGQALLAESGPPRPGPPGQTDGETSPREPTETREPTETREPEDGVAARGTGPAPGPAPAPAPEGNAAPNHPSPAEYAEVLQELQRVESRLQPFLQRYRAILGAAATTDYNNNTEGR... | null | null | 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:0018393]; intrinsic apoptotic sig... | 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;PF00240; | null | null | PTM: Ricin can induce the cleavage by the caspase CASP3. {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... | Ornithorhynchus anatinus (Duckbill platypus) |
A7X657 | ITPK1_SOYBN | MAEKRFGVIGYALAPKKQNSFIRDSLVSLAKSRGIELVRVDSDKPLADQGPFDCVLHKLYGDDWKRQLQEFHTLYPNAVILDAPEAIERLHNRISMLQVVSELRIEDRPETFGIPKQIVIYDKATLLDPQAWESLKFPVIAKPLVADGSAKSHKMALVFTRDALNKLKPPIVLQEFVNHGGVIFKVYVVGEHVRCVKRKSLPDVSDEEKALGGVSEDLMSFSQVSNLATVNDCDGYYRLMHLDDDTEMPPDAFVVDIAGGLRRALKLNLFNFDVIRDARYGNRYLIIDINYFPGYAKMPGYEAVLTQFFCEVMLKKKQQE... | 2.7.1.134; 2.7.1.159; 2.7.4.21 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q13572}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250|UniProtKB:Q13572}; | inositol trisphosphate metabolic process [GO:0032957]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; inositol tetrakisphosphate 1-kinase activity [GO:0047325]; inositol-1,3,4-trisphosphate 5-kinase activity [GO:0052726]; inositol-1,3,4-trisphosphate 6-kinase activity [GO:0052725]; inositol-3,4,6-trisphosphate 1-kinase activity [GO:0052835]; magnesium ion binding [GO:0000287] | PF05770;PF17927; | 3.30.470.20; | ITPK1 family | null | null | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:13253, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895, ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirect... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.7 uM for Ins(1,3,4)P3 {ECO:0000269|PubMed:18474240}; KM=0.28 uM for Ins(3,4,5,6)P4 {ECO:0000269|PubMed:18474240}; Vmax=0.5 umol/min/mg enzyme with Ins(1,3,4)P3 as substrate {ECO:0000269|PubMed:18474240}; Vmax=0.083 umol/min/mg enzyme with Ins(3,4,5,6)P4 as substr... | null | null | null | FUNCTION: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4, Ins(3,4,6)P3 and Ins(1,3,4)P3 (PubMed:18474240). May participate in an inositol lipid-independent pathway of InsP6 synthesis (PubMed:18474240). Able to add a beta-phosphate to InsP6 to yield 5-InsP7, thus exhibiting InsP6 kin... | Glycine max (Soybean) (Glycine hispida) |
A7X665 | ITPK2_SOYBN | MSESEVAGQRYRVGYALQGKKVESFIQPSLLDHAKQHSIDLVQIDPTAPLQQQGPFHCIIHKLHTQHWKNLLQQFSSKHPNTVIIDPPELVDRLHNRVSMLDAVTHLQFSLENATIGVPKQVVVNEPKSFDLHKFEEEQGLRFPVIAKPLAADGGAGSHELCLVFDEEGLHALSVPMVLQEFVNHGGVVFKIYVAGQRVNCVKRKSLGDITEEKLKVLRGSLPFSRVSSLGVEDEGGGAVEDAEMPPQSLVGELARGLREALGLNLFNVDVIRDGKEPTRYLVIDINYFPGYAKLPSYEPFITDFLLDIVRSKTA | 2.7.1.134; 2.7.1.159; 2.7.4.21 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q13572}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250|UniProtKB:Q13572}; | inositol trisphosphate metabolic process [GO:0032957]; myo-inositol hexakisphosphate biosynthetic process [GO:0010264]; phosphorylation [GO:0016310]; response to abscisic acid [GO:0009737]; response to salt stress [GO:0009651]; response to water deprivation [GO:0009414] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; inositol tetrakisphosphate 1-kinase activity [GO:0047325]; inositol-1,3,4-trisphosphate 5-kinase activity [GO:0052726]; inositol-1,3,4-trisphosphate 6-kinase activity [GO:0052725]; inositol-3,4,6-trisphosphate 1-kinase activity [GO:0052835]; magnesium ion binding [GO:0000287] | PF05770;PF17927; | 3.30.1490.220;3.40.50.11370;3.30.470.20; | ITPK1 family | null | null | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:13253, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895, ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirect... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=46.2 uM for Ins(1,3,4)P3 {ECO:0000269|PubMed:18474240}; KM=0.78 uM for Ins(3,4,5,6)P4 {ECO:0000269|PubMed:18474240}; Vmax=1.97 umol/min/mg enzyme with Ins(1,3,4)P3 as substrate {ECO:0000269|PubMed:18474240}; Vmax=0.76 umol/min/mg enzyme with Ins(3,4,5,6)P4 as subst... | null | null | null | FUNCTION: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4, Ins(3,4,6)P3 and Ins(1,3,4)P3 (PubMed:18474240). May participate in an inositol lipid-independent pathway of InsP6 synthesis (PubMed:18474240). Barely able to add a beta-phosphate to InsP6 to yield 5-InsP7, thus exhibiting ne... | Glycine max (Soybean) (Glycine hispida) |
A7X672 | ITPK3_SOYBN | MRLREEVACKNDDVCEKEEVVIENDVTVAQNHWCPVVNAGFSSPKRVVVVGYALTTKKIKSFLQPKLEGLARNKGILFVAIDHNRPLSDQGPFDIVLHKLSGKEWRQVLEDYRLSHPEVTVLDPPDAIQHLRNRQYMLQAVADMNLSDSYGIVGVPRQLVIKRDALAIPELVNKAGLTLPLVAKPLVADGSAKSHELSLAYEHFSLQNLEPPLVLQEFVNHGGVLFKVYIVGDAIKVVRRFSLPDVSKWELSKDAGIYRFPRVSCAAASADDADLDPTVAELPPRPLLEKLAKELRWRLGLRLFNLDIIREYGTRNHFYV... | 2.7.1.134; 2.7.1.159 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q13572}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250|UniProtKB:Q13572}; | inositol trisphosphate metabolic process [GO:0032957]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; inositol tetrakisphosphate 1-kinase activity [GO:0047325]; inositol-1,3,4-trisphosphate 5-kinase activity [GO:0052726]; inositol-1,3,4-trisphosphate 6-kinase activity [GO:0052725]; inositol-3,4,6-trisphosphate 1-kinase activity [GO:0052835]; magnesium ion binding [GO:0000287] | PF05770;PF17927; | 3.30.470.20; | ITPK1 family | null | null | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:13253, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895, ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirect... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=43.4 uM for Ins(1,3,4)P3 {ECO:0000269|PubMed:18474240}; KM=1.05 uM for Ins(3,4,5,6)P4 {ECO:0000269|PubMed:18474240}; Vmax=0.86 umol/min/mg enzyme with Ins(1,3,4)P3 as substrate {ECO:0000269|PubMed:18474240}; Vmax=0.22 umol/min/mg enzyme with Ins(3,4,5,6)P4 as subst... | null | null | null | FUNCTION: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4, Ins(3,4,6)P3 and Ins(1,3,4)P3 (PubMed:18474240). May participate in an inositol lipid-independent pathway of InsP6 synthesis (PubMed:18474240). {ECO:0000269|PubMed:18474240}. | Glycine max (Soybean) (Glycine hispida) |
A7X680 | ITPK4_SOYBN | MRLNGEISSGEEEEEEKQTGTTTFSSQKVVVGYALTSKKKKSFLQPSFTGLARNRGINFVAIDLNKPLPEQGPFDIILHKLSGEVWREIIEDYREKHPEVTVLDPPDAIQHLHNRQSMLQDVLDLNLSDCHGKVGVPRQLVITKEKDPSSIPYEVTKAGMKLPLVAKPLVVDGTAKSHELFLAYDEFSLSAVEPPLVLQEFVNHGGLLFKIYIVGETIKVVRRFSLPNISKRELSKVAGVFRFPRVSCAAASADDADLDPNIAEHPPRPLLERLARELRHRLGLHLFNIDMIREYGTKDVFYVIDINYFPGYGKMPGYEH... | 2.7.1.134; 2.7.1.159 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q13572}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250|UniProtKB:Q13572}; | inositol trisphosphate metabolic process [GO:0032957]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; inositol tetrakisphosphate 1-kinase activity [GO:0047325]; inositol-1,3,4-trisphosphate 5-kinase activity [GO:0052726]; inositol-1,3,4-trisphosphate 6-kinase activity [GO:0052725]; inositol-3,4,6-trisphosphate 1-kinase activity [GO:0052835]; magnesium ion binding [GO:0000287] | PF05770;PF17927; | 3.30.1490.220;3.40.50.11370; | ITPK1 family | null | null | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:13253, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895, ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159; Evidence={ECO:0000269|PubMed:18474240}; PhysiologicalDirect... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.4 uM for Ins(1,3,4)P3 {ECO:0000269|PubMed:18474240}; KM=0.7 uM for Ins(3,4,5,6)P4 {ECO:0000269|PubMed:18474240}; Vmax=0.007 umol/min/mg enzyme with Ins(1,3,4)P3 as substrate {ECO:0000269|PubMed:18474240}; Vmax=0.004 umol/min/mg enzyme with Ins(3,4,5,6)P4 as subst... | null | null | null | FUNCTION: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4, Ins(3,4,6)P3 and Ins(1,3,4)P3 (PubMed:18474240). May participate in an inositol lipid-independent pathway of InsP6 synthesis (PubMed:18474240). {ECO:0000269|PubMed:18474240}. | Glycine max (Soybean) (Glycine hispida) |
A7X8B3 | PRGR_PANTR | MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSNEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQGVLSPLMSRSGCKAGDSSGTAAAHKVLPRGLSPSRQLLLPASGSPHWSGAPVKPSPQPAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPXRSPLATTMMDFIHVPILPLNHALLAART... | null | null | intracellular steroid hormone receptor signaling pathway [GO:0030518]; regulation of transcription by RNA polymerase II [GO:0006357] | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654] | estrogen response element binding [GO:0034056]; nuclear receptor activity [GO:0004879]; nuclear steroid receptor activity [GO:0003707]; steroid binding [GO:0005496]; zinc ion binding [GO:0008270] | PF00104;PF02161;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family | PTM: Phosphorylated on multiple serine sites. Several of these sites are hormone-dependent. Phosphorylation on Ser-294 is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388. Phosphorylation on Ser-102 and Ser-345 requires induction by hormone. Basal phosphorylation on Ser-81, Ser-162, Ser-... | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleoplasmic shuttling is both hormone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G(1) and G(2)/M phases (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcriptional activator of several progesteron-dependent promoters in a variety of cell types. Involved in activation of SRC-dependen... | Pan troglodytes (Chimpanzee) |
A7X8B7 | PRGR_GORGO | MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPYPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLETLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQGVLSPLMSRSGGKAGDSSGTAAAHKVLPRGLSPSRQLLLPVSGSPHWSGAPVKPSPQPAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAART... | null | null | glandular epithelial cell maturation [GO:0002071]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; lung alveolus development [GO:0048286]; maintenance of protein location in nucleus [GO:0051457]; negative regulation of gene expression [GO:0010629]; negative regulation of phosphorylation [GO:00423... | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | ATPase binding [GO:0051117]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; estrogen response element binding [GO:0034056]; identical protein binding [GO:0042802]; nuclear receptor activity [GO:0004879]; nuclear steroid receptor activity [GO:0003707]; steroid binding [GO:0005496]... | PF00104;PF02161;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family | PTM: Phosphorylated on multiple serine sites. Several of these sites are hormone-dependent. Phosphorylation on Ser-294 is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388. Phosphorylation on Ser-102 and Ser-345 also requires induction by hormone. Basal phosphorylation on Ser-81, Ser-162,... | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleoplasmic shuttling is both hormone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G(1) and G(2)/M phases (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcriptional activator of several progesteron-dependent promoters in a variety of cell types. Involved in activation of SRC-dependen... | Gorilla gorilla gorilla (Western lowland gorilla) |
A7XDQ9 | B3GTK_ARATH | MKRVKSESFRGVYSSRRFKLSHFLLAIAGFYLVFLAFKFPHFIEMVAMLSGDTGLDGALSDTSLDVSLSGSLRNDMLNRKLEDEDHQSGPSTTQKVSPEEKINGSKQIQPLLFRYGRISGEVMRRRNRTIHMSPFERMADEAWILGSKAWEDVDKFEVDKINESASIFEGKVESCPSQISMNGDDLNKANRIMLLPCGLAAGSSITILGTPQYAHKESVPQRSRLTRSYGMVLVSQFMVELQGLKTGDGEYPPKILHLNPRIKGDWNHRPVIEHNTCYRMQWGVAQRCDGTPSKKDADVLVDGFRRCEKWTQNDIIDMVD... | 2.4.1.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:26690932}; | arabinogalactan protein metabolic process [GO:0010405]; protein O-linked glycosylation via hydroxyproline [GO:0018258]; root hair cell development [GO:0080147] | endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139] | carbohydrate binding [GO:0030246]; hydroxyproline O-galactosyltransferase activity [GO:1990714] | PF00337;PF01762; | 2.60.120.200;3.90.550.50; | Glycosyltransferase 31 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:23430255}; Single-pass type II membrane protein {ECO:0000305}. | null | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:23430255}; | null | FUNCTION: Possesses hydroxyproline O-galactosyltransferase activity. Transfers galactose from UDP-galactose to hydroxyproline residues in the arabinogalactan proteins (AGPs). Is specific for AGPs containing non-contiguous peptidyl hydroxyproline residues. Utilizes UDP-galactose solely as sugar donor. The addition of ga... | Arabidopsis thaliana (Mouse-ear cress) |
A7XGN8 | LOV1B_ARATH | MAEGVVLFGVHKLWELLNRESARLNGIGEQVDGLKRQLGRLQSLLKDADAKKHESERVRNFLEDVRDIVYDAEDIIESFLLNEFRTKEKGIKKHARRLACFLVDRRKFASDIKGITKKISEVIGGMKSLGIQEIIDGASSMSLQERQREQKEIRQTFANSSESDLVGVEQSVEALAGHLVENDNIQVVSISGMGGIGKTTLARQVFHHDMVQRHFDGFAWVFVSQQFTQKHVWQRIWQELQPQNGDISHMDEHILQGKLFKLLETGRYLVVLDDVWKEEDWDRIKAVFPRKRGWKMLLTSRNEGVGIHADPKSFGFKTRI... | null | null | defense response [GO:0006952]; defense response to other organism [GO:0098542]; response to fungus [GO:0009620]; response to molecule of fungal origin [GO:0002238] | null | ADP binding [GO:0043531]; ATP binding [GO:0005524] | PF00931;PF18052; | 1.20.5.4130;1.10.8.430;3.40.50.300;3.80.10.10;1.10.10.10; | Disease resistance NB-LRR family, RPP8/HRT subfamily | null | null | null | null | null | null | null | FUNCTION: Confers susceptibility to the fungus Cochliobolus victoriae by conditioning victorin-dependent (victorin is a toxin synthesized by C.victoriae) induction of defense-associated proteins. {ECO:0000269|PubMed:17804803, ECO:0000269|PubMed:18052878}. | Arabidopsis thaliana (Mouse-ear cress) |
A7XUJ6 | TRAF6_PIG | MSLLHCENSCGSSQSESDCCAAMAASSCGAAAKDDGVSGTASTGNLSSSFMEEIQGYDVEFDPPLESKYECPICLMALREAVQTPCGHRFCKACIIKSIRDAGHKCPVDNEILLENQLFPDNFAKREILSLTVKCPNVGCLHKMELRHLEDHQAHCEFALMNCPQCQRPFQKCQLNIHILKECPRRQVSCVNCAVSMAFEDKEIHDQNCPLANVICEYCNTVLIREQMPNHYDLDCPTAPVPCTFSTFGCHEKMQRNHLARHLQENTQSHMRMMAQALQGLSLAVAPVPQRDMLPYDSSPLSRISSGCCSDQNFQETIQQ... | 2.3.2.27 | null | DNA damage response [GO:0006974]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of NF-kappaB transcription factor activity [... | cell cortex [GO:0005938]; cytoplasm [GO:0005737]; lipid droplet [GO:0005811]; nucleus [GO:0005634] | tumor necrosis factor receptor binding [GO:0005164]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF21355;PF18048;PF13923;PF02176; | 3.30.40.10; | TNF receptor-associated factor family, A subfamily | PTM: Sumoylated on Lys-125, Lys-143 and Lys-472 with SUMO1. {ECO:0000250|UniProtKB:Q9Y4K3}.; PTM: Polyubiquitinated on Lys-125 by TRAF3IP2; after cell stimulation with IL17A (By similarity). Polyubiquitinated; after cell stimulation with IL1B or TGFB. This ligand-induced cell stimulation leads to dimerization/oligomeri... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4K3}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9Y4K3}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K3}. Lipid droplet {ECO:0000250|UniProtKB:P70196}. Note=RSAD2/viperin recruits it to the lipid droplet. {ECO:0000250|UniProtKB:P70196}. | 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; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as ECSIT, IKBKG, IRAK1, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation. Leads to the activat... | Sus scrofa (Pig) |
A7XY94 | NMDE2_XENLA | MRPTEACCYLKISLIILFYMGCYAQKHPNMDIAVILVGTTEEVAIKDVHEKDDFHHLPVTPRVALVTMNESDPKSIITRICDLMSDKKVQGVVFGDDTDQEAIAQILDFISVQTLTPILGIHGGSSMIMADKEEASMFFQFGPSIEQQASVMLNIMEEYDWYIFSIVTTYFPGYQDFENKVRSTIENSFVGWELEEVIHLDMSLDDIDSKIQNQLKKLQSPVILLYCTKEEATYIFEVAHSVGLTGYGFTWIVPSLVAGDTDTVPDEFPTGLISVSYDEWDYDLPARVRDGIAIITTAASTMLSEHNSIPQSKSSCNNIQ... | null | null | excitatory postsynaptic potential [GO:0060079]; long-term synaptic potentiation [GO:0060291]; response to magnesium ion [GO:0032026]; response to zinc ion [GO:0010043] | late endosome [GO:0005770]; lysosome [GO:0005764]; NMDA selective glutamate receptor complex [GO:0017146]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211] | metal ion binding [GO:0046872]; NMDA glutamate receptor activity [GO:0004972] | PF01094;PF00060;PF10613;PF10565;PF00497; | 3.40.50.2300;3.40.190.10; | Glutamate-gated ion channel (TC 1.A.10.1) family, NR2B/GRIN2B subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18177891, ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:28232581}; Multi-pass membrane protein {ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:28232581}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q00960}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, pl... | Xenopus laevis (African clawed frog) |
A7XYQ1 | SOBP_HUMAN | MAEMEKEGRPPENKRSRKPAHPVKREINEEMKNFAENTMNELLGWYGYDKVELKDGEDIEFRSYPTDGESRQHISVLKENSLPKPKLPEDSVISPYNISTGYSGLATGNGLSDSPAGSKDHGSVPIIVPLIPPPFIKPPAEDDVSNVQIMCAWCQKVGIKRYSLSMGSEVKSFCSEKCFAACRRAYFKRNKARDEDGHAENFPQQHYAKETPRLAFKNNCELLVCDWCKHIRHTKEYLDFGDGERRLQFCSAKCLNQYKMDIFYKETQANLPAGLCSTLHPPMENKAEGTGVQLLTPDSWNIPLTDARRKAPSPVATAGQ... | null | null | animal organ development [GO:0048513]; cochlea development [GO:0090102]; cognition [GO:0050890]; inner ear morphogenesis [GO:0042472]; locomotory behavior [GO:0007626]; sensory perception of sound [GO:0007605] | nucleus [GO:0005634] | metal ion binding [GO:0046872]; SUMO polymer binding [GO:0032184] | PF15279; | null | SOBP family | null | null | null | null | null | null | null | FUNCTION: Implicated in development of the cochlea. {ECO:0000250|UniProtKB:Q0P5V2}. | Homo sapiens (Human) |
A7YE96 | IT70A_DANRE | MPPMTIKDGEYTATVYKMIKEGRYGDAIHILSKEHQKHTKSRAALSLLGYCYYHMQDFTNAAECYEQLTQLHPEVEDYKLYYAQSLYGACAFPEAMKSTFLLDNTTSHTKMIKLQAAIKYGEEDYSGAKTLVEQLPQEDPDYDVDLGCLLYKEGEFEEACKKFMSSMNVLGYQPDLAYNIALCYYSLKQYASALKYIAEIIERGIREHPELSIGMTTEGIDVRSVGNTLILHETALIEAFNLKAAIEYQLKNYAAAQEALTDMPPRSEEELDPVTLHNQALMNMDTKPTEGFEKLAFLLQQNPFPPVTFGNLLLLYCKYE... | null | null | cilium assembly [GO:0060271]; determination of left/right symmetry [GO:0007368]; establishment of planar polarity [GO:0001736]; intraciliary transport [GO:0042073]; opsin transport [GO:0036372]; protein polyglutamylation [GO:0018095] | axonemal microtubule [GO:0005879]; cilium [GO:0005929]; intraciliary transport particle B [GO:0030992]; motile cilium [GO:0031514] | intraciliary transport particle B binding [GO:0120170]; tubulin-glycine ligase activity [GO:0070738] | PF07719;PF13174; | 1.25.40.10; | TTC30/dfy-1/fleer family | null | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:17761526}. | null | null | null | null | null | FUNCTION: Plays a role in anterograde intraflagellar transport (IFT), the process by which cilia precursors are transported from the base of the cilium to the site of their incorporation at the tip (By similarity). Required for polyglutamylation of axonemal tubulin, which is a prerequisite for correct assembly of cilia... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A7YW45 | ANM5_BOVIN | MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFTQEPAKSRPGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTSHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLE... | 2.1.1.320 | null | circadian regulation of gene expression [GO:0032922]; DNA-templated transcription termination [GO:0006353]; endothelial cell activation [GO:0042118]; Golgi ribbon formation [GO:0090161]; peptidyl-arginine methylation [GO:0018216]; regulation of DNA-templated transcription [GO:0006355]; spliceosomal snRNP assembly [GO:0... | cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; methylosome [GO:0034709]; nucleus [GO:0005634] | E-box binding [GO:0070888]; histone arginine N-methyltransferase activity [GO:0008469]; histone H4R3 methyltransferase activity [GO:0044020]; methyl-CpG binding [GO:0008327]; protein-arginine N-methyltransferase activity [GO:0016274]; protein-arginine omega-N symmetric methyltransferase activity [GO:0035243]; transcrip... | PF05185;PF17286;PF17285; | 3.20.20.150;2.70.160.11;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Protein arginine N-methyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14744}. Nucleus {ECO:0000250|UniProtKB:O14744}. Golgi apparatus {ECO:0000250|UniProtKB:O14744}. Note=Localizes to promoter regions of target genes on chromosomes (By similarity). Localizes to methylated chromatin (By similarity). {ECO:0000250|UniProtKB:O14744}. | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48108, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI... | null | null | null | null | FUNCTION: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD... | Bos taurus (Bovine) |
A7YY44 | PAR1_BOVIN | MGPRWLLLWAAGLGLCSPLVSARTRGPRPGTDPTNGTLGPRSFFLRNSNDGYEQIPLPEDEDSSEGEFTEDRLSSGNRSSPPQKSPPGFISKSASGYLTSAWLTVFIPSVYTGVFLVSLPLNIMAVVVFVLKMKVKKPAVVYMLHLAAADVLFVCVLPFKISYYFSGSDWRFGSAMCRFVTAAFYGNMYASIMLMTAISVDRFLAVVYPIQSLSWRTLGRASFICLAIWAMAIAGVAPLLLQEQATQVPGLNITACHDVLNQTLLEGYYSYYFSAFSAVFFFVPLTLSTVSYVSIIRCLSSSTVANQNKKSRALLLSAAV... | null | null | activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; connective tissue replacement involved in inflammatory response wound healing [GO:0002248]; establishment of synaptic specificity at neuromuscular junction [GO:0007529]; G protein-coupled receptor signaling pathway [GO:000718... | caveola [GO:0005901]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; platelet dense tubular network [GO:0031094]; postsynaptic membrane [GO:0045211] | G protein-coupled receptor activity [GO:0004930]; G-protein alpha-subunit binding [GO:0001965]; G-protein beta-subunit binding [GO:0031681]; thrombin-activated receptor activity [GO:0015057] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | PTM: Proteolytic cleavage by thrombin generates a new N-terminus that functions as a tethered ligand. Also proteolytically cleaved by cathepsin CTSG. {ECO:0000250|UniProtKB:P25116}.; PTM: Phosphorylated in the C-terminal tail; probably mediating desensitization prior to the uncoupling and internalization of the recepto... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P26824}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P26824}. | null | null | null | null | null | FUNCTION: High affinity receptor that binds the activated thrombin, leading to calcium release from intracellular stores. The thrombin-activated receptor signaling pathway is mediated through PTX-insensitive G proteins, activation of phospholipase C resulting in the production of 1D-myo-inositol 1,4,5-trisphosphate (In... | Bos taurus (Bovine) |
A7Z019 | SMCA4_BOVIN | MSTPDPALGGTPRPGPSPGPGPSPGAMLGPSPGPSPGSAHSIMGPSPGPPSAGHPIPTQGPGGYPQDNMHQMHKPMESMHEKGMSDDPRYTQMKGMGMRSGGHAGMGPPPSPMDQHSQGYPSPLGGSEHASSPVPASGPSSGPQMSSGPGGAPLDGADPQALGQQNRGPTPFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQGKRPMPGMQPQMPALPPPSVSATGPGPSPGPAPPNYSRPHGMGGPNMPPPGPSGVPPGMPGQPPGGPPKPWPEGPMANAAAPTSTPQKLIPPQPTGRPSPAPPAVPPAASPVMPP... | 3.6.4.- | null | nervous system development [GO:0007399]; positive regulation of transcription by RNA polymerase II [GO:0045944] | nBAF complex [GO:0071565]; npBAF complex [GO:0071564]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; hydrolase activity [GO:0016787]; RNA binding [GO:0003723] | PF07533;PF00439;PF00271;PF07529;PF08880;PF14619;PF00176; | 1.20.5.170;3.40.5.120;1.20.920.10;3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3TKT4}. Note=Colocalizes with long non-coding RNA Evf2 in nuclear RNA clouds (By similarity). Localizes to sites of DNA damage (By similarity). {ECO:0000250|UniProtKB:P51532, ECO:0000250|UniProtKB:Q3TKT4}. | null | null | null | null | null | FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome ... | Bos taurus (Bovine) |
A7Z056 | UBP20_BOVIN | MGDSRDLCPHLDSIGEVTKEDLLLKSKSTCQSCGVSGPNLWACLQVSCSYVGCGESFADHSTLHAQAKKHNLTVNLTTFRVWCYACEKEVFLEPRLAAHPPGPAPKFSEQDSPPPSHPLKAVPIAVADEGESESEDDDLKPRGLTGMKNLGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLVSEVWHRKRPSYVVPTSLSHGIKLVNPMFRGYAQQDTQEFLRCLMDQLHEELKEPVVATAAALTEARDSDSSDTDEKREGDRSPSEDEFLSCDSSSDRGEGDGQGRSGGGSQAEAELLMADEAGR... | 3.4.19.12 | null | endocytosis [GO:0006897]; protein deubiquitination [GO:0016579]; protein K48-linked deubiquitination [GO:0071108]; protein K63-linked deubiquitination [GO:0070536]; proteolysis [GO:0006508]; regulation of G protein-coupled receptor signaling pathway [GO:0008277] | centrosome [GO:0005813]; endoplasmic reticulum [GO:0005783]; perinuclear region of cytoplasm [GO:0048471] | cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; zinc ion binding [GO:0008270] | PF06337;PF00443;PF02148; | 3.90.70.10;3.30.2230.10;3.30.40.10; | Peptidase C19 family, USP20/USP33 subfamily | PTM: Ubiquitinated via a VHL-dependent pathway for proteasomal degradation. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8C6M1}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y2K6}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Y2K6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y2K6}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q9Y2K6}; | null | null | null | null | FUNCTION: Deubiquitinating enzyme that plays a role in many cellular processes including autophagy, cellular antiviral response or membrane protein biogenesis. Attenuates TLR4-mediated NF-kappa-B signaling by cooperating with beta-arrestin-2/ARRB2 and inhibiting TRAF6 autoubiquitination. Promotes cellular antiviral res... | Bos taurus (Bovine) |
A7Z063 | WASH1_BOVIN | MTPTGTQHSLAGQTYAVPLIQPDLRREEAIQQVADALQYLQKVSGDIFSRISQRVELSRSQLQAIGERVSLAQAKIEKIKGSKKAIKVFSSAKYPAPERLQEYGSIFMGAQDPGLQRRPRHRIQSKHRPLDERALQEKLKFFPVCVNTKPEPEDEAEEGLGGLPSNISSVSSLLLFNTTENLYKKYVFLDPLAGAVTKTHVMLGAETEEKLFDAPLSISRREQLERQVPENYFYVPDLGQVPDIDVPSYLPDLPGVADDLMYSADLGPGIAPSAPGAIPELPTFHTEVAQPFKPDLEDGVLTARPPPPPPPPPPPAPAVL... | null | null | Arp2/3 complex-mediated actin nucleation [GO:0034314]; endocytic recycling [GO:0032456]; endosomal transport [GO:0016197]; exocytosis [GO:0006887]; protein transport [GO:0015031]; retrograde transport, endosome to Golgi [GO:0042147] | autophagosome [GO:0005776]; centriole [GO:0005814]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; late endosome [GO:0005770]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; WASH complex [GO:0071203] | actin binding [GO:0003779]; alpha-tubulin binding [GO:0043014]; gamma-tubulin binding [GO:0043015] | PF11945; | null | WASH1 family | null | SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250|UniProtKB:A8K0Z3}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q8VDD8}. Late endosome {ECO:0000250|UniProtKB:A8K0Z3}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q8VDD8}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, c... | null | null | null | null | null | FUNCTION: Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome ... | Bos taurus (Bovine) |
A7Z064 | HMDH_BOVIN | MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKLEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTGLNEALPFFLLLVDLSRASALAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTADNSKVSLGLDENVSKRIEPSVSLWQFYLSKMISMDI... | 1.1.1.34 | null | cholesterol biosynthetic process [GO:0006695]; coenzyme A metabolic process [GO:0015936]; ergosterol biosynthetic process [GO:0006696]; isoprenoid biosynthetic process [GO:0008299]; sterol biosynthetic process [GO:0016126] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; peroxisomal membrane [GO:0005778] | hydroxymethylglutaryl-CoA reductase (NADPH) activity [GO:0004420]; NADP binding [GO:0050661] | PF00368;PF12349; | 1.10.3270.10;3.30.70.420; | HMG-CoA reductase family | PTM: Undergoes sterol-mediated ubiquitination and ER-associated degradation (ERAD). Accumulation of sterols in the endoplasmic reticulum (ER) membrane, triggers binding of the reductase to the ER membrane protein INSIG1 or INSIG2. The INSIG1 binding leads to the recruitment of the ubiquitin ligase, AMFR/gp78, RNF139 or... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P04035}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00347}. Peroxisome membrane {ECO:0000250|UniProtKB:P04035}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00347}. | CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34; Evidence={ECO:0000250|UniProtKB:P04035}; Physiologica... | null | PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. | null | null | FUNCTION: Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis. {ECO:0000250|UniProtKB:P04035}. | Bos taurus (Bovine) |
A7ZN88 | HCHA_ECO24 | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDIAGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Escherichia coli O139:H28 (strain E24377A / ETEC) |
A8A1G6 | HCHA_ECOHS | MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Escherichia coli O9:H4 (strain HS) |
A8ACZ4 | FADB_CITK8 | MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGQALDVLEKQTDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTLSAINGYALGGGCECVLATDYRLVTPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDIGAEQALKIGLVDGVVKPEKLLDGAIAVLRQAIDGSLDWKAKRQPKLEPLKLSKIEAAMSFTIAKGMVAQTAGKHYPAPMIAVKTIEAAARFGREEALNLENKSFVPLAHTNEARALVGIFLNDQFVKGKAKKLTKDVETPKQAAVLG... | 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}. | Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) |
A8AWU7 | HSA_STRGC | MFFKRQKGQYHEVERVTRFKLIKSGKHWLRAATSQFGLLRLMKGADISSVEVKVAEEQSVEKGGLNYLKGIIATGAVLGGAVVTSSSVYAEEEQALEKVIDTRDVLATRGEAVLSEEAATTLSSEGANPVESLSDTLSASESASANSVSTSISISESFSVSASASLSSSSSLSQSSSESASASESLSVSASTSQSFSSTTSSTQSSNNESLISSDSSNSLNTNQSVSARNQNARVRTRRAVAANDTEAPQVKSGDYVVYRGESFEYYAEITDNSGQVNRVVIRNVEGGANSTYLSPNWVKYSTENLGRPGNATVQNPLRT... | null | null | biofilm matrix assembly [GO:0098785]; cell adhesion [GO:0007155]; surface biofilm formation [GO:0090604] | extracellular region [GO:0005576] | null | PF18938;PF00746;PF20164;PF19258; | 2.60.40.4140;3.10.20.890; | Serine-rich repeat protein (SRRP) family | PTM: The protein is glycosylated in vivo; constructs without SR1 and SR2 are not glycosylated. {ECO:0000269|PubMed:15213130, ECO:0000269|PubMed:27616700}. | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000269|PubMed:15213130, ECO:0000269|PubMed:19884334}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. | null | null | null | null | null | FUNCTION: A cell wall protein involved with PadA in host cell interactions required for colonization and pathogensis (Probable) (PubMed:19884334, PubMed:27616700). Mediates hemagglutination and adherence to ghst glycoproteins (PubMed:11854202). Recognizes fetuin-A (AHSG), a highly glycosylated human plasma protein, als... | Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288) |
A8AZP4 | PADA_STRGC | MKDFLKKVLILFTVLLMSMPSSVLNLGTSVVRADDPLNIETRRIDEHTTITQNGCYRKIEKTDATDWTVPRKPIDLVILQDASGSFRTTIPSVKNALKRLTTYVSPEQYDENDPHLVKTDDPRTTDRVFVASYQGLDQVRYFENNDFSGNPANVYTDANSTGKNYTYGNSGLTSDQNKVHNFIDNIAVDGGTPTVPAIDDTIAQYNRVKGNMENGRKTVFLLVTDGVANGYRLPGTNTVVMDKSWTRTDAIQKAWRVDSYPEAAQDIIGRANELKAAGNQLKAAVGSEGSVVVGFWERVDNFTEKYYQYGPAYLNGFGNT... | null | null | biofilm matrix assembly [GO:0098785]; cell adhesion [GO:0007155]; surface biofilm formation [GO:0090604] | extracellular region [GO:0005576] | null | null | 2.60.40.740;3.40.50.410; | null | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000269|PubMed:19884334, ECO:0000269|PubMed:27616700}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. | null | null | null | null | null | FUNCTION: A cell wall protein involved with Hsa in host cell interactions required for colonization and pathogenesis (PubMed:19884334, PubMed:21071690, PubMed:24136582, PubMed:27616700). Involved in recognition of platelets. Interacts with human platelet integrin receptor GPIIbIIIa (a complex of ITGA2B and ITGB3) (PubM... | Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288) |
A8B296 | IFT81_GIAIC | MQPPTSTDQLQTITDGLNLPPFERRMTLITLSEILHDPVRAMQLLADVAYQVRPHSLAEDSKAVPPPVKVNAANLEQVAAGITDFTVCLLNLNESRSMADKQAFVQELVLSDSANMRVLLSAILKDLAASRETIYVSKFKLPPVIPADYMVDPQIQTLLSQLREAQSRFTEALNQNRDVQKDQILQKMERLATDKTTFLTRRDKLFDRVKQAKALSVPKEAVRLASRRRVALSEIEELKTQINSQNEIRRAALNAAKAVVNSARGTPANILEASEAENKRLKQEIINLTAEITEKESLAHLIQSEPGQEAIELMENELET... | null | null | intraciliary anterograde transport [GO:0035720]; intraciliary transport [GO:0042073]; intraciliary transport involved in cilium assembly [GO:0035735] | 9+2 motile cilium [GO:0097729]; axoneme [GO:0005930]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; ciliary pocket collar [GO:1990900]; ciliary tip [GO:0097542]; cilium [GO:0005929]; intraciliary transport particle B [GO:0030992] | tubulin binding [GO:0015631] | PF18383; | 1.10.418.70; | IFT81 family | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:18463165, ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:18463165, ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:31855176}. Note=Localizes to the c... | null | null | null | null | null | FUNCTION: Component of the intraflagellar transport complex B (IFT-B) involved in flagellar assembly (Probable). {ECO:0000305|PubMed:31855176}. | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
A8B2U2 | ALF_GIAIC | MPLCTLRQMLGEARKHKYGVGAFNVNNMEQIQGIMKAVVQLKSPVILQCSRGALKYSDMIYLKKLCEAALEKHPDIPICIHLDHGDTLESVKMAIDLGFSSVMIDASHHPFDENVRITKEVVAYAHARGVSVEAELGTLGGIEEDVQNTVQLTEPQDAKKFVELTGVDALAVAIGTSHGAYKFKSESDIRLAIDRVKTISDLTGIPLVMHGSSSVPKDVKDMINKYGGKMPDAVGVPIESIVHAIGEGVCKINVDSDSRMAMTGAIRKVFVEHPEKFDPRDYLGPGRDAITEMLIPKIKAFGSAGHAGDYKVVSLEEAKA... | 4.1.2.13 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:17166851}; Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000269|PubMed:17166851, ECO:0000269|PubMed:19236002, ECO:0000269|PubMed:21333622}; | fructose 1,6-bisphosphate metabolic process [GO:0030388]; glycolytic process [GO:0006096] | cytosol [GO:0005829] | fructose-bisphosphate aldolase activity [GO:0004332]; tagatose-bisphosphate aldolase activity [GO:0009025]; zinc ion binding [GO:0008270] | PF01116; | 3.20.20.70; | Class II fructose-bisphosphate aldolase family | null | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000269|PubMed:17166851, ECO:0000269|PubMed:19236002, ECO:0000269|PubMed:21333622, ECO:0000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.7 uM for fructose 1,6-bisphosphate (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:17166851}; KM=1.8 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:31409864}; Note=kcat is 3.55 sec(-1) with fructose 1,6-bisphosphate as substrate (at pH 7.5 and 25 deg... | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. {ECO:0000305|PubMed:17166851}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:17166851}; | null | FUNCTION: Plays a key role in glycolysis by catalyzing the cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate (PubMed:17166851). Does not cleave D-tagatose-1,6-bisphosphate (PubMed:17166851, PubMed:19236002). {ECO:0000269|PubMed:17166851, ECO:0000269|PubMed:19236002}. | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
A8BB91 | KIN2B_GIAIC | MSKSKGKGSSDNVMVMVRVRPFNKREEQEGATEIIEMDKTLCTVTLHKPVEKGAGSATSECLPSKKVFTYDAVYPSNSTQVEVFDESVREMIDGCLEGYNATVFAYGQTGSGKTHTMMGQKDNPGMIPLAFQRIFDFIAQAKDDQFLVRASFVEIYNEDLKDLLTGATHLQLKEDPVKGVFIKDLSEHPVSDERHIDKLIQKGNESRAVAATLMNATSSRSHSIFQVVLERMTVIDGRECIRVGKLNLVDLAGSERQEKTGATGDRLKEAAKINLSLTTLGCVISKLVEGSKHIPYRDSKLTRLLQDSLGGNSKTLMVVA... | null | null | cytoskeleton-dependent intracellular transport [GO:0030705]; intraciliary anterograde transport [GO:0035720]; intraciliary transport involved in cilium assembly [GO:0035735]; microtubule-based movement [GO:0007018]; mitotic spindle organization [GO:0007052]; spindle elongation [GO:0051231]; transport along microtubule ... | 9+2 motile cilium [GO:0097729]; axoneme [GO:0005930]; ciliary basal body [GO:0036064]; ciliary pocket collar [GO:1990900]; ciliary tip [GO:0097542]; kinesin complex [GO:0005871]; microtubule [GO:0005874] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; magnesium ion binding [GO:0000287]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; plus-end-directed microtubule motor activity [GO:0008574] | PF00225; | 3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Kinesin II subfamily | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:18463165, ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:18463165, ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:31855176}. Note=Localizes to the c... | null | null | null | null | null | FUNCTION: Involved in anterograde intraflagellar transport (IFT) (Probable). Involved in flagellar assembly (Probable). {ECO:0000305|PubMed:19377039, ECO:0000305|PubMed:31855176}. | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
A8BKD1 | KIN2A_GIAIC | MSSDNIKVIVRCRPLNARETRENALNIIRMDEASAQVIVDPPEQEKSATQAKKVPRTFTFDAVYDQTSCNYGIFQASFKPLIDAVLEGFNSTIFAYGQTGAGKTWTMGGNKEEPGAIPNSFKHLFDAINSSSSNQNFLVIGSYLELYNEEIRDLIKNNTKLPLKEDKTRGIYVDGLSMHRVTTAAELSALMDKGFANRHVAATQMNDTSSRSHSIFMVRIECSEVIENKEVIRVGKLNLVDLAGSERQSKTGATGETLVEGAKINLSLSALGLVISKLVEGATHIPYRDSKLTRLLQDSLGGNSKTLMCANISPASTNYD... | null | null | cilium assembly [GO:0060271]; intraciliary anterograde transport [GO:0035720]; intraciliary transport [GO:0042073]; intraciliary transport involved in cilium assembly [GO:0035735]; microtubule-based movement [GO:0007018]; mitotic spindle organization [GO:0007052]; spindle elongation [GO:0051231] | 9+2 motile cilium [GO:0097729]; axoneme [GO:0005930]; ciliary basal body [GO:0036064]; ciliary pocket collar [GO:1990900]; ciliary tip [GO:0097542]; kinesin complex [GO:0005871]; microtubule [GO:0005874] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; magnesium ion binding [GO:0000287]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; plus-end-directed microtubule motor activity [GO:0008574] | PF00225; | 3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Kinesin II subfamily | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:18463165, ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:18463165, ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:31855176}. Note=Localizes to the c... | null | null | null | null | null | FUNCTION: Involved in anterograde intraflagellar transport (IFT) (Probable). Involved in flagellar assembly (PubMed:18463165). {ECO:0000269|PubMed:18463165, ECO:0000305|PubMed:31855176}. | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
A8BPK8 | PLK_GIAIC | MSHSNAPELHPQIVDPFHNVTYRPGKLLGKGGFAYVYEFHDVNSDSSYACKITPRSALQKKKYYDKFVTEVTIHRGLVHPNICRVLNVFKDQMNYYIILEKCNGGTLTDLIRRRKHLTETEARFFSKRILNALWYLHDLYIIHRDIKTSNIFLMEDFDVKVGDFGLAVKCETPEELHWTMCGTPNFLPSEVIYSHIMKRKASGRGPDPNLDEDCVNLCHQLLPAYSGQGHSFSADMWSFGCLVFSMIYGRPPFEAADIKTTYKRIVRCDFSFPGSISVSEDLKNFIKGLLTPDPRKRFTVKECLDHSWLNPSKYFIPESL... | 2.7.11.21 | null | cell division [GO:0051301]; mitotic spindle organization [GO:0007052]; negative regulation of cilium assembly [GO:1902018]; phosphorylation [GO:0016310] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; membrane [GO:0016020]; motile cilium [GO:0031514]; nucleus [GO:0005634]; spindle pole [GO:0000922] | ATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674] | PF00069;PF00659; | 3.30.1120.30;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily | PTM: Autophosphorylated (PubMed:33789729, PubMed:35772734). Autophosphorylation is critical for its function in cell growth, cytokinesis and formation of flagella (PubMed:33789729). {ECO:0000269|PubMed:33789729, ECO:0000269|PubMed:35772734}. | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:33789729, ECO:0000269|PubMed:35772734}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:33789729, ECO:0000269|PubMed:35772734}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:33789729, ECO:0000269|PubMed:35772... | 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=2.7.11.21; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Involved in cell cycle (PubMed:33789729, PubMed:35772734). Involved in cell division (PubMed:33789729). Involved in cytokinesis (PubMed:33789729). Involved in flagella biogenesis and in regulation of flagella length in interphase (PubMed:33789729, PubMed:35772734). Involved in formation of median bodies durin... | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
A8C927 | NPMA_ECOLX | MLILKGTKTVDLSKDELTEIIGQFDRVHIDLGTGDGRNIYKLAINDQNTFYIGIDPVKENLFDISKKIIKKPSKGGLSNVVFVIAAAESLPFELKNIADSISILFPWGTLLEYVIKPNRDILSNVADLAKKEAHFEFVTTYSDSYEEAEIKKRGLPLLSKAYFLSEQYKAELSNSGFRIDDVKELDNEYVKQFNSLWAKRLAFGRKRSFFRVSGHVSKH | 2.1.1.180 | null | methylation [GO:0032259]; response to antibiotic [GO:0046677] | null | methyltransferase activity [GO:0008168] | null | 3.40.50.150; | Methyltransferase superfamily, Kanamycin-apramycin resistance family | null | null | CATALYTIC ACTIVITY: Reaction=adenosine(1408) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(1408) in 16S rRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42776, Rhea:RHEA-COMP:10227, Rhea:RHEA-COMP:10228, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74491;... | null | null | null | null | FUNCTION: Specifically methylates the N(1) position of adenine 1408 in 16S rRNA. Confers resistance to various aminoglycosides, including kanamycin, neomycin, apramycin, ribostamycin and gentamicin. Methylates only fully assembled 30S subunits. {ECO:0000269|PubMed:17875999, ECO:0000269|PubMed:20667473, ECO:0000269|PubM... | Escherichia coli |
A8C984 | MYLK3_DANRE | MGTSLYRSTLLSTGGFSVSDYIRKFTKNKPDVNNIQPNVGFCHQSTQTSQQVKEVISAELELQQPEVTLPNDPSSQHSPEAHTGASEPLKPVSAGESSKALQKAKEISVKSSEPTHVQTFAPAVHLEQIDVHNVPKQETNSLVAAPADAKCVIETMTKVEKDIALQQERALERADDSHVANKVFLKSIIPGQQLEKIEDPQQQAEVSLFVDEDSLEKSVPGQHLDKKMEVLQKQAKDLPVVDEDSLNLSAPGQRQLEEKVDVPEKAEKKIDEAHKKMEEVPRKDELCIEKPVIRHAGIKTQHEETMGMETTVPKHDESKC... | 2.7.11.18 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | heart morphogenesis [GO:0003007]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of apoptotic process [GO:0043065]; sarcomerogenesis [GO:0048769]; ventricular cardiac myofibril assembly [GO:0055005] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; myosin light chain kinase activity [GO:0004687] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | PTM: Phosphorylated on serine residues. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[myosin light chain] = ADP + H(+) + O-phospho-L-seryl-[myosin light chain]; Xref=Rhea:RHEA:22004, Rhea:RHEA-COMP:13684, Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.18; CATALYTIC ACTIVITY: React... | null | null | null | null | FUNCTION: Kinase that phosphorylates MYL2 in vitro (By similarity). Increases cardiomyocyte contractility (By similarity). Required for sarcomere formation in the developing heart. {ECO:0000250, ECO:0000269|PubMed:17885681}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A8CG34 | P121C_HUMAN | MSPAAAAAGAGERRRPIASVRDGRGRGCGGPAGAALLGLSLVGLLLYLVPAAAALAWLAVGTTAAWWGLSREPRGSRPLSSFVQKARHRRTLFASPPAKSTANGNLLEPRTLLEGPDPAELLLMGSYLGKPGPPQPAPAPEGQDLRNRPGRRPPARPAPRSTPPSQPTHRVHHFYPSLPTPLLRPSGRPSPRDRGTLPDRFVITPRRRYPIHQTQYSCPGVLPTVCWNGYHKKAVLSPRNSRMVCSPVTVRIAPPDRRFSRSAIPEQIISSTLSSPSSNAPDPCAKETVLSALKEKKKKRTVEEEDQIFLDGQENKRRRH... | null | null | mRNA transport [GO:0051028]; protein import into nucleus [GO:0006606]; RNA export from nucleus [GO:0006405] | endoplasmic reticulum membrane [GO:0005789]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654] | nuclear localization sequence binding [GO:0008139]; structural constituent of nuclear pore [GO:0017056] | PF15229; | null | POM121 family | null | SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000269|PubMed:17900573}. Nucleus membrane {ECO:0000269|PubMed:17900573}; Single-pass membrane protein {ECO:0000269|PubMed:17900573}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Stably associated with the NPC thr... | null | null | null | null | null | FUNCTION: Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL). {ECO:0000269|PubMed:17900573}. | Homo sapiens (Human) |
A8CG78 | PA2A2_DABSI | MRTLWIVAVCLIGVEGNLYQFGEMINQKTGNFGLLSYVYYGCYCGWGGKGKPQDATDRCCFVHDCCYGRVKGCDPKTATYSYSFENGDIVCGGDDPCLRAVCECDRVAAICFRENMNTYDKKYMLYSIFDCKEESDQC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | 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]; 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. | 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:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Exhibits high hydrolytic activities and shows strong preference for the anionic micelles (dPPC with deoxycholate) to the zwitterionic micelles (dPPC with Triton X-100). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:17611171}. | Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis) |
A8CG82 | PA2B1_DABSI | MRTLWIVAMCLIGVEGNLFQFARLIDAKQEAFSFFKYISYGCYCGWGGQGTPKDATDRCCFVHDCCYARVKGCNPKLVEYSYGYRTGKIVCENYNRCKRAVCECDRVAAICLGQNVNTYNKGYMFLSSYYCRQKSEQC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | 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]; 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 {ECO:0000269|PubMed:17611171}. | 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:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Exhibits high hydrolytic activities and shows strong preference for the anionic micelles (dPPC with deoxycholate) to the zwitterionic micelles (dPPC with Triton X-100). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:17611171}. | Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis) |
A8CG86 | PA2A1_DABRR | MRTLWIVAVCLIGVEGNLFQFAEMIVKMTGKEAVHSYAIYGCYCGWGGQGKPQDATDRCCFVHDCCYGTVNDCNPKMATYSYSFENGDIVCGDNNLCLKTVCECDRAAAICLGQNVNTYDKNYENYAISHCTEESEQC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | 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]; 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. | 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:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that exhibits high hydrolytic activities and shows strong preference for the anionic micelles (dPPC with deoxycholate) to the zwitterionic micelles (dPPC with Triton X-100). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO... | Daboia russelii (Russel's viper) (Vipera russelii) |
A8CL69 | PBAN_APIME | MIGFAVFSSFNRFTTIFVCVLLCVVYLLSYASGEYDGRDSSSGSNNDRAPSNEFGSCTDGKCIKRTSQDITSGMWFGPRLGRRRRADRKPEINSDIEAFANAFEEPHWAIVTIPETEKRQITQFTPRLGRESGEDYFSYGFPKDQEELYTEEQIYLPLFASRLGRRVPWTPSPRLGRQLHNIVDKPRQNFNDPRF | null | null | neuropeptide signaling pathway [GO:0007218] | extracellular space [GO:0005615] | myostimulatory hormone activity [GO:0016084]; neuropeptide hormone activity [GO:0005184] | null | null | Pyrokinin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17068263}. | null | null | null | null | null | FUNCTION: A hormone that controls sex pheromone production in females and pheromone responsiveness in male. Also mediates visceral muscle contractile activity (myotropic activity) (By similarity). {ECO:0000250|UniProtKB:P09971, ECO:0000269|PubMed:17068263}. | Apis mellifera (Honeybee) |
A8CVX7 | TTLL6_DANRE | MGTPAERSVSEVCRCEPDPGLEGEGWGSDTHAEPSNTPIPLPVANKKKKRKKKLWINLTNCKYESVRRAARRYGIREAAEGEDWTLYWTDCSVSLDRVMDMKRYQKINHFPGMNEICRKDLLARNMNRMLKLFPKEYNIFPRTWCLPADYSDFQAYTRAKKHKTFICKPDSGCQGRGIYLTKSSKDIRPGEHMICQVYMSKPFIIDGFKFDLRIYVLVTSCDPFRVFMYDEGLVRFCTTHYTEPTVSNLEDVCMHLTNYAINKHSENFVRDEDTGSKRKLSSFKKHMEDMSYDTEKLWTDIEDAIIKTLISAHPILKHNY... | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; | axoneme assembly [GO:0035082]; cilium movement [GO:0003341]; microtubule cytoskeleton organization [GO:0000226]; protein polyglutamylation [GO:0018095]; regulation of cilium beat frequency involved in ciliary motility [GO:0060296] | 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:0000250|UniProtKB:A4Q9E8}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A4Q9E8}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:22246503}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:22246503}. Note=CEP41 is required for its transport between the ba... | 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 both tubulin and non-tubulin proteins, generating alpha-linked polyglutamate side chains on the gamma-carboxyl group of specific glutamate residues of target proteins (By similarity). Preferentially mediates ATP-dependent long polyglutamate chain elongation over the initiation s... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A8D8P8 | SIWI_BOMMO | MSEPRGRGRARGRAGRGGDGGGPAPRRPGEQAGPSQQSMPPGPRPQPPSGWGPQSSVPPVRAGVPTPTAQAGRASHRVTPTTHEHPGDIDVQQRMQKLELGPHSSGGGDASSVVGRGSRRGGGRVLPETISILRTRPEAVTSKKGTSGTPLDLLANYFTVETTPKWGLYQYHVDISPEEDSTGVRKALMRVHSKTLGGYLFDGTVLYTVNRLHPDPMELYSDRKTDNERMRILIKLTCEVSPGDYHYIQIFNIIIRKCFNLLKLQLMGRDYFDPEAKIDIPEFKLQIWPGYKTTINQYEDRLLLVTEIAHKVLRMDTVLQ... | 3.1.26.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:27693359}; | cell differentiation [GO:0030154]; meiotic cell cycle [GO:0051321]; piRNA processing [GO:0034587]; spermatogenesis [GO:0007283] | P granule [GO:0043186]; PET complex [GO:1990923] | magnesium ion binding [GO:0000287]; piRNA binding [GO:0034584]; RNA endonuclease activity [GO:0004521] | PF02170;PF02171; | 3.40.50.2300;2.170.260.10;3.30.420.10; | Argonaute family, Piwi subfamily | PTM: Arginine methylation is required for the interaction with Tudor domain-containing protein Papi/TDRKH (PubMed:23970546, PubMed:26919431). {ECO:0000269|PubMed:23970546, ECO:0000269|PubMed:26919431}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25558067}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis (PubMed:25558067). {ECO:0000269|PubMed:25558067}. | null | null | null | null | null | FUNCTION: Endoribonuclease that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity (PubMed:19460866, PubMed:27693359). Plays an essential role in meiotic differentiation of spermatocytes, germ cell differentiat... | Bombyx mori (Silk moth) |
A8DS38 | ERVC2_TABDI | MSTLFIISILLFLASFSYAMDISTIEYKYDKSSAWRTDEEVKEIYELWLAKHDKVYSGLVEYEKRFEIFKDNLKFIDEHNSENHTYKMGLTPYTDLTNEEFQAIYLGTRSDTIHRLKRTINISERYAYEAGDNLPEQIDWRKKGAVTPVKNQGKCGSCWAFSTVSTVESINQIRTGNLISLSEQQLVDCNKKNHGCKGGAFVYAYQYIIDNGGIDTEANYPYKAVQGPCRAAKKVVRIDGYKGVPHCNENALKKAVASQPSVVAIDASSKQFQHYKSGIFSGPCGTKLNHGVVIVGYWKDYWIVRNSWGRYWGEQGYIRM... | 3.4.22.- | null | proteolysis involved in protein catabolic process [GO:0051603] | extracellular space [GO:0005615]; lysosome [GO:0005764] | cysteine-type endopeptidase activity [GO:0004197] | PF08246;PF00112; | 3.90.70.10; | Peptidase C1 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P83654}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.063 mM for N-benzoyl-Phe-Val-Arg-pNA {ECO:0000269|PubMed:18167146}; KM=0.548 mM for D-Val-Leu-Lys-pNA {ECO:0000269|PubMed:18167146}; KM=1.475 mM for D-Ile-Phe-Lys-pNA {ECO:0000269|PubMed:18167146}; KM=0.355 mM for Ala-Ala-Val-Ala-pNA {ECO:0000269|PubMed:18167146}... | null | null | null | FUNCTION: Cysteine proteinase (PubMed:18167146). Hydrolyzes denatured natural substrates such as casein, hemoglobin, azoalbumin and azocasein with a high specific activity (By similarity). Has little or no activity against synthetic substrates (By similarity). {ECO:0000250|UniProtKB:P83654, ECO:0000269|PubMed:18167146}... | Tabernaemontana divaricata (Crepe jasmine) (Ervatamia coronaria) |
A8DYE2 | TRPCG_DROME | MVVTDSPLAPHKYVRRISKDFSTVRRYSNTPAVVVGSFRASTSAFIAAESAAHLPTCSSPTTRTPVSTPRGIRRRQRMRKRSSVSSTLSKVLILNVRDLLKAHAGSEPLKEHQPRSWIETNFQKRECIKFIPCPKDDTKCCCGQAQITHQTIPGIESGSPGDLWLPTKHTRPQPTDAYGTIEFQGGAHPTKAQYVRLSFDTRPELLVQLFTKEWNLELPKLLITVQGGKANFDLQAKLKKEIRKGLLKAAKTTGAWIFTGGTNTGVTKQVGDALLLEGQQRTGRVVSIGIAPWGIVERNHELLGHNREVPCHSISSPRSK... | null | null | intracellular zinc ion homeostasis [GO:0006882]; magnesium ion homeostasis [GO:0010960]; metal ion transport [GO:0030001]; monoatomic cation transmembrane transport [GO:0098655]; protein tetramerization [GO:0051262] | cation channel complex [GO:0034703] | inorganic cation transmembrane transporter activity [GO:0022890]; intracellularly phosphatidylinositol-3,5-bisphosphate-gated monatomic cation channel activity [GO:0097682]; monoatomic cation channel activity [GO:0005261]; zinc ion transmembrane transporter activity [GO:0005385] | PF00520;PF18139;PF16519; | 1.20.5.1010; | Transient receptor (TC 1.A.4) family, LTrpC subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Calcium channel mediating constitutive calcium ion entry. {ECO:0000250}. | Drosophila melanogaster (Fruit fly) |
A8DYP0 | OBSCN_DROME | MDAVADIVFVSRDYQAQSLATDEISVSRGDLVELISSKASEKSRCFVRMFDSGDSPKEGWVPIDILEFNPTMSSSNGKESGDAEFRKLTILRELVETEEEFSRDLLHVVEKYIKGIDKPVVPRSVRDNKDIIFCNFLQIAEFHNNVLKEGLKCYSNQPNMVAKTFLRLERDFDKHVVYCQNEPLAQDYLGSSPDAKKYFQELSKQLGDDKSLAEHLKLPIQRINDYQLLFKDFIKYSLSLKENVKDLERALELMLSVPSRAYDNRFLSSIEGCRGNIYKLGRLLLHAWCNVVDKEGKAHDRYCFLFKSRILVTKVRKISE... | null | null | adult somatic muscle development [GO:0007527]; protein localization to M-band [GO:0036309]; sarcomere organization [GO:0045214] | M band [GO:0031430] | ATP binding [GO:0005524]; guanyl-nucleotide exchange factor activity [GO:0005085]; protein kinase binding [GO:0019901]; tropomyosin binding [GO:0005523] | PF00041;PF07679;PF13927;PF00069;PF00621; | 1.20.900.10;2.60.40.10;2.30.29.30;2.30.30.40;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:22467859, ECO:0000269|PubMed:26251439}. Note=In the embryo, localizes across the muscles in a striped pattern and is positioned laterally to the sites at which muscles are attached to the epidermis. In the larval body wall muscles, locali... | null | null | null | null | null | FUNCTION: Structural component of the muscle M line which is involved in assembly and organization of sarcomere (PubMed:22467859, PubMed:26251439). Required for the development and organization of indirect flight muscle sarcomeres by regulating the formation of M line and H zone and the correct assembly of thick and th... | Drosophila melanogaster (Fruit fly) |
A8DYP7 | CGLR2_DROME | MKESRNLENFVEKKLYECKKKYVDIPKDEGQRYGGKHYEALTSKIFEILRKENPELDIIIAEFSLEGSVGMLKIAKPNEFDLVFKLKFPYYKSIAVTRDPKIPGNVLLDMTRVLELLKDDPREDFQRIRELIQGRLVDAQNFFVVDRLRSWLQSLFSQALNRISYRVELVAGVVSHLKYRTCGPAHTIYVYGDYEYSVDYVPAICLAAEQNVLPTKQLECFKRANTSYWEAIPKPLKPLTETSMISFRSSFYAVEKILLQDVHENCRNAIRFMKKFRDVKTNLGNCKSYYIKTLFLWKIIQEPESYWLNPLSFILADMFD... | 2.7.7.-; 2.7.7.86 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A1ZA55}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A1ZA55}; | cellular response to virus [GO:0098586]; cGAS/STING signaling pathway [GO:0140896]; defense response to virus [GO:0051607]; immune response involved in response to exogenous dsRNA [GO:1902615]; innate immune response [GO:0045087] | cytosol [GO:0005829] | 2',3'-cyclic GMP-AMP synthase activity [GO:0061501]; 3',2'-cyclic GMP-AMP synthase activity [GO:0140700]; ATP binding [GO:0005524]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; metal ion binding [GO:0046872] | PF03281;PF20266; | 1.10.1410.40;3.30.460.90; | Mab-21 family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + GTP = 3',2'-cGAMP + 2 diphosphate; Xref=Rhea:RHEA:68344, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:177334; Evidence={ECO:0000269|PubMed:34261128}; CATALYTIC ACTIVITY: Reaction=ATP + GTP = 2',3'-cGAMP + 2 diphosphate; Xref=Rhea:RHEA:42064, ChEBI:CHEBI:30616, ... | null | null | null | null | FUNCTION: Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP from ATP and GTP and plays a key role in antiviral innate immunity (PubMed:34261128). Directly binds some unknown nucleic acid, activating the nucleotidyltransferase activity, leading to synthesis of both 3',2'-cGAMP and 2',3'-cGAMP second ... | Drosophila melanogaster (Fruit fly) |
A8DYY6 | SCHI1_DROME | MDIYITKGITNPNYPGFQKFAHTLSDDYIEYSDMECNESDLTDSDREDDPTFPSKMAKESGSETFKNGQDSILSNCDNGNTYISEEESVNRSENIPDIVNENYSATSENSKRALQKPDLIYNLSQNYTTNPEFPSWSCTINSKYEGQLQGQSPIDIVGDFGGEVEREFELLLTGYKNKKEADELKGSNLDKICDAELSNGTEALKQTSSTRLSGNSTRKNKKKNTPYGHQIVKTKHPKPSHDERQLPPDTFDYKTYSQRKYIICDADQYSSVPEKNKNDSPNLNQAEIPNMSSLEIGGSGSQQNLDEDNNKVASRKYSNQ... | null | null | negative regulation of growth [GO:0045926]; positive regulation of hippo signaling [GO:0035332]; positive regulation of protein serine/threonine kinase activity [GO:0071902] | adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; cell junction [GO:0030054]; plasma membrane [GO:0005886] | null | PF10148; | null | SCHIP1 family | null | SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:26954546}. Apical cell membrane {ECO:0000269|PubMed:26954546}; Peripheral membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (hpo), in complex with its regulato... | Drosophila melanogaster (Fruit fly) |
A8DZE6 | WTIP_DANRE | MDEYDEDPGRRASKLMETLSIYDVYQDGMYGEPNPDMEKTKRMNGSSSTPGNKVYSAAPVRSVNGNRASVPLDFCSPQREAVYPDPDVYCTKSEVALPCYSGASDRLRRYTHAEVQGHRYSTGCAYDGLVLGKQVAVSGARSNSLCMSSPDGRYTATSPRSSLASSHSSQDQSKHTSPRSSISSPRSSLVSPGQGEGTSVISPRSSYASTASDTSKHSSPRTSLNSYDCGSKPSSNRTSGISMGYDQRHISPRSSTTSPRSSYSDSRFTPAGGHDPESAAVHGIPMASPRSSICSQPAVAANCVVSPRSSISSHSSRSSR... | null | null | cilium assembly [GO:0060271]; cloaca development [GO:0035844]; cytoskeleton organization [GO:0007010]; determination of heart left/right asymmetry [GO:0061371]; determination of left/right asymmetry in lateral mesoderm [GO:0003140]; establishment of mitotic spindle orientation [GO:0000132]; heart looping [GO:0001947]; ... | adherens junction [GO:0005912]; ciliary basal body [GO:0036064]; nucleus [GO:0005634]; P-body [GO:0000932]; transcription regulator complex [GO:0005667] | metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714] | PF00412; | 2.10.110.10; | Zyxin/ajuba family | null | SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250}. Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: May monitor slit diaphragm protein assembly, a specialized adherens junction characteristic of podocytes. In case of podocyte injury, it shuttles into the nucleus and acts as a transcription regulator. Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Acts as a t... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A8DZH4 | XPR1_DANRE | MKFTEHLSAHITPEWRKQYIQYEAFKEMLYSAQDQAPSIEVTDEDTVKRYYAKFEEKFFQTCEKELAKINTFYSEKLAEAQRRFATLQNELQSSLDAQRESSRAAGLRHRRTVFHLSQQERCKHRNIKDLQLAFSEFYLSLILLQNYQNLNFTGFRKILKKHDKIFETSRGADWRVAHVEVAPFYTCKKITQLISETETLVTTELEGGDRQKAMKRLRVPPLGAAQPAPAWTTFRVGLYCGVFVALTVTVIIAGVVKLVEHFGDNTDVWPLIRIYRGGFLLIEFLFLLGINTYGWRQAGVNHVLIFELNPRNNLSHQHLF... | null | null | cellular response to phosphate starvation [GO:0016036]; intracellular phosphate ion homeostasis [GO:0030643]; macrophage differentiation [GO:0030225]; microglia differentiation [GO:0014004]; phosphate ion transmembrane transport [GO:0035435]; phosphate ion transport [GO:0006817]; skeletal system development [GO:0001501... | cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886] | efflux transmembrane transporter activity [GO:0015562]; inositol hexakisphosphate binding [GO:0000822]; phosphate ion transmembrane transporter activity [GO:0015114] | PF03124;PF03105; | null | SYG1 (TC 2.A.94) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:23791524}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Plays a role in phosphate homeostasis. Mediates phosphate export from the cell (PubMed:23791524). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important intracellular signaling molecules (By similarity). {ECO:0... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A8E2V8 | PA2A_TRIGS | MRTLWIMAVLLLGVEGSLMQFEMLIMKLAKSSGMFWYSAYGCYCGWGGQGRPQDATDRCCFVHDCCYGKATGCDPKKDVYTYSEENGDIVCGGDDPCRKEVCECDKAAAICFRDNMDTYNSKTYWMFPAKNCQEESEPC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; envenomation resulting in negative regulation of platelet aggregation in another organism [GO:0044477]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576]; host extracellular space [GO:0043655] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 activity [GO:0004623]; 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. | 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:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits the ADP-(IC(50)=272 nM) and collagen-induced (IC(50)=518 nM) human platelet aggregation in platelet rich plasma. Exhibits very high hydrolytic activities toward the synthetic lecithin, and prefers the anionic micelles (dPPC with deoxycholate) to the zwitterion... | Trimeresurus gracilis (Kikuchi habu) |
A8E5T6 | TCF21_XENTR | MSTGSLSDVEDFQEVEMLECDGIKLDPNKEFGISNDSNEESSTCDNGSPKKGRGTSGKRRKAPSKKSPLGNINQEGKQVQRNAANARERARMRVLSKAFSRLKTTLPWVPPDTKLSKLDTLRLASSYIAHLRQILANDKYENGYIHPVNLTWPFMVAGKPENDLKEVVSTSRLCGPTAS | null | null | branching involved in ureteric bud morphogenesis [GO:0001658]; branchiomeric skeletal muscle development [GO:0014707]; bronchiole development [GO:0060435]; diaphragm development [GO:0060539]; embryonic digestive tract morphogenesis [GO:0048557]; epithelial cell differentiation [GO:0030855]; gland development [GO:004873... | nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983] | PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43680, ECO:0000255|PROSITE-ProRule:PRU00981}. | null | null | null | null | null | FUNCTION: Involved in epithelial-mesenchymal interactions in kidney and lung morphogenesis that include epithelial differentiation and branching morphogenesis. {ECO:0000250|UniProtKB:O43680}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A8E5V9 | STING_XENTR | MACVLAIGSILFVWILGKGKYSGAQLIYRMATNFAISQGCCLVTCACELTEEIKHLHTRYNGHYWRALKASFNLSCAAFVTAILCYVFYEPKLMASLPLTIDITLTLLSWLFCWILGIQGPTPATISEITEIKQLNVAHGLAWSYYVGYLQFVLPALKESIQKFNEENHNLLKFPETCRLHILIPLSCRLYGDLKDVDENITFLKEIPPLYIDRAGIKGRVFKNNVYRILDEDGRPYNCIVEYATPLASLLKMTDIPSAAFSADDRLQQTKLFYRTLKDILENAHELQNTYRLIVYEDFPETKDHSRHLLSQEILKHIRQ... | null | null | activation of innate immune response [GO:0002218]; autophagosome assembly [GO:0000045]; cGAS/STING signaling pathway [GO:0140896]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of macroautophagy [GO:001623... | autophagosome membrane [GO:0000421]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi membrane [GO:0000139]; perinuclear region of cytoplasm [GO:0048471] | 2',3'-cyclic GMP-AMP binding [GO:0061507]; cyclic-di-GMP binding [GO:0035438]; protein homodimerization activity [GO:0042803]; proton channel activity [GO:0015252] | PF15009; | 1.20.5.5200;3.40.50.12100; | STING family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30842662}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000... | CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q86WV6}; | null | null | null | null | FUNCTION: Sensor of cytosolic DNA from bacteria and viruses that promotes autophagy (PubMed:26300263, PubMed:30842662). Acts by recognizing and binding cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA in the cytosol (PubMed:26300263, PubMed:30842662). Exhibits guanine base-specific ligand recogni... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A8FNH9 | NSPC_CAMJ8 | MFYEKIQTPAYILEEDKLRKNCELLASVGEKSGAKVLLALKGFAFSGAMKIVGEYLKGCTCSGLWEAKFAKEYMDKEIHTYSPAFKEDEIGEIASLSHHIVFNSLAQFHKFQSKTQKNSLGLRCNVEFSLAPKELYNPCGRYSRLGIRAKDFENVDLNAIEGLHFHALCEESADALEAVLKVFKEKFGKWIGQMKWVNFGGGHHITKKGYDVEKLIALCKNFSDKYGVQVYLEPGEAVGWQTGNLVASVVDIIENEKQIAILDTSSEAHMPDTIIMPYTSEVLNARILATRENEKISDLKENEFAYLLTGNTCLAGDVMG... | 4.1.1.96 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:20534592}; | lysine biosynthetic process via diaminopimelate [GO:0009089]; nor-spermidine biosynthetic process [GO:0045312]; spermidine biosynthetic process [GO:0008295] | cytoplasm [GO:0005737] | carboxy-lyase activity [GO:0016831]; diaminopimelate decarboxylase activity [GO:0008836]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170] | PF00278; | 3.20.20.10; | Orn/Lys/Arg decarboxylase class-II family, NspC subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=carboxynorspermidine + H(+) = CO2 + norspermidine; Xref=Rhea:RHEA:34099, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57920, ChEBI:CHEBI:65070; EC=4.1.1.96; Evidence={ECO:0000269|PubMed:20534592}; CATALYTIC ACTIVITY: Reaction=carboxyspermidine + H(+) = CO2 + spermidine; Xref=Rhea:RHEA:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.1 mM for carboxyspermidine {ECO:0000269|PubMed:20534592}; KM=2.1 mM for carboxynorspermidine {ECO:0000269|PubMed:20534592}; Note=KM values are given with the protein sequence containing Glu instead of Lys at position 184, the effect of the variation on activity i... | null | null | null | FUNCTION: Catalyzes the decarboxylation of carboxynorspermidine and carboxyspermidine in vitro. In vivo, responsible for synthesizing spermidine, but not sym-norspermidine. {ECO:0000269|PubMed:20534592, ECO:0000269|PubMed:22025614}. | Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828) |
A8FP63 | FADB_SHESH | MIYQSPTIQVELLEDNIARLCFNASGSVNKLDRETINSLDAALDAIQQDSHIQALVLTSAKGAFIVGADITEFLGLFAQEDSVLLPWIAEANVVFNKLEDLPFPTISAINGFALGGGFETVLATDFRIADTTAKIGLPETKLGLIPGFGGTVRLPRLIGTDNALEWITSGKDQRPEAALKVGAIDAVVAPENLQASAIKMLKDALAEKLDWQSRRARKQAALTLPKLEAMMSFATAKGMVFKIAGKHYPAPMAAISVIEQAARCGRADALKVEHQAFVKLAKTDVAQALIGIFLNDQLVKGKAKKAGKLAKNIDTAAVLG... | 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}. | Shewanella sediminis (strain HAW-EB3) |
A8GYG0 | FADB_SHEPA | MIYQSPTIEVELLEDNIAHLCFKAQGSVNKFDRETIDSLNAALDSIKQDSSIKALMLSSAKDAFVVGADITEFLGLFAEEDTVLQSWLEQANVVFNKLEDLPFPTISAINGFALGAGCETILATDFRIADTTARIGLPETKLGIIPGFGGTVRLPRVIGADNALEWITSGKDQRPEAALKVGAIDAVVAPEQLKPAALKMLKDALIEKLDWQTRRAKKQAPLTLPKLEAMMSFATAKGMVFKVAGKHYPAPMAVISVIEQAAQLDRAGALQVEHQAFIKLAKTEVAQALIGIFLNDQLVKGKAKKAGKLAKKVNSAAVLG... | 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}. | Shewanella pealeana (strain ATCC 700345 / ANG-SQ1) |
A8HAL1 | UBP16_DANRE | MGKKKVKDRSAGTDSSSETAGPSCTHIRKGTENSVLKKACLNEHWSSCQDCEQDKPEEKQILEDQTDGESPAVWMCLKCGHRGCGRSGNQHAIKHYETPRSEPHCLVLSLDVWSVWCYICDDEVQYSSTGQLAQLITNIRKQVLTAPDKRNASKKSWKEDISVMNSAEQTQDEEKGKKGKQKSSSKQEDSPKSHQSAAAGSSAVVSVRGLSNLGNTCFFNAVVQSLSQTQYLRELLKQIAEEKSSFSITPALSSELDPLQIQLERPGSLTLAMCQLMNEIQETKKGVVTPKELFTQVCKKAPRFKGFQQQDSQELLRYLL... | 3.4.19.12 | null | cell division [GO:0051301]; DNA damage response [GO:0006974]; mitotic nuclear division [GO:0140014]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of translational elongation [GO:0045901]; protein homotetramerization [GO:0051289]; proteolysis [GO:0006508]; regulation of cell cycle... | nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; histone binding [GO:0042393]; histone H2A deubiquitinase activity [GO:0140950]; transcription coactivator activity [GO:0003713]; ubiquitin binding [GO:0043130]; zinc ion binding [GO:0008270] | PF00443;PF02148; | 3.90.70.10;3.30.40.10; | Peptidase C19 family, USP16 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03062}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000255|HAMAP-Rule:MF_03062}; | null | null | null | null | FUNCTION: Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome seg... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A8HN58 | IFT27_CHLRE | MVKKEVKPIDITATLRCKVAVVGEATVGKSALISMFTSKGSKFLKDYAMTSGVEVVVAPVTIPDTTVSVELFLLDTAGSDLYKEQISQYWNGVYYAILVFDVSSMESFESCKAWFELLKSARPDRERPLRAVLVANKTDLPPQRHQVRLDMAQDWATTNTLDFFDVSANPPGKDADAPFLSIATTFYRNYEDKVAAFQDACRNY | null | null | null | cytoskeleton [GO:0005856]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; intraciliary transport particle B [GO:0030992]; motile cilium [GO:0031514] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:17276912}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:17276912}. Note=Colocalizes with IFT25 at the distal-most portion of basal bodies, probably the transition zones, and concentrates in the basal body region. | null | null | null | null | null | FUNCTION: Small GTPase-like component of the intraflagellar transport (IFT) complex B. Forms a subcomplex within the IFT complex B with IFT25. Has very low GTPase activity either because it lacks the conserved catalytic Gln in position 79 or because it requires some GTPase-activating protein (GAP) for GTP turnover. {EC... | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A8I4E9 | CP100_CHLRE | MPIYDEASVPGTAAGRSTTDVGATAGANPFNIPADEEIFRFREEERARKEQDKLIAQTMRVADKTTFAAQMQATATADARTLLRELRPPKGPKATTTLAASSVGTLDRRKEKENMADFIAKKREIFLLQMSLDTKRAEIKKLEERARQREEALKKSEQMLEEDALRFDAFLKENDEKVQEAIKKAEAEAKAKQDKVLEIKRLNTATAALRSELNKYEEQLEDCRRYKEFLDSITPPEWFEQQAAKLQRRKDALVAEWQSQCEALKQRREAALAAKTAAESDYANARTQQQAERAERAIKESVAALKEIMKEKEPQPPNLD... | null | null | cell motility [GO:0048870]; cilium movement [GO:0003341]; inner dynein arm assembly [GO:0036159] | axonemal outer doublet [GO:0097545]; motile cilium [GO:0031514] | dynein complex binding [GO:0070840] | PF13863; | null | CFAP100 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:23569216}. Note=Localizes to the outer doublet microtubules of the axoneme. {ECO:0000269|PubMed:23569216}. | null | null | null | null | null | FUNCTION: As part of MIA, a complex associated with the outer doublet microtubules of the axoneme, may play a role in ciliary/flagellar motility by regulating the assembly and the activity of axonemal inner dynein arm. {ECO:0000269|PubMed:23569216}. | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A8ID55 | BLD10_CHLRE | MAIDVDRTLAVLRRKLEALGYSDPLEPASLQLVQKLVEDLVHTTDSYTAVKQQCAKQAQEIAAFDTRLESVRQDSVRLQSENSQLHVLVMQHAERHEREAREHYTAVKRLEDTIAELSYWKHAAAEKLASADKENAGLRKRCEELAKLTDRLASGAATPQSVAPKISSRSPIRVAPPPSPPRPRQATVDVLQAANGRILSLQRQLADATAELQELRQRVAEDEDQIRRRDVEIDRLGTRAGTDTNVLALRARNEANESMILQLNGTVESLAARVRELEAVEVRCEELQGALRRAEMDRDQAEERYSRSARDHDALSREVL... | null | null | ciliary basal body organization [GO:0032053]; cytoskeleton organization [GO:0007010]; regulation of cell division [GO:0051302] | centriole [GO:0005814]; ciliary basal body [GO:0036064]; ciliary pro-basal body [GO:0120280]; cytoplasm [GO:0005737]; microtubule [GO:0005874] | identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; protein homodimerization activity [GO:0042803] | null | 1.10.287.1490; | CEP135/TSGA10 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:15173189}. Note=Localized at the cartwheel, the first ninefold symmetrical structure appearing during basal body/centriole assembly near the proximal end of the organelle. {ECO:0000269|PubMed:15173189... | null | null | null | null | null | FUNCTION: Microtubule-binding protein essential for cytoskeletal organization (e.g. rootlet microtubule bundles) and flagellar basal body/centriole assembly. {ECO:0000269|PubMed:15173189, ECO:0000269|PubMed:27477386}. | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A8IKD2 | CAH_AZOC5 | MPIAKVHRIATASPDDVSGLAAAIATGAIAPAGILAIFGKTEGNGCVNDFSRGFAVQSLQMLLRGHMGAAADEVCLVMSGGTEGGMSPHFLVFERAEGNAPEAAPALAIGRAHTPDLPFEALGRMGQVRMVAQAVRRAMAAAGITDPEDVHFVQVKCPLLTAMRVKEAEARGATTATSDTLKSMGLSRGASALGIALALGEVAEDALSDAVICADYGLWSARASCSSGIELLGHEIVVLGMSEGWSGPLAIAHGVMADAIDVTPVKAALSALGAEAGEATIVLAKAEPSRSGRIRGKRHTMLDDSDISPTRHARAFVAGA... | 3.5.2.15 | null | atrazine catabolic process [GO:0019381] | null | cyanuric acid amidohydrolase activity [GO:0018753]; metal ion binding [GO:0046872] | PF09663; | 3.30.1330.160;3.30.1330.170;3.30.1330.180; | Cyclic amide hydrolase (CyAH) family | null | null | CATALYTIC ACTIVITY: Reaction=cyanurate + H2O = 1-carboxybiuret + H(+); Xref=Rhea:RHEA:70363, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:38028, ChEBI:CHEBI:142864; EC=3.5.2.15; Evidence={ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:22730121}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=370 uM for cyanuric acid {ECO:0000269|PubMed:22730121}; Note=kcat is 50 sec(-1) with cyanuric acid as substrate. {ECO:0000269|PubMed:22730121}; | PATHWAY: Xenobiotic degradation; atrazine degradation; biuret from cyanurate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01989}. | null | null | FUNCTION: Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-trihydroxy-s-triazine) to yield carbon dioxide a... | Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB 13405 / ORS 571) |
A8IQT2 | CCD40_CHLRE | MADPMDQPSTSDPVDNQIFGEQGGLRPDHPLLRRAQEALKVQFEANRTRLQEELREKANALKQAKARREALGVELYGFQQNLAKLQLNLETTHQNYQCEDQLNQLKQQLSLEEGDTKGERSRRVCVCVCRVCCRIDTLQDNLKGTQQQLALVSAQLEAQKRETRAALETLAEAEVGGCVRDEALSAIQDGMREQQQQELSLVLEIEGYKKDVVREQLKHESLTAVVRKVEGDAVFVQKQIEGAQERQARLQEILAKLAKSLEHTEAEGEADAVDRAITKVAAEGRAIEEEMLSALSDQTTAEKATSKTAADTQELRKRIR... | null | null | axoneme assembly [GO:0035082]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287]; heart looping [GO:0001947] | cytoplasm [GO:0005737]; motile cilium [GO:0031514] | null | null | null | CCDC40 family | PTM: Asymmetrically dimethylated at Arg-246 and Arg-523 during flagellum resorption. Probably methylated by PRMT1. {ECO:0000269|PubMed:24152136}. | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:25395538}. | null | null | null | null | null | FUNCTION: Required for assembly of dynein regulatory complex (DRC) and inner dynein arm complexes, which are responsible for ciliary beat regulation, by acting as a molecular ruler that determines the 96 nanometer (nm) repeat length and arrangements of components in cilia and flagella (PubMed:25395538). Together with C... | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A8IU92 | CFA20_CHLRE | MFKNAFQSGFLSVLYSIGSKPLEIWDKQVSNGHIKRITDADIQSSVLEIMGQNVSTTYITCPADPNKTLGIKLPFLVLIIKNLNKYFSFEVQVLDDKNVRRRFRASNYQSTTRVKPFICTMPMRLDSGWNQIQFNLSDFTRRAYGTNYIETLRVQVHANCRIRRIYFSDRLYSEEELPAEFKLFLPIQKS | null | null | axoneme assembly [GO:0035082]; cilium assembly [GO:0060271]; establishment of protein localization to organelle [GO:0072594]; positive regulation of cilium-dependent cell motility [GO:2000155]; regulation of cilium beat frequency involved in ciliary motility [GO:0060296] | axonemal central pair [GO:0097540]; axonemal microtubule [GO:0005879]; axonemal outer doublet [GO:0097545]; ciliary basal body [GO:0036064]; microtubule associated complex [GO:0005875]; motile cilium [GO:0031514] | null | PF05018; | null | CFAP20 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q9Y6A4}. Cytoplasm, cytoskeleton, flagellum basal body. Note=Localizes predominantly along the length of all nine axonemal outer doublet microtubules (DMTs). Localizes to the inner junction (IJ) between A- and B-tubules of the DMTs.... | null | null | null | null | null | FUNCTION: Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility (PubMed:24259666, PubMed:24574454). Involved in the control of flagellar beating in an asymmetric and planar waveform (PubMed:24259666, PubMed:24574454). Stabilizes outer doublet microtubules (DMTs) of the... | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A8J637 | PETS_CHLRE | MLRELGRTATVKAHGRSVLRPVRGPAGRRQVAFTGVRPSVRVFAEAPAAEQAAKAIKLEDVKEGSEYEGTVTTVEEFGAFVNFGANTNGLVHISKLASGFTKNAKDVVQPGQKVTVKVLSVDAEKKRVSLELKSAVAAEASAEESDDIITEPDREGADATDDDEDVEVELEDGQVEVRADLPGFEDIPFVMEEADMDAEMSEAAIAALEADLDGAEIRYELEAPAYMEEVTGKVARIEDYGVFLEFEWNGKTLTGLLAKDEMKVPSSALSAEAQAALRAEWADTGFEMPAFVELPDDELDVKKYYQPGESVPAFVLESSL... | null | null | mitochondrial translational elongation [GO:0070125]; response to light stimulus [GO:0009416] | chloroplast [GO:0009507]; chloroplast ribosome [GO:0043253]; mitochondrial matrix [GO:0005759] | mRNA binding [GO:0003729]; translation elongation factor activity [GO:0003746]; translation elongation factor binding [GO:0061770] | PF00889;PF00575; | 1.10.286.20;1.10.8.10;3.30.479.20;2.40.50.140; | EF-Ts family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:12417713, ECO:0000269|PubMed:15548736}. | null | null | null | null | null | FUNCTION: [Elongation factor Ts, chloroplastic]: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP (PubMed:15548736). It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (PubMed:15548736). {ECO:0000269|PubMed:15548736}.; FUNCTION: [Plastid-s... | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A8JB22 | DRC2_CHLRE | MVKAGKKVKGASKVRENETEEEKKIRLEMEALAADEAERKAQEAARVALRERQLREQRYAHLNGIKIHNQWRKIMRMAKVEELRREIEILSQNHEREVDRKDAIMQMLDRDLEEAEEQYSLAVRSHMLVVDNLLDLQYQRMRALEAEFAADLKALEDEFETERTEIVNAHTRQRKDMGDMIAAMEGEFADAEAELRQEYEAQREEIKNRNSEEYNVLKIQLEGIIEELEKSFELAHRAYLESTEHRTNTFRTLTKDDAKAALKIERQMRKLVRLQEALQHWRTKIATNGREWEERNRALRNEKEIMARHYAKLKSSMDAF... | null | null | axonemal dynein complex assembly [GO:0070286]; cilium-dependent cell motility [GO:0060285]; regulation of cilium movement [GO:0003352] | axonemal dynein complex [GO:0005858]; axoneme [GO:0005930]; motile cilium [GO:0031514] | null | PF14772;PF14775; | null | DRC2 family | PTM: Asymmetrically dimethylated at Arg-96 and Arg-142 during flagellum resorption. Probably methylated by PRMT1. {ECO:0000269|PubMed:24152136}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:29167384}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:29167384}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:23427265, ECO:0000269|PubMed:25411337}. | null | null | null | null | null | FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes (PubMed:23427265, PubMed:25411337). Plays a critical role in the assembly of N-DRC and ... | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
A8JQX3 | NOCT_DROME | MDQKTTGLRENYGHRRQPALGKAMPVTALLLNLESNPLDYSRNDIGAELLEDDDKPPQLFSVTDEPPSPNEEDYKPPNHHEDDGKLAGERHREIPCSNCLKTAPGHLIDRQSAINEMCQRLCGPECRRPQGLTLDGVRQDFLRQYEIAEAVAKTSAMTSTVQMKQRLAARKLEFEKEMEMDEQLGVASPRNDINLGQSSTVAATGMGEFEFEPPRDLLLYLVRMGSFNSAPKINNVDSQDDGLVLPSGLSTPALLQHVQQLRGGGIEQPSLLTRGFLKPLLADEDVADGLRCLKLNSVSRVCSAPVEGDDIRLLQWNILS... | 3.1.3.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9UK39}; Note=Binds 2 magnesium ions, but the ions are only loosely bound to the protein. {ECO:0000250|UniProtKB:Q9UK39}; | locomotor rhythm [GO:0045475]; NADP metabolic process [GO:0006739]; response to light stimulus [GO:0009416] | cytoplasm [GO:0005737]; mitochondrion [GO:0005739] | 3'-5'-RNA exonuclease activity [GO:0000175]; metal ion binding [GO:0046872]; NADP phosphatase activity [GO:0019178]; NADPH phosphatase activity [GO:0102757] | PF03372; | 3.60.10.10; | CCR4/nocturin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19581445}. | CATALYTIC ACTIVITY: Reaction=H2O + NADP(+) = NAD(+) + phosphate; Xref=Rhea:RHEA:28050, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:31147539}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28051; Evidence={ECO:0000269|PubMed:31147539}; CATALYTIC ACTIVIT... | null | null | null | null | FUNCTION: Phosphatase which catalyzes the conversion of NADP(+) to NAD(+) and of NADPH to NADH (PubMed:31147539). Shows a small preference for NADPH over NADP(+) (PubMed:31147539). Because of its association with the CCR4-NOT complex, has a role in mRNA deadenylation and decay (PubMed:20504953). Required at the pupal s... | Drosophila melanogaster (Fruit fly) |
A8JUP7 | HAYAN_DROME | MAMISARRYFLLGLLVLTTSAYVTVGDEGDPCQVRSDIPGICLSSSACENIRGYLKSGTLSTSQVPSCGFGAREEIICCPTVACCATDRGREVQFHATSSERSSLPEPKREPTPEPEPLPPTTTEGKRERESRLDENQNFFDFNKLLSTTVKPQKTHESLKLPTQESMKTPTHESMKMPTHESMKLPTHEPMKLPIQSVGAWGIAPSKTQPIASTQRSFMEPEWGREPRIVNRPLTTPRSRPQRPNNSNFNTNPSPNNNNLIHLVNDRLREQGMQIEPAREVPMVLQTTPTPTPAPTPTQLIDPFEPYRFRGQDRDKDTQ... | 3.4.21.- | null | defense response to fungus [GO:0050832]; immune system process [GO:0002376]; melanin biosynthetic process [GO:0042438]; positive regulation of melanization defense response [GO:0035008]; proteolysis [GO:0006508]; regulation of melanization defense response [GO:0035007]; Toll receptor ligand protein activation cascade [... | extracellular region [GO:0005576] | serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family, CLIP subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22227521}. | null | null | null | null | null | FUNCTION: Serine protease which, by converting prophenoloxidase 1 (PPO1) into its active form, plays an essential role in the melanization immune response to physical or septic wounding. May function in diverse PPO1-activating cascades that are negatively controlled by different serpin proteins; Spn27A and Spn28D in th... | Drosophila melanogaster (Fruit fly) |
A8JUV0 | SBNO_DROME | MTSKKRKTLLDADDDNDNFDEDDSGSDFDDDEDPDQIEVPGGGRDLNTAVTYAQNIRSGVGVAPKGGIPIPISGAKIVVGNNKIKPISLLRINNNNNNIVTSVNNRNNNNIISTNGSSNNNNNSINNNSQIIKTTTVTTTPTTVGATPTVGGVALGGKLTVIPIAGRNVALDNNLSNMPKKLNNMVTAMGSPAARSSGNAGTTGSSQGGAIGSTSSYLNSLTTNELMNLAAYVAAKGSNAPPPPPPSTAANSVRHSPTGGIPNPGGNFFGGSAAASTSASAANFNMAASLLAQMSYAGGASQIRALKVAGNIGGVGNNQK... | null | null | imaginal disc-derived wing margin morphogenesis [GO:0008587]; Notch signaling pathway [GO:0007219]; photoreceptor cell development [GO:0042461]; positive regulation of Notch signaling pathway [GO:0045747]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription ... | nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; histone binding [GO:0042393] | PF13872;PF13871; | 3.40.50.300; | SBNO family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9171377}. | null | null | null | null | null | FUNCTION: Notch pathway component, may contribute to the specificity between lateral and inductive Notch signaling pathways in the wing disk. Required during many developmental stages including oogenesis, embryogenesis and imaginal development of the eye, wing and leg. Ebi and sno regulate EGFR-dependent Delta transcri... | Drosophila melanogaster (Fruit fly) |
A8K0Z3 | WASH1_HUMAN | MTPVRMQHSLAGQTYAVPFIQPDLRREEAVQQMADALQYLQKVSGDIFSRISQQVEQSRSQVQAIGEKVSLAQAKIEKIKGSKKAIKVFSSAKYPAPGRLQEYGSIFTGAQDPGLQRRPRHRIQSKHRPLDERALQEKLKDFPVCVSTKPEPEDDAEEGLGGLPSNISSVSSLLLFNTTENLYKKYVFLDPLAGAVTKTHVMLGAETEEKLFDAPLSISKREQLEQQVPENYFYVPDLGQVPEIHVPSYLPDLPGIANDLMYSADLGPGIAPSAPGTIPELPTFHTEVAEPLKVDLQDGVLTPPPPPPPPPPAPEVLASA... | null | null | Arp2/3 complex-mediated actin nucleation [GO:0034314]; endocytic recycling [GO:0032456]; endosomal transport [GO:0016197]; exocytosis [GO:0006887]; extracellular matrix disassembly [GO:0022617]; negative regulation of autophagy [GO:0010507]; positive regulation of cell migration [GO:0030335]; positive regulation of pse... | autophagosome [GO:0005776]; centriole [GO:0005814]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; late endosome [GO:0005770]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; WASH complex [GO:0071203] | actin binding [GO:0003779]; alpha-tubulin binding [GO:0043014]; gamma-tubulin binding [GO:0043015]; phosphatidylinositol 3-kinase inhibitor activity [GO:0141039]; ubiquitin protein ligase binding [GO:0031625] | PF11945; | null | WASH1 family | PTM: Ubiquitinated at Lys-220 via 'Lys-63'-linked ubiquitin chains by the TRIM27:MAGEL2 E3 ubiquitin ligase complex, leading to promote endosomal F-actin assembly. {ECO:0000269|PubMed:23452853}. | SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:19922874}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q8VDD8}. Late endosome {ECO:0000269|PubMed:22114305, ECO:0000269|PubMed:24344185}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q8VDD8}. Cytoplasm, cytoskeleton, microtubule organ... | null | null | null | null | null | FUNCTION: Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome ... | Homo sapiens (Human) |
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