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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
K7WIZ6 | RIBRX_MAIZE | MPLPQPLLGGASPAPARAASSFLHPLLHTRHRVSTAPAAASSFVPASHSSHANDAMLLRRAADVADRSAGLTSPHPNFGCVIARPQLNTDSADSWVVGEGFLYAQGTPCAELLASQEAGEHARGGTAYLNLEPGDCFGDNTAVGSLVQAGITRVVVGLRHPLKHLRGKAIQALRNEGIQVDVVGEDLQSKLFKEALKSCLTVNAPLLYRAAFHVPFSVLKYAMTADGKIAASSGHASWISGKASRGRVFELRGRSDAVIVGGNTVRFDDPRLTARHVKGHVPVRIVMSQSLNLPEEANLWNLNDAYTIVATQRGARRDFQ... | 1.1.1.193; 3.2.2.- | null | carbohydrate derivative metabolic process [GO:1901135]; chloroplast organization [GO:0009658]; FAD metabolic process [GO:0046443]; response to high light intensity [GO:0009644]; riboflavin biosynthetic process [GO:0009231] | chloroplast [GO:0009507] | 5-amino-6-(5-phosphoribosylamino)uracil reductase activity [GO:0008703]; diaminohydroxyphosphoribosylaminopyrimidine deaminase activity [GO:0008835]; dihydropyrimidine dehydrogenase (NADP+) activity [GO:0017113]; hydrolase activity, hydrolyzing N-glycosyl compounds [GO:0016799]; NADP binding [GO:0050661] | PF08719;PF01872; | 3.40.140.10;3.40.430.10;1.10.357.40; | YbiA family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:23150645}. | CATALYTIC ACTIVITY: Reaction=5-amino-6-(5-phospho-D-ribitylamino)uracil + NADP(+) = 5-amino-6-(5-phospho-D-ribosylamino)uracil + H(+) + NADPH; Xref=Rhea:RHEA:17845, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58421, ChEBI:CHEBI:58453; EC=1.1.1.193; Evidence={ECO:0000269|PubMed:23150645}; CATALY... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.94 mM for 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine {ECO:0000269|PubMed:25431972}; KM=0.19 mM for 5-amino-6-(5-phospho-D-ribosylamino)uracil {ECO:0000269|PubMed:25431972}; Note=kcat is 5.0 sec(-1) with 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribos... | PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 3/4. | null | null | FUNCTION: Pyrimidine reductase involved in the riboflavin biosynthesis pathway. Has also a non-functional N-terminal deaminase domain that lacks the catalytically essential zinc-binding residues. 39% activity when NADH replaces NADPH. No evidence for a phosphatase activity conferred by the N-terminal domain. {ECO:00002... | Zea mays (Maize) |
K7WQ45 | CPT2_SOLLC | MNSSIVSQHFFISLKSSLDLQCWKSSSPSSISMGEFKGIHDKLQILKLPLTMSDRGLSKISCSLSLQTEKLRYDNDDNDDLELHEELIPKHIALIMDGNRRWAKAKGLEVYEGHKLIIPKLKEICDISSKLGIQVITAFAFSTENWKRSKEEVDFLMQLFEEFFNEFLRFGVRVSVIGCKSNLPMTLQKCIALTEETTKGNKGLHLVIALNYGGYYDILQATKSIVNKAMNGLLDVEDINKNLFEQELESKCPNPDLLIRTGGEQRVSNFLLWQLAYTEFYFTNTLFPDFGEKDLKKAILNFQQRHRRFGGHTY | 2.5.1.142 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23134568}; | plastid membrane organization [GO:0009668]; polyprenol biosynthetic process [GO:0016094]; response to cold [GO:0009409] | chloroplast [GO:0009507]; chloroplast stroma [GO:0009570] | dehydrodolichyl diphosphate synthase activity [GO:0045547]; dimethylallylcistransferase activity [GO:0047863]; magnesium ion binding [GO:0000287]; polyprenyltransferase activity [GO:0002094]; prenyltransferase activity [GO:0004659] | PF01255; | 3.40.1180.10; | UPP synthase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:23134568}. | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + 3 isopentenyl diphosphate = 3 diphosphate + nerylneryl diphosphate; Xref=Rhea:RHEA:55520, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769, ChEBI:CHEBI:139032; EC=2.5.1.142; Evidence={ECO:0000269|PubMed:23134568, ECO:0000269|PubMed:23757397, ECO:0000269|P... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.8 uM for isopentenyl diphosphate {ECO:0000269|PubMed:25786135}; KM=22.9 uM for (2Z,6Z)-farnesyl diphosphate {ECO:0000269|PubMed:25786135}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:25786135}; | null | FUNCTION: Uses dimethylallyl diphosphate and isopentenyl diphosphate to catalyze the cis-prenyl chain elongation and produce the 20 carbon product nerylneryl diphosphate. {ECO:0000269|PubMed:23134568, ECO:0000269|PubMed:23757397, ECO:0000269|PubMed:25786135}. | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
K7ZP88 | ATAA_ACIS5 | MNKIYKVIWNATLLAWVAVSELAKGKTKSTTSKSKAKSLSSSVIVGGIILTTPLSLIAATVQVGGGTNSGTTATASTNCADLYNYQNPENSGSGAAGNYNAGNPSVCSIAIGENAQGGTSGTGGSPGIAIGGNSKATGGLSVAIGGYAQATNVGSIALGTAALSSGFNSLAISRQAAATNNYSIAIGTTSVSKGVGSIAMGHSTNASGDQSIAIGSSDAVNSATATTTYDGTTNTQASGSKSIAIGASAKASTNNSIALGAGSVTSAQSGNSYLTGVGASATNGVVSVGTSTATRRIQNVADGSAASDAVTVAQLDKAYD... | null | null | cell adhesion [GO:0007155]; protein transport [GO:0015031] | cell outer membrane [GO:0009279]; cell surface [GO:0009986] | null | PF13018;PF03895;PF05658;PF05662; | 1.20.5.170;1.20.5.2280;2.20.70.140;6.10.250.2040;2.150.10.10; | Autotransporter-2 (AT-2) (TC 1.B.40) family | null | SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:23155410, ECO:0000269|PubMed:27074146, ECO:0000269|PubMed:27305955}. Cell outer membrane {ECO:0000269|PubMed:23155410, ECO:0000269|PubMed:27074146}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A1JUB7}. Note=Localizes to thin, peritrichate nanofibers (200 nm ... | null | null | null | null | null | FUNCTION: Responsible for autoagglutination, and for adhesion to abiotic and biotic surfaces such as polystyrene (PS), type I collagen, polypropylene (PP), polyvinylchloride (PVC), glass and stainless steel (SS). Adhesion is much stronger than that mediated by Yersinia YadA in a comparative assay. Confers autoagglutina... | Acinetobacter sp. (strain Tol 5) |
K8DWB5 | CA1D_CONTE | FDGRNAAGNDKMSALMALTTRGCCSHPVCSAMSPICG | null | null | null | extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792] | acetylcholine receptor inhibitor activity [GO:0030550]; toxin activity [GO:0090729] | PF07365; | null | Conotoxin A superfamily | PTM: Unmodified Met-32 is essential for toxin binding to rat alpha-3-beta-4/CHRNA3-CHRNB4 nAChR. An oxidation of this methionine provokes a 13.3-fold decrease in inhibitory potency (IC(50)=245 nM instead of 18 nM). Owing to its potent activity, derivatives of this toxin have a potential in the development of a novel dr... | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24200193}. | null | null | null | null | null | FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin inhibits alpha-3-beta-4/CHRNA3-CHRNB4 (IC(50)=3.6-18.38 nM), alpha-6/alpha-3-beta-4 (CHRNA6/CHRNA3-CHRNB4) (IC(50)=33.9-94.1 nM), and alpha-2-beta-4/CHRNA2-CHRNB4 (IC(50... | Conus textile (Cloth-of-gold cone) |
K8ERR8 | LSY12_CAEEL | MGKKRKPSPERSSDEDEVSTPSPKDRTARPTAAARRENVALSQAVALSLEDASNFCSLAFSLERIKREPVDTDYDDPNQPGPSSVPVSARTDHVLPIRFKIKAEPQEYDSDEYGKDHGAVQIANKEVPAISPIEEVSQKRRGRPRKTDAAQHLFFPHVSIKQEPDDGFINFHESRCVGIAQDPEMQHLHDVNESHSSEIAIFRETKKITERKKKKTEAEKLWDNMSLTEKEVFQSHTRRRRTTRLPIIQNFEETEEGCIVEVPIPLIDLDNDAVESVTGPQHENVTVSENVLSTESTDQEVTETKRLHDSSRDFNPPRIQ... | 2.3.1.48 | null | cell fate specification [GO:0001708]; maintenance of left/right asymmetry [GO:0061968]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymer... | MSL complex [GO:0072487]; NSL complex [GO:0044545]; NuA4 histone acetyltransferase complex [GO:0035267]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; histone H4K16 acetyltransferase activity [GO:0046972]; metal ion binding [GO:0046872]; transcription coregulator activity [GO:0003712] | PF01853;PF17772; | 3.40.630.30;3.30.60.60;1.10.10.10; | MYST (SAS/MOZ) family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU... | null | null | null | null | FUNCTION: Probable histone acetyltransferase (Probable). Required to initiate and then maintain lateralized gene expression in the ASE sensory neurons (PubMed:20923973). Involved in determining cell fate in the ASE neurons (PubMed:20923973). {ECO:0000269|PubMed:20923973, ECO:0000305|PubMed:20923973}. | Caenorhabditis elegans |
K8ESC5 | ATG41_CAEEL | MLSILPLAYSNFSRILQYFEQLPVVDKMTEEILKQGVGIVETSLTFEPPFCESFERISIDNFPIFALGKEISKEDGIEAMKKYVTSRFWFTYRRDFSPIGGTGPSTDQGWGCMLRCAQMLLGEVLLRRHIGRHFEWDIEKTSEIYEKILQMFFDEKDALYSIHQIAQMGVTEGKEVSKWFGPNTAAQVMKKLTIFDDWSNIAVHVALDNILVKEDAITMATSYPSEDAVKLIMENGLVDKNRLSLSPGNIIPEWRPLLLMIPLRLGLTTINPCYLSAIQEFFKIPQCVGIIGGRPNHALYFVGMSGSKLFYLDPHYCRPK... | 3.4.22.- | null | aggrephagy [GO:0035973]; autophagosome assembly [GO:0000045]; mitophagy [GO:0000423]; piecemeal microautophagy of the nucleus [GO:0034727]; protein processing [GO:0016485]; protein transport [GO:0015031] | cytoplasm [GO:0005737] | cysteine-type endopeptidase activity [GO:0004197]; protein-phosphatidylethanolamide deconjugating activity [GO:0019786] | PF03416; | null | Peptidase C54 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255, ECO:0000255|RuleBase:RU363115, ECO:0000269|PubMed:22767594, ECO:0000269|PubMed:30880001}. | CATALYTIC ACTIVITY: Reaction=[protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:67548, Rhea:RHEA-COMP:17323, Rhea:RHEA-COMP:17324, ChEBI:CHEBI:15377, ChEBI:CHEBI:64612, ChEBI:CHEBI:172940, Ch... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18.97 uM for lgg-1 {ECO:0000269|PubMed:22767594}; | null | null | null | FUNCTION: Cysteine protease required for autophagy (PubMed:22767594, PubMed:30880001). Cleaves the C-terminal amino acid of ATG8 family proteins lgg-1, to reveal a C-terminal glycine (PubMed:22767594). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) ... | Caenorhabditis elegans |
K8FE10 | SYT2_CAEEL | MWATGAIVCSPVFRILSTCCPIRRGVPTSNGYHPRPKHVDIGNGAVPILSSKPITVQPTNSDYYEPVNNGTLPLSSSGALIKQYGNIHFRVEYDFEQSKLSVTIVSASDLPAMDRNGMSDPYVKVYVLPERKQKFETRIIRNTLNPTYNETFQFSIPFNELHSKTLMLVVYDYDRLSKDDKMGQLSVPLESIDFGITTDIERPLQKPEKDDEKECRLGDICFSTRYRPATGTVTLTIMEARNLKKMDVGGSSDPYVKIYLHHGRKLLSKKKTSRKYKTLNPYYNESFQFKIEPHMIEKVHLIVSVWDYDKMSKNDFIGEV... | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000250|UniProtKB:Q9R0N7, ECO:0000255|PROSITE-ProRule:PRU00041}; | calcium ion-regulated exocytosis of neurotransmitter [GO:0048791]; cellular response to calcium ion [GO:0071277]; regulation of calcium ion-dependent exocytosis [GO:0017158]; regulation of dopamine secretion [GO:0014059]; synaptic vesicle endocytosis [GO:0048488] | axon [GO:0030424]; dense core granule [GO:0031045]; exocytic vesicle [GO:0070382]; plasma membrane [GO:0005886]; synaptic vesicle membrane [GO:0030672] | calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; clathrin binding [GO:0030276]; phosphatidylserine binding [GO:0001786]; syntaxin binding [GO:0019905] | PF00168; | 2.60.40.150; | Synaptotagmin family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:23583549}. Note=Co-localizes with nlp-40 in cytoplasmic vesicles. {ECO:0000269|PubMed:23583549}. | null | null | null | null | null | FUNCTION: Ca(2+) sensor involved in Ca(2+)-dependent secretion of the nlp-40 neuropeptide from intestinal cells. Involved in the defecation motor program, which is a coordinated series of three muscle contractions that occurs every 45 seconds. {ECO:0000269|PubMed:23583549}. | Caenorhabditis elegans |
K9IMD0 | TRLF_DESRO | MKLLFLALLSLLALGPSLAARRRGVRWCTISKPEAAKCSKLQQNLKRVRGPSLSCISRKSYLECIQAIAAKRADAMSLDAGLVYEAGQDPYRLRPVAAEVYGTEGAPRTHYYAVALVKKDSNLQLNQLQGVRSCHTGLNRSAGWKIPVGTLRPYLGWAGPPAPLQEAVANFFSASCVPCADGNQYPNLCRLCAGTGADKCACSSKEPYFGYSGAFKCLKDGAGDVAFVKDSTVFENLPNKAERDQYELLCPDNTRKPVDEFEQCHLARVPSHAVVARSVGGKEDSIWRLLSKAQEKFGKGTSGSFQLFSSPPGQKDLLFK... | 3.4.21.- | null | antibacterial humoral response [GO:0019731]; iron ion transport [GO:0006826]; negative regulation of blood coagulation [GO:0030195]; ossification [GO:0001503]; proteolysis [GO:0006508] | early endosome [GO:0005769]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037] | metal ion binding [GO:0046872]; serine-type peptidase activity [GO:0008236]; toxin activity [GO:0090729] | PF00405; | 3.40.190.10; | Transferrin family | PTM: N-glycosylated (PubMed:9795244). Glycosylation is important for draculin anticoagulant activity (PubMed:9795244). Probably also O-glycosylated (PubMed:9795244). {ECO:0000269|PubMed:9795244}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10556567, ECO:0000269|PubMed:23748026, ECO:0000269|PubMed:7740503, ECO:0000269|PubMed:9795244}. | null | null | null | null | null | FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. {ECO:0000250|UniProtKB:P02788}.; FUNCTION: [Lactotransferrin]: Major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucos... | Desmodus rotundus (Vampire bat) |
K9JHZ4 | TET3B_XENLA | METQPASVPCVLPQDVYEFSEDRESLGRLRVSEMPSELNGGGDGSKGDGAAVVATEVSQQSNKKRKRCGVCVPCLRKEPCGTCYNCVNRSTSHQICKMRKCEQLKKKRVVPMKGVEAVDKDDAKNQAKEQVPSVKNCSESILVDGPKTDQMEAGPVNHVQEGRLKQECDSTLPSKGSEDLANQLLMEANSWLSNTAAPQDPCNKLNWDKPIIPNHIAANNNSNLEDAKNLVAFSAVAEAMSNYGMPASGTPSSISMQLYEKFNYETNQDNSGHSEGNAPSCPEDLNTLKEALALAKHGVKPPNCNCDGPECPDYLEWLEN... | 1.14.11.80 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q6N021}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6N021}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q6N021}; Note=The zinc ions have a structural role. {ECO:0000250|UniProtKB:Q6N021}; | 5-methylcytosine catabolic process [GO:0006211]; DNA demethylation [GO:0080111]; eye development [GO:0001654]; nervous system development [GO:0007399]; positive regulation of gene expression via CpG island demethylation [GO:0044029]; positive regulation of transcription by RNA polymerase II [GO:0045944] | chromosome [GO:0005694]; nucleus [GO:0005634] | 5-methylcytosine dioxygenase activity [GO:0070579]; methyl-CpG binding [GO:0008327]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270] | PF12851;PF02008; | null | TET family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0JP82}. Chromosome {ECO:0000250|UniProtKB:A0JP82}. Note=Detected on chromatin, where it binds to target gene promoters. {ECO:0000250|UniProtKB:A0JP82}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-methyl-2'-deoxycytidine in DNA + O2 = a 5-hydroxymethyl-2'-deoxycytidine in DNA + CO2 + succinate; Xref=Rhea:RHEA:52636, Rhea:RHEA-COMP:11370, Rhea:RHEA-COMP:13315, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85454, ChEBI:CHEB... | null | null | null | null | FUNCTION: Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in epigenetic chromatin reprogramming during embryonic development. Conversion of 5mC into 5hmC probably constitutes the first step in cytosine demethylation. ... | Xenopus laevis (African clawed frog) |
K9M1U5 | IFNL4_HUMAN | MRPSVWAAVAAGLWVLCTVIAAAPRRCLLSHYRSLEPRTLAAAKALRDRYEEEALSWGQRNCSFRPRRDPPRPSSCARLRHVARGIADAQAVLSGLHRSELLPGAGPILELLAAAGRDVAACLELARPGSSRKVPGAQKRRHKPRRADSPRCRKASVVFNLLRLLTWELRLAAHSGPCL | null | null | cellular response to virus [GO:0098586]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of immune response [GO:0050778]; type III interferon-mediated signaling pathway [GO:0038196]; tyrosine phosphorylation of STAT protein [GO:0007260] | cytoplasm [GO:0005737]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; signaling receptor binding [GO:0005102] | PF15177; | 1.20.1250.60; | Lambda interferon family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23291588}. Secreted {ECO:0000269|PubMed:23291588}. | null | null | null | null | null | FUNCTION: Cytokine that may trigger an antiviral response activating the JAK-STAT pathway and up-regulating specifically some interferon-stimulated genes. {ECO:0000269|PubMed:23291588}. | Homo sapiens (Human) |
K9N4V7 | NCAP_MERS1 | MASPAAPRAVSFADNNDITNTNLSRGRGRNPKPRAAPNNTVSWYTGLTQHGKVPLTFPPGQGVPLNANSTPAQNAGYWRRQDRKINTGNGIKQLAPRWYFYYTGTGPEAALPFRAVKDGIVWVHEDGATDAPSTFGTRNPNNDSAIVTQFAPGTKLPKNFHIEGTGGNSQSSSRASSVSRNSSRSSSQGSRSGNSTRGTSPGPSGIGAVGGDLLYLDLLNRLQALESGKVKQSQPKVITKKDAAAAKNKMRHKRTSTKSFNMVQAFGLRGPGDLQGNFGDLQLNKLGTEDPRWPQIAELAPTASAFMGMSQFKLTHQNND... | null | null | negative regulation of interferon-beta production [GO:0032688]; viral RNA genome packaging [GO:0019074] | host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell Golgi apparatus [GO:0044177]; ribonucleoprotein complex [GO:1990904]; viral capsid [GO:0019028]; viral nucleocapsid [GO:0019013] | RNA binding [GO:0003723] | PF00937; | null | Betacoronavirus nucleocapsid protein family | PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion during infection. {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:29199039}.; PTM: Phosphorylated on serine and threonine residues. {ECO:0000255|HAMAP-Rule:MF_04096}.; PTM: Proteolytically cleaved by host CASP6. The cleavage at Asp-242 leads to t... | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04096}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|HAMAP-Rule:MF_04096}. Host Golgi apparatus {ECO:0000255|HAMAP-Rule:MF_04096}. Note=Located inside the virion, complexed with the viral RNA. Probably associates with ER-derived membranes... | null | null | null | null | null | FUNCTION: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as vi... | Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1) |
K9N5Q8 | SPIKE_MERS1 | MIHSVFLLMFLLTPTESYVDVGPDSVKSACIEVDIQQTFFDKTWPRPIDVSKADGIIYPQGRTYSNITITYQGLFPYQGDHGDMYVYSAGHATGTTPQKLFVANYSQDVKQFANGFVVRIGAAANSTGTVIISPSTSATIRKIYPAFMLGSSVGNFSDGKMGRFFNHTLVLLPDGCGTLLRAFYCILEPRSGNHCPAGNSYTSFATYHTPATDCSDGNYNRNASLNSFKEYFNLRNCTFMYTYNITEDEILEWFGITQTAQGVHLFSSRYVDLYGGNMFQFATLPVYDTIKYYSIIPHSIRSIQSDRKAWAAFYVYKLQP... | null | null | endocytosis involved in viral entry into host cell [GO:0075509]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; membrane fusion [GO:0061025]; positive regulation of viral entry into host cell [GO:0046598]; receptor-mediated virion atta... | host cell endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0044173]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF16451;PF09408;PF19209;PF01601;PF19214; | 1.20.5.300;2.20.210.30;3.30.70.1840;2.60.120.960; | Betacoronaviruses spike protein family | PTM: Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host cell furin or another cellular protease to yield the mature S1 and S2 proteins. Additionally, a second cleavage leads to the release of a fusion peptide after viral attachment to host cell receptor. {ECO:0... | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Hos... | null | null | null | null | null | FUNCTION: [Spike protein S1]: Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Interacts with host DPP4 to mediate virla entry. {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:23486063}.; FUNCTION: [Spike protein S2]: Mediates fusion of the virio... | Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1) |
K9N638 | R1A_MERS1 | MSFVAGVTAQGARGTYRAALNSEKHQDHVSLTVPLCGSGNLVEKLSPWFMDGENAYEVVKAMLLKKEPLLYVPIRLAGHTRHLPGPRVYLVERLIACENPFMVNQLAYSSSANGSLVGTTLQGKPIGMFFPYDIELVTGKQNILLRKYGRGGYHYTPFHYERDNTSCPEWMDDFEADPKGKYAQNLLKKLIGGDVTPVDQYMCGVDGKPISAYAFLMAKDGITKLADVEADVAARADDEGFITLKNNLYRLVWHVERKDVPYPKQSIFTINSVVQKDGVENTPPHYFTLGCKILTLTPRNKWSGVSDLSLKQKLLYTFYG... | 2.7.7.50; 3.4.19.12; 3.4.22.-; 3.4.22.69 | null | induction by virus of host autophagy [GO:0039520]; methylation [GO:0032259]; proteolysis [GO:0006508]; symbiont-mediated degradation of host mRNA [GO:0039595]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signa... | host cell membrane [GO:0033644]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020] | cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; endonuclease activity [GO:0004519]; G-quadruplex RNA binding [GO:0002151]; methyltransferase activity [GO:0008168]; omega peptidase activity [GO:0008242]; single-stranded RNA binding [GO:0003727]; zinc ion binding [GO... | PF16251;PF11501;PF11633;PF09401;PF19212;PF19211;PF19218;PF16348;PF19217;PF19213;PF08716;PF08717;PF08710;PF08715;PF01661;PF05409; | 1.10.8.1190;2.60.120.1680;3.10.20.350;3.10.20.540;6.10.140.2090;1.10.150.420;3.40.220.10;1.10.1840.10;3.40.220.20;1.10.8.370;3.30.70.3540;2.40.10.250;3.40.50.11020;2.40.10.10; | Coronaviruses polyprotein 1ab family | PTM: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: [Papain-like protease nsp3]: Host membrane; Multi-pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}.; SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane; Multi-pass membrane protein. Host cytoplasm. Note=Localizes in virally-induced cytoplasmic double-membrane vesic... | CATALYTIC ACTIVITY: [Papain-like protease nsp3]: 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:P0DTC1}... | null | null | null | null | FUNCTION: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {EC... | Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1) |
K9N7C7 | R1AB_MERS1 | MSFVAGVTAQGARGTYRAALNSEKHQDHVSLTVPLCGSGNLVEKLSPWFMDGENAYEVVKAMLLKKEPLLYVPIRLAGHTRHLPGPRVYLVERLIACENPFMVNQLAYSSSANGSLVGTTLQGKPIGMFFPYDIELVTGKQNILLRKYGRGGYHYTPFHYERDNTSCPEWMDDFEADPKGKYAQNLLKKLIGGDVTPVDQYMCGVDGKPISAYAFLMAKDGITKLADVEADVAARADDEGFITLKNNLYRLVWHVERKDVPYPKQSIFTINSVVQKDGVENTPPHYFTLGCKILTLTPRNKWSGVSDLSLKQKLLYTFYG... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 2.7.7.50; 3.1.13.-; 3.4.19.12; 3.4.22.-; 3.6.4.12; 3.6.4.13; 4.6.1.- | COFACTOR: [Uridylate-specific endoribonuclease nsp15]: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P0C6X7}; Note=Likely affects Nsp15 binding to RNA. {ECO:0000250|UniProtKB:P0C6X7}; COFACTOR: [RNA-directed RNA polymerase nsp12]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProt... | DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont-mediated degradation of host mRNA [GO:0039595]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of host ISG15-protein conjugation [GO:... | host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell membrane [GO:0033644]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020] | 3'-5'-RNA exonuclease activity [GO:0000175]; 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; endonuclease activity [GO:0004519]; G-quadruplex RNA binding [GO:0... | PF13087;PF13604;PF16251;PF11501;PF11633;PF06471;PF06460;PF09401;PF20631;PF20633;PF20632;PF19215;PF19216;PF19219;PF19212;PF19211;PF19218;PF16348;PF19217;PF19213;PF08716;PF08717;PF08710;PF08715;PF06478;PF01661;PF05409;PF00680; | 1.10.8.1190;2.60.120.1680;3.10.20.350;3.10.20.540;3.40.50.11580;6.10.140.2090;1.10.150.420;3.40.220.10;1.10.1840.10;3.30.160.820;3.40.220.20;1.10.8.370;3.30.70.3540;3.40.50.300;2.40.10.250;3.40.50.11020;2.40.10.10;3.40.50.150; | Coronaviruses polyprotein 1ab family | PTM: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: [Papain-like proteinase nsp3]: Host membrane; Multi-pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}.; SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane; Multi-pass membrane protein. Host cytoplasm. Note=Localizes in virally-induced cytoplasmic double-membrane ves... | CATALYTIC ACTIVITY: [RNA-directed RNA polymerase nsp12]: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; ... | null | null | null | null | FUNCTION: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {EC... | Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1) |
K9NBS6 | AAM_RHOER | MTEQNLHWLSATEMAASVASNNLSPNEIAEAMIQRVDAVNPSINAIVQFDREQVTRDAAELSRQQEAGEKLGPLHGVPFTIKDLTAVDGLPTTFGMKPMADNIATGNAVVVDRLRGAGGLFLGKTNTPESGYYGGTDNHLYGPTHNPWKLGNSAGGSSGGASAAVAAGLGPLAEGSDGAGSVRIPSALCGVVGLKPTTGVIPQTILAGRFYNWAYHGPITRTVADNALMLDIMAGPDNADPLSIERAETSYVEASKGDVKGLRVAWSPNLGLGHVDPEVLAVCLDALAAFEELGAQITEATPQWGNPSESMWSGIWVPGF... | 3.5.1.13; 3.5.1.14; 3.5.1.4 | null | amide catabolic process [GO:0043605]; glutaminyl-tRNAGln biosynthesis via transamidation [GO:0070681] | glutamyl-tRNA(Gln) amidotransferase complex [GO:0030956] | amidase activity [GO:0004040]; aminoacylase activity [GO:0004046]; aryl-acylamidase activity [GO:0047680]; glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity [GO:0050567]; indoleacetamide hydrolase activity [GO:0043864] | PF01425; | 3.90.1300.10; | Amidase family | null | null | CATALYTIC ACTIVITY: Reaction=a monocarboxylic acid amide + H2O = a monocarboxylate + NH4(+); Xref=Rhea:RHEA:12020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:35757, ChEBI:CHEBI:83628; EC=3.5.1.4; Evidence={ECO:0000269|PubMed:21073421}; CATALYTIC ACTIVITY: Reaction=an anilide + H2O = a carboxylate + aniline + H(+... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for Gly-para-nitroanilide {ECO:0000269|PubMed:21073421}; KM=0.48 mM for Leu-para-nitroanilide {ECO:0000269|PubMed:21073421}; KM=0.55 mM for Ala-para-nitroanilide {ECO:0000269|PubMed:21073421}; Vmax=104.5 umol/min/mg enzyme with Gly-para-nitroanilide as subs... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8. At low pH values the enzyme is rapidly inactivated, whereas in basic medium inactivation is rather slow. {ECO:0000269|PubMed:21073421}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. Shows a drastic decrease in activity above the optimal temperature. Is stable for 15 hours at 22 degrees Celsius and for 0.5 hour at 45 degrees Celsius. {ECO:0000269|PubMed:21073421}; | FUNCTION: Amidase with broad substrate specificity, catalyzing the hydrolysis of a wide range of N-substituted amides, and, to a lesser extent, the hydrolysis of non-substituted amides. Acid para-nitroanilides (4'-nitroacetanilide, Gly-pNA, Ala-pNA, Leu-pNA) are the best substrates for this enzyme. N-substituted acryla... | Rhodococcus erythropolis (Arthrobacter picolinophilus) |
K9UJK2 | TM175_CHAP6 | MVEAPEQSETGRIEAFSDGVFAIAITLLVLEIKVPQHKIVETVGLVSSLLSLWPSYLAFLTSFASILVMWVNHHRIFSLVARTDHAFFYWNGLLLMLVTFVPFPTALLAEYLIHPQARVAASVYAGIFLAIAIVFNRLWKHAATADRLLAQKADRHEVDAITKQYRFGPGLYLVAFALSFISVWLSVGVCFVLAIYFALRSNA | null | null | potassium ion transmembrane transport [GO:0071805]; protein homotetramerization [GO:0051289] | membrane [GO:0016020] | identical protein binding [GO:0042802]; potassium channel activity [GO:0005267]; proton channel activity [GO:0015252] | PF06736; | null | TMEM175 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000269|PubMed:28723891}. | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:28723891}; | null | null | null | null | FUNCTION: Potassium channel (PubMed:28723891). The channel is permeable for K(+), Rb(+) and Cs(+), while it is unable to conduct Na(+) (PubMed:28723891). {ECO:0000269|PubMed:28723891}. | Chamaesiphon minutus (strain ATCC 27169 / PCC 6605) |
K9USW8 | A1O_LOXGA | ADNRRPIWVMGHMVNSLAQIDEFVGLGSNSIETDVSFDKQANPEYTYHGIPCDCGRACLHSTKFNDFLKGLRKVTTPGDSKYLEKLILVVFDLKTGSLYDNQAYDAGTKLAKNLLQHYWNNGNNGGRAYIILSIPNLNHYKLITGFKETLKNEGHEELLEKVGTDFSGNDDISDVQKTYNKAGVTGHVWQSDGITNCLLRGLTRVKAAVANRDSGSGIINKVYYWTVDKRQSTRDTLDANVDGIMTNYPDITVEILNEAAYKKKFRIATYEDNPWETFKG | 4.6.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8I914}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8I914}; | defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | lyase activity [GO:0016829]; metal ion binding [GO:0046872]; phosphoric diester hydrolase activity [GO:0008081]; toxin activity [GO:0090729] | null | 3.20.20.190; | Arthropod phospholipase D family, Class II subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30563217}. | CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60652, ChEBI:CHEBI:15354, ChEBI:CHEBI:64583, ChEBI:CHEBI:143892; Evidence={ECO:0000305|PubMed:23770445}; CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphoethanolamine = an N... | null | null | null | null | FUNCTION: [Dermonecrotic toxin LgSicTox-alphaIC1]: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM)... | Loxosceles gaucho (Spider) |
L0DSL2 | NIR_THIND | MNDLNRLGRVGRWIAGAACLFLASAAHAEPGENLKPVDAMQCFDCHTQIEDMHTVGKHATVNCVHCHDATEHVETASSRRMGERPVTRMDLEACATCHTAQFNSFVEVRHESHPRLEKATPTSRSPMFDKLIAGHGFAFEHAEPRSHAFMLVDHFVVDRAYGGRFQFKNWQKVTDGMGAVRGAWTVLTDADPESSDQRRFLSQTATAANPVCLNCKTQDHILDWAYMGDEHEAAKWSRTSEVVEFARDLNHPLNCFMCHDPHSAGPRVVRDGLINAVVDRGLGTYPHDPVKSEQQGMTKVTFQRGREDFRAIGLLDTADS... | 1.7.2.2 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:16500161, ECO:0000269|PubMed:19393666, ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743}; Note=Binds 1 Ca(2+) ion per monomer. {ECO:0000269|PubMed:16500161, ECO:0000269|PubMed:19393666, ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22... | ammonium ion metabolic process [GO:0097164]; anaerobic electron transport chain [GO:0019645]; nitrate assimilation [GO:0042128] | outer membrane-bounded periplasmic space [GO:0030288] | calcium ion binding [GO:0005509]; heme binding [GO:0020037]; nitrite reductase (cytochrome, ammonia-forming) activity [GO:0042279] | PF02335; | 1.10.287.3080;1.20.140.10; | Cytochrome c-552 family | PTM: The thioether cross-link between Tyr-331 and Cys-333 may play a structural role in the active site cavity (PubMed:19393666). Besides, it may lower the pKa of the Tyr hydroxyl group (PubMed:19393666). An additional covalent bond between Tyr-331 and Gln-388 has been observed in some protein crystals, but this may be... | SUBCELLULAR LOCATION: Periplasm. | CATALYTIC ACTIVITY: Reaction=6 Fe(III)-[cytochrome c] + 2 H2O + NH4(+) = 6 Fe(II)-[cytochrome c] + 8 H(+) + nitrite; Xref=Rhea:RHEA:13089, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:28938, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.2; Evidence={E... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16700 uM for nitrite {ECO:0000269|PubMed:16500161}; KM=16400 uM for hydroxylamine {ECO:0000269|PubMed:16500161}; Vmax=4080 umol/min/mg enzyme toward nitrite {ECO:0000269|PubMed:16500161}; Vmax=45 umol/min/mg enzyme toward hydroxylamine {ECO:0000269|PubMed:16500161}... | PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation). | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-10 for nitrite reduction, and the optimum pH is 7 for sulfite reduction with only 20% residual activity at pH 7.8. {ECO:0000269|PubMed:16500161, ECO:0000269|PubMed:20944237}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius. {ECO:0000269|PubMed:16500161}; | FUNCTION: Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process (PubMed:16500161, PubMed:22281743). Has very low activity toward hydroxylamine (PubMed:16500161). Has even lower activity toward sulfite (PubMed:16500161, PubMed:22281743). Sulfite reductase activity is maximal at neutral pH... | Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2) |
L0E155 | MALA_MALAU | MAPTPKYTFTERAAAGNLSDAEILNSNNPTGSELPDESDVVVGGAGIHGLIYALHASKYKPNNLKISVIEKNTRPGYKIGESTLPIFYTWCKLHGISAAYLLRLFGLKDGLCFYFLDRENQGQYTDFCSVGAPGLVLASLQIERPMSELLFTILAQRNGVNVYHGREVDFKSTVVQGGGQGNKIAVSRGKYDSTPKTIDSALFVDATGRFRQFCSKKAPRHRFDGWNCNAFWGYFTAPKDESKIPFDLYEGDHTNHLCFPEGWVWVIRLPSWEGSLIANLMDMVTYILECADAGVPGDELPSSEELARMFGLKFQWVTSI... | 1.14.-.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:28777910}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:28777910}; | secondary metabolite biosynthetic process [GO:0044550] | null | flavin-dependent halogenase activity [GO:0140907]; monooxygenase activity [GO:0004497] | PF04820; | 3.50.50.60; | Flavin-dependent halogenase family | null | null | CATALYTIC ACTIVITY: Reaction=(+)-premalbrancheamide + 2 chloride + 2 FAD + 4 H(+) = (+)-malbrancheamide + 2 FADH2; Xref=Rhea:RHEA:62296, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:145651, ChEBI:CHEBI:145658; Evidence={ECO:0000269|PubMed:28777910}; PhysiologicalDirection=left... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7 uM for premalbrancheamide (to yield malbrancheamide B) {ECO:0000269|PubMed:28777910}; KM=7.5 uM for premalbrancheamide (to yield isomalbrancheamide B) {ECO:0000269|PubMed:28777910}; KM=4.4 uM for malbrancheamide B (to yield malbrancheamide) {ECO:0000269|PubMed:28... | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:28777910}. | null | null | FUNCTION: Flavin-dependent halogenase; part of the gene cluster that mediates the biosynthesis of malbrancheamide, a dichlorinated fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core (PubMed:23213353, PubMed:28777910, PubMed:31548667). The first... | Malbranchea aurantiaca |
L0E4H0 | PHQK_PENFE | MGSLGEEVQVIIVGLGIVGLAAAIECREKGHSVHAFEKSNILKSIGDCIGLQSNATRIIKRWGDGAVHEALRPWIVSSKEIRIHNSSGRLIIRQDLSEVCEQPNYLLPRSELIRVMYEHALKIGVEISLGVEVCEPSEDEEGASVVALTRDGERQIVRGDFIICSDGVHSKMRKAIMPQPVEPRPSGYAAFRALVDTETLKGDPEASWVFEGVEENDRFDVFFLSGAQIALQSCNKGKVFSWFCIHQDTRNLLDVWTSPADPNEMLDLIKVWPIGQRLWSVIRHTQPQKFINYPLLNHKPLDHWVSSHGRLILIGDAAHP... | 1.-.-.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:31904957}; | null | null | FAD binding [GO:0071949]; monooxygenase activity [GO:0004497] | PF01494; | 3.50.50.60; | PaxM FAD-dependent monooxygenase family | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=92.1 uM for paraherquamide K {ECO:0000269|PubMed:31904957}; KM=19.4 uM for paraherquamide L {ECO:0000269|PubMed:31904957}; | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:31904957}.; PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:31904957}. | null | null | FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of paraherquamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core (PubMed:23213353, PubMed:31904957). Within the pathway, phqK catalyzes spiroc... | Penicillium fellutanum |
L0L3V3 | FRE21_SPHLA | MAFLKKSLFLVLFLGLVSLSMGEREKREEEEEEEEENKEEEANEEGKGESEEKRGLVGTLLGHIGKAILGG | null | null | defense response to bacterium [GO:0042742]; innate immune response [GO:0045087]; regulation of defense response to virus [GO:0050688] | extracellular region [GO:0005576] | DNA binding [GO:0003677] | PF03032; | null | Frog skin active peptide (FSAP) family, Frenatin subfamily | PTM: Frenatin 2.3S is not amidated. {ECO:0000269|PubMed:24704757}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24704757}. | null | null | null | null | null | FUNCTION: [Frenatin 2.1S]: Antimicrobial peptide with potent activity against Gram-negative bacteria (PubMed:24704757). Shows immunostimulatory actions both in vitro and in vivo (PubMed:24704757, PubMed:25861850, PubMed:28526557). In vitro, is cytotoxic to non-small cell lung adenocarcinoma A549 cells (PubMed:24704757)... | Sphaenorhynchus lacteus (Orinoco lime treefrog) (Hyla lactea) |
L0N7N1 | KIF14_MOUSE | MSVHTSHSRHNIGSLEVSSSQKISASSGLVHSSRLELHLKADMSECENHDPFVNAGSKTIDINSTYVISACKKTRETPVTSDPRRLSLQRRATCGDRESSLLGSELGNRRTADTSLRLQRRHGRADYVGKWETLNPVGGNPGSDSASQASRTEAKGVNNDTRVLSSVVSVKDSNDTGLTRCKDPGPPVGASNEKVTVKDTNSRAPVGSQRQTEAMRSGHLVVQLTESKSDTPVSGGRNSHRGNAGKDTAKQVGTFGSSDTRTPVKCVLEHRWTPRHDPPPPKSPALSTPKNNGKDIPKHGSTFRSASSESRTPVKCVPEH... | null | null | activation of protein kinase activity [GO:0032147]; cell division [GO:0051301]; cell proliferation in forebrain [GO:0021846]; cerebellar cortex development [GO:0021695]; cerebellar granular layer structural organization [GO:0021685]; cerebellar Purkinje cell layer structural organization [GO:0021693]; cerebral cortex d... | cytosol [GO:0005829]; Flemming body [GO:0090543]; kinesin complex [GO:0005871]; membrane [GO:0016020]; microtubule [GO:0005874]; midbody [GO:0030496]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; spindle midzone [GO:0051233] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; PDZ domain binding [GO:0030165]; plus-end-directed microtubule motor activity [GO:0008574]; protein kinase binding [GO:0019901]; tubulin binding [GO:0015631] | PF00498;PF00225;PF16183; | 2.60.200.20;3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15058}. Cytoplasm {ECO:0000250|UniProtKB:Q15058}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q15058}. Midbody {ECO:0000250|UniProtKB:Q15058}. Note=Nuclear localization observed during interphase. Nuclear localization triggered by entry into mitosis. Cyt... | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=62 uM for ATP {ECO:0000269|PubMed:24949858}; KM=33 uM for ATP (in the presence of microtubule) {ECO:0000269|PubMed:24949858}; | null | null | null | FUNCTION: Microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity (PubMed:24949858). Plays a role in many processes like cell division, cytokinesis and also in cell proliferation and apoptosis (By similarity). During cytokinesis, targets to cen... | Mus musculus (Mouse) |
L0PIN3 | BRKP1_AGADC | MSFLKKSLFLVLFLGFVSFSICEEEKREDEEEENEREENKESEEKRNQEERPPGFTPFRVD | null | null | defense response [GO:0006952]; vasodilation [GO:0042311] | extracellular region [GO:0005576] | toxin activity [GO:0090729] | PF03032; | null | Frog skin active peptide (FSAP) family, Bradykinin-related peptide subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000255, ECO:0000269|PubMed:24394432}. | null | null | null | null | null | FUNCTION: [[Thr6]-bradykinin]: Induces relaxation of rat smooth muscle from tail artery (EC(50)=16.8 nM) and contraction of that from ileum (EC(50)=205 nM), urinary bladder (EC(50)=895 nM) and uterus (EC(50)=60.3 nM). Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2). {ECO:0000269|PubMed:24394432}.; FUNCTIO... | Agalychnis dacnicolor (Giant Mexican leaf frog) (Pachymedusa dacnicolor) |
L0PJV8 | BRKP1_AGACL | MSFLKKSLFLVLFLGLVSFSICEEEKRETEEEENEDEMDKESEEKRESPERPPGFTPFRVD | null | null | defense response [GO:0006952]; vasodilation [GO:0042311] | extracellular region [GO:0005576] | toxin activity [GO:0090729] | PF03032; | null | Frog skin active peptide (FSAP) family, Bradykinin-related peptide subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000255, ECO:0000269|PubMed:24394432}. | null | null | null | null | null | FUNCTION: [[Thr6]-bradykinin]: Induces relaxation of rat smooth muscle from tail artery (EC(50)=16.8 nM) and contraction of that from ileum (EC(50)=205 nM), urinary bladder (EC(50)=895 nM) and uterus (EC(50)=60.3 nM). Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2). {ECO:0000269|PubMed:24394432}.; FUNCTIO... | Agalychnis callidryas (Red-eyed tree frog) (Phyllomedusa callidryas) |
L0R8F8 | MIDUO_HUMAN | MAPWSREAVLSLYRALLRQGRQLRYTDRDFYFASIRREFRKNQKLEDAEARERQLEKGLVFLNGKLGRII | null | null | mitochondrial fission [GO:0000266]; mitochondrial large ribosomal subunit assembly [GO:1902775]; mitochondrial respiratory chain complex I assembly [GO:0032981]; positive regulation of mitochondrial translation [GO:0070131] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | mitochondrial large ribosomal subunit binding [GO:0140978] | PF05347; | null | Complex I LYR family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:28892042, ECO:0000269|PubMed:29083303, ECO:0000269|PubMed:30215512}. | null | null | null | null | null | FUNCTION: Assembly factor involved in the biogenesis of the mitochondrial-specific ribosomes (mitoribosomes) (PubMed:28892042, PubMed:30215512, PubMed:31666358). Specifically associates with intermediates of the mitochondrial ribosome large subunit (mt-LSU) and is required for proper ribosome assembly, possibly prevent... | Homo sapiens (Human) |
L0T905 | RSEA_MYCTU | MADPGSVGHVFRRAFSWLPAQFASQSDAPVGAPRQFRSTEHLSIEAIAAFVDGELRMNAHLRAAHHLSLCAQCAAEVDDQSRARAALRDSHPIRIPSTLLGLLSEIPRCPPEGPSKGSSGGSSQGPPDGAAAGFGDRFADGDGGNRGRQSRVRR | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250}; | regulation of DNA-templated transcription [GO:0006355] | cytoplasm [GO:0005737] | anti-sigma factor antagonist activity [GO:0043856]; metal ion binding [GO:0046872] | null | 1.10.10.1320; | Zinc-associated anti-sigma factor (ZAS) superfamily | PTM: Phosphorylated by PknB on Thr-39; can be dephosphorylated (at least in vitro) by PstP. Phosphorylation is the signal for subsequent degradation by the ClpC1-ClpP2 complex. {ECO:0000269|PubMed:20025669}.; PTM: Degraded following vancomycin treatment (surface stress) by a ClpC1-ClpP2 complex. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: An anti-sigma factor for extracytoplasmic function (ECF) sigma factor SigE. ECF sigma factors are held in an inactive form by an anti-sigma factor. {ECO:0000269|PubMed:18606740, ECO:0000269|PubMed:20025669}. | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
L0T911 | PBPB_MYCTU | MSRAAPRRASQSQSTRPARGLRRPPGAQEVGQRKRPGKTQKARQAQEATKSRPATRSDVAPAGRSTRARRTRQVVDVGTRGASFVFRHRTGNAVILVLMLVAATQLFFLQVSHAAGLRAQAAGQLKVTDVQPAARGSIVDRNNDRLAFTIEARALTFQPKRIRRQLEEARKKTSAAPDPQQRLRDIAQEVAGKLNNKPDAAAVLKKLQSDETFVYLARAVDPAVASAICAKYPEVGAERQDLRQYPGGSLAANVVGGIDWDGHGLLGLEDSLDAVLAGTDGSVTYDRGSDGVVIPGSYRNRHKAVHGSTVVLTLDNDIQF... | null | null | cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360] | plasma membrane [GO:0005886] | penicillin binding [GO:0008658] | PF03717;PF00905; | 3.30.450.330;3.40.710.10;3.90.1310.10; | Transpeptidase family | PTM: Cleaved by Rip1 in response to oxidative stress (H(2)O(2)), prevented by Wag31. Cleavage probably occurs near residues 102-103. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | null | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. | null | null | FUNCTION: Synthesis of cross-linked peptidoglycan from the lipid intermediates. {ECO:0000250, ECO:0000269|PubMed:19496931}. | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
L0TC47 | LIPV_MYCTU | MIIDLHVQRYGPSGPARVLTIHGVTEHGRIWHRLAHHLPEIPIAAPDLLGHGRSPWAAPWTIDANVSALAALLDNQGDGPVVVVGHSFGGAVAMHLAAARPDQVAALVLLDPAVALDGSRVREVVDAMLASPDYLDPAEARAEKATGAWADVDPPVLDAELDEHLVALPNGRYGWRISLPAMVCYWSELARDIVLPPVGTATTLVRAVRASPAYVSDQLLAALDKRLGADFELLDFDCGHMVPQAKPTEVAAVIRSRLGPR | 3.1.1.1 | null | cellular response to acidic pH [GO:0071468]; fatty acid catabolic process [GO:0009062] | null | carboxylesterase activity [GO:0106435]; fatty acid binding [GO:0005504]; hydrolase activity [GO:0016787]; lipase activity [GO:0016298] | PF12697; | 3.40.50.1820; | AB hydrolase superfamily | null | null | CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000269|PubMed:24234750}; CATALYTIC ACTIVITY: Reaction=a tetradecanoate ester + H2O = ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=714.28 uM for pNP-myristate {ECO:0000269|PubMed:24234750}; Note=kcat is 1312 sec(-1) with pNP-myristate as substrate. {ECO:0000269|PubMed:24234750}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. Retains nearly 60% enzyme activity at pH 6.0. The relative stability of purified enzyme is high at acidic pH and neutral pH (4.0-7.0) as compared to its relative stability at higher pH (9.0-10.0). {ECO:0000269|PubMed:24234750}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:24234750}; | FUNCTION: Lipase that displays broad substrate specificity and preferentially hydrolyzes p-nitrophenyl myristate in vitro. Also shows significant activity with pNP-butyrate (68%), pNP-octanoate (82%), pNP-decanoate (90%), and pNP-laurate (74%). Is probably involved in lipid catabolism. Is active at low pH, and might pl... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
L5KLU7 | S39A4_PTEAL | MAILAWLEPRPLLAVLVLVLTMRMAQPAHLLTLLSSGQGALDRVALGGLLNTLAARVHCTSGPCGKCLSVDDLLALGRPEEPGHLARLSAAAALYLSDPEGTCEDIRAGRWASRADHLLALLEGPKALAPGLSRLLQRIQAQTTGQPSAGEACVDPPQLLREAGVAGAPGSPGPVLATLLEHVGRGSCFHTLPTPQYFVDFVFQQSHGNTPNISVAELAALMQRLGVGGVTETHSDHHHQEKRVNRQGPTPLTAPNSSSDTWDTVCLSARDVMAVYGLSEQTGVTPEAWAQLSPALLQQQLSGACSPQPSHPAQNQLSQA... | null | null | intracellular zinc ion homeostasis [GO:0006882]; zinc ion import across plasma membrane [GO:0071578]; zinc ion transmembrane transport [GO:0071577] | apical plasma membrane [GO:0016324]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038] | identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monoatomic cation:bicarbonate symporter activity [GO:0140410]; zinc ion sensor activity [GO:0106219]; zinc ion transmembrane transporter activity [GO:0005385] | PF21116;PF02535;PF18292; | null | ZIP transporter (TC 2.A.5) family | PTM: The extracellular N-terminal ectodomain is cleaved when cells are Zn(2+) deficient, N-terminally cleaved SLC39A4 is internalized at a faster rate. {ECO:0000250|UniProtKB:Q78IQ7}.; PTM: Under excess Zn(2+) conditions, SLC39A4 on the cell surface is rapidly endocytosed, ubiquitinated and degraded. {ECO:0000250|UniPr... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q78IQ7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A0H3LM39}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q78IQ7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A0H3LM39}. Apical cell membrane {ECO:0000250|UniProtKB:Q78IQ7}; Multi-pass ... | CATALYTIC ACTIVITY: Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351, ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:27321477}; | null | null | null | null | FUNCTION: Selective transporter that mediates the uptake of Zn(2+) (PubMed:27321477). Plays an essential role for dietary zinc uptake from small intestine (By similarity). The Zn(2+) uniporter activity is regulated by zinc availability. Exhibits also polyspecific binding and transport of Cu(2+), Cd(2+) and possibly Ni(... | Pteropus alecto (Black flying fox) |
L7N1X6 | FBW15_MOUSE | MAIHLPCLPMMKILSYLDAYSLLQAAQVNKDWNELASSDVLWRKLCQKRWLYCDMDTLQLQGKETWKQFFIDRIWQERAKFRAKAKDFTYKEIPLMCGLFGYACYISGCGLTRKGQDKSVVCMVNSKNTISTWDVHKSVITWKSPEQPASIKLLTTLPEMHIAVTVDIQSTIKLWDCHNREALATNNLKSPCKSLKAVFTKDGPIVLIGDTLGNIHIFRIPDLYLISTVNVLPYGFDGIYCSPQKKWVLLSKKHPHILPKVFYMSSFLRTSEFSAPVSTVLKLSLYERVFWTPRREDRITLMSRSGFPQVKMFETYDIKL... | null | null | protein ubiquitination [GO:0016567] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634] | null | PF12937; | 1.20.1280.50;2.130.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18094359, ECO:0000269|PubMed:23319590}. Endoplasmic reticulum {ECO:0000269|PubMed:18094359}. Nucleus {ECO:0000269|PubMed:23319590}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:23319590}. | null | null | FUNCTION: Substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Promotes KAT7 ubiquitination and subsequent degradation in collaboration with MAP2K1 kinase, leading to reduced histone H3K14 acetylation and increased cell proliferation. {ECO:0000269|PubMed:23319590}. | Mus musculus (Mouse) |
L7N6F8 | DEP23_DERPT | MKFNIIIVFISLAILVHSSYAANDNDDDPTTTVHPTTTEQPDDKFECPSRFGYFADPKDPHKFYICSNWEAVHKDCPGNTRWNEDEETCT | null | null | null | cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576] | IgE binding [GO:0019863] | PF01607; | 2.170.140.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23460742}. Endoplasmic reticulum {ECO:0000269|PubMed:23460742}. Cytoplasmic vesicle {ECO:0000269|PubMed:23460742}. Note=Localizes to the peritrophic matrix ligning the midgut and on the surface of fecal pellets. {ECO:0000269|PubMed:23460742}. | null | null | null | null | null | FUNCTION: Does not bind chitin in vitro. {ECO:0000269|PubMed:26602749}. | Dermatophagoides pteronyssinus (European house dust mite) |
L7NCQ3 | TBSYN_GARMA | MAPAMDSAQNGHQSRGSANVLAIGTANPPNVILQEDYPDFYFKVTNSEHLTDLKEKFKRICVKSKTRKRHFYLTEQILKENPGIATYGAGSLDSRQKILETEIPKLGKEAAMVAIQEWGQPVSKITHVVFATTSGFMMPGADYSITRLLGLNPNVRRVMIYNQGCFAGGTALRVAKDLAENNKGARVLVVCAENTAMTFHGPNENHLDVLVGQAMFSDGAAALIIGANPNLPEERPVYEMVAAHQTIVPESDGAIVAHFYEMGMSYFLKENVIPLFGNNIEACMEAAFKEYGISDWNSLFYSVHPGGRAIVDGIAEKLGL... | 2.3.1.220 | null | benzoyl-CoA metabolic process [GO:1901787]; malonyl-CoA metabolic process [GO:2001293]; polyketide biosynthetic process [GO:0030639] | null | acyltransferase activity [GO:0016746]; tetrahydroxybenzophenone synthase activity [GO:0047181]; trihydroxybenzophenone synthase activity [GO:0102735] | PF02797;PF00195; | 3.40.47.10; | Thiolase-like superfamily, Chalcone/stilbene synthases family | null | null | CATALYTIC ACTIVITY: Reaction=benzoyl-CoA + 2 H(+) + 3 malonyl-CoA = 2,4,6-trihydroxybenzophenone + 3 CO2 + 4 CoA; Xref=Rhea:RHEA:35143, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57369, ChEBI:CHEBI:57384, ChEBI:CHEBI:77765; EC=2.3.1.220; Evidence={ECO:0000269|PubMed:22390826}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.65 uM for benzoyl-CoA {ECO:0000269|PubMed:22390826}; KM=16.38 uM for malonyl-CoA {ECO:0000269|PubMed:22390826}; Note=kcat is 2.97 min(-1) with benzoyl-CoA as substrate. kcat is 3.49 min(-1) with malonyl-CoA as substrate.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:22390826}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:22390826}; | FUNCTION: Type III polyketide synthase involved in the biosynthesis of benzophenones and xanthones. Produces mainly 2,4,6-trihydroxybenzophenone together with minor amounts of tetraketide lactone, triketide lactone and diketide lactone. The preferred substrate is benzoyl-CoA, but can also use acetyl-CoA, phenylacetyl-C... | Garcinia mangostana (Mangosteen) |
L7R9Z0 | EOBI_PETHY | MDKRTCNSQDVEVRKGPWTMEEDLILINYIANHGEGVWNSLARSAGLKRTGKSCRLRWLNYLRPDVRRGNITPEEQLLIMELHAKWGNRWSKIAKHLPGRTDNEIKNYWRTRIQKHIKQADQNMKKPSKCEQNDQKAISTSQASTGPTDTIDSYSPSSYTENTNNNMENITFQGNFPTETNENIWSMEDLWSLQLLNDATN | null | null | circadian rhythm [GO:0007623]; green leaf volatile biosynthetic process [GO:0010597]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of phenylpropanoid metabolic process [GO:2000762]; shikimate metabolic process [GO:0019632] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976] | PF00249; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:23275577}. | null | null | null | null | null | FUNCTION: MYB-type transcription factor controlling the production of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) by regulating the expression of ODO1, a key regulator of the shikimate pathway, and ... | Petunia hybrida (Petunia) |
L7X3S1 | MSH_PAPSO | MRTESIKTNRPMDLLLQYLQPISVALVVIALVWNYGRRNPTKKLAPEASGGRPIMGHLHLFNDGELTHRKLGAMADTYGPVFNIRFGSHKTLVVSDWEIVKECFTTNDKLFSNRPGTLGIKLMFYDADSVGYAPYGAYWRDLRKISTLKLLSNHRIDTIKHLRSSEVESCFESLYSQWGNGEKSGEFAPVRMDSWLGDLTFNVVARIVAGKKNFSANGDVGAQRYKAAMDEAMRLMRFFAFSDVIPSLSWLDNLRGLVREMKKCASEIDSIMATWVEEHRVKRNSGGNSQLEHDFIDVCLDIMEHSSLPGDDPDLVVKST... | 1.14.14.97 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | isoquinoline alkaloid biosynthetic process [GO:0033075] | membrane [GO:0016020] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; methyltetrahydroprotoberberine 14-monooxygenase activity [GO:0047084] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(S)-cis-N-methylcanadine + O2 + reduced [NADPH--hemoprotein reductase] = allocryptopine + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:23684, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17390, ChE... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.5 uM for cis-N-methylcanadine {ECO:0000269|Ref.2}; KM=62.5 uM for NADPH {ECO:0000269|Ref.2}; | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:23313486, ECO:0000269|Ref.2}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|Ref.2}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|Ref.2}; | FUNCTION: Involved in the biosynthesis of the isoquinoline alkaloid sanguinarine (PubMed:23313486, Ref.2). Catalyzes the conversion of N-methylated protoberberine alkaloids N-methylstylopine and N-methylcanadine into protopine and allocryptopine, respectively (PubMed:23313486, Ref.2). Can also use (S)-cis-N-methyltetra... | Papaver somniferum (Opium poppy) |
L7YAI7 | B4GA1_DANRE | MHFSKKCSVFKVVLSALLIVALLQLLYLSFLSKLHGKQQRYKYSELFGSKKNANQGEKNPRREHLRYSLSTGGIFDGSGQYRVYKNLIKSDFSTNQKPGADPRSHHLALATHTTINNLHHLESLLERWKNPISVAIFANGEDVKFATAIIYALSLFCPQVQALVDFHLVCHSGEMATFPDQDREHFVGLQEMGCPAVFAKLESHRDKYKNYAIGSNVSYPNNLLRNVARGGTDAAYILVIDIDMIPSANLHHQFVTMLMKREPAADEVLVLPAFEIRHIRKMPASKPELVQLYQVGEVRPFYDELCSRCQAPTNYSLWVN... | 2.4.1.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O43505}; | muscle cell development [GO:0055001]; protein glycosylation [GO:0006486]; protein O-linked mannosylation [GO:0035269] | Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139] | glucuronosyltransferase activity [GO:0015020]; metal ion binding [GO:0046872] | PF13896; | null | Glycosyltransferase 49 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O43505, ECO:0000250|UniProtKB:Q8BWP8}; Single-pass type II membrane protein. Note=Localizes near the trans-Golgi apparatus. {ECO:0000250|UniProtKB:O43505}. | CATALYTIC ACTIVITY: Reaction=3-O-[beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + UDP-alpha-D-glucuronate = 3-O-[beta-D-GlcA-(1->3)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + H(... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:O43505, ECO:0000250|UniProtKB:Q8BWP8}. | null | null | FUNCTION: Beta-1,4-glucuronyltransferase involved in O-mannosylation of alpha-dystroglycan (DAG1) (PubMed:23359570). Transfers a glucuronic acid (GlcA) residue onto a xylose (Xyl) acceptor to produce the glucuronyl-beta-1,4-xylose-beta disaccharide primer, which is further elongated by LARGE, during synthesis of phosph... | Danio rerio (Zebrafish) (Brachydanio rerio) |
L8B068 | MALA_HALJT | MHHPGPPRFVATGDEVELAPRDPDPTATYTWRLTQAPAQSTVSLGDDPVEHFVPDAPGRYVVRLTAPDGEHDLTVRAFPGTLESSGTHTSGRSGGHSGGVSGGRSGPGRSGSGEYTQAGDGSDGGGGGQPRLTLRPDIEGDEAVVRADCSPHPEGTETAADLAVEFLLDDRDDVDADAVTRDGTALRIPLDALPERARIHAVAVGNHGYSVPDAVEFTRGGDGVETVTSGAGVAARRPYDAPAWAEDSVIYEIYVRTFAGERDESPFDAITDRLDYLDSLGVDAIWLTPVLQNDHAPHGYNITDFFEIASDLGTRADYER... | 3.2.1.1 | null | amylopectin catabolic process [GO:2000897]; carbohydrate catabolic process [GO:0016052]; glycogen catabolic process [GO:0005980]; glycogen metabolic process [GO:0005977]; starch catabolic process [GO:0005983] | cytoplasm [GO:0005737] | alpha-1,4-glucosidase activity [GO:0004558]; alpha-amylase activity [GO:0004556] | PF00128; | 3.20.20.80;2.60.40.1180;2.60.40.10; | Glycosyl hydrolase 13 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23391916}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:23391916}; | null | PATHWAY: Glycan degradation; starch degradation. {ECO:0000250|UniProtKB:Q8A1G3}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 in 2.0 M NaCl. Stable over a range of pH 5.7-9.2. {ECO:0000269|PubMed:23391916}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius in 2.0 M NaCl and at pH 6.5. Relatively stable up to 55 degrees Celsius. {ECO:0000269|PubMed:23391916}; | FUNCTION: Alpha-amylase that cleaves starch into oligosaccharides, the first step in starch degradation (By similarity). Endo-acting enzyme which prefers a linear polysaccharide to branched polysaccharides hydrolyzing alpha-1,4 glucosidic bonds efficiently. Has also transglycosylation activity, but does not act on alph... | Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1) |
L8E946 | UNC42_CAEEL | MSDNLLNGANGASTVSQFQEKVKDLGVSLHDFTAYYPSSLDTVSASLRPISDPSSDGAFKKIKTEGLGGSVFGSSIAGVTNTPARLCSLERPESERLNSRRRHRTTFTQEQLQELDAAFQKSHYPDIYVREELARITKLNEARIQVWFQNRRAKHRKHEKQLNKAINPPHSFLSNPANTLMRQGMYPAALNRDGFWYQSYQRPMPYPTASPSYSNSFTNPIANFGHSITSFQADDEFYQKSLALRMTTTPSAATAATSLANINYQQTQPSEASTNPPSI | null | null | axon development [GO:0061564]; axon guidance [GO:0007411]; larval locomotory behavior [GO:0008345]; neuron differentiation [GO:0030182]; neuron fate specification [GO:0048665]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of gene expression [GO:0010468]; regulation of transcription... | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF00046; | 1.10.10.60; | Paired homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|RuleBase:RU000682}. | null | null | null | null | null | FUNCTION: Probable transcription factor (PubMed:11222641, PubMed:34165428, PubMed:9216999). Required for initial outgrowth and pathfinding of axon growth cones along the ventral nerve cord (VNC) (PubMed:11222641, PubMed:34165428, PubMed:9216999). Involved in specifying neuron identity, in concert with nuclear hormone r... | Caenorhabditis elegans |
M0QWB7 | ASCL5_MOUSE | MNSNFCRALVDRGPPGGMQLGVVAPAGQTPLAATEPLSNVPFLLYPGHSEPPYYDAYTGVFPYVPFPGAFGVYDYPFEPAFIQKRNERERQRVKCVNEGYARLRGHLPGALTEKRLSKVETLRAAIRYIKYLQELLSATPDGAPPPATSPPPAHTGHSNVPQPSSLVAESSGSPFSSSPFLESEEPSL | null | null | ameloblast differentiation [GO:0036305]; amelogenesis [GO:0097186]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; protein... | PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:30426815). Probably binds E-box motifs 5'-CANNTG-3' in complex with transcription factor TCF3/E12 (PubMed:30426815). Negatively modulates transcription of target genes such as CDH1/E-cadherin, perhaps by recruiting the PRC2 repressive complex to regulatory elements (PubMed:3042681... | Mus musculus (Mouse) |
M0R2J8 | DCDC1_HUMAN | MAKTGAEDHREALSQSSLSLLTEAMEVLQQSSPEGTLDGNTVNPIYKYILNDLPREFMSSQAKAVIKTTDDYLQSQFGPNRLVHSAAVSEGSGLQDCSTHQTASDHSHDEISDLDSYKSNSKNNSCSISASKRNRPVSAPVGQLRVAEFSSLKFQSARNWQKLSQRHKLQPRVIKVTAYKNGSRTVFARVTVPTITLLLEECTEKLNLNMAARRVFLADGKEALEPEDIPHEADVYVSTGEPFLNPFKKIKDHLLLIKKVTWTMNGLMLPTDIKRRKTKPVLSIRMKKLTERTSVRILFFKNGMGQDGHEITVGKETMKK... | null | null | cell cycle [GO:0007049]; cell division [GO:0051301]; intracellular signal transduction [GO:0035556]; regulation of mitotic cytokinesis [GO:1902412] | cytoplasm [GO:0005737]; Flemming body [GO:0090543]; microtubule [GO:0005874]; midbody [GO:0030496]; mitotic spindle [GO:0072686] | carbohydrate binding [GO:0030246]; microtubule binding [GO:0008017] | null | 2.80.10.50;3.10.20.230; | null | null | SUBCELLULAR LOCATION: Midbody, Midbody ring {ECO:0000269|PubMed:22159412}. Midbody {ECO:0000269|PubMed:22159412}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:22159412}. Note=Associated with microtubules, in particular, with stabilized microtubules of the mitotic spindle during metaphase and with midbody microt... | null | null | null | null | null | FUNCTION: Microtubule-binding protein which plays an important role in mediating dynein-dependent transport of RAB8A-positive vesicles to the midbody during cytokinesis (PubMed:22159412). {ECO:0000269|PubMed:22159412}. | Homo sapiens (Human) |
M0R4F8 | DNMBP_RAT | MEPGSVVRAIFDFCPSVSEELPLFVGDVIEVLTVVDEFWLLGKKEDVTGQFPSSFVEIVTIPSLKEGERLFVCTCDFISREPNSLSLHRGDLVIIDGTPTAGWLQGRSSLGARGFFPSSCIHELCLSSQSRQWHSQNMLLQVPEYSMGQARALMGLSAQLDEELDFREGDVITIIGVPEPGWFEGELEGRRGIFPEGFVELLGPLRTADESVNAGSGDDSTLNDEVDVSPEEVESEGDEDDQQAGTYGIALYRFQALESNELDFEVGDKIRILGTLEDGWLEGRLKGKTGIFPHRFVKLCPSNRSEETMALPQGDSFPKN... | null | null | cilium assembly [GO:0060271]; intracellular signal transduction [GO:0035556]; regulation of cell shape [GO:0008360] | cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; Golgi apparatus [GO:0005794]; Golgi stack [GO:0005795]; presynapse [GO:0098793]; synapse [GO:0045202] | guanyl-nucleotide exchange factor activity [GO:0005085] | PF03114;PF00621;PF00018;PF07653;PF14604; | 1.20.1270.60;1.20.900.10;2.30.30.40; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6XZF7}. Golgi apparatus, Golgi stack {ECO:0000250|UniProtKB:Q6TXD4}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6TXD4}. Synapse {ECO:0000269|PubMed:14506234}. Cell junction {ECO:0000250|UniProtKB:Q6XZF7}. Note=Localizes to the apical junction, colocalizes wit... | null | null | null | null | null | FUNCTION: Plays a critical role as a guanine nucleotide exchange factor (GEF) for CDC42 in several intracellular processes associated with the actin and microtubule cytoskeleton. Regulates the structure of apical junctions in epithelial cells (By similarity). Participates in the normal lumenogenesis of epithelial cell ... | Rattus norvegicus (Rat) |
M0R5D6 | RN157_RAT | MGALTSRQHAGVEEVDIPSNSVYRYPPKSGSYFASHFIMGGEKFDCTHPEGYLFGENSDLNFLGNRPVSFPYAAPPPHEPVKTLRSLINIRKDTLRLVKCAEEVKSHGEEAGKAKVHYNVEFTFDTDARVAITIYYQATEEFQNGIASYIPKDNSLQSETVHYKRGVCQQFCLPSHTVDPSEWAEEELGFDLDREVYPLVVHAVVDEGDEYFGHCHVLLGTFEKHSDGTFCVKPLKQKQVWDGVTYLLQEDYGIENKSNTQDFKVAEDDVRDNSAECVVCLSDVRDTLILPCRHCASCNVHCADTLRYQANNCPICRLPF... | 2.3.2.27 | null | negative regulation of apoptotic process [GO:0043066]; positive regulation of dendrite extension [GO:1903861]; protein ubiquitination [GO:0016567] | cell body [GO:0044297]; cytoplasm [GO:0005737] | metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630] | PF13920; | 3.30.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25342469}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q96PX1}; | null | null | null | null | FUNCTION: E3 ubiquitin ligase that ubiquitinates APBB1 for its degradation by the proteasome and thus prevents apoptosis and promotes survival of neurons (By similarity). Has a dual role in neurons as it is also required for dendrite growth and maintenance for which its ligase activity is not critical (By similarity). ... | Rattus norvegicus (Rat) |
M0R6D8 | MNX1_RAT | MEKSKNFRIDALLAVDPPRAASTQSAPLALVTSLAATPSGPGRGGSGGGGTSSGASRSCSPASSEATAAPGDRLRAESPSPPRLLTAHCALLPKPGFLGAGGGGGAAGGPGTPHHHAHPGAAAAAAAAAAAAAAGGLALGLHPGGAQGGAGLPAQAALYGHPVYSYSAAAAAAALAGQHPALSYSYPQVQGAHPAHPADPIKLGAGTFQLDQWLRASTAGMILPKMPDFSSQAQSNLLGKCRRPRTAFTSQQLLELEHQFKLNKYLSRPKRFEVATSLMLTETQVKIWFQNRRMKWKRSKKAKEQAAQEAEKQKGSGGGA... | null | null | cell morphogenesis involved in neuron differentiation [GO:0048667]; central nervous system development [GO:0007417]; central nervous system neuron differentiation [GO:0021953]; diaphragm development [GO:0060539]; dorsal/ventral neural tube patterning [GO:0021904]; endocrine pancreas development [GO:0031018]; motor neur... | chromatin [GO:0000785]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00046; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9QZW9}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:18539116). Recognizes and binds to the regulatory elements of target genes, such as visual system homeobox CHX10, negatively modulating transcription (By similarity). Plays a role in establishing motor neuron identity, in concert with LIM domain transcription factor LMO4 (By simil... | Rattus norvegicus (Rat) |
M0R7T6 | RBM24_RAT | MHTTQKDTTYTKIFVGGLPYHTTDASLRKYFEVFGDIEEAVVITDRQTGKSRGYGFVTMADRAAAERACKDPNPIIDGRKANVNLAYLGAKPRIMQPGFAFGVQQLHPALIQRPFGIPAHYVYPQAFVQPGVVIPHVQPTAAAASTTPYIDYTGAAYAQYSAAAAAAAAAAAYDQYPYAASPAATGYVTTGGYSYAVQQPITAAAPGTAAAAAAAAAAAAAFGQYQPQQLQTDRMQ | null | null | 3'-UTR-mediated mRNA destabilization [GO:0061158]; cell differentiation [GO:0030154]; DNA damage response [GO:0006974]; endocardial cushion development [GO:0003197]; mRNA destabilization [GO:0061157]; mRNA processing [GO:0006397]; mRNA stabilization [GO:0048255]; negative regulation of cytoplasmic translation [GO:20007... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA 3'-UTR binding [GO:0003730]; mRNA CDS binding [GO:1990715]; pre-mRNA intronic binding [GO:0097157]; sequence-specific mRNA binding [GO:1990825] | PF00076; | 3.30.70.330; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6GQD3}. Cytoplasm {ECO:0000250|UniProtKB:D3Z4I3}. | null | null | null | null | null | FUNCTION: Multifunctional RNA-binding protein involved in the regulation of pre-mRNA splicing, mRNA stability and mRNA translation important for cell fate decision and differentiation (PubMed:27289039). Plays a major role in pre-mRNA alternative splicing regulation (By similarity). Mediates preferentially muscle-specif... | Rattus norvegicus (Rat) |
M0R7Z9 | PLIN5_RAT | MDQRGKDTTLALHSRMSGDQTAQDPGSSLGELDQHNVVKRVVALPLVRATCTAVSGAYNSAKDRHPLLGSACRFAEHCVCSVATCALDHAQPLLEHLQPKLATVNDLACRGLDKLEEKLPFLQQPSDTVVTSAKDAVAKSVTGVVDLAQRGRRWSGELRRSVSQAMDTVLRRSVSQAMDTVLGKSEELVDHFLPMTEAELVALATESQGPEVGSVEEQRQKQGYFVRLGSLSARLRHLAYQHSLGKLRESKHRTQEMLAQLQKTLELIQHMQSRASPTPTFHHPKVQELCGDWSPCLENGYRHSQVELETLALSRSLTLE... | null | null | lipid droplet organization [GO:0034389]; lipid storage [GO:0019915]; mitochondrion localization [GO:0051646]; negative regulation of fatty acid beta-oxidation [GO:0031999]; negative regulation of lipase activity [GO:0060192]; negative regulation of lipid catabolic process [GO:0050995]; negative regulation of peroxisome... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; lipid droplet [GO:0005811]; mitochondrion [GO:0005739] | identical protein binding [GO:0042802]; lipase binding [GO:0035473] | PF03036; | 1.20.120.340;3.30.720.170; | Perilipin family | PTM: Phosphorylated by PKA. Phosphorylated on serine in skeletal muscle at rest or upon lipolytic stimulation. {ECO:0000269|PubMed:24303154}. | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:21885430, ECO:0000269|PubMed:22127648}. Cytoplasm {ECO:0000250|UniProtKB:Q8BVZ1}. Mitochondrion {ECO:0000269|PubMed:21885430, ECO:0000269|PubMed:22127648}. Note=Lipid droplet surface-associated. Exchanges between lipid droplets and the cytoplasm. {ECO:0000250|UniP... | null | null | null | null | null | FUNCTION: Lipid droplet-associated protein that maintains the balance between lipogenesis and lipolysis and also regulates fatty acid oxidation in oxidative tissues. Recruits mitochondria to the surface of lipid droplets and is involved in lipid droplet homeostasis by regulating both the storage of fatty acids in the f... | Rattus norvegicus (Rat) |
M0R8L2 | SPXN_RAT | MKGPSILAVAALALLLVLSVLENSSGAPQRLSEKRNWTPQAMLYLKGAQGHRFISDQSRRKELADRPPPERRNPNLQLLTLPEAAALFLASLEKPQKDEGGDFDKSKLLEDRRFYW | null | null | long-chain fatty acid import into cell [GO:0044539]; negative regulation of appetite [GO:0032099]; positive regulation of gastro-intestinal system smooth muscle contraction [GO:1904306]; positive regulation of transcription by RNA polymerase II [GO:0045944] | cytoplasm [GO:0005737]; dense core granule [GO:0031045]; extracellular space [GO:0005615]; transport vesicle [GO:0030133] | neuropeptide hormone activity [GO:0005184]; type 2 galanin receptor binding [GO:0031765]; type 3 galanin receptor binding [GO:0031766] | PF15171; | null | Spexin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Secreted, extracellular space {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Note=Secreted via the classical ER/Golgi-dependent pathway into the extracellular medium largely as a full-length protein without the signal peptide, and not as a hydrolyzed a... | null | null | null | null | null | FUNCTION: Plays a role as a central modulator of cardiovascular and renal function and nociception. Also plays a role in energy metabolism and storage. Inhibits adrenocortical cell proliferation with minor stimulation on corticosteroid release (PubMed:20045034, PubMed:22038051). {ECO:0000269|PubMed:20045034, ECO:000026... | Rattus norvegicus (Rat) |
M0R8U1 | DYH5_RAT | MFRIGRRQLWKQSVTRVLTQRLKEEKEAKRARLDGRHDYLFAIVASCLDLNKPEVEDALLEGNQIERIDQLFAVGGLRHLMFYYQDVEGAEAGQFGSSGGVNPASGKMKKPKVFVTEGKDVALMGACVFFTRADPSKAITAENIHREVSFNTLDTADGGLLNSVRRLLSDIFIPALRASSHGWGELEGLQDASSIQQEFLSSLEGFVGILSGAQNSLKEKVNLQKCDIVELKSLKEPMDYLALASNPETVEKVECCMRVWIKQMEQILAENNQLRKEADDVGPRAELEHWKKRLSKFNYLLDQLKSPDVKAVLAMLAAAK... | null | null | cilium assembly [GO:0060271]; cilium movement [GO:0003341]; cilium movement involved in cell motility [GO:0060294]; determination of left/right symmetry [GO:0007368]; epithelial cilium movement involved in extracellular fluid movement [GO:0003351]; establishment of localization in cell [GO:0051649]; flagellated sperm m... | 9+0 motile cilium [GO:0097728]; 9+2 motile cilium [GO:0097729]; axonemal dynein complex [GO:0005858]; axoneme [GO:0005930]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; microtubule [GO:0005874]; motile cilium [GO:0031514]; outer dynein arm [GO:0036157] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; dynein intermediate chain binding [GO:0045505]; dynein light intermediate chain binding [GO:0051959]; microtubule motor activity [GO:0003777]; minus-end-directed microtubule motor activity [GO:0008569] | PF12774;PF12775;PF12780;PF17857;PF08385;PF08393;PF17852;PF12777; | 1.10.287.2620;1.10.472.130;1.10.8.710;1.20.58.1120;1.20.920.20;1.20.920.30;1.20.140.100;3.20.180.20;3.40.50.300; | Dynein heavy chain family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q8TE73}. | null | null | null | null | null | FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required for structural and functional integrity of the cilia of ependymal cells lining the brain ventricles... | Rattus norvegicus (Rat) |
M0RC99 | RAB5A_RAT | MANRGATRPNGPNTGNKICQFKLVLLGESAVGKSSLVLRFVKGQFHEFQESTIGAAFLTQTVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNEESFSRAKNWVKELQRQASPNIVIALSGNKADLANKRAVDFQEAQSYADDNSLLFMETSAKTPMNVNEIFMAIAKKLPKNEPQNPGANSARGRGVDLTEPAQPARSQCCSN | 3.6.5.2 | null | amyloid-beta clearance by transcytosis [GO:0150093]; canonical Wnt signaling pathway [GO:0060070]; early endosome to late endosome transport [GO:0045022]; endocytosis [GO:0006897]; endosome organization [GO:0007032]; intracellular protein transport [GO:0006886]; phagocytosis [GO:0006909]; positive regulation of exocyto... | actin cytoskeleton [GO:0015629]; axon [GO:0030424]; axon terminus [GO:0043679]; cytoplasm [GO:0005737]; cytoplasmic side of early endosome membrane [GO:0098559]; cytosol [GO:0005829]; dendrite [GO:0030425]; early endosome [GO:0005769]; early phagosome [GO:0032009]; endocytic vesicle [GO:0030139]; endomembrane system [G... | G protein activity [GO:0003925]; GDP binding [GO:0019003]; GDP-dissociation inhibitor binding [GO:0051021]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; guanyl nucleotide binding [GO:0019001] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | PTM: Phosphorylation of Ser-84 in the switch II region by LRRK2 prevents the association of RAB regulatory proteins, including RAB GDP dissociation inhibitors GDI1 and GDI2. {ECO:0000250|UniProtKB:P20339}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20339}; Lipid-anchor {ECO:0000250|UniProtKB:P20339}; Cytoplasmic side {ECO:0000250|UniProtKB:P18066}. Early endosome membrane {ECO:0000250|UniProtKB:P20339}; Lipid-anchor {ECO:0000250|UniProtKB:P20339}. Melanosome {ECO:0000250|UniProtKB:P20339}. Cytoplasmic ve... | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P20339}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|Uni... | null | null | null | null | FUNCTION: Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Active GTP-bound... | Rattus norvegicus (Rat) |
M1C146 | ATG8C_SOLTU | MAKSSFKLEHPLERRQAEAARIREKYPDRIPVIVEKAERSDIPDIDKKKYLVPADLTVGQFVYVVRKRIKLSAEKAIFIFVKNILPPTAAMMSAIYEEHKDEDGFLYMTYSGENTFGSF | null | null | autophagosome assembly [GO:0000045]; autophagosome maturation [GO:0097352]; cellular response to nitrogen starvation [GO:0006995]; defense response to fungus [GO:0050832] | autophagosome membrane [GO:0000421]; cytoplasmic vesicle [GO:0031410]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; plant-type vacuole membrane [GO:0009705] | phosphatidylethanolamine binding [GO:0008429]; ubiquitin protein ligase binding [GO:0031625] | PF02991; | null | ATG8 family | PTM: The C-terminal 2 residues are removed by ATG4 to expose Gly-117 at the C-terminus (By similarity). The C-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin (Probable). The phosphatidylethanolamine amidated glycine is required for autophagosome formatio... | SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:26765567, ECO:0000269|PubMed:29932422}; Lipid-anchor {ECO:0000250|UniProtKB:P38182}. Vacuole membrane {ECO:0000269|PubMed:29932422}; Lipid-anchor {ECO:0000250|UniProtKB:P38182}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8LEM4}. | null | null | null | null | null | FUNCTION: Ubiquitin-like modifier involved in autophagosomes formation (Probable). May mediate the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton (Probable). ATG8CL-mediated selective autophagy contributes to defense against the fungal pathogen Phytophtora infestans (PubMed:26765567, Pub... | Solanum tuberosum (Potato) |
M1J8U6 | IFI4E_PRUDO | MATEVAAAVPPPQLDAEENSGLEAAAAEAKIQPSSGPHKLERKWTFWFDNQSKPKQGAAWGSSLRKAYTFETVQEFWCLYDQVFKPSKFPPNADFHLFRAGVEPKWEDPECANGGKWTVTSRSKASLDTMWLETLMALIGEQFDEADEICGVVASVRQRQDKLALWTRNAANEAAQMGIGRKWKEIIDVTDKITYSFHDDSKRERSAKPRYNV | null | null | defense response to virus [GO:0051607] | cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634] | RNA 7-methylguanosine cap binding [GO:0000340]; translation initiation factor activity [GO:0003743] | PF01652; | 3.30.760.10; | Eukaryotic initiation factor 4E family | PTM: According to the redox status, the Cys-111-Cys-150 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23382802}. Nucleus {ECO:0000269|PubMed:23382802}. Note=(Microbial infection) Binds to potyvirus viral genome-linked protein (VPg) in cytoplasm and nucleus. {ECO:0000269|PubMed:23382802}. | null | null | null | null | null | FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiatio... | Prunus domestica (Garden plum) |
M1MR49 | JAP_RHIAP | MKVLRCLVCSFYIIVSLITTMTIGTPSMPAINTQTLYLAGHSSKLFERNVGCVKTRYLNQTGDWVTRSLIYVFTFDTEPWVTQAGAFQVKWEPYSPLLRVKASDYVRDNLGAKPDYFIRTYDNDFLLLSDLKEVRSTCSLWVTLKYVDRIPETINRTFYTICPDPVPVPFDERCYP | null | null | null | extracellular region [GO:0005576] | null | null | 2.40.128.20; | Calycin superfamily, Lipocalin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23825947}. | null | null | null | null | null | FUNCTION: Salivary tick protein that modulates host immune response. This protein blocks dendritic cell (DC) differentiation from monocytes (PubMed:23825947). In addition, it inhibits up-regulation of costimulatory molecules and pro-inflammatory cytokines in response to stimuli and promotes up-regulation of co-inhibito... | Rhipicephalus appendiculatus (Brown ear tick) |
M1RNJ8 | ATH1_CANGB | MGFKDKILFWKDEVQYRTLAVADQVANRFLHSFENVYQGDESVEDADSRPVGLTNETLSHSSDFFVLPEERISTRVKIRRQNILNTTLILGMLIALVIWTAILSTNSYFSSSLASASPLFNKEGRVVRPMRESNLGLHADPQTRKSSKTLYDLLSDFDNAFYDDENMILGSLAFGENTYSRQPYVANGYIGSRIPNIGFGYALDTLNLYADAPGALNNGWPLRNRRFAGSFVSDFYSLQAKLNSTNFPELDEKGYTTVISSIPEWTDLQFTVDLNGTKWFNPQSVLIDDVINYNQNLSMKDGIVSTNMDWLNGMINIKSE... | 3.2.1.28 | null | carbon utilization [GO:0015976]; trehalose catabolic process [GO:0005993] | cell wall-bounded periplasmic space [GO:0030287]; cytosol [GO:0005829]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; fungal-type vacuole lumen [GO:0000328]; membrane [GO:0016020]; periplasmic space [GO:0042597] | alpha,alpha-trehalase activity [GO:0004555]; carbohydrate binding [GO:0030246]; protein-glucosylgalactosylhydroxylysine glucosidase activity [GO:0047402] | PF03632;PF03636; | 1.50.10.10;2.70.98.40; | Glycosyl hydrolase 65 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26411890, ECO:0000269|PubMed:33146242}. Periplasm {ECO:0000269|PubMed:26411890, ECO:0000269|PubMed:33146242}. Membrane {ECO:0000250|UniProtKB:P48016}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P48016}. | CATALYTIC ACTIVITY: Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28; Evidence={ECO:0000305|PubMed:26411890, ECO:0000305|PubMed:33146242}; | null | null | null | null | FUNCTION: Periplasmic/secreted acid trehalase that catalyzes hydrolysis of the disaccharide trehalose and required for growth on trehalose as carbon source (PubMed:26411890, PubMed:33146242). Growth on trehalose is not restricted to respiration (PubMed:26411890). {ECO:0000269|PubMed:26411890, ECO:0000269|PubMed:3314624... | Candida glabrata (Yeast) (Torulopsis glabrata) |
M1T7M3 | HOG1B_WALI9 | MADFVNASIFGTLFQITSRYVNLEPVGMGAFGLVCSAKDQLTSSPVAIKKIMKPFSTPVLSKRTYRELKLLKHIRHENIISLSDIFISPSEDIYFVTELLGTDLHRLLTARPLEKQFIQYFLYQILRGLKYVHSAGVVHRDLKPSNILVNENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVAVDIWSTGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVIQTICSENTLRFVQSLPKKPRIPFNEKFKTNDPLALDLVEKMLSFDPRTRITASQALAHPYLAPYHDPNDEPVAAEQFDWSFN... | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | cellular response to oxidative stress [GO:0034599]; osmosensory signaling pathway [GO:0007231]; phosphorylation [GO:0016310]; stress-activated MAPK cascade [GO:0051403] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, MAP kinase subfamily. HOG1 sub-subfamily | PTM: Phosphorylated. Dually phosphorylated on Thr-171 and Tyr-173, which activates the enzyme (By similarity). Rapidly dephosphorylated upon either hypo- or hyperosmotic shock. {ECO:0000250, ECO:0000269|PubMed:23712906}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {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=2.7.11.24; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription of target genes. {ECO:0000269|PubMed:23712906}. | Wallemia ichthyophaga (strain EXF-994 / CBS 113033) |
M1V4Y8 | CFA73_CHLRE | MDEEGSATARAKMMPQTLVLDHVSPATRLLEKRRQMFEVQEALEAQKQDFNRKEEVFKRREEALKLKDLELQESLIRFSKFLQENDSKRARAEKKANDEIKARIQKEKEIEQLTEVLEELKSEKERILEVLEKNMRYQHYLESVLEVADEYQEVADLLLRHATLSATNADLKDHQRKCSELAEKVRTELQIYVKQKTDEILNLNNQVAKLKTELEGYEAEAMVQEAKKDSSLQIASQRTLEYGQVVLSADNIFNRCRSKSSIGHPAESNPLHQLDVIGNFVSDLGSIIKQFKQEQAKRASLASRAEIE | null | null | cell motility [GO:0048870]; cilium movement [GO:0003341]; inner dynein arm assembly [GO:0036159]; spermatid development [GO:0007286] | axonemal outer doublet [GO:0097545]; motile cilium [GO:0031514] | dynein complex binding [GO:0070840] | PF13863; | null | CFAP73 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 inner dynein arm. {ECO:0000269|PubMed:23569216}. | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
M1VMF7 | FDHL_GLUJA | MSNETLSADVVIIGAGICGSLLAHKLVRNGLSVLLLDAGPRRDRSQIVENWRNMPPDNKSQYDYATPYPSVPWAPHTNYFPDNNYLIVKGPDRTAYKQGIIKGVGGTTWHWAASSWRYLPNDFKLHSTYGVGRDYAMSYDELEPYYYEAECEMGVMGPNGEEITPSAPRQNPWPMTSMPYGYGDRTFTEIVSKLGFSNTPVPQARNSRPYDGRPQCCGNNNCMPICPIGAMYNGVYAAIKAEKLGAKIIPNAVVYAMETDAKNRITAISFYDPDKQSHRVVAKTFVIAANGIETPKLLLLAANDRNPHGIANSSDLVGRN... | 1.1.5.14 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305|PubMed:23275508, ECO:0000305|PubMed:7462161}; | fructose metabolic process [GO:0006000] | plasma membrane [GO:0005886] | flavin adenine dinucleotide binding [GO:0050660]; fructose 5-dehydrogenase activity [GO:0047904] | PF05199;PF00732;PF13450; | 3.50.50.60; | GMC oxidoreductase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23275508, ECO:0000269|PubMed:7462161}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + keto-D-fructose = 5-dehydro-D-fructose + a ubiquinol; Xref=Rhea:RHEA:22304, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:16389, ChEBI:CHEBI:17011, ChEBI:CHEBI:17976, ChEBI:CHEBI:48095; EC=1.1.5.14; Evidence={ECO:0000269|PubMed:23275508, ECO:0000269|PubMed:7462161}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.02 M for D-fructose {ECO:0000269|PubMed:7462161}; Note=Measured for the whole complex.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0. {ECO:0000269|PubMed:7462161}; | null | FUNCTION: Catalytic subunit of fructose dehydrogenase, an enzyme that catalyzes the oxidation of D-fructose to produce 5-keto-D-fructose. {ECO:0000269|PubMed:23275508, ECO:0000269|PubMed:24386392, ECO:0000269|PubMed:7462161}. | Gluconobacter japonicus |
M2XHU6 | HEXB_DOTSN | MGSQHQSQHNSALIQAARDGEATLSVAFGGQGPSNLNCFNDLLELNKTYGSTLRPLIHTADATLSELASLPHRSGFHEDEGFETLDWLQDPKQAPSREYLALSPMSFPINTLLSLCNYCVTLRALRLDPGQFRSSLHNVVGHSQGIFAAAAIAKADSWESFLEAAEIALKISFWVGLESHTAAPPSHISAAAVQDCVEHGEGQPSSMLGITGLNRAQVEMLVERVNKSLSDDDRHVCLALANSRDKYTIAGPPHSLRAVCVQIREIRAADGVDQSRILFNKRKQEVDALFLPISAPYHSQYLKQVSNNVLDALDVDLVGS... | 1.3.1.9; 2.3.1.38; 2.3.1.39; 2.3.1.86; 3.1.2.14; 4.2.1.59 | null | long-chain fatty acid biosynthetic process [GO:0042759] | fatty acid synthase complex [GO:0005835] | (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity [GO:0004317]; [acyl-carrier-protein] S-acetyltransferase activity [GO:0004313]; [acyl-carrier-protein] S-malonyltransferase activity [GO:0004314]; enoyl-[acyl-carrier-protein] reductase (NADH) activity [GO:0004318]; fatty acid synthase activity [GO:000... | PF00698;PF08354;PF17951;PF13452;PF01575;PF16073; | 1.20.930.70;3.30.1120.100;3.30.70.3330;6.10.140.1400;6.10.60.10;6.20.240.10;3.20.20.70;3.10.129.10;3.40.366.10; | Fungal fatty acid synthetase subunit beta family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+); Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChE... | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000303|PubMed:22069571, ECO:0000305|PubMed:23207690}. | null | null | FUNCTION: Fatty acid synthase beta subunit; part of the fragmented gene cluster that mediates the biosynthesis of dothistromin (DOTH), a polyketide toxin very similar in structure to the aflatoxin precursor, versicolorin B (PubMed:12039746, PubMed:17683963, PubMed:22069571, PubMed:23207690, PubMed:23448391). The first ... | Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight fungus) (Mycosphaerella pini) |
M2YJJ3 | HEXA_DOTSN | MGQKTIKRKIQSAERPAEADVAFLASTQHSKDLCYEYDAPEEVAVEEPVDETPAPETAPERPPLSRAKTAAVKPQETAAPTTATIADVPLSAEEIVRALVARKLKKPILSIPTSKSVKELCNGKSTLQNEIVGDFHSEFTNLPDRPEDIPLKELVPASQSLMLGRVSSALLSKLVSSKMPARFNADAIGKYLASKWGLGPLRSVAVMLFAIAAEPEARLGSVAAAEKYLDDTAAKYAEWAGITLQERSTQSSAGGGGSSGTVDPTVLAELTKTNTRLAKRQFQALAEYLQVDLMKPSSEQESEALAVELQQKLDAWTAEF... | 1.1.1.100; 2.3.1.41; 2.3.1.86 | null | long-chain fatty acid biosynthetic process [GO:0042759]; secondary metabolite biosynthetic process [GO:0044550] | fatty acid synthase complex [GO:0005835] | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity [GO:0004316]; 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; fatty-acyl-CoA synthase activity [GO:0004321]; holo-[acyl-carrier-protein] synthase activity [GO:0008897]; magnesium ion binding [GO:00002... | PF01648;PF00106;PF18325;PF18314;PF00109;PF02801; | 3.30.70.2490;3.40.47.10;6.10.250.1930;3.90.470.20;3.40.50.720; | Thiolase-like superfamily, Fungal fatty acid synthetase subunit alpha family | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of the acyl carrier domain by the C-terminal PPT domain. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group. {ECO:0000305}. | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+); Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChE... | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000303|PubMed:22069571, ECO:0000305|PubMed:23207690}. | null | null | FUNCTION: Fatty acid synthase alpha subunit; part of the fragmented gene cluster that mediates the biosynthesis of dothistromin (DOTH), a polyketide toxin very similar in structure to the aflatoxin precursor, versicolorin B (PubMed:12039746, PubMed:17683963, PubMed:22069571, PubMed:23207690, PubMed:23448391). The first... | Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight fungus) (Mycosphaerella pini) |
M3TYT0 | ROCK2_PIG | MSRPPPTGKMPGAPEAVSGDGAGASRQRKLEALIRDPRSPINVESLLDGLNSLVLDLDFPALRKNKNIDNFLNRYEKIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKHGHLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLCFPEDAE... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | actomyosin structure organization [GO:0031032]; aortic valve morphogenesis [GO:0003180]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cortical actin cytoskeleton organization [GO:0030866]; embryonic morphogenesis [GO:0048598]; mitotic cytokinesis [GO:0000281]; negative regulation of biomi... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; Rho-dependent protein serine/threonine kinase activity [GO:0072518]; small GTPase binding [GO:0031267] | PF00069;PF08912; | 1.20.5.340;3.30.60.20;2.30.29.30;1.20.5.730;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family | PTM: Autophosphorylated. Phosphorylation at Tyr-722 reduces its binding to RHOA and is crucial for focal adhesion dynamics. Dephosphorylation by PTPN11 stimulates its RHOA binding activity (By similarity). {ECO:0000250}.; PTM: Cleaved by granzyme B during apoptosis. This leads to constitutive activation of the kinase a... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Cytoplasmic, and associated with actin microfilaments and the plasma membrane. | 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: Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2... | Sus scrofa (Pig) |
M3W955 | APOA4_FELCA | MFLRAVVLTLALVAVTGARAEVSPDQVATVVWDYFSQLSNNAKEAVEHLQQSELTQQLNALFQDKLGQVNTYADNLQKKLVPFATELHERLTKDSEKLKEEIRKELEELRARLLPHANEVSQKIGDNVRELQQRLGPYADELRTQVNTHAEHLRRHLTSHAQRMEAVLRENVDNLQSSLTPYADEFKAKIDQNIEELKGHLTPYADELKVKIDQNVEELRRSLAPYAQDVQEKLNHQLEGLAFQMKKNAEELKAKITANADELRQRLAPVAEDVRSKLRDNAKGLQESLAQLNSHLDRQVEEFRRNLGPYGDTFNRALVQ... | null | null | acylglycerol homeostasis [GO:0055090]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; lipoprotein metabolic process [GO:0042157]; phosphatidylcholine metabolic process [GO:0046470]; phospholipid efflux [GO:0033700]; positive regulation of fatty acid bi... | blood microparticle [GO:0072562]; chylomicron [GO:0042627]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; very-low-density lipoprotein particle [GO:0034361] | cholesterol transfer activity [GO:0120020]; phosphatidylcholine binding [GO:0031210]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P06727}. | null | null | null | null | null | FUNCTION: May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons. {ECO:0000250|UniProtKB:P06727}. | Felis catus (Cat) (Felis silvestris catus) |
M3X9S6 | FGF5_FELCA | MSLSFLLLLFLSHLILSAWAHGEKHLAPKGQPGPAATGRNPAGASSSRSSRGTTSSSSSSVSSSHSASLGNQGSGLEQSSFQWSPSGRRTGSLYCRVGIGFHLQIYPDGKVNGSHEANMLSILEIFAVSQGIVGIRGVFSNKFLAMSKKGKLHASAKFTDDCKFRERFQENSYNTYASAIHRTEPAGREWYVALNKRGKAKRGCSPRVKPQHISTHFLPRFKQLEQPELSFTVTVPEKKKPPSPVKPKVPLSAPRKSPNTVKYRLKFRFG | null | null | animal organ morphogenesis [GO:0009887]; cell differentiation [GO:0030154]; fibroblast growth factor receptor signaling pathway [GO:0008543]; positive regulation of cell division [GO:0051781]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positiv... | cytoplasm [GO:0005737]; extracellular space [GO:0005615] | fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083] | PF00167; | 2.80.10.50; | Heparin-binding growth factors family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Plays an important role in the regulation of cell proliferation and cell differentiation. Required for normal regulation of the hair growth cycle. Functions as an inhibitor of hair elongation by promoting progression from anagen, the growth phase of the hair follicle, into catagen the apoptosis-induced regres... | Felis catus (Cat) (Felis silvestris catus) |
M3XFH7 | AMPQ_FELCA | MGPPSSSGFYVSRAVALLLAALAAALLLALAVLAALYGRCARVQPSDLHHSGVPDAASSPRGTQEEPLPTWPPRPTREPAGTATPGHWRPPGPWDQLRLPPWLVPLHYELELWPRLRPNEFQSPTLSFTGRVNITVRCAAATARLLLHSLFLDCESAEVRGPLSSGPRDGALGRVPVDDVWFAFDMQYMVLELGATLQPGSRYELQLSFSGLVYRDLREGLFFSIYTDQGERRALLASQMEPTFARSVFPCFDEPALKATFNITIIHHPSYGALSNMPKLGQSEKRDVNGSVWTVTTFSTTPHMPTYLVALAICDYDHVS... | 3.4.11.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|RuleBase:RU364040}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|RuleBase:RU364040}; | peptide catabolic process [GO:0043171]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; membrane [GO:0016020] | metalloaminopeptidase activity [GO:0070006]; peptide binding [GO:0042277]; zinc ion binding [GO:0008270] | PF11838;PF01433;PF17900; | 1.25.50.20;2.60.40.1910;1.10.390.10;2.60.40.1730; | Peptidase M1 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q6Q4G3}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6Q4G3}. | null | null | null | null | null | FUNCTION: Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface (By similarity). Involved in coat pigmentation patterns. During skin development, may be required to establish the periodicity of tabby markings, initiating a pre-pattern ... | Felis catus (Cat) (Felis silvestris catus) |
M4DUF2 | ASO_BRARP | MGMWWIVAVAILAHTASAAVREYAWEVEYKFGWPDCKEGMVMAVNGQFPGPTIHALAGDTIVVHLTNKLATEGLVIHWHGIRQLGSPWADGAAGVTQCAISPGETFTYNFTVDKPGTHFYHGHYGMQRSAGLYGSLIIDVAKGKKEPLRYDGEFNLLLSDWWHEDVLSQEIGLSSRPMRWIGEAQSILINGRGQFNCSLAAQFSSTSLPTCTFKEGDQCAPQRLHVEPNKTYRIRLASSTALASLNFAVQGHKLVVVEADGNYITPFTTDDIDIYSGETYSVLLTTDQDPSQNYYITAGVRGRKPNTPPALTVLNYVTAP... | 1.10.3.3 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P37064}; Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:P37064}; | defense response [GO:0006952]; L-ascorbic acid catabolic process [GO:0019854]; negative regulation of defense response to virus [GO:0050687]; response to hydrogen peroxide [GO:0042542]; response to jasmonic acid [GO:0009753]; response to virus [GO:0009615] | extracellular region [GO:0005576]; plasmodesma [GO:0009506] | copper ion binding [GO:0005507]; L-ascorbate oxidase activity [GO:0008447]; oxidoreductase activity [GO:0016491] | PF00394;PF07731;PF07732; | 2.60.40.420; | Multicopper oxidase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P37064}. | CATALYTIC ACTIVITY: Reaction=4 L-ascorbate + O2 = 2 H2O + 4 monodehydro-L-ascorbate radical; Xref=Rhea:RHEA:30243, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513; EC=1.10.3.3; Evidence={ECO:0000250|UniProtKB:Q8LPL3}; | null | PATHWAY: Cofactor degradation; L-ascorbate degradation. {ECO:0000250|UniProtKB:Q8LPL3}. | null | null | FUNCTION: Ascorbate oxidase involved in a redox system involving ascorbic acid (AsA) (PubMed:27255930). The oxidation of AsA represses responses to high salinity and oxidative stress conditions such as vegetative growth and seed production reductions (By similarity). Negative regulator of defense responses toward incom... | Brassica rapa subsp. pekinensis (Chinese cabbage) (Brassica pekinensis) |
M4GGR9 | LYR_PROMI | MSLGIRYLALLPLFVITACQQPVNYNPPATQVAQVQPAIVNNSWIEISRSALDFNVKKVQSLLGKQSSLCAVLKGDAYGHDLSLVAPIMIENNVKCIGVTNNQELKEVRDLGFKGRLMRVRNATEQEMAQATNYNVEELIGDLDMAKRLDAIAKQQNKVIPIHLALNSGGMSRNGLEVDNKSGLEKAKQISQLANLKVVGIMSHYPEEDANKVREDLARFKQQSQQVLEVMGLERNNVTLHMANTFATITVPESWLDMVRVGGIFYGDTIASTDYKRVMTFKSNIASINYYPKGNTVGYDRTYTLKRDSVLANIPVGYAD... | 5.1.1.5 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:23118975, ECO:0000269|Ref.1}; | peptidoglycan biosynthetic process [GO:0009252] | cytosol [GO:0005829]; periplasmic space [GO:0042597]; plasma membrane [GO:0005886] | alanine racemase activity [GO:0008784]; arginine racemase activity [GO:0047679]; lysine racemase activity [GO:0018113]; pyridoxal phosphate binding [GO:0030170] | PF00842;PF01168; | 3.20.20.10; | Alanine racemase family, Bsr subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}; Periplasmic side {ECO:0000305}. Periplasm {ECO:0000250|UniProtKB:I0J1I6}. | CATALYTIC ACTIVITY: Reaction=L-lysine = D-lysine; Xref=Rhea:RHEA:22864, ChEBI:CHEBI:32551, ChEBI:CHEBI:32557; EC=5.1.1.5; Evidence={ECO:0000269|PubMed:23118975, ECO:0000269|Ref.1}; CATALYTIC ACTIVITY: Reaction=L-arginine = D-arginine; Xref=Rhea:RHEA:18069, ChEBI:CHEBI:32682, ChEBI:CHEBI:32689; Evidence={ECO:0000269|Pub... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21.8 mM for L-lysine {ECO:0000269|Ref.1}; KM=15 mM for D-lysine {ECO:0000269|Ref.1}; KM=14.9 mM for L-arginine {ECO:0000269|Ref.1}; Note=kcat is 3326 min(-1) with L-lysine as substrate. kcat is 650 min(-1) with L-arginine as substrate. {ECO:0000269|Ref.1}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-9.0. {ECO:0000269|Ref.1}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. More than 78% of maximal activity is observed at 40 degrees Celsius and 60 degrees Celsius. {ECO:0000269|Ref.1}; | FUNCTION: Amino-acid racemase that catalyzes the interconversion of L-lysine and D-lysine. To a lesser extent, is also able to interconvert arginine enantiomers (PubMed:23118975, Ref.1). Cannot use methionine, asparagine, alanine, leucine, glutamine, phenylalanine and histidine as substrates (Ref.1). {ECO:0000269|PubMe... | Proteus mirabilis |
M4IQQ5 | CCL4_HUMLU | MEDLKPRPASSSPLTPLGFLERAATVYGDCTSVVYDAVSYTWSQTHRRCLCLASSIASLGIENGHVVSVLAPNVPQMYELHFAVPMAGAILNAVNLRLDARTISILLHHSESKLIFVDHLSRDLILEAIALFPKQAPVPRLVFMADESESGNSSELGKEFFCSYKDLIDRGDPDFKWVMPKSEWDPMILNYTSGTTSSPKGVVHCHRGIFIMTVDSLIDWGVPKQPVYLWTLPMFHANGWSYPWGMAAVGGTNICLRKFDSEIIYDMIKRHGVTHMCGAPVVLNMLSNAPGSEPLKTTVQIMTAGAPPPSAVLFRTESLG... | 6.2.1.-; 6.2.1.17 | null | null | cytosol [GO:0005829] | 2-methylbutanoate-CoA ligase activity [GO:0043759]; ATP binding [GO:0005524]; butyrate-CoA ligase activity [GO:0047760]; CoA-ligase activity [GO:0016405]; propionate-CoA ligase activity [GO:0050218] | PF00501;PF13193; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23300257}. | CATALYTIC ACTIVITY: Reaction=2-methylpropanoate + ATP + CoA = 2-methylpropanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:46176, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:48944, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=164 uM for 2-methylpropanoate {ECO:0000269|PubMed:23300257}; KM=25.2 uM for 2-methylbutanoate {ECO:0000269|PubMed:23300257}; KM=356 uM for CoA {ECO:0000269|PubMed:23300257}; Note=kcat is 18.3 min(-1) with 2-methylpropanoate as substrate (PubMed:23300257). kcat is 1... | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:30468448}. | null | null | FUNCTION: Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Catalyzes the ligation of CoA on 2-methylpropanoate (isobutyric acid) and 2-methylbutanoate to produce 2-methylpropanoyl-CoA and 2-methylbutano... | Humulus lupulus (European hop) |
M4IRL4 | CCL2_HUMLU | MDNYRRLHTPVALCVASPPAPPTTSWKSMEGLVQCSANHVPLSPITFLERSSKAYRDNTSLVYGSVRYTWAQTHHRCLKLASALTTHLGISPGDVVATFSYNLPEIYELHFAVPMAGGILCTLNARNDSAMVSTLLAHSEAKLIFVEPQLLETARAALDLLAQKDIKPPTLVLLTDSESFTSSSYDHYNHLLANGSDDFEIRRPKNEWDPISINYTSGTTARPKAVVYSHRGAYLNSIATVLLHGMGTTSVYLWSVPMFHCNGWCFPWGAAAQGATNICIRKVSPKAIFDNIHLHKVTHFGAAPTVLNMIVNSPEGNLHT... | 6.2.1.- | null | null | cytosol [GO:0005829] | ATP binding [GO:0005524]; butyrate-CoA ligase activity [GO:0047760]; CoA-ligase activity [GO:0016405] | PF00501;PF13193; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23300257}. | CATALYTIC ACTIVITY: Reaction=3-methylbutanoate + ATP + CoA = 3-methylbutanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:46184, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:48942, ChEBI:CHEBI:57287, ChEBI:CHEBI:57345, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; Xr... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=69.7 uM for isovalerate {ECO:0000269|PubMed:23300257}; KM=110 uM for CoA {ECO:0000269|PubMed:23300257}; Note=kcat is 17.2 min(-1) with isovalerate as substrate (PubMed:23300257). kcat is 23.3 min(-1) with CoA as substrate (PubMed:23300257). {ECO:0000269|PubMed:2330... | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:30468448}. | null | null | FUNCTION: Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Catalyzes the ligation of CoA on isovalerate to produce 3-methylbutanoyl-CoA (PubMed:23300257). Can also use butanoate, hexanoate, pentanoate, ... | Humulus lupulus (European hop) |
M4IS88 | CCL3_HUMLU | MGMVGRDIDDLPKNAANYTALTPLWFLERAATVHPTRTSVIHGSRHYTWLQTYHRCRQFASALNNHSIGLGSTVAVIAPNVPALYEAHFAVPMAGAVVNCVNIRLNASTIAFLLGHSSAAAVMVDQEFFSLAEEALKILAQESKSHYKPPLLVVIGDESCDPKTLEYALKTGAIEYEKFLEGGDPEFDWKPPEDEWQSISLGYTSGTTASPKGVVLSHRGAYLMSLSASVVWGINEGAIYLWTLPMFHCNGWCYTWGMAAFCGTNICLRQVTAKGVYSAIAKYGVTHFCAAPVVLNTIVNAPPEEAIIPLPHLVHVMTAG... | 6.2.1.-; 6.2.1.1; 6.2.1.17 | null | null | cytosol [GO:0005829] | 2-methylbutanoate-CoA ligase activity [GO:0043759]; acetate-CoA ligase activity [GO:0003987]; ATP binding [GO:0005524]; butyrate-CoA ligase activity [GO:0047760]; CoA-ligase activity [GO:0016405]; propionate-CoA ligase activity [GO:0050218] | PF00501;PF13193; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:M4IRL4}. | CATALYTIC ACTIVITY: Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:456215; EC=6.2.1.1; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; Xref=Rhea:... | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:30468448}. | null | null | FUNCTION: Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Catalyzes the ligation of CoA on propanoate to produce propanoyl-CoA (PubMed:23300257). Can also use 2-methylpropanoate (isobutyric acid), acet... | Humulus lupulus (European hop) |
M4QN28 | WBDA_ECOLX | MHILIDVQGYQSESKVRGIGRSTPAMSRAIIENAGEHRVSILINGMYPIDNINDVKMAYRDLLTDEDMFIFSAVAPTAYRHIENHGRSKAAQAARDIAIANIAPDIVYVISFFEGHSDSYTVSIPADNVPWKTVCVCHDLIPLLNKERYLGDPNFREFYMNKLAEFERADAIFAISQSAAQEVIEYTDIASDRVLNISSAVGEEFAVIDYSAERIQSLKDKYSLPDEFILSLAMIEPRKNIEALIHAYSLLPAELQQRYPMVLAYKVQPEQLERILRLAESYGLSRSQLIFTGFLTDDDLIALYNLCKLFVFPSLHEGFG... | 2.4.1.371 | null | O antigen biosynthetic process [GO:0009243] | plasma membrane [GO:0005886] | glycosyltransferase activity [GO:0016757] | PF00534; | 3.40.50.2000; | Glycosyltransferase group 1 family, Glycosyltransferase 4 subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:19734145}; Peripheral membrane protein {ECO:0000269|PubMed:19734145}. Note=Proper localization requires WbdD. {ECO:0000269|PubMed:19734145}. | CATALYTIC ACTIVITY: Reaction=[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)](n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + 2 GDP-alpha-D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man... | null | PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis. {ECO:0000269|PubMed:22875852, ECO:0000269|PubMed:22989876}. | null | null | FUNCTION: Mannosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region (PubMed:19734145, PubMed:22875852, PubMed:22989876, PubMed:25422321). Catalyzes the polymerization of a tetrasaccharide repeat unit containing two alpha-(1->3)- and two alpha-(1->2)-linked mann... | Escherichia coli |
M5A7P9 | SL9A3_TRISC | MGRNRSGCVARCVSLTALVLLLCCPVVRSSEAETDPDSHTEHGDSHGGSREGNDTGFQIVTFRWEHVQTPYVIALWILVASLGKIVFHLSEKVTSVVPESALLIVLGLILGGIVWAADHSASFTLTPTVFFFYLLPPIVLDAGYFMPNRHFFGNLGTILTYAVIGTVWNAATTGLSLYGVFLLGLMGDLKAGLLEFLLFGSLIAAVDPVAVLAVFEEVHVNEVLFIIVFGESLLNDAVTVVLYNVFNSFVEVGAGNVQGLDYFKGIVSFFVVSLGGTAVGIIFAFILSLVTRFTKHVRVIEPGFVFVISYLSYLTADMLS... | null | null | regulation of intracellular pH [GO:0051453]; sodium ion import across plasma membrane [GO:0098719] | apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; early endosome membrane [GO:0031901]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038] | identical protein binding [GO:0042802]; phosphatidylinositol binding [GO:0035091]; potassium:proton antiporter activity [GO:0015386]; sodium:proton antiporter activity [GO:0015385] | PF00999; | 6.10.140.1330; | Monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:23485868}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P48764}. Cell membrane {ECO:0000250|UniProtKB:P48764}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P48764}. Recycling endosome membrane {ECO:0000250|UniProtKB:P48764}; Multi-pass membrane ... | CATALYTIC ACTIVITY: Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out); Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P48764}; | null | null | null | null | FUNCTION: Plasma membrane Na(+)/H(+) antiporter. Exchanges intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry, playing a key role in salt and fluid absorption and pH homeostasis. Major apical Na(+)/H(+) exchanger in kidney and intestine playing an important role in renal and intestine Na(+) absorption... | Triakis scyllium (Banded houndshark) (Hemigaleus pingi) |
M5AAG8 | POL_BPNNR | MIMEIPAIKALSRYAQWVIWKKERDTKIPYNPNNGKKASSTDPLAWGDIDEAQAGLVRYGANGLGFVLTKSDPFVFIDLDHVLDENKRVKCEWARQLLKEIKSYTEISPSGDGLHVVVSGKLPDYIKHKTKFDDGSALEVYESGRYMTITGEVFDGRDDIKELDLSILGEFAEHKIETKNAPVQIESATTLDDEAIIDLMKRKGQWPDAPKDGDDWSSLDMSFANRLAFWCGKDIERMDRIFRQSPLMRQKWDRPTAGSTYGRITLKKACDFVDSVYDPALRNESDCPFEPYNEEGGPRNDKEEKDPLWLYKVLLTKGIE... | 2.7.7.-; 2.7.7.7; 3.6.4.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:28265063, ECO:0000269|PubMed:31176489, ECO:0000269|PubMed:34975792}; | DNA replication [GO:0006260]; viral DNA genome replication [GO:0039693] | null | ATP binding [GO:0005524]; helicase activity [GO:0004386]; hydrolase activity [GO:0016787]; transferase activity [GO:0016740] | PF19263; | 3.40.50.300; | null | null | null | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000269|PubMed:28265063, ECO:0000269|PubMed:30739783}; CATALYTIC ... | null | null | null | null | FUNCTION: Multifunctional protein with primer synthesis, DNA polymerization, and DNA helicase activities (PubMed:28265063, PubMed:32016421). Recognizes a specific sequence motif 5'-TTTGGTTA-3' and initiates DNA synthesis (PubMed:28265063). {ECO:0000269|PubMed:28265063, ECO:0000269|PubMed:32016421}. | Nitratiruptor phage NrS-1 |
M9MRD1 | MS300_DROME | MADSGGPGSKHMDPTTIDAGGGGAGAAGGDDVPPVPAVRRRRAHEQKSSREQVLEEEKSQQLETSTVTRTYMKTITTSLTTSSSSNVEEFILGEHAAGAAAAPSPNQQRLRQKVAQYEKVWSDGSSPVKRPAEQSSDELRLTDDQDEYDAENPFEIDVHEIERRLRQERQRGLAEAEAAKLAFQQVQLRHTTPPRRVEVTSDQVASPFNVTLRTTSRMSPGAEHGNVEEHLAPFNVTLRTTRRTKKKEFKELENFLEGERTVREVPSADGVRTIITSSMTSDGGYAEEKIYRHGEGYVSPRDSPSWSRSSYSSERSSVTP... | null | null | actin filament organization [GO:0007015]; cell migration [GO:0016477]; endoplasmic reticulum localization [GO:0051643]; female germline ring canal stabilization [GO:0008335]; flight [GO:0060361]; larval visceral muscle development [GO:0007523]; locomotion [GO:0040011]; mesoderm development [GO:0007498]; microtubule anc... | cytoplasm [GO:0005737]; meiotic nuclear membrane microtubule tethering complex [GO:0034993]; microtubule organizing center [GO:0005815]; nuclear envelope [GO:0005635]; nuclear outer membrane [GO:0005640]; perinuclear region of cytoplasm [GO:0048471]; Z disc [GO:0030018] | actin binding [GO:0003779]; actin filament binding [GO:0051015]; protein kinase binding [GO:0019901] | PF00307;PF10541;PF00435; | 1.20.58.60;1.10.418.10; | Nesprin family | null | SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:22927463}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:22927463}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:32066907}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:32066907}. Note=The recruitment to the Z-di... | null | null | null | null | null | FUNCTION: Component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton (By similarity). Collaborates with Klar to promote even spacing of the myonuclei at the periphery of striated muscle fibers by mediating a tight association betw... | Drosophila melanogaster (Fruit fly) |
M9MRI4 | TRIM9_DROME | MEDELRCPTCKQLYANPVLLPCFHALCLGCALDIQTPYSPGSALPGAVNGAGAASAAGHNGLHGNGGGAGGGAAAPVTNPNGPGTRHSSHSSAASTASSNTGSESVTSDQDQSDKVSIFSEADSGVVCCSNTSRPVSYAGTGLLPGVGNVVAPPGAAYCLTCPLCRKLVFFDDGGVRNLPTYRAMEAIVDRFCAREALRCQMCETDPKVASLICEQCEIRYCDACRELTHPARGPLAKHTLVKPRGAAQQRESVCGEHEETLSQYCLSCKAPACGLCIGELRHQAHDVQSINVTCKAQKTELSHNLQQLSEKARSTTEFI... | 2.3.2.27 | null | axon guidance [GO:0007411]; axon midline choice point recognition [GO:0016199]; axonogenesis [GO:0007409]; compound eye development [GO:0048749]; negative regulation of glycolytic process [GO:0045820]; netrin-activated signaling pathway [GO:0038007]; peripheral nervous system neuron axonogenesis [GO:0048936]; proteasom... | axonal growth cone [GO:0044295]; cytoplasm [GO:0005737]; neuron projection [GO:0043005]; perikaryon [GO:0043204] | ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF00041;PF00622;PF00643; | 1.20.5.170;2.60.120.920;4.10.830.40;3.30.160.60;2.60.40.10;3.30.40.10; | TRIM/RBCC family | null | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:22084112}. Perikaryon {ECO:0000269|PubMed:22084112}. Note=Colocalizes with fra and pico. {ECO:0000269|PubMed:22084112}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9C026}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9C026}. | null | null | FUNCTION: E3 ubiquitin-protein ligase activity (By similarity). During embryonic and larval development, regulates the pattern of axonal projections of class IV nociceptive sensory neurons (C4da) downstream of netrin receptor fra (PubMed:21338947, PubMed:22084112). Regulates fine-scale topography of C4da axon terminals... | Drosophila melanogaster (Fruit fly) |
M9MSG8 | PIEZO_DROME | MVFSYACMVLQRIVVPAVLVLAALMRPVGISFVYLLMFFVSPFVPLATRRNFKGSVTAFFIILLTLSTLVLLGHITLQILAVSLTLPIYNCSFSERLLRHIGFVSFIDLQPFAIIEWLVPEVLVFATSLGSYLTVKRVASQPVGAEQLENGEVVDGQAENAQTSSQPSAADANGGDVQQATVTTPLQQQQQQLRKRVSMISQHIHFEGLVKISPLFCLATLFFAAVLRPSVPGGFYFLIFLLSGTYWATCQTLQRGFALLLRCVMVVLVLHSLSIVSYQTPWMQSHLNHTTLTARLIGLEPLIESYCSPDIRVFLYNNKL... | null | null | cellular response to mechanical stimulus [GO:0071260]; detection of mechanical stimulus [GO:0050982]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; mechanosensory behavior [GO:0007638]; monoatomic cation transmembrane transport [GO:0098655]; monoatomic ion transmembrane transpor... | plasma membrane [GO:0005886] | mechanosensitive monoatomic ion channel activity [GO:0008381]; monoatomic cation channel activity [GO:0005261] | PF15917;PF12166; | null | PIEZO (TC 1.A.75) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22343900}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Component of a mechanosensitive channel required for rapidly adapting mechanically activated (MA) currents (PubMed:22343891, PubMed:22343900). Plays a major role in nociception (response to strong or painful touch) (PubMed:22343891). Required for maintaining the mechanosensitivity of tarsal bristle mechanosen... | Drosophila melanogaster (Fruit fly) |
M9NDE3 | BARK_DROME | MKLQHHKTNRQRISKPHRDPKWASICLWLLVTLAFSTHLARSQESRQTEDSKEVELLQDNDIEFASLDGASQLLPATRHSGADVTVAPQGSTPSMTSSSSYTELQGGEILSDRILRRSESPYLARDDIEVLRGARLTIEPGVTIEFAPTKGLKINGVLQAVGTPTSRIVLKSQSNTANYKLELPDDQEKGIRLVDGPTPVEGRLQLFHKGAWRSVCSNSRNWTLADYGVACKQLGYRGGRFWNWVERTPGYYPRLLYEQPKCKGGEGSLQDCAWTSRQMGAGACDYHNDLGIQCLPVHSETLGHWRGIYFDNAPSTKALG... | null | null | cell-cell junction maintenance [GO:0045217]; liquid clearance, open tracheal system [GO:0035002]; regulation of tube length, open tracheal system [GO:0035159]; response to endoplasmic reticulum stress [GO:0034976]; tricellular tight junction assembly [GO:1904274] | adherens junction [GO:0005912]; bicellular tight junction [GO:0005923]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; septate junction [GO:0005918]; tricellular tight junction [GO:0061689] | carbohydrate binding [GO:0030246] | PF00530; | 3.10.100.10;2.60.120.290;3.10.250.10; | null | PTM: N-glycosylated. {ECO:0000269|PubMed:25982676}.; PTM: May be proteolytically cleaved in the extracellular domain. {ECO:0000269|PubMed:25982676}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, septate junction {ECO:0000269|PubMed:25704509, ECO:0000269|PubMed:25982676}. Cell junction, adherens junction {ECO:0000269|PubMed:25704509}. Note=Found at specialized septate junction structures, known a... | null | null | null | null | null | FUNCTION: Required for the maturation but not the establishment of septate junctions in developing epithelial cells and is involved in epithelial cell adhesion during septate junction maturation (PubMed:25704509). Plays a role in the proper localization of the septate junction core components pck/mega, kune, Nrx-IV and... | Drosophila melanogaster (Fruit fly) |
M9NEY8 | TET_DROME | MASSILAQSSTGATVDSSNLGATAAAATSVEATVSSLHNTHLNQLSSLSQHYTTPYHHPHSHSHPHHHYQQHYPQQQHLQQQQQQQHHAQQQHQQQQQQQQQQQQQHWDYYARQQQQHQQQQQQQQQPAAATGNTNGNSSNNGNNGNNGNNSNPDGSNTTVPAPLGSSNNSSSNHANAASGGNSGQRHGDANANAISAASAAVGNPGNQQPNNSAGNANSNSNSNSNSNGSYTRPWEMESKDNGPQPPQTQPHLQLKSGFEPFSKLPSFQSQFHGFNEQLLPDGTPMPVPIGAGVPPGSAAAVAAATGSIPPGSVGPNSV... | 1.14.11.51; 1.14.11.80 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q6N021}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6N021}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q6N021}; Note=Binds 3 zinc ions per subunit. The zinc ions have a structural role. {... | 5-methylcytosine catabolic process [GO:0006211]; DNA demethylation [GO:0080111]; germ cell development [GO:0007281]; positive regulation of transcription by RNA polymerase II [GO:0045944]; RNA modification [GO:0009451] | chromosome [GO:0005694]; nucleus [GO:0005634] | 5-methylcytosine dioxygenase activity [GO:0070579]; broad specificity oxidative DNA demethylase activity [GO:0035516]; DNA binding [GO:0003677]; DNA demethylase activity [GO:0035514]; DNA N6-methyladenine demethylase activity [GO:0141131]; zinc ion binding [GO:0008270] | PF12851; | null | TET family | null | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:30078725}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + an N(6)-methyl-2'-deoxyadenosine in DNA + O2 = a 2'-deoxyadenosine in DNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:49524, Rhea:RHEA-COMP:12418, Rhea:RHEA-COMP:12419, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI... | null | null | null | null | FUNCTION: Dioxygenase that specifically demethylates DNA methylated on the 6th position of adenine (N(6)-methyladenosine) DNA (PubMed:25936838, PubMed:30078725). N(6)-methyladenosine (m6A) DNA is present at a relatively high level at the very earliest embryonic stages but at low levels at the late embryonic stages and ... | Drosophila melanogaster (Fruit fly) |
M9PBE2 | HAKAI_DROME | MDTEEVKRGRGRGRGTRARGRGRGRGRGRGKKIDDSSIADAAALAASSCAALEDSPGRLDASEDSVMQELDKDGELETPGALEEPLPHGALGAVAASGNMTPATQQPQVLQQVPPPVMSQTTISLSLARAVDMEADISQLEAPTFTTLSRGPPEPMLRLKWNHKVSLIGEKVLNPMIHCCDQCDKPILVYGRMIPCKHVFCLKCARAEPIKSCPRCTDKVLRVEQSGLGTVFMCTHGGSRYGSSGCRRTYLSQRDLQAHINHRHVAPQPPPLQPQPQLSAMAEQPKMTDLGGVGLGLELHKQRKLSESSVPISVSASIAS... | 2.3.2.27 | null | actin filament organization [GO:0007015]; chitin-based cuticle development [GO:0040003]; dorsal closure [GO:0007391]; epithelial cell migration, open tracheal system [GO:0007427]; epithelium development [GO:0060429]; female sex determination [GO:0030237]; head involution [GO:0008258]; midgut development [GO:0007494]; p... | cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; RNA N6-methyladenosine methyltransferase complex [GO:0036396] | cadherin binding [GO:0045296]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF18408; | 6.10.140.2210;3.30.40.10; | Hakai family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cell membrane {ECO:0000305|PubMed:19682089}. Cytoplasmic vesicle {ECO:0000305|PubMed:19682089}. Cytoplasm, perinuclear region {ECO:0000305|PubMed:19682089}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9JIY2}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:19682089}. | null | null | FUNCTION: E3 ubiquitin-protein ligase required during early development (PubMed:19682089). E3 ubiquitin-protein ligases mediate ubiquitination of target proteins (PubMed:19682089). Required for epithelial integrity and midgut morphogenesis (PubMed:19682089). Associated component of the WMM complex, a complex that media... | Drosophila melanogaster (Fruit fly) |
M9PE65 | AXO_DROME | MAFPYIWALLPLICSASGLSLPNMTSTDAVVAGGGILPILVAGNPGNLGSSNMSLSGGGGLAGSSTGGQSLPDTGGGNSAGGSPAGGSSGTGGGGSNSGISGNNSAMIQGQKSNQYEKCAGPGDPGPCKQYIYKWRYEPTTNECTNFIWGGCEGNPQNRFGTEAECLFHCIGGPHTLPPFLQSTTREPSTTESSMLLGLPYTQSPAQSPDGMGGAEGGDGTTPVPIEQRGPELTFAETGQGKTFIFAKNNTFIQMDGDIIQTFQLRLCREISFQFRTRLPHGLLVYHNVKNPDRINLDPYALYVIVEKGQLKVVHVFGKH... | null | null | transmission of nerve impulse [GO:0019226] | axon [GO:0030424]; membrane [GO:0016020] | serine-type endopeptidase inhibitor activity [GO:0004867] | PF00014;PF02210; | 2.60.120.1000;2.60.120.200;2.10.25.10;4.10.410.10; | null | null | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:10037607}. Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Note=Localizes to longitudinal axon tracts as well as to an axonal scaffold in the brain (PubMed:10037607). A secreted form might exist (Probable). {ECO:0000269|PubMed:10... | null | null | null | null | null | FUNCTION: May have serine protease inhibitor activity (Probable). Might play a role in the glial-neuronal signaling pathway that is important in establishing the electrical properties of axonal membranes (PubMed:10037607). {ECO:0000269|PubMed:10037607, ECO:0000305}. | Drosophila melanogaster (Fruit fly) |
M9PFN0 | HZG_DROME | MDATSIITQVSRDDEQLNVYPSYPNDKDAWLGFSGSVWLPDCPADHAQLTHDVDRLKPQKRGLFHSLLCCWRRNRTKTNQNGTQIDGSTTPPPLPDQQRYLLPQVRLTDMHRKCMVIDLDETLVHSSFKPIPNADFIVPVEIDGTVHQVYVLKRPHVDEFLQKMGELYECVLFTASLAKYADPVADLLDKWNVFRARLFRESCVYYRGNYIKDLNRLGRDLQKIVIVDNSPASYIFHPDNAVPVKSWFDDVTDCELRELIPLFEKLSKVDSVYSVLCNSNQPLNNQTNQQQHPQELQQAPNQLHQQLQQQQQQQTISATT... | 3.1.3.16 | null | positive regulation of embryonic development [GO:0040019]; protein dephosphorylation [GO:0006470] | plasma membrane [GO:0005886] | myosin phosphatase activity [GO:0017018]; phosphoprotein phosphatase activity [GO:0004721]; RNA polymerase II CTD heptapeptide repeat phosphatase activity [GO:0008420] | PF03031; | 3.40.50.1000; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31491385}; Peripheral membrane protein {ECO:0000269|PubMed:31491385}. Note=During embryonic development shows diffuse localization between stages 1-5 and then shows foci formation at the cell membrane that persist till later stages. {ECO:0000269|PubMed:31491385}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:31491385}; | null | null | null | null | FUNCTION: Prion-like membrane-associated phosphatase (PubMed:31491385). Phosphatase activity depends on amyloid-like assembly at the membrane (PubMed:31491385). Might have a role in establishment of segment polarity in embryos (PubMed:31491385). {ECO:0000269|PubMed:31491385}. | Drosophila melanogaster (Fruit fly) |
M9PGC5 | WNK_DROME | MGQTLCDFVRQQEVVPANRARKGSAISEDGTTSCTTQPQRNTSISSEEQTVQGANIQKSGHRSFNRSASSRQKPNPTSKLKDTLNRKPTCKQGTLSAHTSTSSTTSIQSSPIEPASSLPTLNTTPTPPAASKSNLFVRVLRRFSNNTLPGKTASSPKNVDDVPKVNDNNNGDLGKQQSTDVEVLCSQDNQSREQNEDEMDSKIEPADAISNQKAGLTSGKPKKDKSVKGTSQAVVSDTKKMEARKSSSDTVIEPLIKQQAPLHSSKTTPTTLTANFVQNIRFVRKNVEQSGRNTNPLQFVELETEFPRDYDDNIEMLSRE... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:X5M5N0}; | cell volume homeostasis [GO:0006884]; cellular hyperosmotic response [GO:0071474]; intracellular signal transduction [GO:0035556]; monoatomic ion homeostasis [GO:0050801]; negative regulation of sodium ion transport [GO:0010766]; non-membrane-bounded organelle assembly [GO:0140694]; positive regulation of canonical Wnt... | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; molecular condensate scaffold activity [GO:0140693]; potassium channel inhibitor activity [GO:0019870]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF12202;PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, WNK subfamily | PTM: Autophosphorylated (PubMed:23797875). Autophosphorylation at Ser-628 and Ser-632 promotes its activity (By similarity). {ECO:0000250|UniProtKB:Q9H4A3, ECO:0000269|PubMed:23797875}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H4A3}. Note=Mediates formation and localizes to cytoplasmic membraneless compartment in response to hyperosmotic stress. {ECO:0000250|UniProtKB:Q9H4A3}. | 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:0000269|PubMed:23797875, ECO:000026... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase component of the WNK-SPAK/OSR1 kinase cascade, which plays an important role in the regulation of electrolyte homeostasis and regulatory volume increase in response to hyperosmotic stress (PubMed:23797875, PubMed:25086033, PubMed:36318922). Wnk mediates regulatory volume increa... | Drosophila melanogaster (Fruit fly) |
M9Z1G5 | MOMT3_SOLHA | MALSMDNIVISNEEEIYMMKAMHIPCGLYLNMVLKAAIELDLFEIIAKSTTQKLSSYEIASQIPTKNPNASSLVLERILRFLASQSFLTCNITKNDDGIVHTSYNLTPLSQSLISDKDGSSIAPFLLLATDPVAVNSWFHFKDAILEGEIPFNKAHGVHAFEYHGKDSRMNGLFNRAMQNVTCTEMKRIVECYNGFQGVKEIIDVGGGLGISLATIISKYPNIKGINFDLPHVIKDAPTYEGIEHVGGDMFKSVPQRELILLKAILHDWDDEYCVKILKNCWRALPKDGKVVVIEQMQPEYPETNLISKNSSSVDMLMMT... | 2.1.1.-; 2.1.1.76 | null | aromatic compound biosynthetic process [GO:0019438]; flavonoid biosynthetic process [GO:0009813]; methylation [GO:0032259] | null | kaempferol 3-O-methyltransferase activity [GO:0102449]; O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; quercetin 3-O-methyltransferase activity [GO:0030755] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=kaempferol + S-adenosyl-L-methionine = 3-O-methylkaempferol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74743, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58573, ChEBI:CHEBI:59789, ChEBI:CHEBI:194073; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right;... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.55 uM for myricetin (in the presence of S-adenosylmethionine) {ECO:0000269|PubMed:22711283}; KM=2.07 uM for 3'-methyl myricetin (in the presence of S-adenosylmethionine) {ECO:0000269|PubMed:22711283}; KM=9.98 uM for 7-methyl quercetin (in the presence of S-adenos... | PATHWAY: Flavonoid metabolism. {ECO:0000269|PubMed:22711283}. | null | null | FUNCTION: Flavonoid 3-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as myricetin derivatives, aroma compounds possessing antioxidant properties and exhibiting pharmacological activities such as anti-carcinogen, anti-viral, anti-thrombotic, anti-diabetic, anti-athe... | Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum) |
N0A3C0 | POLG_FCV | MSQTLSFVLKTHSVRKDFVHSVKRTLARRRDLQYLNNKLSRSMRAEACPSCASYDVCPNCTSGDIPDDGSSTMTIPSWEEITKTSTYSLLLSEDTSDELCPDDLVNVAAHIRKALSTQSHPANVEMCKEQLTSLLVMAEAMLPQRSRSMIPLHQQHQTARLEWREKFFSKPIDFLLERIGVSKDILQITAIWKIILEKACYCKSYGEEWFNIAKQKLREIKCFEGNTLKPLVGAFIDGLRLMTVDNPNPMAFLPKLIGLIKPLNLAMIIDNHENTTSGWIITLTAIMELYGITECTIDIITSLITTFYDKLAKATKFYSQ... | 2.7.7.48; 3.4.22.66; 3.6.1.15 | null | DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral RNA genome replication [GO:0039694] | null | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968] | PF03510;PF00680;PF00910;PF20915; | 1.10.260.110;1.20.960.20;3.30.70.270;6.10.250.3230;3.40.50.300; | null | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Pro-Pol is first autocatalytically cleaved, then processes the whole polyprotein. {ECO:0000250|UniProtKB:Q66914}.; PTM: [Viral genome-linked protein]: VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of ... | null | CATALYTIC ACTIVITY: [NTPase]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; CATALYTIC ACTIVITY: [Protease-polymerase p76]: Reaction=a ... | null | null | null | null | FUNCTION: [NTPase]: NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.; FUNCTION: [Viral genome-linked protein]: Viral genome-linked protein is covalently linked to the 5'-end of the positive-strand, negative-strand genomic RNAs and... | Feline calicivirus (FCV) |
N0A5N4 | VAE2_GLOHA | MILGDDECNINEHRFLVALYTSRTLFCGGTLINQEWVLTAAHCNMEDIQIKLGMHSKKVPNEDEQKRVPKEKFFCLSSKNYTLWDKDIMLIRLDSPVKNSAHIAPLSLPSSPPSVGSVCRTMGWGRISSTKETYPDVPHCVNINLLEYEMCRAPYPEFELPATSRTLCAGILEGGKDTCVGDSGGPLICNGQFQGIASWGDDPCAQPHKPAAYTKVFDHLDWIENIIAGNTDASCPP | 3.4.21.- | null | envenomation resulting in modulation of blood coagulation in another organism [GO:0044468]; induction of platelet aggregation in another organism [GO:0035894]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; extraorganismal space [GO:0043245] | serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27666486}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=9.1 umol/min/mg enzyme for the hydrolysis of TAMe (tosyl-arginine methyl ester) substrate {ECO:0000269|PubMed:28579355}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius for the hydrolysis of TAMe (tosyl-arginine methyl ester) substrate. Thermolabile. Activity is reduced about 50% after incubation at 50-55 degrees Celsius for 30 min. Loss of activity after incubation at >60 degrees Celsius... | FUNCTION: Thrombin-like enzyme that shows fibrinogenolytic activity against bovine fibrinogen alpha and beta chains, but not gamma chain. Hydrolyzes fibrin. Enhances ADP-induced human platelet aggregation. Has arginine esterase activity for TAMe (tosyl-arginine methyl ester) substrate. Reduces thrombin-induced thrombos... | Gloydius halys (Chinese water mocassin) (Agkistrodon halys) |
N1NVB7 | GCY6_CAEEL | MIGVYLRSVIFPLLFVIQTICQPPGNVFHLGFLHCDVLENNVEGSTTYINYRTSASAASIAIDKIKREGLLLGYDFKFTILYDQCDENIAAGNAIKLFAEHNVDVLFGPTTNNAAMPVFILATYYNIPLITWGITSSATLDDESRFPTAGMLSIGSRSLAVTFREVMKEYGWDQFVFAYSLEMNDEKCETLRDDFQNMVAYYGDIVLSYAVQIMDHSEEGLLAILKDVSTRGRIIVPCFHEGNSRGLHRRWMLVAARNGFVNDEYVYIFPSLRSRGYAVPQADGTFRYPWTEATGPQPGDQEALLGFQKSIFIVDMQGQG... | 4.6.1.2 | null | cGMP biosynthetic process [GO:0006182]; chemosensory behavior [GO:0007635]; chemotaxis [GO:0006935]; intracellular signal transduction [GO:0035556]; positive regulation of calcium-mediated signaling [GO:0050850]; receptor guanylyl cyclase signaling pathway [GO:0007168]; response to inorganic substance [GO:0010035]; res... | plasma membrane [GO:0005886] | adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; guanylate cyclase activity [GO:0004383]; peptide receptor activity [GO:0001653]; protein kinase activity [GO:0004672] | PF01094;PF00211;PF07701;PF07714; | 3.40.50.2300;3.30.70.1230;1.10.510.10; | Adenylyl cyclase class-4/guanylyl cyclase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000250|UniProtKB:Q19187}; | null | null | null | null | FUNCTION: Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). Regulates chemotaxis responses toward the salt ion Mg(2+) and to a lesser extent toward Cl(1-) in ASE left (ASEL) sensory neuron (PubMed:19523832). {ECO:0000250|UniProtKB:Q19187, ECO:0000269|PubMed:19523832}. | Caenorhabditis elegans |
N1P212 | ATH1_YEASC | MKRIRSLWFNAEASYSNLNNSPSLRNKNSTGNNSRSKNYRSFSRFDLINSILLLMMLFLLAIFVTALYLTKSSRLTYSHASRAALFNPLGVISPSLGNHTLNYDPEARESSKKLYELLSDFNTAYYDDENMILGSNLFSKNTYSRQPYVANGYIGSRIPNIGFGYALDTLNFYTDAPGALNNGWPLRNHRFAGAFVSDFYCLQPKLNSTNFPELDDVGYSTVISSIPQWTNLQFSLVNDSKWFNPQNVTLDDVTNYSQNLSMKDGIVTTELDWLNSQIHVKSEIWAHRHIHPLGVVSLEISLNTDHLPSDFDSLDVNIWD... | 3.2.1.28 | null | carbon utilization [GO:0015976]; trehalose catabolic process [GO:0005993] | cell wall-bounded periplasmic space [GO:0030287]; cytosol [GO:0005829]; fungal-type cell wall [GO:0009277]; membrane [GO:0016020]; vacuolar lumen [GO:0005775] | alpha,alpha-trehalase activity [GO:0004555]; carbohydrate binding [GO:0030246]; protein-glucosylgalactosylhydroxylysine glucosidase activity [GO:0047402] | PF03632;PF03636; | 1.50.10.10;2.70.98.40; | Glycosyl hydrolase 65 family | PTM: Glycosylated. {ECO:0000250|UniProtKB:P48016}. | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P48016}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P48016}. Vacuole lumen {ECO:0000250|UniProtKB:P48016}. Periplasm {ECO:0000269|PubMed:15128531}. Note=May localize to the periplasm either as a membrane-bound or as a free protein (PubMed:15128531).... | CATALYTIC ACTIVITY: Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28; Evidence={ECO:0000305|PubMed:15128531}; | null | null | null | null | FUNCTION: Periplasmic acid trehalase that catalyzes hydrolysis of the disaccharide trehalose and required for growth on trehalose as carbon source (PubMed:15128531). Growth on trehalose is strictly respiratory (PubMed:15128531). {ECO:0000269|PubMed:15128531}. | Saccharomyces cerevisiae (strain CEN.PK113-7D) (Baker's yeast) |
N4V6D4 | BTCA_COLOR | MTTIWEHCVDVDGEVAASTGCFTTLPIRIHRRNDIADDATKQSIHDWGAYVGDGWEQRSGSSWSPVGNWGAFIFPESLPDRLGVITYLANMGNIHDDLCDELPFEEALKEHSNLSQAMEVSNSDTRQCSKASDRSMKMKKYISKCLLEAMEIDRARALRMINSYRSKWLDVMESQNVNDMQTLEEYLAFRNLNGGMEAFWSMVEFGMAIDISESEKTHTRPLFQAAESALVLTNDYWSWDREWRLAQRTQDPRIVNAVHLFMRTEGLSVDQAREKVRERIVDYEREYLRLKEEFYTQNPNLPLYLRRYVEVCGVITAGNH... | 2.5.1.29; 2.5.1.81; 4.2.3.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P9WEV7}; | alcohol biosynthetic process [GO:0046165]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386]; terpenoid biosynthetic process [GO:0016114] | null | lyase activity [GO:0016829]; metal ion binding [GO:0046872]; prenyltransferase activity [GO:0004659] | PF00348;PF19086; | 1.10.600.10; | Terpene synthase family; FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000269|Ref.3}; PhysiologicalDirection=left-to-right;... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|Ref.3}. | null | null | FUNCTION: Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of betaestacins (Ref.3). The bifunctional terpene synthase btcA converts isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into the sesterterpene betaestacin I (Ref.3). The C-terminal prenyltransferase (PT... | Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum lagenarium) |
O00085 | PHYA1_ASPTE | MGFLAIVLSVALLFRSTSGTPLGPRGKHSDCNSVDHGYQCFPELSHKWGLYAPYFSLQDESPFPLDVPEDCHITFVQVLARHGARSPTHSKTKAYAATIAAIQKSATAFPGKYAFLQSYNYSLDSEELTPFGRNQLRDLGAQFYERYNALTRHINPFVRATDASRVHESAEKFVEGFQTARQDDHHANPHQPSPRVDVAIPEGSAYNNTLEHSLCTAFESSTVGDDAVANFTAVFAPAIAQRLEADLPGVQLSTDDVVNLMAMCPFETVSLTDDAHTLSPFCDLFTATEWTQYNYLLSLDKYYGYGGGNPLGPVQGVGWA... | 3.1.3.-; 3.1.3.8 | null | null | extracellular region [GO:0005576] | 3-phytase activity [GO:0016158]; acid phosphatase activity [GO:0003993] | PF00328; | 3.40.50.1240; | Histidine acid phosphatase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:16989, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, ChEBI:CHEBI:58130; EC=3.1.3.8; Evidence={ECO:0000269|PubMed:9025298, ECO:0000269|PubMed:9925555}; PhysiologicalDir... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.6 uM for phytate {ECO:0000269|PubMed:9925555}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. Active from 2.5 to 7.5 with phytic acid as substrate. The optimum pH is shifted to more acidic values with 4-nitrophenyl phosphate as substrate. {ECO:0000269|PubMed:9925555}; | null | FUNCTION: Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate (PubMed:9025298, PubMed:9925555). Myo-inositol 2-monophos... | Aspergillus terreus |
O00092 | PHYA_ASPFU | MVTLTFLLSAAYLLSGRVSAAPSSAGSKSCDTVDLGYQCSPATSHLWGQYSPFFSLEDELSVSSKLPKDCRITLVQVLSRHGARYPTSSKSKKYKKLVTAIQANATDFKGKFAFLKTYNYTLGADDLTPFGEQQLVNSGIKFYQRYKALARSVVPFIRASGSDRVIASGEKFIEGFQQAKLADPGATNRAAPAISVIIPESETFNNTLDHGVCTKFEASQLGDEVAANFTALFAPDIRARAEKHLPGVTLTDEDVVSLMDMCSFDTVARTSDASQLSPFCQLFTHNEWKKYNYLQSLGKYYGYGAGNPLGPAQGIGFTNE... | 3.1.3.-; 3.1.3.8 | null | null | extracellular region [GO:0005576] | 3-phytase activity [GO:0016158]; acid phosphatase activity [GO:0003993] | PF00328; | 3.40.50.1240; | Histidine acid phosphatase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:16989, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, ChEBI:CHEBI:58130; EC=3.1.3.8; Evidence={ECO:0000269|PubMed:9925555}; PhysiologicalDirection=left-to-right; Xref=R... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Highly active from pH 3 to 5 with 4-nitrophenyl phosphate as substrate, and from 2.5 to 7.5 with phytic acid. {ECO:0000269|PubMed:9143104, ECO:0000269|PubMed:9925555}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Able to withstand temperatures up to 100 degrees Celsius over a period of 20 minutes, with a loss of only 10% of the initial enzymatic activity. {ECO:0000269|PubMed:9143104}; | FUNCTION: Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate (PubMed:9143104, PubMed:9925555). Myo-inositol 2-monophos... | Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) |
O00093 | PHYA_EMENI | MAFFTVALSLYYLLSRVSTQAPVVQNHSCNTADGGYQCFPNVSHVWGQYSPYFSIEQESAISEDVPHGCEVTFVQVLSRHGARYPTESKSKAYSGLIEAIQKNATSFWGQYAFLESYNYTLGADDLTIFGENQMVDSGAKFYRRYKNLARKNTPFIRASGSDRVVASAEKFINGFRKAQLHDHGSKRATPVVNVIIPEIDGFNNTLDHSTCVSFENDERADEIEANFTAIMGPPIRKRLENDLPGIKLTNENVIYLMDMCSFDTMARTAHGTELSPFCAIFTEKEWLQYDYLQSLSKYYGYGAGSPLGPAQGIGFTNELI... | 3.1.3.-; 3.1.3.8 | null | null | extracellular region [GO:0005576] | 3-phytase activity [GO:0016158]; acid phosphatase activity [GO:0003993] | PF00328; | 3.40.50.1240; | Histidine acid phosphatase family | PTM: Seems to be cleaved into at least two pieces, most likely due to proteases in the supernatant. The N-terminal fragment, called phyB seems to retain phytase activity. {ECO:0000269|PubMed:9349716}. | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:16989, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, ChEBI:CHEBI:58130; EC=3.1.3.8; Evidence={ECO:0000269|PubMed:9349716, ECO:0000269|PubMed:9925555}; PhysiologicalDir... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:9925555}; | null | FUNCTION: Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate (PubMed:9349716, PubMed:9925555). Myo-inositol 2-monophos... | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
O00100 | PHYA2_ASPTE | MGVFVVLLSIATLFGSTSGTALGPRGNHSDCTSVDRGYQCFPELSHKWGLYAPYFSLQDESPFPLDVPDDCHITFVQVLARHGARSPTDSKTKAYAATIAAIQKNATALPGKYAFLKSYNYSMGSENLNPFGRNQLQDLGAQFYRRYDTLTRHINPFVRAADSSRVHESAEKFVEGFQNARQGDPHANPHQPSPRVDVVIPEGTAYNNTLEHSICTAFEASTVGDAAADNFTAVFAPAIAKRLEADLPGVQLSADDVVNLMAMCPFETVSLTDDAHTLSPFCDLFTAAEWTQYNYLLSLDKYYGYGGGNPLGPVQGVGWA... | 3.1.3.-; 3.1.3.8 | null | null | extracellular region [GO:0005576] | 3-phytase activity [GO:0016158]; acid phosphatase activity [GO:0003993] | PF00328; | 3.40.50.1240; | Histidine acid phosphatase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:16989, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, ChEBI:CHEBI:58130; EC=3.1.3.8; Evidence={ECO:0000269|PubMed:9925555}; PhysiologicalDirection=left-to-right; Xref=R... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=23.2 uM for phytate {ECO:0000269|PubMed:9925555}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. Active from 4 to 6.5. {ECO:0000269|PubMed:9925555}; | null | FUNCTION: Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate (PubMed:9925555). Myo-inositol 2-monophosphate is the end... | Aspergillus terreus |
O00102 | UBC7_SCHPO | MSKAMALRRLMKEYKELTENGPDGITAGPSNEDDFFTWDCLIQGPDGTPFEGGLYPATLKFPSDYPLGPPTLKFECEFFHPNVYKDGTVCISILHAPGDDPNMYESSSERWSPVQSVEKILLSVMSMLAEPNDESGANIDACKMWREDREEYCRVVRRLARKTLGL | 2.3.2.23 | null | ERAD pathway [GO:0036503]; inner nuclear membrane-associated protein degradation pathway [GO:0180027]; protein ubiquitination [GO:0016567] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Hrd1p ubiquitin ligase complex [GO:0000836]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ubiquitin conjugating enzyme activity [GO:0061631] | PF00179; | 3.10.110.10; | Ubiquitin-conjugating enzyme family | PTM: Autoubiquitinated at Cys-90; undergoes 'Lys-48'-linked polyubiquitination, which leads to proteasome-dependent protein degradation. {ECO:0000250|UniProtKB:Q02159}. | null | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROS... | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388}. | null | null | FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the doa10 ubiquitin ligase complex, which is part o... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O00103 | UBC11_SCHPO | MDSDMQNQNPHTNSKNSSSAGMAVDGHSVTKRLRSELMSLMMSNTPGISAFPDSDSNLLHWAGTITGPSDTYYEGLKFKISMSFPANYPYSPPTIIFTSPMWHPNVDMSGNICLDILKDKWSAVYNVQTILLSLQSLLGEPNNASPLNAQAAELWSKDPIEYKRLLMQRYKEIDEI | 2.3.2.23 | null | anaphase-promoting complex-dependent catabolic process [GO:0031145]; cell cycle [GO:0007049]; cell division [GO:0051301]; deactivation of mitotic spindle assembly checkpoint [GO:1902426]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; protein polyubiquitination [GO:0000209]; regulation of mi... | cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ubiquitin conjugating enzyme activity [GO:0061631] | PF00179; | 3.10.110.10; | Ubiquitin-conjugating enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROS... | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388}. | null | null | FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O00115 | DNS2A_HUMAN | MIPLLLAALLCVPAGALTCYGDSGQPVDWFVVYKLPALRGSGEAAQRGLQYKYLDESSGGWRDGRALINSPEGAVGRSLQPLYRSNTSQLAFLLYNDQPPQPSKAQDSSMRGHTKGVLLLDHDGGFWLVHSVPNFPPPASSAAYSWPHSACTYGQTLLCVSFPFAQFSKMGKQLTYTYPWVYNYQLEGIFAQEFPDLENVVKGHHVSQEPWNSSITLTSQAGAVFQSFAKFSKFGDDLYSGWLAAALGTNLQVQFWHKTVGILPSNCSDIWQVLNVNQIAFPGPAGPSFNSTEDHSKWCVSPKGPWTCVGDMNRNQGEEQ... | 3.1.22.1 | null | apoptotic DNA fragmentation [GO:0006309]; DNA metabolic process [GO:0006259]; enucleate erythrocyte differentiation [GO:0043353]; regulation of immune response [GO:0050776] | extracellular exosome [GO:0070062]; lysosome [GO:0005764] | deoxyribonuclease II activity [GO:0004531]; DNA binding [GO:0003677] | PF03265; | null | DNase II family | PTM: Glycosylated. Genetic variations that affect N-glycosylation sites reduce activity, but enzymatic deglycosylation has no effect. {ECO:0000269|PubMed:11906178, ECO:0000269|PubMed:12558498, ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19159218}. | SUBCELLULAR LOCATION: Lysosome. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products.; EC=3.1.22.1; Evidence={ECO:0000269|PubMed:29259162, ECO:0000269|PubMed:31775019}; | null | null | null | null | FUNCTION: Hydrolyzes DNA under acidic conditions with a preference for double-stranded DNA. Plays a major role in the clearance of nucleic acids generated through apoptosis, hence preventing autoinflammation (PubMed:29259162, PubMed:31775019). Necessary for proper fetal development and for definitive erythropoiesis in ... | Homo sapiens (Human) |
O00116 | ADAS_HUMAN | MAEAAAAAGGTGLGAGASYGSAADRDRDPDPDRAGRRLRVLSGHLLGRPREALSTNECKARRAASAATAAPTATPAAQESGTIPKKRQEVMKWNGWGYNDSKFIFNKKGQIELTGKRYPLSGMGLPTFKEWIQNTLGVNVEHKTTSKASLNPSDTPPSVVNEDFLHDLKETNISYSQEADDRVFRAHGHCLHEIFLLREGMFERIPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADETRTIISLDTSQMNRILWVDENNLTAHVEAGITGQELERQLKESGYCTGHEPDSLEFSTVGGWVSTRASG... | 2.5.1.26 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P97275}; | ether lipid biosynthetic process [GO:0008611]; lipid biosynthetic process [GO:0008610] | cytosol [GO:0005829]; membrane [GO:0016020]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777] | alkylglycerone-phosphate synthase activity [GO:0008609]; FAD binding [GO:0071949] | PF02913;PF01565; | 3.30.160.650;3.30.300.330;3.30.465.10;3.30.70.3450;3.30.43.10; | FAD-binding oxidoreductase/transferase type 4 family | null | SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250|UniProtKB:P97275}. Peroxisome {ECO:0000250|UniProtKB:P97275}. | CATALYTIC ACTIVITY: Reaction=a 1-acylglycerone 3-phosphate + a long chain fatty alcohol = 1-O-alkylglycerone 3-phosphate + a long-chain fatty acid + H(+); Xref=Rhea:RHEA:36171, ChEBI:CHEBI:15378, ChEBI:CHEBI:17135, ChEBI:CHEBI:57534, ChEBI:CHEBI:57560, ChEBI:CHEBI:73315; EC=2.5.1.26; Evidence={ECO:0000269|PubMed:839934... | null | PATHWAY: Glycerolipid metabolism; ether lipid biosynthesis. | null | null | FUNCTION: Catalyzes the exchange of the acyl chain in acyl-dihydroxyacetonephosphate (acyl-DHAP) for a long chain fatty alcohol, yielding the first ether linked intermediate, i.e. alkyl-dihydroxyacetonephosphate (alkyl-DHAP), in the pathway of ether lipid biosynthesis. {ECO:0000269|PubMed:8399344, ECO:0000269|PubMed:95... | Homo sapiens (Human) |
O00124 | UBXN8_HUMAN | MASRGVVGIFFLSAVPLVCLELRRGIPDIGIKDFLLLCGRILLLLALLTLIISVTTSWLNSFKSPQVYLKEEEEKNEKRQKLVRKKQQEAQGEKASRYIENVLKPHQEMKLRKLEERFYQMTGEAWKLSSGHKLGGDEGTSQTSFETSNREAAKSQNLPKPLTEFPSPAEQPTCKEIPDLPEEPSQTAEEVVTVALRCPSGNVLRRRFLKSYSSQVLFDWMTRIGYHISLYSLSTSFPRRPLAVEGGQSLEDIGITVDTVLILEEKEQTN | null | null | ERAD pathway [GO:0036503]; single fertilization [GO:0007338] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151] | protein-macromolecule adaptor activity [GO:0030674]; ubiquitin binding [GO:0043130] | PF00789; | null | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21949850}; Multi-pass membrane protein {ECO:0000269|PubMed:21949850}. | null | null | null | null | null | FUNCTION: Involved in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins, possibly by tethering VCP to the endoplasmic reticulum membrane. May play a role in reproduction. {ECO:0000269|PubMed:21949850}. | Homo sapiens (Human) |
O00139 | KIF2A_HUMAN | MATANFGKIQIGIYVEIKRSDGRIHQAMVTSLNEDNESVTVEWIENGDTKGKEIDLESIFSLNPDLVPDEEIEPSPETPPPPASSAKVNKIVKNRRTVASIKNDPPSRDNRVVGSARARPSQFPEQSSSAQQNGSVSDISPVQAAKKEFGPPSRRKSNCVKEVEKLQEKREKRRLQQQELREKRAQDVDATNPNYEIMCMIRDFRGSLDYRPLTTADPIDEHRICVCVRKRPLNKKETQMKDLDVITIPSKDVVMVHEPKQKVDLTRYLENQTFRFDYAFDDSAPNEMVYRFTARPLVETIFERGMATCFAYGQTGSGKT... | null | null | cell differentiation [GO:0030154]; cell division [GO:0051301]; microtubule cytoskeleton organization [GO:0000226]; microtubule depolymerization [GO:0007019]; microtubule-based movement [GO:0007018]; mitotic spindle assembly [GO:0090307]; mitotic spindle organization [GO:0007052]; nervous system development [GO:0007399]... | centriolar subdistal appendage [GO:0120103]; centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; kinesin complex [GO:0005871]; membrane [GO:0016020]; microtubule [GO:0005874]; nuclear body [GO:0016604]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; spindle [GO:0005819]; sp... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cytoskeletal motor activity [GO:0003774]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777] | PF00225; | 3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, MCAK/KIF2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, spindle. Note=Localized to the spindle microtubules and spindle poles from prophase to metaphase. Efficient targeting to spindle microtubules... | null | null | null | null | null | FUNCTION: Plus end-directed microtubule-dependent motor required for normal brain development. May regulate microtubule dynamics during axonal growth. Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate. Required for normal spindle dynamics during mitosis.... | Homo sapiens (Human) |
O00141 | SGK1_HUMAN | MTVKTEAAKGTLTYSRMRGMVAILIAFMKQRRMGLNDFIQKIANNSYACKHPEVQSILKISQPQEPELMNANPSPPPSPSQQINLGPSSNPHAKPSDFHFLKVIGKGSFGKVLLARHKAEEVFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTADKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEHNSTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNI... | 2.7.11.1 | null | apoptotic process [GO:0006915]; cellular response to aldosterone [GO:1904045]; DNA damage response [GO:0006974]; intracellular signal transduction [GO:0035556]; long-term memory [GO:0007616]; neuron projection morphogenesis [GO:0048812]; positive regulation of transporter activity [GO:0032411]; protein phosphorylation ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; calcium channel regulator activity [GO:0005246]; chloride channel regulator activity [GO:0017081]; potassium channel regulator activity [GO:0015459]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase act... | PF00069;PF00433; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family | PTM: Regulated by phosphorylation (PubMed:10191262, PubMed:11096081, PubMed:18925875, PubMed:20338997, PubMed:36373794). Activated by phosphorylation on Ser-422 by mTORC2, transforming it into a substrate for PDPK1 which phosphorylates it on Thr-256 (PubMed:10191262, PubMed:18925875, PubMed:20338997, PubMed:36373794). ... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endoplasmic reticulum membrane. Cell membrane. Mitochondrion. Note=The subcellular localization is controlled by the cell cycle, as well as by exposure to specific hormones and environmental stress stimuli. In proliferating cells, it shuttles between the nucleus and cytoplasm 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... | Homo sapiens (Human) |
O00142 | KITM_HUMAN | MLLWPLRGWAARALRCFGPGSRGSPASGPGPRRVQRRAWPPDKEQEKEKKSVICVEGNIASGKTTCLEFFSNATDVEVLTEPVSKWRNVRGHNPLGLMYHDASRWGLTLQTYVQLTMLDRHTRPQVSSVRLMERSIHSARYIFVENLYRSGKMPEVDYVVLSEWFDWILRNMDVSVDLIVYLRTNPETCYQRLKKRCREEEKVIPLEYLEAIHHLHEEWLIKGSLFPMAAPVLVIEADHHMERMLELFEQNRDRILTPENRKHCP | 2.7.1.-; 2.7.1.21; 2.7.1.74 | null | deoxycytidine metabolic process [GO:0046092]; DNA biosynthetic process [GO:0071897]; nucleobase-containing compound metabolic process [GO:0006139]; phosphorylation [GO:0016310]; pyrimidine nucleoside salvage [GO:0043097]; thymidine metabolic process [GO:0046104] | cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; deoxycytidine kinase activity [GO:0004137]; deoxynucleoside kinase activity [GO:0019136]; nucleoside kinase activity [GO:0019206]; thymidine kinase activity [GO:0004797] | PF01712; | 3.40.50.300; | DCK/DGK family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9989599}. | CATALYTIC ACTIVITY: Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129, ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21; Evidence={ECO:0000269|PubMed:11687801, ECO:0000269|PubMed:9989599}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16 uM for thymidine {ECO:0000269|PubMed:9989599}; KM=36 uM for 2'-deoxycytidine {ECO:0000269|PubMed:9989599}; | null | null | null | FUNCTION: Phosphorylates thymidine, deoxycytidine, and deoxyuridine in the mitochondrial matrix (PubMed:11687801, PubMed:9989599). In non-replicating cells, where cytosolic dNTP synthesis is down-regulated, mtDNA synthesis depends solely on TK2 and DGUOK (PubMed:9989599). Widely used as target of antiviral and chemothe... | Homo sapiens (Human) |
O00144 | FZD9_HUMAN | MAVAPLRGALLLWQLLAAGGAALEIGRFDPERGRGAAPCQAVEIPMCRGIGYNLTRMPNLLGHTSQGEAAAELAEFAPLVQYGCHSHLRFFLCSLYAPMCTDQVSTPIPACRPMCEQARLRCAPIMEQFNFGWPDSLDCARLPTRNDPHALCMEAPENATAGPAEPHKGLGMLPVAPRPARPPGDLGPGAGGSGTCENPEKFQYVEKSRSCAPRCGPGVEVFWSRRDKDFALVWMAVWSALCFFSTAFTVLTFLLEPHRFQYPERPIIFLSMCYNVYSLAFLIRAVAGAQSVACDQEAGALYVIQEGLENTGCTLVFLLL... | null | null | B cell differentiation [GO:0030183]; bone regeneration [GO:1990523]; canonical Wnt signaling pathway [GO:0060070]; learning or memory [GO:0007611]; negative regulation of mitochondrial depolarization [GO:0051902]; negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathw... | cell surface [GO:0009986]; cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; filopodium membrane [GO:0031527]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [G... | G protein-coupled receptor activity [GO:0004930]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; Wnt receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147] | PF01534;PF01392; | 1.10.2000.10;1.20.1070.10; | G-protein coupled receptor Fz/Smo family | PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9R216}; Multi-pass membrane protein {ECO:0000255}. Note=Relocalizes DVL1 to the cell membrane leading to phosphorylation of DVL1 and AXIN1 relocalization to the cell membrane. {ECO:0000250|UniProtKB:Q8K4C8}. | null | null | null | null | null | FUNCTION: Receptor for WNT2 that is coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (By similarity). Plays a role in neuromuscular junction (NMJ) assembly by... | Homo sapiens (Human) |
O00148 | DX39A_HUMAN | MAEQDVENDLLDYDEEEEPQAPQESTPAPPKKDIKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQIEPVNGQVTVLVMCHTRELAFQISKEYERFSKYMPSVKVSVFFGGLSIKKDEEVLKKNCPHVVVGTPGRILALVRNRSFSLKNVKHFVLDECDKMLEQLDMRRDVQEIFRLTPHEKQCMMFSATLSKDIRPVCRKFMQDPMEVFVDDETKLTLHGLQQYYVKLKDSEKNRKLFDLLDVLEFNQVIIFVKSVQRCMALAQLLVEQNFPAIAIHRGM... | 3.6.4.13 | null | mRNA export from nucleus [GO:0006406]; mRNA splicing, via spliceosome [GO:0000398]; RNA export from nucleus [GO:0006405] | cytoplasm [GO:0005737]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; identical protein binding [GO:0042802]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724] | PF00270;PF00271; | 3.40.50.300; | DEAD box helicase family, DECD subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21859714}. Cytoplasm {ECO:0000269|PubMed:21859714}. Note=Can translocate to the cytoplasm in the presence of MX1. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; | null | null | null | null | FUNCTION: [Isoform 1]: Involved in pre-mRNA splicing. Required for the export of mRNA out of the nucleus. {ECO:0000269|PubMed:15047853, ECO:0000269|PubMed:17548965}. | Homo sapiens (Human) |
O00151 | PDLI1_HUMAN | MTTQQIDLQGPGPWGFRLVGGKDFEQPLAISRVTPGSKAALANLCIGDVITAIDGENTSNMTHLEAQNRIKGCTDNLTLTVARSEHKVWSPLVTEEGKRHPYKMNLASEPQEVLHIGSAHNRSAMPFTASPASSTTARVITNQYNNPAGLYSSENISNFNNALESKTAASGVEANSRPLDHAQPPSSLVIDKESEVYKMLQEKQELNEPPKQSTSFLVLQEILESEEKGDPNKPSGFRSVKAPVTKVAASIGNAQKLPMCDKCGTGIVGVFVKLRDRHRHPECYVCTDCGTNLKQKGHFFVEDQIYCEKHARERVTPPEG... | null | null | actin cytoskeleton organization [GO:0030036]; establishment or maintenance of actin cytoskeleton polarity [GO:0030950]; fibroblast migration [GO:0010761]; heart development [GO:0007507]; maintenance of cell polarity [GO:0030011]; muscle structure development [GO:0061061]; regulation of transcription by RNA polymerase I... | adherens junction [GO:0005912]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; filamentous actin [GO:0031941]; focal adhesion [GO:0005925]; stress fiber [GO:0001725]; transcription regulator complex [GO:0005667]; Z disc [GO:0030018] | actin binding [GO:0003779]; cadherin binding involved in cell-cell adhesion [GO:0098641]; metal ion binding [GO:0046872]; muscle alpha-actinin binding [GO:0051371]; transcription coactivator activity [GO:0003713] | PF15936;PF00412;PF00595; | 2.30.42.10;2.10.110.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10861853, ECO:0000269|PubMed:11110697}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10861853, ECO:0000269|PubMed:11110697}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:10861853}. Note=Associates with actin stress fibers. {ECO:0000269|PubMed:11110697}. | null | null | null | null | null | FUNCTION: Cytoskeletal protein that may act as an adapter that brings other proteins (like kinases) to the cytoskeleton (PubMed:10861853). Involved in assembly, disassembly and directioning of stress fibers in fibroblasts. Required for the localization of ACTN1 and PALLD to stress fibers. Required for cell migration an... | Homo sapiens (Human) |
O00154 | BACH_HUMAN | MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVPLSLKNVDKVLEVPPVVYSRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDSSQ... | 3.1.2.2 | null | acyl-CoA metabolic process [GO:0006637]; coenzyme A biosynthetic process [GO:0015937]; fatty acid catabolic process [GO:0009062]; long-chain fatty-acyl-CoA catabolic process [GO:0036116]; medium-chain fatty acid biosynthetic process [GO:0051792]; medium-chain fatty-acyl-CoA catabolic process [GO:0036114]; palmitic acid... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654] | carboxylic ester hydrolase activity [GO:0052689]; fatty-acyl-CoA binding [GO:0000062]; long-chain fatty acyl-CoA binding [GO:0036042]; long-chain fatty acyl-CoA hydrolase activity [GO:0052816]; protein homodimerization activity [GO:0042803] | PF03061; | 3.10.129.10; | null | null | SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm, cytosol {ECO:0000305|PubMed:12435388}.; SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm, cytosol {ECO:0000305|PubMed:12435388}.; SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:12435388}.; SUBCELLULAR LOCATION: [Isoform 5]: Mitochondrion {ECO:0000269|PubMe... | CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000269|PubMed:10578051}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={... | null | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:10578051}. | null | null | FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (PubMed:10578051). Preferentially hydrolyzes palmitoyl-CoA, but has a broad specificity acting on other fatty acyl-CoAs with chain-lengths of C8-C18 (PubMed:10578051). May play ... | Homo sapiens (Human) |
O00155 | GPR25_HUMAN | MAPTEPWSPSPGSAPWDYSGLDGLEELELCPAGDLPYGYVYIPALYLAAFAVGLLGNAFVVWLLAGRRGPRRLVDTFVLHLAAADLGFVLTLPLWAAAAALGGRWPFGDGLCKLSSFALAGTRCAGALLLAGMSVDRYLAVVKLLEARPLRTPRCALASCCGVWAVALLAGLPSLVYRGLQPLPGGQDSQCGEEPSHAFQGLSLLLLLLTFVLPLVVTLFCYCRISRRLRRPPHVGRARRNSLRIIFAIESTFVGSWLPFSALRAVFHLARLGALPLPCPLLLALRWGLTIATCLAFVNSCANPLIYLLLDRSFRARALD... | null | null | calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; G protein-coupled receptor signaling pathway [GO:0007186]; immune response [GO:0006955]; positive regulation of cytosolic calcium ion concentration [GO:0007204] | external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; G protein-coupled receptor activity [GO:0004930] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Orphan receptor. | Homo sapiens (Human) |
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