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 | MPLPQPLLGGASPAPARAASSFLHPLLHTRHRVSTAPAAASSFVPASHSSHANDAMLLRRAADVADRSAGLTSPHPNFGCVIARPQLNTDSADSWVVGEGFLYAQGTPCAELLASQEAGEHARGGTAYLNLEPGDCFGDNTAVGSLVQAGITRVVVGLRHPLKHLRGKAIQALRNEGIQVDVVGEDLQSKLFKEALKSCLTVNAPLLYRAAFHVPFSVLKYAMTADGKIAASSGHASWISGKASRGRVFELRGRSDAVIVGGNTVRFDDPRLTARHVKGHVPVRIVMSQSLNLPEEANLWNLNDAYTIVATQRGARRDFQRKLAMKGVEVVEFDMLNPRAVMSYCYDRGYLAVLWECGGTLAASAISASVIHKVYAFWAPKIIGGLNAPTPVGELGMSQMTQAINLIDVSYEQIDRDMLMSGFIEPIPDLSPVIPSVEEIPSIDPEVSPYETNIISFYKTWDIFGAFSNFSPHSIQMPDENGDYFTWPTVEHYYQAHKFVGVDNPQARDIVQEIKLAKSPEEAARIGRTRQKGFPELVRTDWESTKIDVMYRAIKCKFSTYPHLTNMLLSTAGSVLVEASPHDLFWGGGREGEGLNYLGRLLMQLRSEILGTVPASAEVGEAD | 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}; CATALYTIC ACTIVITY: Reaction=2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H2O = 2,5,6-triamino-4-hydroxypyrimidine + D-ribose 5-phosphate; Xref=Rhea:RHEA:23436, ChEBI:CHEBI:15377, ChEBI:CHEBI:58614, ChEBI:CHEBI:78346, ChEBI:CHEBI:137796; Evidence={ECO:0000269|PubMed:25431972}; CATALYTIC ACTIVITY: Reaction=5-amino-6-(5-phospho-D-ribosylamino)uracil + H2O = 5,6-diaminouracil + D-ribose 5-phosphate; Xref=Rhea:RHEA:55020, ChEBI:CHEBI:15377, ChEBI:CHEBI:46252, ChEBI:CHEBI:58453, ChEBI:CHEBI:78346; Evidence={ECO:0000269|PubMed:25431972}; | 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-ribosylamino)pyrimidine as substrate. kcat is 9.39 sec(-1) with 5-amino-6-(5-phospho-D-ribosylamino)uracil as substrate. {ECO:0000269|PubMed:25431972}; | 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:0000269|PubMed:23150645}.; FUNCTION: Catalyzes the hydrolysis of the N-glycosidic bond in the first two intermediates of riboflavin biosynthesis, which are highly reactive metabolites, yielding relatively innocuous products. Thus, can divert a surplus of harmful intermediates into relatively harmless products and pre-empt the damage these intermediates would otherwise do. Has no activity against GTP, nucleoside monophosphates or ADP-ribose. {ECO:0000269|PubMed:25431972}. | 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|PubMed:25786135}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55521; Evidence={ECO:0000269|PubMed:23134568, ECO:0000269|PubMed:23757397, ECO:0000269|PubMed:25786135}; CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + neryl diphosphate; Xref=Rhea:RHEA:11328, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:57665, ChEBI:CHEBI:128769; Evidence={ECO:0000269|PubMed:25786135}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11329; Evidence={ECO:0000269|PubMed:25786135}; CATALYTIC ACTIVITY: Reaction=isopentenyl diphosphate + neryl diphosphate = (2Z,6Z)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:64572, ChEBI:CHEBI:33019, ChEBI:CHEBI:57665, ChEBI:CHEBI:60374, ChEBI:CHEBI:128769; Evidence={ECO:0000269|PubMed:25786135}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64573; Evidence={ECO:0000269|PubMed:25786135}; CATALYTIC ACTIVITY: Reaction=(2Z,6Z)-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + nerylneryl diphosphate; Xref=Rhea:RHEA:64580, ChEBI:CHEBI:33019, ChEBI:CHEBI:60374, ChEBI:CHEBI:128769, ChEBI:CHEBI:139032; Evidence={ECO:0000269|PubMed:25786135}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64581; Evidence={ECO:0000269|PubMed:25786135}; | 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 | MNKIYKVIWNATLLAWVAVSELAKGKTKSTTSKSKAKSLSSSVIVGGIILTTPLSLIAATVQVGGGTNSGTTATASTNCADLYNYQNPENSGSGAAGNYNAGNPSVCSIAIGENAQGGTSGTGGSPGIAIGGNSKATGGLSVAIGGYAQATNVGSIALGTAALSSGFNSLAISRQAAATNNYSIAIGTTSVSKGVGSIAMGHSTNASGDQSIAIGSSDAVNSATATTTYDGTTNTQASGSKSIAIGASAKASTNNSIALGAGSVTSAQSGNSYLTGVGASATNGVVSVGTSTATRRIQNVADGSAASDAVTVAQLDKAYDDTNGRLAAALGTGSGAAYNAANNTYTAPTNIGGTGKNTIDDAIKATQRSVVAGSNIVVTPTTASDGSISYSVATSATPTFTSITVNNAPTAGTDATNKTYVDSKAAASRTEVAAGSNVSGVVKTTGANGQDVYTVNANGTTASAGSSAVTVTPGTKDANNVTDYKVDLSATTKTDIQKGVDAKNAVDTAGLKFKGDTATTSNTKKLGDTVSITGDTNISTVATTDGVQVKLNPNLDLGATGSVKTGNTTINNAGVTADQVTVGGVVINNTSGINAGGKAITNVAAPTNNTDAANKKYVDDAGTALTNLGFGLKAQDGTTVNKKLGEAVDIVGSNSNISTKVNAGKVEVALSNTLDLGTTGSVTTGSTVINNAGVTATQVTANKVTINNAPTAGTDATNKTYVDSKAAASRTEVAAGSNVSGVVKTTGANGQDIYAVNANGTTASAGSSAVTVTPGTKDANNVTDYKVDLSATTKTDIQKGVDAKNAVDTAGLKFKGDTATTSNTKKLGDTVSITGDTNISTVATTDGVQVKLNPNLDLGATGSVKTGNTTINNAGVTADQVTVGGVVINNTSGINAGGKAITNVAAPTNNTDAANKKYVDDAGTALTNLGFGLKAQDGTTVNKKLGEAVDIVGSNSNISTKVNAGKVEVALSNTLDLGTTGSVTTGSTVINNAGVTATQVTANKVTVNNAPTAGTDATNKTYVDSKAAASRTEVAAGSNVSGVVKTTGANGQDVYTVNANGTTASAGSSAVTVTPGTKDANNVTDYKVDLSATTKTDIQKGVDAKNAVDTAGLKFKGDTATTSNTKKLGDTVSITGDTNISTVATTDGVQVKLNPNLDLGATGSVKTGNTTINNAGVTADQVTVGGVVINNTSGINAGGKAITNVAAPTNNTDAANKKYVDDAGTALTNLGFGLKAQDGTTVNKKLGEAVEVVGADSNITTKVAGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISVKDGSGNTIAGVDNTALTVKDGSGNTETSINQAINTLNAAQGETDKFAVKYDKNADGSVNYNNITLAGTTASSTQDATTGKITTTGGTSLNNVASAGDYKDVANASKGVNAGDLNNAVVDATNAATSKGFALQAADGAKVQKNLGEAVEVVGADSNITTKVAGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISVKDGSGNTIAGVDNTALTVKDGSGNTETSINQAINTLNAAQGETDKFAVKYDKNTDGSTNYNSITAGNGNGTAATIGTDTAGNSVVTSGGTKISNVANGVNASDAVNKGQLDSLSTGLTNTGFGLKAADGNTVNKKLGEAVDVVGADSNITTKVAGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISIKDGSGNTIAGVDNTALTVKDGSGNTETSINQAINTLNAAQGETDKFAVKYDKNADGSANYNNITLAGTTASSTQDATTGKITTTGGTSLNNVASAGDYKDVANASKGVNAGDLNNAVVDATNAATSKGFALQAADGAKVQKNLGEAVEVVGADSNITTKVVGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISVKDGSGNTIAGVDNTALTVKDGSGNTETSINQAINTLNAAQGETDKFAVKYDKNADGSVNYNNITLAGTTASSTQDATTGKITTTGGTSLNNVASAGDYKDVANASKGVNAGDLNNAVVDATNAATSKGFALQAADGAKVQKNLGEAVEVVGADSNITTKVAGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISVKDGSGNTIAGVDNTALTVKDGSGNTETSINQAINTLNAAQGETDKFAVKYDKNADGSVNYNNITLAGTTASSTQDATTGKITTTGGTSLNNVASAGDYKDVANASKGVNAGDLNNAVVDATNAATSKGFALQAADGAKVQKNLGEAVEVVGADSNITTKVAGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISVKDGSGNTIAGVDNTALTVKDGSGNTETSINQAINTLNAAQGETDKFAVKYDKNADGSANYNNVTLAGTNGTIISNVKAGAVTSTSTDAINGSQLYGVANSVKNAIGGSTTIDATTGAITTTNIGGTGSNTIDGAISSIKDSATKAKTTVSAGDNVVVTSGTNADGSTNYEVATAKDVNFDKVTVGSVVVDKSSNTIKGLSNTTWNGTAVSGQAATEDQLKTVSDAQGETDKFAVKYDKNADGSANYNSITAGNGNGTAATIGTDTAGNSVVTSGGTKISNVANGVNASDAVNKGQLDSLSTGLTNTGFGLKAADGNTVNKKLGEAVDVVGADSNITTKVAGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISIKDGSGNTIAGVDNTALTVKDSSGNTETSINQAINTLNAAQGETDKFAVKYDKNADGSVNYNNVTLAGTNGTIIRNVKAGAVTSTSTDAINGSQLYDIANSVKNAIGGSTTRDVTTGAITTTNIGGTGSNTIDGAISSIKDSATKAKTTISAGDNVVVTSGTNADGSTNYEVATAKDVNFDKVTVGNVVVDKANDTIQGLSNKDLNSTDFATKGRAATEEQLKAVITSNITEVVDGNGNKVNIIDQVVNTKPDNKNQDSLFLTYDKQGQETTDRLTIGQTVQKMNTDGIKFFHTNADTSKGDLGTTNDSSAGGLNSTAIGVNAIVANGADSSVALGHNTKVNGKQSIAIGSGAEALGNQSISIGTGNKVTGDHSGAIGDPTIVNGANSYSVGNNNQVLTDDTFVLGNNVTKTIAGSVVLGNGSAATTGAGEAGYALSVATNADKAAITKTTSSTGAVAVGDASSGIYRQITGVAAGSVDSDAVNVAQLKAVGNQVVTTQTTLVNSLGGNAKVNADGTITGPTYNVAQGNQTNVGDALTALDNAINTAATTSKSTVSNGQNIVVSKSKNADGSDNYEVSTAKDLTVDSVKAGDTVLNNAGITIGNNAVVLNNTGLTISGGPSVTLAGIDAGNKTIQNVANAVNATDAVNKGQLDSAINNVNNNVNELANNAVKYDDASKDKITLGGGATGTTITNVKDGTVAQGSKDAVNGGQLWNVQQQVDQNTTDISNIKNDINNGTVGLVQQAGKDAPVTVAKDTGGTTVNVAGTDGNRVVTGVKEGAVNATSKDAVNGSQLNTTNQAVVNYLGGGAGYDNITGSFTAPSYTVGDSKYNNVGGAIDALNQADQALNSKIDNVSNKLDNAFRITNNRIDDVEKKANAGIAAAMALESAPYVPGKYTYAAGAAYHGGENAVGVTLRKTADNGRWSITGGVAAASQGDASVRIGISGVID | 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 long, 3.5 nm diameter) on the cell surface; an antibody against residues 699-1014 only labels the distal tip of these fibers (PubMed:23155410, PubMed:27074146). The C-terminal translocator domain is probably localized in the outer membrane (Probable). {ECO:0000269|PubMed:23155410, ECO:0000269|PubMed:27074146, ECO:0000305|PubMed:23155410}. | 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 autoagglutination and binding to PS, type I collagen, PP, PVC, glass and SS upon expression in Acinetobacter baylyi strain ADP1 (PubMed:23155410). Involved in rapid, irreversible adherence to polyurethane (PubMed:17090933). Forms an unusual biofilm (PubMed:31972092). An extended, surface exposed fiber binds to quartz crystals, PS and glass. It can be removed by washing in distilled water (PubMed:27305955, PubMed:28720107). {ECO:0000269|PubMed:17090933, ECO:0000269|PubMed:23155410, ECO:0000269|PubMed:27305955, ECO:0000269|PubMed:28720107, ECO:0000269|PubMed:31972092}. | 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 drug. Unfortunately, the oxidation of the methionine is readily to happen during toxin synthesis and oxidation steps as well as under oxidative environment in vivo, which should still be considered to find a solution to this major drawback. {ECO:0000269|PubMed:29925760}. | 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)=4550 nM) nAChRs (PubMed:24200193, PubMed:28603989, PubMed:29925760). The toxin competes with agonists in the orthosteric binding site of alpha-3-beta-4/CHRNA3-CHRNB4 and alpha-6-beta-4/CHRNA6-CHRNB4 (PubMed:30252466). {ECO:0000269|PubMed:24200193, ECO:0000269|PubMed:28603989, ECO:0000269|PubMed:29925760, ECO:0000305|PubMed:30252466}. | Conus textile (Cloth-of-gold cone) |
K8ERR8 | LSY12_CAEEL | MGKKRKPSPERSSDEDEVSTPSPKDRTARPTAAARRENVALSQAVALSLEDASNFCSLAFSLERIKREPVDTDYDDPNQPGPSSVPVSARTDHVLPIRFKIKAEPQEYDSDEYGKDHGAVQIANKEVPAISPIEEVSQKRRGRPRKTDAAQHLFFPHVSIKQEPDDGFINFHESRCVGIAQDPEMQHLHDVNESHSSEIAIFRETKKITERKKKKTEAEKLWDNMSLTEKEVFQSHTRRRRTTRLPIIQNFEETEEGCIVEVPIPLIDLDNDAVESVTGPQHENVTVSENVLSTESTDQEVTETKRLHDSSRDFNPPRIQDTPSTVIRPEGDQKDPMSSTSSKRRNTNNSRCASLLSNPHSTPVTRLMRGILDSENSDNDEMLSNDQSEIAKRPRTPRPRYSPEAQRRTNSRLSALTIDTNRSNDLNVDGSAPSSSSAASCGLSTPDPDRTSQQRRKGNQSAARSRKIKTPSPPLSQEDEPMELDSDDDPVNELDNLPIVIDDPSYVLTKEHKEIFEQVKKSVSDRNEFSPAQISEIYRSSKGEQARLPERIHFGAFIMKTWYGSPFPAEFINVKKLFICEFCFFYARSDEIMQNHAKKCMLRAPPGLEIYRKGDISVFEVDGRLQKEYCQTLCLVSRMFLESKTVFYDTEPFFFYIVTINDDIGCHFAGYFSKEKYEPDVNNLSCIMTLPCYQEMGLGRFLIDISYALSRKEKWFGGPEQPLSELGRKAYGGYWRTTIASCLGRLKDELEFGSGISIKMIADDTGVNCHDILEVVCSLGWAKPVDPDEKNHYKLEWDVDWDMVSIILRESEASKETKVQYDPECLDWVPRKMRPSMDGYHELSKEEIEQDEQRRKSIQKTPVHVSMEKATPTSTTSLPVGSVKKELRSRGHNRSVGRNLKHEVNRKVKVPEWAAARDLTDEEITVEENKKQQKQNRKIFTRCADSVLDKSNIREETPEDDEPGPSTKPSGKRQRGNKCNNTESEPNPSGRKTSATSSGRGKYRNRRTDGTEEEEEDDDPTDSEPLTTDDEKPFETSVNKEKNEKSRRGKKVSKKRRSVAGKKFPPNFGVRDRDEPKKAENSEDGEGLESKPGPSTEMILVEKVEEEEAKVTVSDINMQASESKIEGIEQTSEVDIPKSDEDHQSTEAYDRVEDEVPITDYNIPTPDSYHSSPPHSPTPSPQPQLMQAQQNIYQDNDCHFAENDSKPPHLVSEVDDPAAPQPTVTLQSGPSDAPPLSHNSVDGYSTGDDDAPPNLSPQIGKSENNEEEMPLIAPIVQHNGITHHEESTAQHYHDSMNAGPSTSSHVTPQMSMINTTPQQPPFSHPNSQQQATPGSGGVPSCGPAYTHHTPEQQSQQFMSPPMAGMPASVASNHSIHNSNSIEMVGGPASLQHTPQQYEMGHSMAQMSQESAIGGINTVPSIEQQNQLMLQHHQFSSPPAAPPPSQQQQVVQPPIPPAPTTANGRRRSESAATQRTKARQQHQHQQQQPQQPQQRIAAPGVPQGVHPQMQFPMNAMNMMPAYPPFYPYTNYPNIWQPPYQNYPYNQVDYQQPWLYNNGHIPHQTNGTATNQFHPGHMGYFPNNNGR | 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 polymerase II [GO:0006357] | 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:PRU01063}; | 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 | MLSILPLAYSNFSRILQYFEQLPVVDKMTEEILKQGVGIVETSLTFEPPFCESFERISIDNFPIFALGKEISKEDGIEAMKKYVTSRFWFTYRRDFSPIGGTGPSTDQGWGCMLRCAQMLLGEVLLRRHIGRHFEWDIEKTSEIYEKILQMFFDEKDALYSIHQIAQMGVTEGKEVSKWFGPNTAAQVMKKLTIFDDWSNIAVHVALDNILVKEDAITMATSYPSEDAVKLIMENGLVDKNRLSLSPGNIIPEWRPLLLMIPLRLGLTTINPCYLSAIQEFFKIPQCVGIIGGRPNHALYFVGMSGSKLFYLDPHYCRPKTESTAKMYAEKDSTATTDDVGFSHLEELVPLPSQTADVYTKMDDSTYHCQMMLWIEYENVDPSLALAMFCETRDEFENLCETLQKTTLPASQPPMFEFLQRRPKYLPKFEPYTGVSMKIEMKEFDDIGAANVKIDDDFEVLDVHTEEEDADEDNDDDVANA | 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, ChEBI:CHEBI:172941; Evidence={ECO:0000250|UniProtKB:Q9Y4P1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67549; Evidence={ECO:0000250|UniProtKB:Q9Y4P1}; | 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) and insertion to membranes, which is necessary for autophagy (Probable). Its cleavage activity is functionally redundant to atg-4.2, but it cleaves lgg-1 precursors more efficiently than atg-4.2 (Probable). Acts redundantly with atg-4.2 to promote the lgg-1 delipidation to release the protein from membranes, which facilitates multiple events during macroautophagy (PubMed:22767594). Unlike atg-4.2 does not seem to be required for autophagosome maturation (PubMed:30880001). {ECO:0000269|PubMed:22767594, ECO:0000269|PubMed:30880001}. | Caenorhabditis elegans |
K8FE10 | SYT2_CAEEL | MWATGAIVCSPVFRILSTCCPIRRGVPTSNGYHPRPKHVDIGNGAVPILSSKPITVQPTNSDYYEPVNNGTLPLSSSGALIKQYGNIHFRVEYDFEQSKLSVTIVSASDLPAMDRNGMSDPYVKVYVLPERKQKFETRIIRNTLNPTYNETFQFSIPFNELHSKTLMLVVYDYDRLSKDDKMGQLSVPLESIDFGITTDIERPLQKPEKDDEKECRLGDICFSTRYRPATGTVTLTIMEARNLKKMDVGGSSDPYVKIYLHHGRKLLSKKKTSRKYKTLNPYYNESFQFKIEPHMIEKVHLIVSVWDYDKMSKNDFIGEVTLGSKHLNLPQITHACSEQWAEMMTSRRPVVQWHTLQERMEKEKKKDDD | 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 | MKLLFLALLSLLALGPSLAARRRGVRWCTISKPEAAKCSKLQQNLKRVRGPSLSCISRKSYLECIQAIAAKRADAMSLDAGLVYEAGQDPYRLRPVAAEVYGTEGAPRTHYYAVALVKKDSNLQLNQLQGVRSCHTGLNRSAGWKIPVGTLRPYLGWAGPPAPLQEAVANFFSASCVPCADGNQYPNLCRLCAGTGADKCACSSKEPYFGYSGAFKCLKDGAGDVAFVKDSTVFENLPNKAERDQYELLCPDNTRKPVDEFEQCHLARVPSHAVVARSVGGKEDSIWRLLSKAQEKFGKGTSGSFQLFSSPPGQKDLLFKDGAQGFLRIPSRVDAELYLGPSYLTVIKNLKESAAEVEARGARVVWCAVGPEELRKCQQWSGQSNGTVTCTTAADTEDCIALVLKGEADAMSLDGGVIYIAGKCGLAPVLAESQRSEGGSNLDCVNRPLEGDRAVAVVRKSSAGLTWNSRRGTKSCHTAVGRTAGWNIPMGLLFNQTRSCNFDEFFSQSCAPGADPNSNLCALCVGNEQGQDKCAPNSNERYFSYAGSFRCLVENAGDVAFVKASTVLENPDGRGTEAWAKDLKLEDFELLCLDGTRKPVSEFETCHLARAPSHGVVSRKDRVQYLEQVLLDQQGKFGRNGPLCPGKFCLFQSETKNLLFNDNTECLAKLQGKTTYEKYLGPEYVTAVANLRQCSTSPLLEACTFLRN | 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 mucosal secretions. Has antimicrobial activity. Antimicrobial properties may include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane. May have anabolic, differentiating and anti-apoptotic effects on osteoblasts and may also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. May interfere with the lipopolysaccharide (LPS)-stimulated TLR4 signaling. {ECO:0000250|UniProtKB:P02788}.; FUNCTION: The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites. {ECO:0000250|UniProtKB:P02788}.; FUNCTION: Acts as an anticoagulant of the blood coagulation cascade of the bat's prey by inhibiting coagulation factor IX and activated coagulation factor X. {ECO:0000269|PubMed:10556567, ECO:0000269|PubMed:7740503, ECO:0000269|PubMed:9795244}. | Desmodus rotundus (Vampire bat) |
K9JHZ4 | TET3B_XENLA | METQPASVPCVLPQDVYEFSEDRESLGRLRVSEMPSELNGGGDGSKGDGAAVVATEVSQQSNKKRKRCGVCVPCLRKEPCGTCYNCVNRSTSHQICKMRKCEQLKKKRVVPMKGVEAVDKDDAKNQAKEQVPSVKNCSESILVDGPKTDQMEAGPVNHVQEGRLKQECDSTLPSKGSEDLANQLLMEANSWLSNTAAPQDPCNKLNWDKPIIPNHIAANNNSNLEDAKNLVAFSAVAEAMSNYGMPASGTPSSISMQLYEKFNYETNQDNSGHSEGNAPSCPEDLNTLKEALALAKHGVKPPNCNCDGPECPDYLEWLENKIKSTGKGSQESPFPSLGQVSKKLVQKSYHKEQVLNLENTNVTCPSGNLPFSQNALSLAKEKNISLQTAIAIEALTQLSSALPQTNNEYPNAPSQPLINHNDQLTHFPTAKGNQLPMLPLSCNELFQNQQAQLYTGKNALPVPQSPRQASWEQNKKPGYQESEYIPENLSQSSSVLPSDASTPQKKEFLQQWVQNADLLKSPSDPMTGLKQLLGNTDEYIKSAFKGPEGLSKKIKNVKSKHTIKSIKKESADFTKMSPDQQLSQLLQGNDFHRNTQAALQQHLHHKRNLFVDSNTMEACTQEQQNWWVPNSQQAPVSKTTEKPVKERKKRRQSPSQKQVEPKPKPPRKQVQIKKPRVKEGNAVFMPVSQISLDSFRRVEKEENQVKELDLENSLPINVQPDLLGSQSIQLTGSQANLENQKTVNTQETCNENQTSIGKANNFALCVNKTNSLVAKGRCPTPSTGDSSSGQGDSANQHTNLTDVPGQNDLSCIDDKFEDLIKQFAAEFGEDFSLPGSEVPSQNGERPPKQQTSGVPQFKMPFPSQLPSENATHSNPALSNNLLTHNASHKFDSLFSSKSPKQIKIESSGAITVVSTTCSYSEENQHLDGTPTKSELPFNPTLSGFLESPLKYLTSPTKSLIDTPAKMAQAEFPTCDCVEQINEKDEGPYYTHLGSGPTVASIRELMEERFGEKGEAIRIEKVIYTGKEGKSSRGCPIAKWVIRRQSEDEKLMCLVRQRAGHHCENAVIIILIMAWEGIPRALGDSLYDDISGTITKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWSMYFNGCKYARSKTPRKFRLIGDNPKEEEFLKDSFQDLATKVAPVYKMLAPQAYQNQANNEDVAIDCRLGLEEGRPFSGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRMIGKIAEDEQLHVLPLYKVSTTDEFGSEERQLEKIRKGGIQVLSSFPREVRKLSEPAKSCRQRQLDAKKATAEKKKLQKEKLVSPDKTKQEPSDTKTCQQNPGVPQQQTKPCVKVEPSNHYNTFKYNGNGVVESYSVLGSCRPSDPYSMNSVYSYHSFYAQPNLPSVNGFHSKFALPPFGFYSFPNNPVVPNQFMNYGTGDARNSGWMNNSFEKKPELQSLADGMNQSYGSELPEQNYRRSSEVPHHYSLQNSNSQKSVGVPHRTTPAPMETTPYSNVPCYNKVIKKEPVCDPLVDPFQRSNSVHSQSPGVNHSLQTNDLSYKANGALPSSGRTNKEGPCSMFLPSDKNGLEKRDYFGVHSNVPGLKEKQWTPYGIDVPVGQRDSLDSQCSGKVWSSCKLSDSPAVMPSTVQDKNWTGRQASLNQGVKEPMPFQEKLWNSVAASGRCSTTPNDRSSVTPCAELQDKNWMSFPNPAVNSLKTDSSQNHWDPYSLDDNMDDGQSKSVKEEEDEEEIWSDSEHNFLDGNIGGVAVAPGHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLAERARVKEEEAAKLGIKQEVKSLGKKRKWGGAATTETPPVEKKDFIPTRQAATSLTDSTTTAFSYAYTKVTGPYSRFI | 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:CHEBI:136731; EC=1.14.11.80; Evidence={ECO:0000269|PubMed:23217707}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-hydroxymethyl-2'-deoxycytidine in DNA + O2 = a 5-formyl-2'-deoxycytidine in DNA + CO2 + H2O + succinate; Xref=Rhea:RHEA:53828, Rhea:RHEA-COMP:13315, Rhea:RHEA-COMP:13656, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:136731, ChEBI:CHEBI:137731; EC=1.14.11.80; Evidence={ECO:0000250|UniProtKB:Q6N021}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-formyl-2'-deoxycytidine in DNA + O2 = a 5-carboxyl-2'-deoxycytidine in DNA + CO2 + H(+) + succinate; Xref=Rhea:RHEA:53832, Rhea:RHEA-COMP:13656, Rhea:RHEA-COMP:13657, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:137731, ChEBI:CHEBI:137732; EC=1.14.11.80; Evidence={ECO:0000250|UniProtKB:Q6N021}; | 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. Selectively binds to the promoter region of target genes and contributes to regulate the expression of numerous developmental genes, including pax6, rax, sox9 and six3. May also contribute to the regulation of target genes in ways that do not require its enzyme activity. {ECO:0000269|PubMed:23217707}. | 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 | MASPAAPRAVSFADNNDITNTNLSRGRGRNPKPRAAPNNTVSWYTGLTQHGKVPLTFPPGQGVPLNANSTPAQNAGYWRRQDRKINTGNGIKQLAPRWYFYYTGTGPEAALPFRAVKDGIVWVHEDGATDAPSTFGTRNPNNDSAIVTQFAPGTKLPKNFHIEGTGGNSQSSSRASSVSRNSSRSSSQGSRSGNSTRGTSPGPSGIGAVGGDLLYLDLLNRLQALESGKVKQSQPKVITKKDAAAAKNKMRHKRTSTKSFNMVQAFGLRGPGDLQGNFGDLQLNKLGTEDPRWPQIAELAPTASAFMGMSQFKLTHQNNDDHGNPVYFLRYSGAIKLDPKNPNYNKWLELLEQNIDAYKTFPKKEKKQKAPKEESTDQMSEPPKEHRVQGTQRTRTRPSVQPGPMIDVNTD | 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 two fragments and facilitates viral replication by inhibiting host IFN signaling. The two fragments interact with IRF3 inhibiting its nuclear translocation after activation and reduce the expression of IFNB and IFN-stimulated genes. {ECO:0000269|PubMed:35922005}. | 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 where it participates in viral RNA synthesis and virus budding. {ECO:0000255|HAMAP-Rule:MF_04096}. | 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 viral replication. {ECO:0000255|HAMAP-Rule:MF_04096}. | Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1) |
K9N5Q8 | SPIKE_MERS1 | MIHSVFLLMFLLTPTESYVDVGPDSVKSACIEVDIQQTFFDKTWPRPIDVSKADGIIYPQGRTYSNITITYQGLFPYQGDHGDMYVYSAGHATGTTPQKLFVANYSQDVKQFANGFVVRIGAAANSTGTVIISPSTSATIRKIYPAFMLGSSVGNFSDGKMGRFFNHTLVLLPDGCGTLLRAFYCILEPRSGNHCPAGNSYTSFATYHTPATDCSDGNYNRNASLNSFKEYFNLRNCTFMYTYNITEDEILEWFGITQTAQGVHLFSSRYVDLYGGNMFQFATLPVYDTIKYYSIIPHSIRSIQSDRKAWAAFYVYKLQPLTFLLDFSVDGYIRRAIDCGFNDLSQLHCSYESFDVESGVYSVSSFEAKPSGSVVEQAEGVECDFSPLLSGTPPQVYNFKRLVFTNCNYNLTKLLSLFSVNDFTCSQISPAAIASNCYSSLILDYFSYPLSMKSDLSVSSAGPISQFNYKQSFSNPTCLILATVPHNLTTITKPLKYSYINKCSRFLSDDRTEVPQLVNANQYSPCVSIVPSTVWEDGDYYRKQLSPLEGGGWLVASGSTVAMTEQLQMGFGITVQYGTDTNSVCPKLEFANDTKIASQLGNCVEYSLYGVSGRGVFQNCTAVGVRQQRFVYDAYQNLVGYYSDDGNYYCLRACVSVPVSVIYDKETKTHATLFGSVACEHISSTMSQYSRSTRSMLKRRDSTYGPLQTPVGCVLGLVNSSLFVEDCKLPLGQSLCALPDTPSTLTPRSVRSVPGEMRLASIAFNHPIQVDQLNSSYFKLSIPTNFSFGVTQEYIQTTIQKVTVDCKQYVCNGFQKCEQLLREYGQFCSKINQALHGANLRQDDSVRNLFASVKSSQSSPIIPGFGGDFNLTLLEPVSISTGSRSARSAIEDLLFDKVTIADPGYMQGYDDCMQQGPASARDLICAQYVAGYKVLPPLMDVNMEAAYTSSLLGSIAGVGWTAGLSSFAAIPFAQSIFYRLNGVGITQQVLSENQKLIANKFNQALGAMQTGFTTTNEAFHKVQDAVNNNAQALSKLASELSNTFGAISASIGDIIQRLDVLEQDAQIDRLINGRLTTLNAFVAQQLVRSESAALSAQLAKDKVNECVKAQSKRSGFCGQGTHIVSFVVNAPNGLYFMHVGYYPSNHIEVVSAYGLCDAANPTNCIAPVNGYFIKTNNTRIVDEWSYTGSSFYAPEPITSLNTKYVAPQVTYQNISTNLPPPLLGNSTGIDFQDELDEFFKNVSTSIPNFGSLTQINTTLLDLTYEMLSLQQVVKALNESYIDLKELGNYTYYNKWPWYIWLGFIAGLVALALCVFFILCCTGCGTNCMGKLKCNRCCDRYEEYDLEPHKVHVH | 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 attachment to host cell [GO:0046813] | 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:0000255|HAMAP-Rule:MF_04099}.; PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike glycoprotein is digested within host endosomes. {ECO:0000255|HAMAP-Rule:MF_04099}. | 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}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Some S oligomers are transported to the host plasma membrane, where they may mediate cell-cell fusion. {ECO:0000255|HAMAP-Rule:MF_04099}. | 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 virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. {ECO:0000255|HAMAP-Rule:MF_04099}.; FUNCTION: [Spike protein S2']: Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis. {ECO:0000255|HAMAP-Rule:MF_04099}. | Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1) |
K9N638 | R1A_MERS1 | MSFVAGVTAQGARGTYRAALNSEKHQDHVSLTVPLCGSGNLVEKLSPWFMDGENAYEVVKAMLLKKEPLLYVPIRLAGHTRHLPGPRVYLVERLIACENPFMVNQLAYSSSANGSLVGTTLQGKPIGMFFPYDIELVTGKQNILLRKYGRGGYHYTPFHYERDNTSCPEWMDDFEADPKGKYAQNLLKKLIGGDVTPVDQYMCGVDGKPISAYAFLMAKDGITKLADVEADVAARADDEGFITLKNNLYRLVWHVERKDVPYPKQSIFTINSVVQKDGVENTPPHYFTLGCKILTLTPRNKWSGVSDLSLKQKLLYTFYGKESLENPTYIYHSAFIECGSCGNDSWLTGNAIQGFACGCGASYTANDVEVQSSGMIKPNALLCATCPFAKGDSCSSNCKHSVAQLVSYLSERCNVIADSKSFTLIFGGVAYAYFGCEEGTMYFVPRAKSVVSRIGDSIFTGCTGSWNKVTQIANMFLEQTQHSLNFVGEFVVNDVVLAILSGTTTNVDKIRQLLKGVTLDKLRDYLADYDVAVTAGPFMDNAINVGGTGLQYAAITAPYVVLTGLGESFKKVATIPYKVCNSVKDTLTYYAHSVLYRVFPYDMDSGVSSFSELLFDCVDLSVASTYFLVRLLQDKTGDFMSTIITSCQTAVSKLLDTCFEATEATFNFLLDLAGLFRIFLRNAYVYTSQGFVVVNGKVSTLVKQVLDLLNKGMQLLHTKVSWAGSNISAVIYSGRESLIFPSGTYYCVTTKAKSVQQDLDVILPGEFSKKQLGLLQPTDNSTTVSVTVSSNMVETVVGQLEQTNMHSPDVIVGDYVIISEKLFVRSKEEDGFAFYPACTNGHAVPTLFRLKGGAPVKKVAFGGDQVHEVAAVRSVTVEYNIHAVLDTLLASSSLRTFVVDKSLSIEEFADVVKEQVSDLLVKLLRGMPIPDFDLDDFIDAPCYCFNAEGDASWSSTMIFSLHPVECDEECSEVEASDLEEGESECISETSTEQVDVSHEISDDEWAAAVDEAFPLDEAEDVTESVQEEAQPVEVPVEDIAQVVIADTLQETPVVSDTVEVPPQVVKLPSEPQTIQPEVKEVAPVYEADTEQTQSVTVKPKRLRKKRNVDPLSNFEHKVITECVTIVLGDAIQVAKCYGESVLVNAANTHLKHGGGIAGAINAASKGAVQKESDEYILAKGPLQVGDSVLLQGHSLAKNILHVVGPDARAKQDVSLLSKCYKAMNAYPLVVTPLVSAGIFGVKPAVSFDYLIREAKTRVLVVVNSQDVYKSLTIVDIPQSLTFSYDGLRGAIRKAKDYGFTVFVCTDNSANTKVLRNKGVDYTKKFLTVDGVQYYCYTSKDTLDDILQQANKSVGIISMPLGYVSHGLDLIQAGSVVRRVNVPYVCLLANKEQEAILMSEDVKLNPSEDFIKHVRTNGGYNSWHLVEGELLVQDLRLNKLLHWSDQTICYKDSVFYVVKNSTAFPFETLSACRAYLDSRTTQQLTIEVLVTVDGVNFRTVVLNNKNTYRSQLGCVFFNGADISDTIPDEKQNGHSLYLADNLTADETKALKELYGPVDPTFLHRFYSLKAAVHKWKMVVCDKVRSLKLSDNNCYLNAVIMTLDLLKDIKFVIPALQHAFMKHKGGDSTDFIALIMAYGNCTFGAPDDASRLLHTVLAKAELCCSARMVWREWCNVCGIKDVVLQGLKACCYVGVQTVEDLRARMTYVCQCGGERHRQIVEHTTPWLLLSGTPNEKLVTTSTAPDFVAFNVFQGIETAVGHYVHARLKGGLILKFDSGTVSKTSDWKCKVTDVLFPGQKYSSDCNVVRYSLDGNFRTEVDPDLSAFYVKDGKYFTSEPPVTYSPATILAGSVYTNSCLVSSDGQPGGDAISLSFNNLLGFDSSKPVTKKYTYSFLPKEDGDVLLAEFDTYDPIYKNGAMYKGKPILWVNKASYDTNLNKFNRASLRQIFDVAPIELENKFTPLSVESTPVEPPTVDVVALQQEMTIVKCKGLNKPFVKDNVSFVADDSGTPVVEYLSKEDLHTLYVDPKYQVIVLKDNVLSSMLRLHTVESGDINVVAASGSLTRKVKLLFRASFYFKEFATRTFTATTAVGSCIKSVVRHLGVTKGILTGCFSFVKMLFMLPLAYFSDSKLGTTEVKVSALKTAGVVTGNVVKQCCTAAVDLSMDKLRRVDWKSTLRLLLMLCTTMVLLSSVYHLYVFNQVLSSDVMFEDAQGLKKFYKEVRAYLGISSACDGLASAYRANSFDVPTFCANRSAMCNWCLISQDSITHYPALKMVQTHLSHYVLNIDWLWFAFETGLAYMLYTSAFNWLLLAGTLHYFFAQTSIFVDWRSYNYAVSSAFWLFTHIPMAGLVRMYNLLACLWLLRKFYQHVINGCKDTACLLCYKRNRLTRVEASTVVCGGKRTFYITANGGISFCRRHNWNCVDCDTAGVGNTFICEEVANDLTTALRRPINATDRSHYYVDSVTVKETVVQFNYRRDGQPFYERFPLCAFTNLDKLKFKEVCKTTTGIPEYNFIIYDSSDRGQESLARSACVYYSQVLCKSILLVDSSLVTSVGDSSEIATKMFDSFVNSFVSLYNVTRDKLEKLISTARDGVRRGDNFHSVLTTFIDAARGPAGVESDVETNEIVDSVQYAHKHDIQITNESYNNYVPSYVKPDSVSTSDLGSLIDCNAASVNQIVLRNSNGACIWNAAAYMKLSDALKRQIRIACRKCNLAFRLTTSKLRANDNILSVRFTANKIVGGAPTWFNALRDFTLKGYVLATIIVFLCAVLMYLCLPTFSMVPVEFYEDRILDFKVLDNGIIRDVNPDDKCFANKHRSFTQWYHEHVGGVYDNSITCPLTVAVIAGVAGARIPDVPTTLAWVNNQIIFFVSRVFANTGSVCYTPIDEIPYKSFSDSGCILPSECTMFRDAEGRMTPYCHDPTVLPGAFAYSQMRPHVRYDLYDGNMFIKFPEVVFESTLRITRTLSTQYCRFGSCEYAQEGVCITTNGSWAIFNDHHLNRPGVYCGSDFIDIVRRLAVSLFQPITYFQLTTSLVLGIGLCAFLTLLFYYINKVKRAFADYTQCAVIAVVAAVLNSLCICFVASIPLCIVPYTALYYYATFYFTNEPAFIMHVSWYIMFGPIVPIWMTCVYTVAMCFRHFFWVLAYFSKKHVEVFTDGKLNCSFQDAASNIFVINKDTYAALRNSLTNDAYSRFLGLFNKYKYFSGAMETAAYREAAACHLAKALQTYSETGSDLLYQPPNCSITSGVLQSGLVKMSHPSGDVEACMVQVTCGSMTLNGLWLDNTVWCPRHVMCPADQLSDPNYDALLISMTNHSFSVQKHIGAPANLRVVGHAMQGTLLKLTVDVANPSTPAYTFTTVKPGAAFSVLACYNGRPTGTFTVVMRPNYTIKGSFLCGSCGSVGYTKEGSVINFCYMHQMELANGTHTGSAFDGTMYGAFMDKQVHQVQLTDKYCSVNVVAWLYAAILNGCAWFVKPNRTSVVSFNEWALANQFTEFVGTQSVDMLAVKTGVAIEQLLYAIQQLYTGFQGKQILGSTMLEDEFTPEDVNMQIMGVVMQSGVRKVTYGTAHWLFATLVSTYVIILQATKFTLWNYLFETIPTQLFPLLFVTMAFVMLLVKHKHTFLTLFLLPVAICLTYANIVYEPTTPISSALIAVANWLAPTNAYMRTTHTDIGVYISMSLVLVIVVKRLYNPSLSNFALALCSGVMWLYTYSIGEASSPIAYLVFVTTLTSDYTITVFVTVNLAKVCTYAIFAYSPQLTLVFPEVKMILLLYTCLGFMCTCYFGVFSLLNLKLRAPMGVYDFKVSTQEFRFMTANNLTAPRNSWEAMALNFKLIGIGGTPCIKVAAMQSKLTDLKCTSVVLLSVLQQLHLEANSRAWAFCVKCHNDILAATDPSEAFEKFVSLFATLMTFSGNVDLDALASDIFDTPSVLQATLSEFSHLATFAELEAAQKAYQEAMDSGDTSPQVLKALQKAVNIAKNAYEKDKAVARKLERMADQAMTSMYKQARAEDKKAKIVSAMQTMLFGMIKKLDNDVLNGIISNARNGCIPLSVIPLCASNKLRVVIPDFTVWNQVVTYPSLNYAGALWDITVINNVDNEIVKSSDVVDSNENLTWPLVLECTRASTSAVKLQNNEIKPSGLKTMVVSAGQEQTNCNTSSLAYYEPVQGRKMLMALLSDNAYLKWARVEGKDGFVSVELQPPCKFLIAGPKGPEIRYLYFVKNLNNLHRGQVLGHIAATVRLQAGSNTEFASNSSVLSLVNFTVDPQKAYLDFVNAGGAPLTNCVKMLTPKTGTGIAISVKPESTADQETYGGASVCLYCRAHIEHPDVSGVCKYKGKFVQIPAQCVRDPVGFCLSNTPCNVCQYWIGYGCNCDSLRQAALPQSKDSNFLNESGVLL | 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 signaling pathway via inhibition of IRF3 activity [GO:0039548]; symbiont-mediated suppression of host ISG15-protein conjugation [GO:0039579]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral genome replication [GO:0019079]; viral protein processing [GO:0019082]; virus-mediated perturbation of host defense response [GO:0019049] | 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:0008270] | 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 vesicles. {ECO:0000250|UniProtKB:P0C6X7}.; SUBCELLULAR LOCATION: [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [RNA-capping enzyme subunit nsp9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}. | 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}; CATALYTIC ACTIVITY: [3C-like proteinase nsp5]: Reaction=TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.; EC=3.4.22.69; Evidence={ECO:0000250|UniProtKB:P0DTC1}; CATALYTIC ACTIVITY: [RNA-capping enzyme subunit nsp9]: Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate; Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50; Evidence={ECO:0000250|UniProtKB:P0DTC1}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67014; 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. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Host translation inhibitor nsp1]: Promotes the degradation of host mRNAs by inducing an endonucleolytic RNA cleavage in template mRNAs, and inhibits of host mRNA translation, a function that is separable from its RNA cleavage activity. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000269|PubMed:26311885}.; FUNCTION: [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Papain-like protease nsp3]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates, together with nsp4, in the assembly of virally induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B. signaling. {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:25142582}.; FUNCTION: [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [3C-like proteinase nsp5]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE-ProRule:PRU00772}.; FUNCTION: [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [RNA-capping enzyme subunit nsp9]: Catalytic subunit of viral RNA capping enzyme which catalyzes the RNA guanylyltransferase reaction for genomic and sub-genomic RNAs. The kinase-like NiRAN domain of NSP12 transfers RNA to the amino terminus of NSP9, forming a covalent RNA-protein intermediate. Subsequently, the NiRAN domain transfers RNA to GDP, forming the core cap structure GpppA-RNA. The NSP14 and NSP16 methyltransferases then add methyl groups to form functional cap structures. {ECO:0000250|UniProtKB:P0DTC1}.; FUNCTION: [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. | Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1) |
K9N7C7 | R1AB_MERS1 | MSFVAGVTAQGARGTYRAALNSEKHQDHVSLTVPLCGSGNLVEKLSPWFMDGENAYEVVKAMLLKKEPLLYVPIRLAGHTRHLPGPRVYLVERLIACENPFMVNQLAYSSSANGSLVGTTLQGKPIGMFFPYDIELVTGKQNILLRKYGRGGYHYTPFHYERDNTSCPEWMDDFEADPKGKYAQNLLKKLIGGDVTPVDQYMCGVDGKPISAYAFLMAKDGITKLADVEADVAARADDEGFITLKNNLYRLVWHVERKDVPYPKQSIFTINSVVQKDGVENTPPHYFTLGCKILTLTPRNKWSGVSDLSLKQKLLYTFYGKESLENPTYIYHSAFIECGSCGNDSWLTGNAIQGFACGCGASYTANDVEVQSSGMIKPNALLCATCPFAKGDSCSSNCKHSVAQLVSYLSERCNVIADSKSFTLIFGGVAYAYFGCEEGTMYFVPRAKSVVSRIGDSIFTGCTGSWNKVTQIANMFLEQTQHSLNFVGEFVVNDVVLAILSGTTTNVDKIRQLLKGVTLDKLRDYLADYDVAVTAGPFMDNAINVGGTGLQYAAITAPYVVLTGLGESFKKVATIPYKVCNSVKDTLTYYAHSVLYRVFPYDMDSGVSSFSELLFDCVDLSVASTYFLVRLLQDKTGDFMSTIITSCQTAVSKLLDTCFEATEATFNFLLDLAGLFRIFLRNAYVYTSQGFVVVNGKVSTLVKQVLDLLNKGMQLLHTKVSWAGSNISAVIYSGRESLIFPSGTYYCVTTKAKSVQQDLDVILPGEFSKKQLGLLQPTDNSTTVSVTVSSNMVETVVGQLEQTNMHSPDVIVGDYVIISEKLFVRSKEEDGFAFYPACTNGHAVPTLFRLKGGAPVKKVAFGGDQVHEVAAVRSVTVEYNIHAVLDTLLASSSLRTFVVDKSLSIEEFADVVKEQVSDLLVKLLRGMPIPDFDLDDFIDAPCYCFNAEGDASWSSTMIFSLHPVECDEECSEVEASDLEEGESECISETSTEQVDVSHEISDDEWAAAVDEAFPLDEAEDVTESVQEEAQPVEVPVEDIAQVVIADTLQETPVVSDTVEVPPQVVKLPSEPQTIQPEVKEVAPVYEADTEQTQSVTVKPKRLRKKRNVDPLSNFEHKVITECVTIVLGDAIQVAKCYGESVLVNAANTHLKHGGGIAGAINAASKGAVQKESDEYILAKGPLQVGDSVLLQGHSLAKNILHVVGPDARAKQDVSLLSKCYKAMNAYPLVVTPLVSAGIFGVKPAVSFDYLIREAKTRVLVVVNSQDVYKSLTIVDIPQSLTFSYDGLRGAIRKAKDYGFTVFVCTDNSANTKVLRNKGVDYTKKFLTVDGVQYYCYTSKDTLDDILQQANKSVGIISMPLGYVSHGLDLIQAGSVVRRVNVPYVCLLANKEQEAILMSEDVKLNPSEDFIKHVRTNGGYNSWHLVEGELLVQDLRLNKLLHWSDQTICYKDSVFYVVKNSTAFPFETLSACRAYLDSRTTQQLTIEVLVTVDGVNFRTVVLNNKNTYRSQLGCVFFNGADISDTIPDEKQNGHSLYLADNLTADETKALKELYGPVDPTFLHRFYSLKAAVHKWKMVVCDKVRSLKLSDNNCYLNAVIMTLDLLKDIKFVIPALQHAFMKHKGGDSTDFIALIMAYGNCTFGAPDDASRLLHTVLAKAELCCSARMVWREWCNVCGIKDVVLQGLKACCYVGVQTVEDLRARMTYVCQCGGERHRQIVEHTTPWLLLSGTPNEKLVTTSTAPDFVAFNVFQGIETAVGHYVHARLKGGLILKFDSGTVSKTSDWKCKVTDVLFPGQKYSSDCNVVRYSLDGNFRTEVDPDLSAFYVKDGKYFTSEPPVTYSPATILAGSVYTNSCLVSSDGQPGGDAISLSFNNLLGFDSSKPVTKKYTYSFLPKEDGDVLLAEFDTYDPIYKNGAMYKGKPILWVNKASYDTNLNKFNRASLRQIFDVAPIELENKFTPLSVESTPVEPPTVDVVALQQEMTIVKCKGLNKPFVKDNVSFVADDSGTPVVEYLSKEDLHTLYVDPKYQVIVLKDNVLSSMLRLHTVESGDINVVAASGSLTRKVKLLFRASFYFKEFATRTFTATTAVGSCIKSVVRHLGVTKGILTGCFSFVKMLFMLPLAYFSDSKLGTTEVKVSALKTAGVVTGNVVKQCCTAAVDLSMDKLRRVDWKSTLRLLLMLCTTMVLLSSVYHLYVFNQVLSSDVMFEDAQGLKKFYKEVRAYLGISSACDGLASAYRANSFDVPTFCANRSAMCNWCLISQDSITHYPALKMVQTHLSHYVLNIDWLWFAFETGLAYMLYTSAFNWLLLAGTLHYFFAQTSIFVDWRSYNYAVSSAFWLFTHIPMAGLVRMYNLLACLWLLRKFYQHVINGCKDTACLLCYKRNRLTRVEASTVVCGGKRTFYITANGGISFCRRHNWNCVDCDTAGVGNTFICEEVANDLTTALRRPINATDRSHYYVDSVTVKETVVQFNYRRDGQPFYERFPLCAFTNLDKLKFKEVCKTTTGIPEYNFIIYDSSDRGQESLARSACVYYSQVLCKSILLVDSSLVTSVGDSSEIATKMFDSFVNSFVSLYNVTRDKLEKLISTARDGVRRGDNFHSVLTTFIDAARGPAGVESDVETNEIVDSVQYAHKHDIQITNESYNNYVPSYVKPDSVSTSDLGSLIDCNAASVNQIVLRNSNGACIWNAAAYMKLSDALKRQIRIACRKCNLAFRLTTSKLRANDNILSVRFTANKIVGGAPTWFNALRDFTLKGYVLATIIVFLCAVLMYLCLPTFSMVPVEFYEDRILDFKVLDNGIIRDVNPDDKCFANKHRSFTQWYHEHVGGVYDNSITCPLTVAVIAGVAGARIPDVPTTLAWVNNQIIFFVSRVFANTGSVCYTPIDEIPYKSFSDSGCILPSECTMFRDAEGRMTPYCHDPTVLPGAFAYSQMRPHVRYDLYDGNMFIKFPEVVFESTLRITRTLSTQYCRFGSCEYAQEGVCITTNGSWAIFNDHHLNRPGVYCGSDFIDIVRRLAVSLFQPITYFQLTTSLVLGIGLCAFLTLLFYYINKVKRAFADYTQCAVIAVVAAVLNSLCICFVASIPLCIVPYTALYYYATFYFTNEPAFIMHVSWYIMFGPIVPIWMTCVYTVAMCFRHFFWVLAYFSKKHVEVFTDGKLNCSFQDAASNIFVINKDTYAALRNSLTNDAYSRFLGLFNKYKYFSGAMETAAYREAAACHLAKALQTYSETGSDLLYQPPNCSITSGVLQSGLVKMSHPSGDVEACMVQVTCGSMTLNGLWLDNTVWCPRHVMCPADQLSDPNYDALLISMTNHSFSVQKHIGAPANLRVVGHAMQGTLLKLTVDVANPSTPAYTFTTVKPGAAFSVLACYNGRPTGTFTVVMRPNYTIKGSFLCGSCGSVGYTKEGSVINFCYMHQMELANGTHTGSAFDGTMYGAFMDKQVHQVQLTDKYCSVNVVAWLYAAILNGCAWFVKPNRTSVVSFNEWALANQFTEFVGTQSVDMLAVKTGVAIEQLLYAIQQLYTGFQGKQILGSTMLEDEFTPEDVNMQIMGVVMQSGVRKVTYGTAHWLFATLVSTYVIILQATKFTLWNYLFETIPTQLFPLLFVTMAFVMLLVKHKHTFLTLFLLPVAICLTYANIVYEPTTPISSALIAVANWLAPTNAYMRTTHTDIGVYISMSLVLVIVVKRLYNPSLSNFALALCSGVMWLYTYSIGEASSPIAYLVFVTTLTSDYTITVFVTVNLAKVCTYAIFAYSPQLTLVFPEVKMILLLYTCLGFMCTCYFGVFSLLNLKLRAPMGVYDFKVSTQEFRFMTANNLTAPRNSWEAMALNFKLIGIGGTPCIKVAAMQSKLTDLKCTSVVLLSVLQQLHLEANSRAWAFCVKCHNDILAATDPSEAFEKFVSLFATLMTFSGNVDLDALASDIFDTPSVLQATLSEFSHLATFAELEAAQKAYQEAMDSGDTSPQVLKALQKAVNIAKNAYEKDKAVARKLERMADQAMTSMYKQARAEDKKAKIVSAMQTMLFGMIKKLDNDVLNGIISNARNGCIPLSVIPLCASNKLRVVIPDFTVWNQVVTYPSLNYAGALWDITVINNVDNEIVKSSDVVDSNENLTWPLVLECTRASTSAVKLQNNEIKPSGLKTMVVSAGQEQTNCNTSSLAYYEPVQGRKMLMALLSDNAYLKWARVEGKDGFVSVELQPPCKFLIAGPKGPEIRYLYFVKNLNNLHRGQVLGHIAATVRLQAGSNTEFASNSSVLSLVNFTVDPQKAYLDFVNAGGAPLTNCVKMLTPKTGTGIAISVKPESTADQETYGGASVCLYCRAHIEHPDVSGVCKYKGKFVQIPAQCVRDPVGFCLSNTPCNVCQYWIGYGCNCDSLRQAALPQSKDSNFLKRVRGSIVNARIEPCSSGLSTDVVFRAFDICNYKAKVAGIGKYYKTNTCRFVELDDQGHHLDSYFVVKRHTMENYELEKHCYDLLRDCDAVAPHDFFIFDVDKVKTPHIVRQRLTEYTMMDLVYALRHFDQNSEVLKAILVKYGCCDVTYFENKLWFDFVENPSVIGVYHKLGERVRQAILNTVKFCDHMVKAGLVGVLTLDNQDLNGKWYDFGDFVITQPGSGVAIVDSYYSYLMPVLSMTDCLAAETHRDCDFNKPLIEWPLTEYDFTDYKVQLFEKYFKYWDQTYHANCVNCTDDRCVLHCANFNVLFAMTMPKTCFGPIVRKIFVDGVPFVVSCGYHYKELGLVMNMDVSLHRHRLSLKELMMYAADPAMHIASSNAFLDLRTSCFSVAALTTGLTFQTVRPGNFNQDFYDFVVSKGFFKEGSSVTLKHFFFAQDGNAAITDYNYYSYNLPTMCDIKQMLFCMEVVNKYFEIYDGGCLNASEVVVNNLDKSAGHPFNKFGKARVYYESMSYQEQDELFAMTKRNVIPTMTQMNLKYAISAKNRARTVAGVSILSTMTNRQYHQKMLKSMAATRGATCVIGTTKFYGGWDFMLKTLYKDVDNPHLMGWDYPKCDRAMPNMCRIFASLILARKHGTCCTTRDRFYRLANECAQVLSEYVLCGGGYYVKPGGTSSGDATTAYANSVFNILQATTANVSALMGANGNKIVDKEVKDMQFDLYVNVYRSTSPDPKFVDKYYAFLNKHFSMMILSDDGVVCYNSDYAAKGYIAGIQNFKETLYYQNNVFMSEAKCWVETDLKKGPHEFCSQHTLYIKDGDDGYFLPYPDPSRILSAGCFVDDIVKTDGTLMVERFVSLAIDAYPLTKHEDIEYQNVFWVYLQYIEKLYKDLTGHMLDSYSVMLCGDNSAKFWEEAFYRDLYSSPTTLQAVGSCVVCHSQTSLRCGTCIRRPFLCCKCCYDHVIATPHKMVLSVSPYVCNAPGCGVSDVTKLYLGGMSYFCVDHRPVCSFPLCANGLVFGLYKNMCTGSPSIVEFNRLATCDWTESGDYTLANTTTEPLKLFAAETLRATEEASKQSYAIATIKEIVGERQLLLVWEAGKSKPPLNRNYVFTGYHITKNSKVQLGEYIFERIDYSDAVSYKSSTTYKLTVGDIFVLTSHSVATLTAPTIVNQERYVKITGLYPTITVPEEFASHVANFQKSGYSKYVTVQGPPGTGKSHFAIGLAIYYPTARVVYTACSHAAVDALCEKAFKYLNIAKCSRIIPAKARVECYDRFKVNETNSQYLFSTINALPETSADILVVDEVSMCTNYDLSIINARIKAKHIVYVGDPAQLPAPRTLLTRGTLEPENFNSVTRLMCNLGPDIFLSMCYRCPKEIVSTVSALVYNNKLLAKKELSGQCFKILYKGNVTHDASSAINRPQLTFVKNFITANPAWSKAVFISPYNSQNAVARSMLGLTTQTVDSSQGSEYQYVIFCQTADTAHANNINRFNVAITRAQKGILCVMTSQALFESLEFTELSFTNYKLQSQIVTGLFKDCSRETSGLSPAYAPTYVSVDDKYKTSDELCVNLNLPANVPYSRVISRMGFKLDATVPGYPKLFITREEAVRQVRSWIGFDVEGAHASRNACGTNVPLQLGFSTGVNFVVQPVGVVDTEWGNMLTGIAARPPPGEQFKHLVPLMHKGAAWPIVRRRIVQMLSDTLDKLSDYCTFVCWAHGFELTSASYFCKIGKEQKCCMCNRRAAAYSSPLQSYACWTHSCGYDYVYNPFFVDVQQWGYVGNLATNHDRYCSVHQGAHVASNDAIMTRCLAIHSCFIERVDWDIEYPYISHEKKLNSCCRIVERNVVRAALLAGSFDKVYDIGNPKGIPIVDDPVVDWHYFDAQPLTRKVQQLFYTEDMASRFADGLCLFWNCNVPKYPNNAIVCRFDTRVHSEFNLPGCDGGSLYVNKHAFHTPAYDVSAFRDLKPLPFFYYSTTPCEVHGNGSMIEDIDYVPLKSAVCITACNLGGAVCRKHATEYREYMEAYNLVSASGFRLWCYKTFDIYNLWSTFTKVQGLENIAFNFVKQGHFIGVEGELPVAVVNDKIFTKSGVNDICMFENKTTLPTNIAFELYAKRAVRSHPDFKLLHNLQADICYKFVLWDYERSNIYGTATIGVCKYTDIDVNSALNICFDIRDNGSLEKFMSTPNAIFISDRKIKKYPCMVGPDYAYFNGAIIRDSDVVKQPVKFYLYKKVNNEFIDPTECIYTQSRSCSDFLPLSDMEKDFLSFDSDVFIKKYGLENYAFEHVVYGDFSHTTLGGLHLLIGLYKKQQEGHIIMEEMLKGSSTIHNYFITETNTAAFKAVCSVIDLKLDDFVMILKSQDLGVVSKVVKVPIDLTMIEFMLWCKDGQVQTFYPRLQASADWKPGHAMPSLFKVQNVNLERCELANYKQSIPMPRGVHMNIAKYMQLCQYLNTCTLAVPANMRVIHFGAGSDKGIAPGTSVLRQWLPTDAIIIDNDLNEFVSDADITLFGDCVTVRVGQQVDLVISDMYDPTTKNVTGSNESKALFFTYLCNLINNNLALGGSVAIKITEHSWSVELYELMGKFAWWTVFCTNANASSSEGFLLGINYLGTIKENIDGGAMHANYIFWRNSTPMNLSTYSLFDLSKFQLKLKGTPVLQLKESQINELVISLLSQGKLLIRDNDTLSVSTDVLVNTYRKLR | 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|UniProtKB:P0DTD1}; | 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:0039579]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral protein processing [GO:0019082]; viral RNA genome replication [GO:0039694]; virus-mediated perturbation of host defense response [GO:0019049] | 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:0002151]; lyase activity [GO:0016829]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; omega peptidase activity [GO:0008242]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; single-stranded RNA binding [GO:0003727]; zinc ion binding [GO:0008270] | 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 vesicles. {ECO:0000250|UniProtKB:P0C6X7}.; SUBCELLULAR LOCATION: [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Viral protein genome-linked nsp9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Helicase nsp13]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}.; SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease nsp15]: Host cytoplasm, host perinuclear region {ECO:0000250}. | 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}; CATALYTIC ACTIVITY: [Helicase nsp13]: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; CATALYTIC ACTIVITY: [Helicase nsp13]: 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; CATALYTIC ACTIVITY: [Papain-like proteinase 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; CATALYTIC ACTIVITY: [2'-O-methyltransferase nsp16]: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; EC=2.1.1.57; Evidence={ECO:0000250|UniProtKB:P0C6X7}; CATALYTIC ACTIVITY: [Uridylate-specific endoribonuclease nsp15]: Reaction=uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-RNA; Xref=Rhea:RHEA:67732, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:17334, Rhea:RHEA-COMP:17335, ChEBI:CHEBI:138284, ChEBI:CHEBI:173079, ChEBI:CHEBI:173080; Evidence={ECO:0000250|UniProtKB:P0C6X7}; CATALYTIC ACTIVITY: [RNA-directed RNA polymerase nsp12]: Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate; Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50; Evidence={ECO:0000250|UniProtKB:P0DTD1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013; Evidence={ECO:0000250|UniProtKB:P0DTD1}; CATALYTIC ACTIVITY: [Guanine-N7 methyltransferase nsp14]: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000250|UniProtKB:P0C6X7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67009; Evidence={ECO:0000250|UniProtKB:P0C6X7}; | 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. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Host translation inhibitor nsp1]: Promotes the degradation of host mRNAs by inducing an endonucleolytic RNA cleavage in template mRNAs, and inhibits of host mRNA translation, a function that is separable from its RNA cleavage activity. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000269|PubMed:26311885}.; FUNCTION: [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Papain-like proteinase nsp3]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates, together with nsp4, in the assembly of virally induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B. signaling. {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:25142582}.; FUNCTION: [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [3C-like proteinase nsp5]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN] (By similarity). May cleave human NLRP1 in lung epithelial cells, thereby activating the NLRP1 inflammasome pathway (PubMed:35594856). Also able to bind an ADP-ribose-1''-phosphate (ADRP) (By similarity). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE-ProRule:PRU00772, ECO:0000269|PubMed:35594856}.; FUNCTION: [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Viral protein genome-linked nsp9]: Forms a primer, NSP9-pU, which is utilized by the polymerase for the initiation of RNA chains. Interacts with ribosome signal recognition particle RNA (SRP). Together with NSP8, suppress protein integration into the cell membrane, thereby disrupting host immune defenses. {ECO:0000250|UniProtKB:P0DTD1}.; FUNCTION: [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [RNA-directed RNA polymerase nsp12]: RNA-directed RNA polymerase that catalyzes the transcription of viral genomic and subgenomic RNAs. Acts in complex with nsp7 and nsp8 to transcribe both the minus and positive strands of genomic RNA. The kinase-like NiRAN domain of NSP12 attaches one or more nucleotides to the amino terminus of NSP9, forming a covalent RNA-protein intermediate that serves as transcription/replication primer. Subgenomic RNAs (sgRNAs) are formed by discontinuous transcription: The polymerase has the ability to pause at transcription-regulating sequences (TRS) and jump to the leader TRS, resulting in a major deletion. This creates a series of subgenomic RNAs that are replicated, transcribed and translated. In addition, Nsp12 is a subunit of the viral RNA capping enzyme that catalyzes the RNA guanylyltransferase reaction for genomic and sub-genomic RNAs. Subsequently, the NiRAN domain transfers RNA to GDP, and forms the core cap structure GpppA-RNA. {ECO:0000250|UniProtKB:P0DTD1}.; FUNCTION: [Helicase nsp13]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Guanine-N7 methyltransferase nsp14]: Plays a role in viral RNA synthesis through two distinct activities: an N7-guanine methyltransferase activity involved in the formation of the cap structure GpppA-RNA; a proofreading exoribonuclease for RNA replication that reduces the sensitivity of the virus to RNA mutagens. This activity acts on both ssRNA and dsRNA in a 3'-5' direction. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Uridylate-specific endoribonuclease nsp15]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [2'-O-methyltransferase nsp16]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}. | Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1) |
K9NBS6 | AAM_RHOER | MTEQNLHWLSATEMAASVASNNLSPNEIAEAMIQRVDAVNPSINAIVQFDREQVTRDAAELSRQQEAGEKLGPLHGVPFTIKDLTAVDGLPTTFGMKPMADNIATGNAVVVDRLRGAGGLFLGKTNTPESGYYGGTDNHLYGPTHNPWKLGNSAGGSSGGASAAVAAGLGPLAEGSDGAGSVRIPSALCGVVGLKPTTGVIPQTILAGRFYNWAYHGPITRTVADNALMLDIMAGPDNADPLSIERAETSYVEASKGDVKGLRVAWSPNLGLGHVDPEVLAVCLDALAAFEELGAQITEATPQWGNPSESMWSGIWVPGFASEYDLLDWENQRGEVDDYLIEIMHEAERLTGVDVGRADAFRGDMWDTWTTFMNDYDVLVSPTLASATFPLRQFAPSWLEGASLREQLLDWLFTYPYNMLNNPAITVPAGFTADGRPVGLQIAARHRRDALVLRTAANFEAVRPWADKKPADSLVVA | 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(+); Xref=Rhea:RHEA:20297, ChEBI:CHEBI:13248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17296, ChEBI:CHEBI:29067; EC=3.5.1.13; Evidence={ECO:0000269|PubMed:21073421, ECO:0000269|Ref.1}; CATALYTIC ACTIVITY: Reaction=an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-amino acid; Xref=Rhea:RHEA:15565, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067, ChEBI:CHEBI:59869, ChEBI:CHEBI:59874; EC=3.5.1.14; Evidence={ECO:0000269|PubMed:21073421}; CATALYTIC ACTIVITY: Reaction=an N-acetyl-L-cysteine-S-conjugate + H2O = acetate + an S-substituted L-cysteine; Xref=Rhea:RHEA:36855, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:58717, ChEBI:CHEBI:58718; EC=3.5.1.14; | 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 substrate {ECO:0000269|PubMed:21073421}; Vmax=17 umol/min/mg enzyme with Leu-para-nitroanilide as substrate {ECO:0000269|PubMed:21073421}; Vmax=35.5 umol/min/mg enzyme with Ala-para-nitroanilide as substrate {ECO:0000269|PubMed:21073421}; | 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 acrylamides (isopropyl acrylamide, N,N-dimethyl-aminopropyl acrylamide, and methylene-bis-acrylamide), N-acetyl derivatives of glycine, alanine and leucine, and aliphatic amides (acetamide, acrylamide, isobutyramide, n-butyramide, and valeramide) can also be used as substrates but with less efficiency. {ECO:0000269|PubMed:21073421}. | 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-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine; Xref=Rhea:RHEA:60648, ChEBI:CHEBI:57603, ChEBI:CHEBI:143891, ChEBI:CHEBI:143892; Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60700, ChEBI:CHEBI:15354, ChEBI:CHEBI:58168, ChEBI:CHEBI:143947; Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine; Xref=Rhea:RHEA:60704, ChEBI:CHEBI:57603, ChEBI:CHEBI:64381, ChEBI:CHEBI:143947; Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1}; | 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) with high activity (PubMed:23770445). It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces platelet aggregation in platelet rich plasma, but not in washed platelet, indicating that this activity is dependent on plasma components (PubMed:23770445). Also induces hemolysis (PubMed:23770445). In vivo, the recombinant protein evokes an intense inflammatory reaction and dermonecrosis, similar to those induced by L.gaucho total venom (PubMed:23770445). Is a good immunogen, capable of inducing immunoprotection in test animals (PubMed:23770445). {ECO:0000250|UniProtKB:A0A0D4WTV1, ECO:0000269|PubMed:23770445}.; FUNCTION: [U1-sicaritoxin-Lg1a]: Anionic antimicrobial peptide that shows antimicrobial activity against Gram-negative bacteria (MIC=1.15-4.6 uM) (tested on E.coli, P.aeruginosa, and E.cloacae), but not on Gram-negative bacteria (M.luteus, S.aureus, and B.subtilis), neither on fungi and yeasts (A.niger, C.albicans and C.krusei). Does not show hemolytic effects against human erythrocytes, and has no cytotoxic effects against human cervical carcinoma cells (HeLa). {ECO:0000269|PubMed:30563217}. | Loxosceles gaucho (Spider) |
L0DSL2 | NIR_THIND | MNDLNRLGRVGRWIAGAACLFLASAAHAEPGENLKPVDAMQCFDCHTQIEDMHTVGKHATVNCVHCHDATEHVETASSRRMGERPVTRMDLEACATCHTAQFNSFVEVRHESHPRLEKATPTSRSPMFDKLIAGHGFAFEHAEPRSHAFMLVDHFVVDRAYGGRFQFKNWQKVTDGMGAVRGAWTVLTDADPESSDQRRFLSQTATAANPVCLNCKTQDHILDWAYMGDEHEAAKWSRTSEVVEFARDLNHPLNCFMCHDPHSAGPRVVRDGLINAVVDRGLGTYPHDPVKSEQQGMTKVTFQRGREDFRAIGLLDTADSNVMCAQCHVEYNCNPGYQLSDGSRVGMDDRRANHFFWANVFDYKEAAQEIDFFDFRHATTGAALPKLQHPEAETFWGSVHERNGVACADCHMPKVQLENGKVYTSHSQRTPRDMMGQACLNCHAEWTEDQALYAIDYIKNYTHGKIVKSEYWLAKMIDLFPVAKRAGVSEDVLNQARELHYDAHLYWEWWTAENSVGFHNPDQARESLMTSISKSKEAVSLLNDAIDAQVASR | 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:22281743}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:16500161, ECO:0000269|PubMed:19393666, ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743}; Note=Binds 8 heme groups covalently per monomer. {ECO:0000269|PubMed:16500161, ECO:0000269|PubMed:19393666, ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743}; | 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 an artifact that is due to the formation of tyrosyl radicals when the protein is exposed to oxygen (PubMed:22281743). {ECO:0000269|PubMed:19393666, ECO:0000269|PubMed:22281743}. | 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={ECO:0000269|PubMed:16500161, ECO:0000269|PubMed:22281743}; | 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 (PubMed:20944237). {ECO:0000269|PubMed:16500161, ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743}. | Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2) |
L0E155 | MALA_MALAU | MAPTPKYTFTERAAAGNLSDAEILNSNNPTGSELPDESDVVVGGAGIHGLIYALHASKYKPNNLKISVIEKNTRPGYKIGESTLPIFYTWCKLHGISAAYLLRLFGLKDGLCFYFLDRENQGQYTDFCSVGAPGLVLASLQIERPMSELLFTILAQRNGVNVYHGREVDFKSTVVQGGGQGNKIAVSRGKYDSTPKTIDSALFVDATGRFRQFCSKKAPRHRFDGWNCNAFWGYFTAPKDESKIPFDLYEGDHTNHLCFPEGWVWVIRLPSWEGSLIANLMDMVTYILECADAGVPGDELPSSEELARMFGLKFQWVTSIGFAVRNDVKYPEDLSAYGTREAEQKFNYFVQKYELLQQFMSNFELIENLYGPGTTWFIRKTLAYQSPVVSGPGWLAIGDACGFTNPLYSPGINVGMSTSTWAAQLSHRIVEIGKSAPADAAESSIRKLLVPYDDYCKSLVPALEQMNRFNYVCYRDTRLGPQVACLWQFFAGIERYLSDVNIETFAHYAIKWVWGAMVPEYQQVAQKCIEHIETVPLDERLPDAMVDELLAFSNRIKSAAVAADDFSLRWDAILRSFDRSLNFVEGKTSRDIYTRQCSGCGAWLQLRPDWKKCHSCGLLGTEPQTAVTFDPPLTAEEEALLYAAWNTAPKYDPSKELKLPTPTRPAA | 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-to-right; Xref=Rhea:RHEA:62297; Evidence={ECO:0000269|PubMed:28777910}; CATALYTIC ACTIVITY: Reaction=(+)-premalbrancheamide + chloride + FAD + 2 H(+) = (+)-malbrancheamide B + FADH2; Xref=Rhea:RHEA:62308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:145658, ChEBI:CHEBI:145677; Evidence={ECO:0000269|PubMed:28777910}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62309; Evidence={ECO:0000269|PubMed:28777910}; CATALYTIC ACTIVITY: Reaction=(+)-premalbrancheamide + chloride + FAD + 2 H(+) = (+)-isomalbrancheamide B + FADH2; Xref=Rhea:RHEA:62320, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:145658, ChEBI:CHEBI:145678; Evidence={ECO:0000269|PubMed:28777910}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62321; Evidence={ECO:0000269|PubMed:28777910}; CATALYTIC ACTIVITY: Reaction=(+)-malbrancheamide B + chloride + FAD + 2 H(+) = (+)-malbrancheamide + FADH2; Xref=Rhea:RHEA:62324, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:145651, ChEBI:CHEBI:145677; Evidence={ECO:0000269|PubMed:28777910}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62325; Evidence={ECO:0000269|PubMed:28777910}; CATALYTIC ACTIVITY: Reaction=(+)-isomalbrancheamide B + chloride + FAD + 2 H(+) = (+)-malbrancheamide + FADH2; Xref=Rhea:RHEA:62328, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:145651, ChEBI:CHEBI:145678; Evidence={ECO:0000269|PubMed:28777910}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62329; Evidence={ECO:0000269|PubMed:28777910}; CATALYTIC ACTIVITY: Reaction=(+)-premalbrancheamide + bromide + FAD + 2 H(+) = (+)-malbrancheamide C + FADH2; Xref=Rhea:RHEA:62340, ChEBI:CHEBI:15378, ChEBI:CHEBI:15858, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:145658, ChEBI:CHEBI:145679; Evidence={ECO:0000269|PubMed:28777910}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62341; Evidence={ECO:0000269|PubMed:28777910}; CATALYTIC ACTIVITY: Reaction=(+)-premalbrancheamide + bromide + FAD + 2 H(+) = (+)-isomalbrancheamide C + FADH2; Xref=Rhea:RHEA:62724, ChEBI:CHEBI:15378, ChEBI:CHEBI:15858, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:145658, ChEBI:CHEBI:145680; Evidence={ECO:0000269|PubMed:28777910}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62725; Evidence={ECO:0000269|PubMed:28777910}; CATALYTIC ACTIVITY: Reaction=(+)-malbrancheamide B + bromide + FAD + 2 H(+) = (+)-malbrancheamide D + FADH2; Xref=Rhea:RHEA:62728, ChEBI:CHEBI:15378, ChEBI:CHEBI:15858, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:145677, ChEBI:CHEBI:145929; Evidence={ECO:0000269|PubMed:28777910}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62729; Evidence={ECO:0000269|PubMed:28777910}; CATALYTIC ACTIVITY: Reaction=(+)-isomalbrancheamide B + bromide + FAD + 2 H(+) = (+)-isomalbrancheamide D + FADH2; Xref=Rhea:RHEA:62732, ChEBI:CHEBI:15378, ChEBI:CHEBI:15858, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:145678, ChEBI:CHEBI:145930; Evidence={ECO:0000269|PubMed:28777910}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62733; Evidence={ECO:0000269|PubMed:28777910}; | 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:28777910}; KM=4 uM for isomalbrancheamide B (to yield malbrancheamide) {ECO:0000269|PubMed:28777910}; Note=The catalytic efficiencies were calculated for each of the four reactions, resulting in the kcat/Km values of 11.5, 12.0, 27.3, and 29.7 min(-1) mM(-1), respectively. {ECO:0000269|PubMed:28777910}; | 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 step of malbrancheamide biosynthesis involves coupling of L-proline and L-tryptophan by malG, a bimodular NRPS, to produce L-Pro-L-Trp aldehyde through reductive offloading (PubMed:23213353, PubMed:31548667). This compound undergoes spontaneous cyclization and dehydration to give a dienamine which is reverse prenylated at C-2 by malE (PubMed:31548667). The other prenyltransferase present in the cluster, malB, displays modest activity, suggesting that may be a redundant gene in the pathway (PubMed:31548667). Subsequently, a [4+2] Diels-Alder cyclo-addition catalyzed by the bifunctional enzyme malC forms the characteristic bicyclo[2.2.2]diazaoctane ring of premalbrancheamid (PubMed:31548667). Finally, the flavin-dependent halogenase malA catalyzes the iterative dichlorination of the indole ring of premalbrancheamide to yield C-9 monochlorinated malbrancheamide B, C-8 monochlorinated isomalbrancheamide B, and dichlorinated malbrancheamide (PubMed:28777910, PubMed:31548667). MalA is also able to brominate premalbrancheamide at C-9 to yield malbrancheamide C, and, to a lesser extend, at C-8 to yield isomalbrancheamide C (PubMed:28777910). Finally, malA can brominate C-9 monochlorinated malbrancheamide B at C-8 to yield malbrancheamide D, or C-8 monochlorinated isomalbrancheamide B at C-9 to produce isomalbrancheamide D (PubMed:28777910). {ECO:0000269|PubMed:23213353, ECO:0000269|PubMed:28777910, ECO:0000269|PubMed:31548667}. | Malbranchea aurantiaca |
L0E4H0 | PHQK_PENFE | MGSLGEEVQVIIVGLGIVGLAAAIECREKGHSVHAFEKSNILKSIGDCIGLQSNATRIIKRWGDGAVHEALRPWIVSSKEIRIHNSSGRLIIRQDLSEVCEQPNYLLPRSELIRVMYEHALKIGVEISLGVEVCEPSEDEEGASVVALTRDGERQIVRGDFIICSDGVHSKMRKAIMPQPVEPRPSGYAAFRALVDTETLKGDPEASWVFEGVEENDRFDVFFLSGAQIALQSCNKGKVFSWFCIHQDTRNLLDVWTSPADPNEMLDLIKVWPIGQRLWSVIRHTQPQKFINYPLLNHKPLDHWVSSHGRLILIGDAAHPLSPAAGQGASQGIEDANVLATSLSLAGRQRVSLALHVAERIRYARASAVQLISHRVNEGWRNQDWDAYEPNEQNIASLPLETWIYGHDSQAYTEQEFEMVVRAVQEGEEYHATNLPDKLRVQLGIRNVDVKEPLQNKSP | 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 spirocycle formation through two parallel pathways in the biosynthesis of paraherquamides A and G, using as substrates paraherquamides K and L, with paraherquamide L, bearing the dioxepin, being likely the favored substrate (PubMed:31904957). The first steps in the biosynthesis of paraherquamide is the production of the beta-methyl-proline precursor from L-isoleucine. They require oxidation of a terminally hydroxylated L-isoleucine to the corresponding aldehyde by enzymes which have still to be identified. Spontaneous cyclization and dehydration would yield the 4-methyl pyrolline-5-carboxylic acid, which is then reduced by the pyrroline-5-carboxylate reductase phqD leading to the beta-methyl-proline precursor. The next step of paraherquamide biosynthesis involves coupling of beta-methyl-proline and L-tryptophan by the bimodular NRPS phqB, to produce a monooxopiperazine intermediate. The reductase (R) domain of phqB utilizes NADPH for hydride transfer to reduce the thioester bond of the T domain-tethered linear dipeptide to a hemithioaminal intermediate, which spontaneously cleaves the C-S bond to release the aldehyde product. This compound undergoes spontaneous cyclization and dehydration to give a dienamine which is reverse prenylated at C-2 by the reverse prenyltransferase phqJ. The other prenyltransferase present in the cluster, phqI may be a redundant gene in the pathway. During biosynthetic assembly, the key step to produce the polycyclic core is catalyzed by the bifunctional reductase and intramolecular [4+2] Diels-Alderase, phqE, resulting in formation of the [2.2.2] diazaoctane intermediate preparaherquamide. Following formation of preparaherquamide, an indole 2,3-epoxidation-initiated pinacol-like rearrangement is catalyzed by the phqK FAD-dependent monooxygenase. The prenyltransferase phqA, the cytochrome P450 monooxygenase phqL, and the FAD-linked oxidoreductase phqH (or the cytochrome P450 monooxygenase phqM), are proposed to be involved in the formation of the pyran ring. The FAD-dependent monooxygenase phqK is likely responsible for generation of the spiro-oxindole, and the N-methylation is likely mediated by the phqN methyltransferase leading to the isolable natural product paraherquamide F. However, the order of these biosynthetic steps has still to be determined. In late-stage paraherquamide biosynthesis, the third P450 monooxygenase, phqO, is probably responsible for the C-14 hydroxylation, transforming paraherquamide F to paraherquamide G, and paraherquamide E to the final product paraherquamide A. The expansion from the 6-membered ring pyran (in paraherquamides F and G) to the 7-membered dioxepin ring (in paraherquamides A and E) represents a poorly understood but intriguing process that probably involves the 2-oxoglutarate-dependent dioxygenase phqC. Finally, the remaining members of the paraherquamide cluster, including phqI as well as phqM (or phqH), do not have a clearly prescribed role and appear to be redundant (Probable). {ECO:0000269|PubMed:23213353, ECO:0000269|PubMed:31904957, ECO:0000305|PubMed:23213353}. | 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). Also, stimulates production of pro-inflammatory cytokines by mouse peritoneal macrophages and down-regulates production of the anti-inflammatory cytokine IL-10 by lipopolysaccharide (LPS)-stimulated cells (PubMed:24704757). In vivo, intraperitoneal injection in mice enhances the activation state and homing capacity of Th1 type lymphocytes and promotes the recruitment, activation and tumoricidal capacities of peritoneal NK cells (PubMed:25861850, PubMed:28526557). Has a very weak activity in stimulation of insulin release and a weak hemolytic activity (PubMed:27049440, PubMed:30244134). {ECO:0000269|PubMed:24704757, ECO:0000269|PubMed:25861850, ECO:0000269|PubMed:27049440, ECO:0000269|PubMed:28526557, ECO:0000269|PubMed:30244134}.; FUNCTION: [Frenatin 2.3S]: Antimicrobial peptide with potent activity against some Gram-positive and Gram-negative bacteria (PubMed:30044391). Has a multifunctional mode of action (PubMed:30044391). It displays depolarization and bacterial cell leakage, and can also internalize into bacterial cells and alter specific gene expression involved in bacterial resistance mechanisms (PubMed:30044391). Does not agglutinate bacteria and lipid vesicles, even a high concentrations (PubMed:30044391). Also displays moderate cellular protection against yellow fever virus (YFV)-infected Vero cells without causing significant cytotoxicity (PubMed:27049440). Shows a weak hemolytic activity, and is not cytotoxic to monocytes (PubMed:30044391). Frenatin 2.3S (version without Gly-71) shows no or very weak antibacterial activity, shows no or very weak cytotoxicity to lung adenocarcinoma A549 cells and shows very weak hemolysis (PubMed:24704757). It only stimulates production of pro-inflammatory cytokines IL-23 (but not IL-1beta and TNF-alpha) by mouse peritoneal macrophages and has no effect on the production of the anti-inflammatory cytokine IL-10 (PubMed:24704757). Frenatin 2.3S (version without Gly-71) very weakly stimulates insulin release (PubMed:30244134). {ECO:0000269|PubMed:24704757, ECO:0000269|PubMed:27049440, ECO:0000269|PubMed:30044391, ECO:0000269|PubMed:30244134}. | Sphaenorhynchus lacteus (Orinoco lime treefrog) (Hyla lactea) |
L0N7N1 | KIF14_MOUSE | MSVHTSHSRHNIGSLEVSSSQKISASSGLVHSSRLELHLKADMSECENHDPFVNAGSKTIDINSTYVISACKKTRETPVTSDPRRLSLQRRATCGDRESSLLGSELGNRRTADTSLRLQRRHGRADYVGKWETLNPVGGNPGSDSASQASRTEAKGVNNDTRVLSSVVSVKDSNDTGLTRCKDPGPPVGASNEKVTVKDTNSRAPVGSQRQTEAMRSGHLVVQLTESKSDTPVSGGRNSHRGNAGKDTAKQVGTFGSSDTRTPVKCVLEHRWTPRHDPPPPKSPALSTPKNNGKDIPKHGSTFRSASSESRTPVKCVPEHRWTPRHDLPPPKSPALSTLKNRIASPRVKPRPKSSLFANKRESSRESTLPPEENSLVQKTFTEPDSLKVENSQVTVAVRVRPFSKREKTEKASQVVFTNGEEITVEHPDMKQVYSFIYDVSFWSFDECHPGYASQTTVYETLAAPLLDRAFEGYNTCLFAYGQTGSGKSYTMMGLNEEPGIIPRFCEDLFAQIAKKQTSEVSYHLEMSFFEVYNEKIHDLLVCKGENGQRKQPLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEVVEGEEHDHRITSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSEQANGKRVFIPYRESTLTWLLKESLGGNSKTAMIATVSPAASNIEETLSTLRYATQARLIVNIAKVNEDMNAKLIRELKAEIEKLKAAQRSNRNIDPERYRLCRQEITSLRMKLHQQERDMAEIQRVWKEKFEQAEKRKLQETKELQKAGVTFQMDNHLPNLVNLNEDPQLSEMLLYMVKEGVTTVGKHTPSSSHDIQLSGVLIADDHCTIRNFGGTVSIVPAGEAKTYVNGTHISEPTVLHHGDRVVLGGDHYFRFNHPVEVQKGKKLSSRNNLTTSEGPKDFEFAKNELLTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKAVYERKIQALEAELREESQRKRLEELNNQKASHKIEELERAKQHLEQEVYVNKRRLEMETLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQENRGNRDKTFTIQPNWNSMKLSTMIQEANAISDKFKKCYIFGRHDASDKGRSDTSVRVRNLQLGISTFWSLEKFESKLAAMKELYESNGGDRDEDVFCDPADEWEPDITSTPVSSLSRRRSRSLMKNRRVSGCLHDIHPIQSMQSSHSSGLMEKPSTIYSNSSESFLPGICKELIGSSIDFLGQSFDEEKTIADSLINNLLRLHNGVIAISKAHEEQDEESQDNLFSDRAAQALTIQVACAFEQLVVLFKHWLGDFLPCTGSARLEDELRQDIKKLGGYLQLFLQGCCSDISSMVKEAQNKVMKIIQQAVQCVGQLAVLKGSKLCVLENSSKVSSTQEFMAALQDGVTSGMKSLLDSGLETAQDLRQDLSRQSAREEVTKQMKASTVEWVGSLENAVAEWRTKSFRTQAQEGSRQQVSKLLSLASEFLKLKSCLQQTVEMIVSALRGCPSDLHCLRSCTETICSLARKLHSDFSAHSASAGSCGNELPRADCEELESLAKSLLLCFECGESPGLSKPWESCSSNSKEEQCKSDRADCGKSGPRRACEPHGDATPAVSSGDCTPNRIQWV | 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 development [GO:0021987]; establishment of protein localization [GO:0045184]; hippocampus development [GO:0021766]; microtubule-based movement [GO:0007018]; mitotic metaphase chromosome alignment [GO:0007080]; negative regulation of apoptotic process [GO:0043066]; negative regulation of integrin activation [GO:0033624]; negative regulation of neuron apoptotic process [GO:0043524]; olfactory bulb development [GO:0021772]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cytokinesis [GO:0032467]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of cell adhesion [GO:0030155]; regulation of cell growth [GO:0001558]; regulation of cell maturation [GO:1903429]; regulation of cell migration [GO:0030334]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; regulation of G2/M transition of mitotic cell cycle [GO:0010389]; regulation of myelination [GO:0031641]; regulation of neuron apoptotic process [GO:0043523]; regulation of Rap protein signal transduction [GO:0032487]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; substrate adhesion-dependent cell spreading [GO:0034446] | 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. Cytoplasmic in interphase. Cytoplasmic in metaphase cells. From prophase to metaphase, accumulates at the developing spindle poles and their associated microtubules. During anaphase, accumulates at the spindle midzone. Localization to the central spindle and midbody during anaphase is dependent upon PRC1 and CIT presence. In cells ready to undergo abscission, concentrates at the contractile ring. {ECO:0000250|UniProtKB:Q15058}. | 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 central spindle and midbody through its interaction with PRC1 and CIT respectively (By similarity). Regulates cell growth through regulation of cell cycle progression and cytokinesis. During cell cycle progression acts through SCF-dependent proteasomal ubiquitin-dependent protein catabolic process which controls CDKN1B degradation, resulting in positive regulation of cyclins, including CCNE1, CCND1 and CCNB1 (By similarity). During late neurogenesis, regulates the cerebellar and cerebral cortex development and olfactory bulb development through regulation of apoptosis, cell proliferation and cell division (PubMed:23308235, PubMed:24931760). Also is required for chromosome congression and alignment during mitotic cell cycle process (By similarity). Regulates cell spreading, focal adhesion dynamics, and cell migration through its interaction with RADIL resulting in regulation of RAP1A-mediated inside-out integrin activation by tethering RADIL on microtubules (By similarity). {ECO:0000250|UniProtKB:Q15058, ECO:0000269|PubMed:23308235, ECO:0000269|PubMed:24931760, ECO:0000269|PubMed:24949858}. | 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}.; FUNCTION: [Hyp3,Thr6]-bradykinin: Induces relaxation of rat smooth muscle from tail artery (EC(50)=56.7 nM) and contraction of that from ileum (EC(50)=588 nM), urinary bladder (EC(50)=4.6 uM) and uterus (EC(50)=3.9 nM). Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2). In arterial smooth muscle, the effect via BDKRB1 is stronger, in uterus, ileum and urinary bladder the effect via BDKRB2. {ECO:0000269|PubMed:24394432}.; FUNCTION: [[Thr6]-bradykinyl-Val,Asp]: Induces relaxation of rat smooth muscle from tail artery (EC(50)=10.8 nM) and contraction of that from ileum (EC(50)=645 nM), urinary bladder (EC(50)=1.1 uM) and uterus (EC(50)=1.2 uM). Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2). Apart from uterus smooth muscle, the effect via BDKRB2 is stronger. {ECO:0000269|PubMed:24394432}.; FUNCTION: [Hyp3,Thr6]-bradykinyl-Val,Asp: Induces relaxation of rat smooth muscle from tail artery (EC(50)=3.5 nM) and contraction of that from ileum (EC(50)=223 nM), urinary bladder (EC(50)=1.5 uM) and uterus (EC(50)=356 nM). Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2); the effects via BDKRB2 are stronger. {ECO:0000269|PubMed:24394432}. | 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}.; FUNCTION: [Hyp3,Thr6]-bradykinin: Induces relaxation of rat smooth muscle from tail artery (EC(50)=56.7 nM) and contraction of that from ileum (EC(50)=588 nM), urinary bladder (EC(50)=4.6 uM) and uterus (EC(50)=3.9 nM). Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2). In arterial smooth muscle, the effect via BDKRB1 is stronger, in uterus, ileum and urinary bladder that via BDKRB2. {ECO:0000269|PubMed:24394432}.; FUNCTION: [[Thr6]-bradykinyl-Val,Asp]: Induces relaxation of rat smooth muscle from tail artery (EC(50)=10.8 nM) and contraction of that from ileum (EC(50)=645 nM), urinary bladder (EC(50)=1.1 uM) and uterus (EC(50)=1.2 uM). Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2). Apart from uterus smooth muscle, the effect via B2 is stronger. {ECO:0000269|PubMed:24394432}.; FUNCTION: [Hyp3,Thr6]-bradykinyl-Val,Asp: Induces relaxation of rat smooth muscle from tail artery (EC(50)=3.5 nM) and contraction of that from ileum (EC(50)=223 nM), urinary bladder (EC(50)=1.5 uM) and uterus (EC(50)=356 nM). Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2); the effects via B2 a stronger. {ECO:0000269|PubMed:24394432}. | 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 preventing premature association of the large and small ribosomal subunits (PubMed:28892042, PubMed:30215512, PubMed:31666358). Thereby, indirectly regulates mitochondrial translation (PubMed:28892042, PubMed:30215512, PubMed:31666358). It is also required for complete assembly of the mitochondrial respiratory chain complex I (PubMed:31666358). May also function in DNM1L-mediated mitochondrial fission (PubMed:29083303). {ECO:0000269|PubMed:28892042, ECO:0000269|PubMed:29083303, ECO:0000269|PubMed:30215512, ECO:0000269|PubMed:31666358}. | 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 | MSRAAPRRASQSQSTRPARGLRRPPGAQEVGQRKRPGKTQKARQAQEATKSRPATRSDVAPAGRSTRARRTRQVVDVGTRGASFVFRHRTGNAVILVLMLVAATQLFFLQVSHAAGLRAQAAGQLKVTDVQPAARGSIVDRNNDRLAFTIEARALTFQPKRIRRQLEEARKKTSAAPDPQQRLRDIAQEVAGKLNNKPDAAAVLKKLQSDETFVYLARAVDPAVASAICAKYPEVGAERQDLRQYPGGSLAANVVGGIDWDGHGLLGLEDSLDAVLAGTDGSVTYDRGSDGVVIPGSYRNRHKAVHGSTVVLTLDNDIQFYVQQQVQQAKNLSGAHNVSAVVLDAKTGEVLAMANDNTFDPSQDIGRQGDKQLGNPAVSSPFEPGSVNKIVAASAVIEHGLSSPDEVLQVPGSIQMGGVTVHDAWEHGVMPYTTTGVFGKSSNVGTLMLSQRVGPERYYDMLRKFGLGQRTGVGLPGESAGLVPPIDQWSGSTFANLPIGQGLSMTLLQMTGMYQAIANDGVRVPPRIIKATVAPDGSRTEEPRPDDIRVVSAQTAQTVRQMLRAVVQRDPMGYQQGTGPTAGVPGYQMAGKTGTAQQINPGCGCYFDDVYWITFAGIATADNPRYVIGIMLDNPARNSDGAPGHSAAPLFHNIAGWLMQRENVPLSPDPGPPLVLQAT | 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 = an aliphatic alcohol + H(+) + tetradecanoate; Xref=Rhea:RHEA:47388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:87691; Evidence={ECO:0000269|PubMed:24234750}; CATALYTIC ACTIVITY: Reaction=decanoate ester + H2O = an aliphatic alcohol + decanoate + H(+); Xref=Rhea:RHEA:47360, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:87658; Evidence={ECO:0000269|PubMed:24234750}; CATALYTIC ACTIVITY: Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) + octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657; Evidence={ECO:0000269|PubMed:24234750}; CATALYTIC ACTIVITY: Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659; Evidence={ECO:0000269|PubMed:24234750}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:24234750}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoate ester = an aliphatic alcohol + H(+) + hexadecanoate; Xref=Rhea:RHEA:47392, ChEBI:CHEBI:2571, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25835; Evidence={ECO:0000269|PubMed:24234750}; CATALYTIC ACTIVITY: Reaction=H2O + octadecanoate ester = an aliphatic alcohol + H(+) + octadecanoate; Xref=Rhea:RHEA:47396, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75925; Evidence={ECO:0000269|PubMed:24234750}; | 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 play some important role in mycobacterial biology in macrophages where the bacteria encounters acidic stress. {ECO:0000269|PubMed:24234750}. | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
L5KLU7 | S39A4_PTEAL | MAILAWLEPRPLLAVLVLVLTMRMAQPAHLLTLLSSGQGALDRVALGGLLNTLAARVHCTSGPCGKCLSVDDLLALGRPEEPGHLARLSAAAALYLSDPEGTCEDIRAGRWASRADHLLALLEGPKALAPGLSRLLQRIQAQTTGQPSAGEACVDPPQLLREAGVAGAPGSPGPVLATLLEHVGRGSCFHTLPTPQYFVDFVFQQSHGNTPNISVAELAALMQRLGVGGVTETHSDHHHQEKRVNRQGPTPLTAPNSSSDTWDTVCLSARDVMAVYGLSEQTGVTPEAWAQLSPALLQQQLSGACSPQPSHPAQNQLSQAEKYLYGSLATLLICLCSTFGLLLLTCAACSTAAHYVIQTFLGMAVGALTGDALLHLTPKVLGLHQHGGDSEHRADSHGPQTTWRLVVALSGLYVFFLFEKLCDLLLPQDPEDRKGTPRSHSGHSHGMSLQLAPRELRPPKQPHEGSRADLVAEESPELLSPEPRRKSPELRLLPYMITLGDGLHNFADGLAVGAAFASSWKTGLATSLAVFCHEVPHELGDFAALLHAGLPVSRALLLNLASGLTAFAGLYVALALGVGEESESWTLAVAIGLFLYVALCDMLPAMLNVRDPRPWLLFLLHNVGLLGGWAVLLLLSLYEDSIAL | 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|UniProtKB:Q6P5W5}.; PTM: Glycosylated. {ECO:0000250|UniProtKB:Q6P5W5}. | 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 membrane protein {ECO:0000250|UniProtKB:A0A0H3LM39}. Note=Colocalized with TFRC in the recycling endosomes. Cycles between endosomal compartments and the plasma membrane in response to zinc availability. Translocates to the apical membrane during zinc deficiency. {ECO:0000250|UniProtKB:Q78IQ7}. | 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(2+) but at higher concentrations (By similarity). {ECO:0000250|UniProtKB:Q6P5W5, ECO:0000250|UniProtKB:Q78IQ7, ECO:0000269|PubMed:27321477}. | Pteropus alecto (Black flying fox) |
L7N1X6 | FBW15_MOUSE | MAIHLPCLPMMKILSYLDAYSLLQAAQVNKDWNELASSDVLWRKLCQKRWLYCDMDTLQLQGKETWKQFFIDRIWQERAKFRAKAKDFTYKEIPLMCGLFGYACYISGCGLTRKGQDKSVVCMVNSKNTISTWDVHKSVITWKSPEQPASIKLLTTLPEMHIAVTVDIQSTIKLWDCHNREALATNNLKSPCKSLKAVFTKDGPIVLIGDTLGNIHIFRIPDLYLISTVNVLPYGFDGIYCSPQKKWVLLSKKHPHILPKVFYMSSFLRTSEFSAPVSTVLKLSLYERVFWTPRREDRITLMSRSGFPQVKMFETYDIKLEEFGNKRIVKGKLIASFELQCHKVNPQRFGVSDKNVIVCSTESSLLLFDINGLRLKTFQYCPEMIVKLSVDPLHVIVICNTGSMDVYAWEERSLLLRKCYRLHIERPLPLYGFIYKAACDDVSIIQLITDELSLSSLTSYALNICS | 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 | MAPAMDSAQNGHQSRGSANVLAIGTANPPNVILQEDYPDFYFKVTNSEHLTDLKEKFKRICVKSKTRKRHFYLTEQILKENPGIATYGAGSLDSRQKILETEIPKLGKEAAMVAIQEWGQPVSKITHVVFATTSGFMMPGADYSITRLLGLNPNVRRVMIYNQGCFAGGTALRVAKDLAENNKGARVLVVCAENTAMTFHGPNENHLDVLVGQAMFSDGAAALIIGANPNLPEERPVYEMVAAHQTIVPESDGAIVAHFYEMGMSYFLKENVIPLFGNNIEACMEAAFKEYGISDWNSLFYSVHPGGRAIVDGIAEKLGLDEENLKATRHVLSEYGNMGSACVIFILDELRKKSKEEKKLTTGDGKEWGCLIGLGPGLTVETVVLRSVPIA | 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-CoA, hexanoyl-CoA, cinnamoyl-CoA, p-coumaroyl-CoA and salicoyl-CoA. | 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 of several biosynthetic floral scent-related genes (e.g. IGS, EGS, BSMT1, BSMT2, PAL1, PAL2, EPSPS, DAHPS, CS, CM1, ADT1 and PPA-AT) (PubMed:23275577). Binds to and activates the promoters of at least ODO1, IGS1 and PAL1 (PubMed:23275577). {ECO:0000269|PubMed:23275577}. | Petunia hybrida (Petunia) |
L7X3S1 | MSH_PAPSO | MRTESIKTNRPMDLLLQYLQPISVALVVIALVWNYGRRNPTKKLAPEASGGRPIMGHLHLFNDGELTHRKLGAMADTYGPVFNIRFGSHKTLVVSDWEIVKECFTTNDKLFSNRPGTLGIKLMFYDADSVGYAPYGAYWRDLRKISTLKLLSNHRIDTIKHLRSSEVESCFESLYSQWGNGEKSGEFAPVRMDSWLGDLTFNVVARIVAGKKNFSANGDVGAQRYKAAMDEAMRLMRFFAFSDVIPSLSWLDNLRGLVREMKKCASEIDSIMATWVEEHRVKRNSGGNSQLEHDFIDVCLDIMEHSSLPGDDPDLVVKSTCLDMILGGSDTTTVTLTWAMSLLLNHPQVLQKAKEELETQVGKNRQVDDSDIPNLPFIQAIIKETMRLYPAGPLIERRTMEDCEVAGYQVPAGTRLLVNVWKMQRDGNVYKGDPLEFRPDRFLTSNADVDLKGQHYELIPFGAGRRICPGVSFAVQLMHLVLARLLHEFEITTVEPETKVDMAESGGLLCYKIMPLEVLIKPRLEI | 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, ChEBI:CHEBI:50540, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.97; Evidence={ECO:0000269|PubMed:23313486, ECO:0000269|Ref.2}; CATALYTIC ACTIVITY: Reaction=(S)-cis-N-methylstylopine + O2 + reduced [NADPH--hemoprotein reductase] = 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + protopine; Xref=Rhea:RHEA:76035, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:444, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16415, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.97; Evidence={ECO:0000269|PubMed:23313486, ECO:0000269|Ref.2}; CATALYTIC ACTIVITY: Reaction=(S)-cis-N-methyltetrahydrothalifendine + O2 + reduced [NADPH--hemoprotein reductase] = 7-hydroxy-8-methoxy-11-methyl-17,19-dioxa-11-azatetracyclo[12.7.0.0(4,9).0(16,20)]henicosa-1(21),4(9),5,7,14,16(20)-hexaen-2-one + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:76039, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194521, ChEBI:CHEBI:194522; EC=1.14.14.97; Evidence={ECO:0000269|Ref.2}; CATALYTIC ACTIVITY: Reaction=(S)-cis-N-methyltetrahydropalmatine + O2 + reduced [NADPH--hemoprotein reductase] = 2 H(+) + H2O + muramine + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:76043, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:194514, ChEBI:CHEBI:194523; EC=1.14.14.97; Evidence={ECO:0000269|Ref.2}; | 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-methyltetrahydrothalifendine and (S)-cis-N-methyltetrahydropalmatine as substrates (Ref.2). {ECO:0000269|PubMed:23313486, ECO:0000269|Ref.2}. | Papaver somniferum (Opium poppy) |
L7YAI7 | B4GA1_DANRE | MHFSKKCSVFKVVLSALLIVALLQLLYLSFLSKLHGKQQRYKYSELFGSKKNANQGEKNPRREHLRYSLSTGGIFDGSGQYRVYKNLIKSDFSTNQKPGADPRSHHLALATHTTINNLHHLESLLERWKNPISVAIFANGEDVKFATAIIYALSLFCPQVQALVDFHLVCHSGEMATFPDQDREHFVGLQEMGCPAVFAKLESHRDKYKNYAIGSNVSYPNNLLRNVARGGTDAAYILVIDIDMIPSANLHHQFVTMLMKREPAADEVLVLPAFEIRHIRKMPASKPELVQLYQVGEVRPFYDELCSRCQAPTNYSLWVNLASKSSGPLEVSYTINWVDPWEPFYIGARSVPLYDESFRQYGFNRISQACELHIAGYRFSVVSNAFLLHKGFKVQGEFHSRKDEENRKNRILFRSFKESLKAKYPTSPRRC | 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(+) + UDP; Xref=Rhea:RHEA:46860, Rhea:RHEA-COMP:15023, Rhea:RHEA-COMP:17482, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:142405, ChEBI:CHEBI:177336; Evidence={ECO:0000269|PubMed:23359570}; | 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 phosphorylated O-mannosyl glycan (By similarity). Phosphorylated O-mannosyl glycan is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (By similarity). Required for axon guidance; via its function in O-mannosylation of alpha-dystroglycan (DAG1) (By similarity). {ECO:0000250|UniProtKB:O43505, ECO:0000250|UniProtKB:Q8BWP8, ECO:0000269|PubMed:23359570}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
L8B068 | MALA_HALJT | MHHPGPPRFVATGDEVELAPRDPDPTATYTWRLTQAPAQSTVSLGDDPVEHFVPDAPGRYVVRLTAPDGEHDLTVRAFPGTLESSGTHTSGRSGGHSGGVSGGRSGPGRSGSGEYTQAGDGSDGGGGGQPRLTLRPDIEGDEAVVRADCSPHPEGTETAADLAVEFLLDDRDDVDADAVTRDGTALRIPLDALPERARIHAVAVGNHGYSVPDAVEFTRGGDGVETVTSGAGVAARRPYDAPAWAEDSVIYEIYVRTFAGERDESPFDAITDRLDYLDSLGVDAIWLTPVLQNDHAPHGYNITDFFEIASDLGTRADYERFIEAAHDRGFKVLFDLVCNHSARTHPYFESAVEGPDADYREWYEWRSDTEPETYFEWEHIANFNFDHLPVRRHLLDAVAQWADLVDGFRCDMAWAVPNGFWREIHDYCKDRDSEFLLLDETIPYIPDFQAGLFDMHFDSTTYAALRQVGGGGDAEAILGAIEGRAEIGFPEHASFMLYAENHDETRYIVDYGREAAEAAAGALFTLPGAPLLYAGQEFGQRGRRDDLAWDHADETLQSFVSDLASARHDQPALSADADLVRIPYEVRDGPSDRVVAYARTTENDAAVVVLNFGSEPTTVGLPAGTDGTDLVSGEYRGAAGDGDATVTVDSVSVFPADENDLRQ | 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 alpha-1,6 bonds. Higher activities of 100%, 79% and 67.8% against amylose, soluble starch and amylopectin, respectively. Lower activity of 22% against glycogen and faint or no activity against alpha-, beta- and gamma-cyclodextrin. {ECO:0000250|UniProtKB:Q8A1G3, ECO:0000269|PubMed:23391916}. | 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 by RNA polymerase II [GO:0006357]; synapse organization [GO:0050808] | 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 receptor family member fax-1, or with transcription factors unc-3, cfi-1, or hlh-34, perhaps acting via positive feedforward loops (PubMed:10207148, PubMed:16183052, PubMed:34165428). Establishes electrically- and chemically-interconnected neuron circuits, acting by modulating the expression of neurotransmitter pathway genes, neurotransmitter receptors, neuropeptides, and neuropeptide receptors (PubMed:34165428). Required for cholinergic and glutamatergic synaptic communication (PubMed:34165428). Plays a role in locomotion and mechanosensory response, perhaps via regulation of chemosensory receptor expression, and is required for expression of glutamate receptors, including glr-1, glr-4 and glr-5 (PubMed:10207148, PubMed:11222641, PubMed:34165428). {ECO:0000269|PubMed:10207148, ECO:0000269|PubMed:11222641, ECO:0000269|PubMed:16183052, ECO:0000269|PubMed:9216999}. | 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 dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | 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:30426815, PubMed:30504223). Regulates ameloblast development and tooth germ growth, perhaps acting by positively modulating migration of inner enamel epithelium (IEE) cells (PubMed:30426815, PubMed:30504223, PubMed:34812512). Plays a role in enamel formation (PubMed:34812512). {ECO:0000269|PubMed:30426815, ECO:0000269|PubMed:30504223, ECO:0000269|PubMed:34812512}. | Mus musculus (Mouse) |
M0R2J8 | DCDC1_HUMAN | MAKTGAEDHREALSQSSLSLLTEAMEVLQQSSPEGTLDGNTVNPIYKYILNDLPREFMSSQAKAVIKTTDDYLQSQFGPNRLVHSAAVSEGSGLQDCSTHQTASDHSHDEISDLDSYKSNSKNNSCSISASKRNRPVSAPVGQLRVAEFSSLKFQSARNWQKLSQRHKLQPRVIKVTAYKNGSRTVFARVTVPTITLLLEECTEKLNLNMAARRVFLADGKEALEPEDIPHEADVYVSTGEPFLNPFKKIKDHLLLIKKVTWTMNGLMLPTDIKRRKTKPVLSIRMKKLTERTSVRILFFKNGMGQDGHEITVGKETMKKVLDTCTIRMNLNLPARYFYDLYGRKIEDISKVPLLEKCLQNSITPLRGLLWVSKGEGFSPSGAKMYIQGVLLALYQRLKSAKKYYKQLNLVMNEQKEKITEKVILSMTAKEHHKEQEEVSRLIDELQTAIKSNIGHLCKLGPQLQAEQEQFSSYVYQHIKSLPANTLVPGGLQLKVFENGKNTGEISVGISKKDLGSDSPIQTDHMMERLLLKIHQRLQGSSINPPGLNYSSMRLFDENGQEIKNPLSLKNEQKIWVSYGRAYRSPLNLALGLTFDRVSAFARGDIMVAYKTFLDPNAVLLPGCGNWEVCEGFPINFNCTSQQIPDQFEKVDLENHFLQNKVDPNIVLHASVSIGKWSFSGSEASSRSQIAPSILWPVASVWLITKTGMILSRAITQGCLAIGHPIRVKAAEGTSLEGYKLILQKRHSGDDSQKWVFGTDGCIYSKAYPQFVLTYLEELNAQVDVTQTEYHIHHGAWTTAHQEHGRNLAEEVLQESASNLGLKQLPEPSDTHLMPEGSLEETGELTVALVRKLEEKHPKASAQRWAIKHEGTSKPGQWKHSRVENPLWNKLTYMWPVLPSGQLNEEFDWPIQGLLVPSSPPMKKPICKTTEPYAPVRLRVLQNGEKNKNRSVTILGPDISPGRKTQCTEILNLPSAARRLYNEKGKEIFALKDLQRDELVYVSCGELWINPDLSIAQQKKQIFLRNLESDIAKIQIFCSTHKIEALVLEVQSDIVSGSKLAVHKPVAIFGEEKQVTEPEEKQMQEDPLTTENASSEILDSHVRAHLRMKACHTLPRYAWQETSHDFDEDDSLPKKTEKGLFENVEPQKKHSCSPKHSKLHKHCHQQFEYRDGQIISHAAPQLVLGVQGPNLRSGMEVVLVEKKSDGSHQRWIHQEDSRTFHLVSNPDLVLAVSMTKTRNEVCGYPVIVQKYKPYNNGAANQKWHYMKNIKALVAFHSTALDKEITSANYAGVCTSSVIKEENIDQPGYCYLSPDGKRKTMLCLACGQSMRTEKGLKQLLPGVPFLCISGTKTQKPFLQGPFKVISVAEVDLSCDKAEKTLSYYQARLLSLRMKTCTQAASHSGMAATHQKAVKIIAYKNGDGYRNGKLIVAGTFPMLLTECTEQLGLARAASKVYTKDGTPIFTLRDLVLWALDESFLQRDSEKQKQDAAPVGKEQIIVEKNPRMKVKNRLFAKSVTSDSLDGIDKSLLTLILRNPIAIWVSCGEPFLPPNALQKAEKLEKQNWLKKDRILADLDTMRHKMRQLKGRRVAACQPATMVPTKSPVQPVVVEGGWTEQTQQEIKLMELIRHTEAHLSEIQEMESKINFPIATKRIAVKPSNLYKQPNTKRVWIYLNGGRPEDGTYAWGKTISELLQDCSSRLKMTHPARALYTPSGEPIQSWDDIERDMVICVSMGHGFKTPKELKQLMEIRANYARIRRQQGPQATDIVVSPSTKLLSLAHLHN | 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 microtubules during cytokinesis. {ECO:0000269|PubMed:22159412}. | 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 | MEPGSVVRAIFDFCPSVSEELPLFVGDVIEVLTVVDEFWLLGKKEDVTGQFPSSFVEIVTIPSLKEGERLFVCTCDFISREPNSLSLHRGDLVIIDGTPTAGWLQGRSSLGARGFFPSSCIHELCLSSQSRQWHSQNMLLQVPEYSMGQARALMGLSAQLDEELDFREGDVITIIGVPEPGWFEGELEGRRGIFPEGFVELLGPLRTADESVNAGSGDDSTLNDEVDVSPEEVESEGDEDDQQAGTYGIALYRFQALESNELDFEVGDKIRILGTLEDGWLEGRLKGKTGIFPHRFVKLCPSNRSEETMALPQGDSFPKNSESSAGEMGDSVVEEARQDPQECEEETPDSGLPEQTSEEPLDHVAPECVVDKISGQDEDASGSSPDVDLEGPRAEDPSTPDLSQEVNGISSLPPQVPLQPEEEKSQHYLTAGGSRQCPDTFSKLFPLEAKTRNYSSLPPRRTYTQGWSLQKPAPHLHRASSLTASRVNRPGHFSHTAMASCAQKHQTSAENAASLCCAPERPKRRPGLPDKEPATEITPASQGDNLDLDSKLTQQLIEFEKSLSGPSTEPKKIVRRFSIMDFYSEKDIVRGSSNSLPSRNFPERRKALRPPPPRPHTPTSTSPHLLVDQSPKPGPPLVVRPSRPAPLPPPTQQRLNTASPKPTSCALPGWEAPEKEGSEYTEKSPAQLFPCPSVLARIQDVEHDLDMHTRAQEELNLLLEEKQDESLRAETLETLKSYESTIQSLNLELQQLREMTLLSSQSSSLAAPSGSVSTEKPEQRMLEKRAKVVAELLQTEKDYIRDLEMCVERVMVPLQQAQVPNIDFEGLFGNMQTVIKVSKQLLAALEITDAVGPVFLDHRDELEGTYRLYCQNHDEAISLLDIYEKDERIQKHLQDYLADLKSLYHEWGCTNYINLGSFLIKPVQRIMRYPLLLMELLNSTPESHPDKAPLTSAVLAIKEINANINEYKRRKDLVLKYRKADEDSLMEKISKLNIHSIIKKSSRVSSHLKHLTGFAPQLKDEAFEETEKNFRMQERLIKSFIRDLSLYLQHIRESACVKVVAAMSIWDLCMERGHHDLEQFEKVHRYISDQLFTRFKERTERLVINPLNQLLNMFTGPYKLVQKRFDKLLDFYNCTERAEKLKDKKTLEDLQSARNNYEALNSQLLDELPKFQQYAQSLFTNCIHGYAEAHCDFVQKALEQLQPLLSLLKASDREGNLIAIFHEEHSRVLQQLQVFTFFPEALPAPRKPFERKTTDRQSSRKALLGMPSYMLQSEELRSSLLARYPPEKLFHVQRNFNAAQDLDVSLLEGDLVGVIKKKDPMGSQNRWLVDNGVTKGFVYSSFLKPYNPRCSHSDSSVVSHSSTESEHSGSSPSFHRQNSSSALTFNSNSMTVSFTSGLPQKQPQDTSPLRECVPETLGVSSNTGNPETGPSPCPSDPGFSCQRRPGNPADGTREISQPASTLRGCQRRSLHSEVLGYPVPGRSDQGSDSIKGTSRACQTAGDRDRGLGSSEAEGNQVYFAIYTFKARNPNELTVLANQRLRILEFKDVTGNTEWWLAEVNGKKGYVPSNYIRKTEYT | 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 with TJP1. {ECO:0000250|UniProtKB:Q6XZF7}. | 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 cysts by regulating spindle orientation (By similarity). Plays a role in ciliogenesis (By similarity). May play a role in membrane trafficking between the cell surface and the Golgi (PubMed:14506234). {ECO:0000250|UniProtKB:E2RP94, ECO:0000250|UniProtKB:Q6XZF7, ECO:0000269|PubMed:14506234}. | Rattus norvegicus (Rat) |
M0R5D6 | RN157_RAT | MGALTSRQHAGVEEVDIPSNSVYRYPPKSGSYFASHFIMGGEKFDCTHPEGYLFGENSDLNFLGNRPVSFPYAAPPPHEPVKTLRSLINIRKDTLRLVKCAEEVKSHGEEAGKAKVHYNVEFTFDTDARVAITIYYQATEEFQNGIASYIPKDNSLQSETVHYKRGVCQQFCLPSHTVDPSEWAEEELGFDLDREVYPLVVHAVVDEGDEYFGHCHVLLGTFEKHSDGTFCVKPLKQKQVWDGVTYLLQEDYGIENKSNTQDFKVAEDDVRDNSAECVVCLSDVRDTLILPCRHCASCNVHCADTLRYQANNCPICRLPFRALLQIRAMRKKLGPLSPSSFNPIISSQTSDSEEHSSSENIPAGYEVVSLLEALNGPLTSSPAVPPLHVLGDGHLSGMLPSYGSDGHLPPVRTLSPLDHLSDCNSQGLKLNKSLSKSISQNSSVLHEEEDERSCSESDTQLSQRLSAQHPEEGPDVTPESENLTLSSSGAVDQSSCTGTPLSSTISSPEDPASSSLAQSVMSMASSQISTDTVSSMSGSYIAPGTEEEGEAPPSPRAASRAPSEEEETPAESPDSNFAGLPAGEQDAEGNDIMEEEDRSPVQEDGQRTCAFLGMECDNNNDFDVASVKALDNKLCSEVCLPGTWQHDAAIINRHNTQRRRLSPSSLEDPEEDRPCVWDPLAV | 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). May act as a scaffold molecule to regulate this process (By similarity). Acts as a downstream effector of the interconnected PI3K and MAPK signaling pathways and thus participates in the regulation of the cell cycle (By similarity). {ECO:0000250|UniProtKB:Q96PX1}. | Rattus norvegicus (Rat) |
M0R6D8 | MNX1_RAT | MEKSKNFRIDALLAVDPPRAASTQSAPLALVTSLAATPSGPGRGGSGGGGTSSGASRSCSPASSEATAAPGDRLRAESPSPPRLLTAHCALLPKPGFLGAGGGGGAAGGPGTPHHHAHPGAAAAAAAAAAAAAAGGLALGLHPGGAQGGAGLPAQAALYGHPVYSYSAAAAAAALAGQHPALSYSYPQVQGAHPAHPADPIKLGAGTFQLDQWLRASTAGMILPKMPDFSSQAQSNLLGKCRRPRTAFTSQQLLELEHQFKLNKYLSRPKRFEVATSLMLTETQVKIWFQNRRMKWKRSKKAKEQAAQEAEKQKGSGGGAGKGGTEEKTEEELLGPPVSGDKASGRRLRDLRDSDPDEDEDDEEDHFPYSNGVGAHAASSDCSSEDDSPPPRPGGPGHQPLPQ | 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 neuron axon guidance [GO:0008045]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nerve development [GO:0021675]; neuron differentiation [GO:0030182]; neuron migration [GO:0001764]; neuron projection morphogenesis [GO:0048812]; pancreas development [GO:0031016]; post-embryonic development [GO:0009791]; respiratory system development [GO:0060541]; spinal cord motor neuron cell fate specification [GO:0021520] | 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 similarity). Involved in negatively modulating transcription of interneuron genes in motor neurons, acting, at least in part, by blocking regulatory sequence interactions of the ISL1-LHX3 complex (By similarity). Involved in pancreas development and function; may play a role in pancreatic cell fate specification (By similarity). {ECO:0000250|UniProtKB:Q9QZW9, ECO:0000269|PubMed:18539116}. | 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:2000766]; positive regulation of 3'-UTR-mediated mRNA stabilization [GO:1905870]; positive regulation of myotube differentiation [GO:0010831]; positive regulation of skeletal muscle fiber differentiation [GO:1902811]; positive regulation of stem cell differentiation [GO:2000738]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of mRNA stability [GO:0043488]; regulation of myotube differentiation [GO:0010830]; RNA splicing [GO:0008380] | 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-specific exon inclusion in numerous mRNAs important for striated cardiac and skeletal muscle cell differentiation (By similarity). Binds to intronic splicing enhancer (ISE) composed of stretches of GU-rich motifs localized in flanking intron of exon that will be included by alternative splicing (By similarity). Involved in embryonic stem cell (ESC) transition to cardiac cell differentiation by promoting pre-mRNA alternative splicing events of several pluripotency and/or differentiation genes (By similarity). Plays a role in the regulation of mRNA stability (By similarity). Binds to 3'-untranslated region (UTR) AU-rich elements in target transcripts, such as CDKN1A and MYOG, leading to maintain their stabilities (By similarity). Involved in myogenic differentiation by regulating MYOG levels (By similarity). Binds to multiple regions in the mRNA 3'-UTR of TP63 isoform 2, hence inducing its destabilization (By similarity). Promotes also the destabilization of the CHRM2 mRNA via its binding to a region in the coding sequence (By similarity). Plays a role in the regulation of mRNA translation (By similarity). Mediates repression of p53/TP53 mRNA translation through its binding to U-rich element in the 3'-UTR, hence preventing EIF4E from binding to p53/TP53 mRNA and translation initiation (By similarity). Binds to a huge amount of mRNAs (By similarity). Required for embryonic heart development, sarcomer and M-band formation in striated muscles (By similarity). Together with RBM20, promotes the expression of short isoforms of PDLIM5/ENH in cardiomyocytes (PubMed:27289039). {ECO:0000250|UniProtKB:D3Z4I3, ECO:0000250|UniProtKB:Q9BX46, ECO:0000269|PubMed:27289039}. | Rattus norvegicus (Rat) |
M0R7Z9 | PLIN5_RAT | MDQRGKDTTLALHSRMSGDQTAQDPGSSLGELDQHNVVKRVVALPLVRATCTAVSGAYNSAKDRHPLLGSACRFAEHCVCSVATCALDHAQPLLEHLQPKLATVNDLACRGLDKLEEKLPFLQQPSDTVVTSAKDAVAKSVTGVVDLAQRGRRWSGELRRSVSQAMDTVLRRSVSQAMDTVLGKSEELVDHFLPMTEAELVALATESQGPEVGSVEEQRQKQGYFVRLGSLSARLRHLAYQHSLGKLRESKHRTQEMLAQLQKTLELIQHMQSRASPTPTFHHPKVQELCGDWSPCLENGYRHSQVELETLALSRSLTLELQSAVDALAGCVRGLPPSAQAKVAEVQRSVDALQATFADAHCLGDVAPTALAEGQDSVAQAHACVDEFLDLVLRAMPLAWLVGPFAPILVERSEPLINLATCVDEVVGDPDPRWAHMDWPAQQRAWEAEPADPGGQEAEPPLGQVKHTMMPELDF | 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 proliferator activated receptor signaling pathway [GO:0035359]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; negative regulation of triglyceride catabolic process [GO:0010897]; positive regulation of fatty acid beta-oxidation [GO:0032000]; positive regulation of lipase activity [GO:0060193]; positive regulation of lipid storage [GO:0010884]; positive regulation of sequestering of triglyceride [GO:0010890]; positive regulation of triglyceride biosynthetic process [GO:0010867] | 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|UniProtKB:Q8BVZ1}. | 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 form of triglycerides and the release of fatty acids for mitochondrial fatty acid oxidation. In lipid droplet triacylglycerol hydrolysis, plays a role as a scaffolding protein for three major key lipolytic players: ABHD5, PNPLA2 and LIPE. Reduces the triacylglycerol hydrolase activity of PNPLA2 by recruiting and sequestering PNPLA2 to lipid droplets. Phosphorylation by PKA enables lipolysis probably by promoting release of ABHD5 from the perilipin scaffold and by facilitating interaction of ABHD5 with PNPLA2. Also increases lipolysis through interaction with LIPE and upon PKA-mediated phosphorylation of LIPE. {ECO:0000269|PubMed:21885430, ECO:0000269|PubMed:22127648, ECO:0000269|PubMed:23353597}. | 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 and amidated peptide. Localized extracellularly surrounding the villous trophoblastic cells. Detected in the serum (By similarity). {ECO:0000250}. | 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:0000269|PubMed:22038051}.; FUNCTION: [Spexin-1]: Acts as a ligand for galanin receptors GALR2 and GALR3 (By similarity). Intracerebroventricular administration of the peptide induces an increase in arterial blood pressure, a decrease in both heart rate and renal excretion and delayed natriuresis. Intraventricular administration of the peptide induces antinociceptive activity. Intraperitoneal administration of the peptide induces a reduction in food consumption and body weight. Inhibits long chain fatty acid uptake into adipocytes. Also induces contraction of muscarinic-like stomach smooth muscles (PubMed:24550067). {ECO:0000250, ECO:0000269|PubMed:24550067}.; FUNCTION: [Spexin-2]: Intracerebroventricular administration of the peptide induces a decrease in heart rate, but no change in arterial pressure, and an increase in urine flow rate. Intraventricular administration of the peptide induces antinociceptive activity (PubMed:22038051). {ECO:0000269|PubMed:22038051}. | Rattus norvegicus (Rat) |
M0R8U1 | DYH5_RAT | MFRIGRRQLWKQSVTRVLTQRLKEEKEAKRARLDGRHDYLFAIVASCLDLNKPEVEDALLEGNQIERIDQLFAVGGLRHLMFYYQDVEGAEAGQFGSSGGVNPASGKMKKPKVFVTEGKDVALMGACVFFTRADPSKAITAENIHREVSFNTLDTADGGLLNSVRRLLSDIFIPALRASSHGWGELEGLQDASSIQQEFLSSLEGFVGILSGAQNSLKEKVNLQKCDIVELKSLKEPMDYLALASNPETVEKVECCMRVWIKQMEQILAENNQLRKEADDVGPRAELEHWKKRLSKFNYLLDQLKSPDVKAVLAMLAAAKSKLLKVWRDADIRVTDAANEAKDNVKYLYTLEKCCDPLYSSDPVTMVDAIPTLINAIKMIYSISHYYNTSERITSLFVKVTNQMISACKAHITNNGTATIWSQPQDIVMQKIAAAIKLKQGYQCCFQETKQKLKQNPSEKQFDFSEMYIFGKFETFHQRLAKIMDIFTTFKTYSVLQDSKIEGLEDMVTKYQDVVAGIKKKEYNFLDQRKMDFDQDYDEFCKQTNELHSELQRFMDTTFEKIQSTRQALSTLKKFERLNIPNLGIEAKYQIVFQNFGTDIDMISKLYTKQKYDPPLARDQPPIAGKILWARQLFHRLEQPMQLFQQHPFVLRTVEAKPVIRSYNRIAKVLLEFEVLYHRAWLQQIEEIHVGLEASLLVKAPGTGQLFVNFDPQILILFRETQCMSQMGLPVSPFAAALFEKRDMYKKNFSDMKMMLSEYQRVKLKMPPAIEQLMLPHLARVDEALQPGLAVLTWTSLNIGTYLENAFEKIKDLELLLDRINDLIEFRIHAILEEMSSVALCQLPQDDPLTCEEFLQMTKDLCVNGAQKLHFKSSLVEEAVNELINMLLDVDVLPEEASEKVRHENASPNGDTSGGGEGCAEALASSFNAGTSSLPLTTIARKKKEMEVLEEARELLSYFNHQNTDALLKVTRNTLEAIRRRIHFSHMINFRDSKGASKVKQNHLPIFRASVTLAIPNISMTPALEDIQQTLNKAVECIISVPKGVRQWSSELLSKRKMRERKMAAVQSNEDSDSDTEVEESELQETLELASVNLPIPVQTQNYYKNISDNKEIVKLVSVLSTVISSTKKEVITSMDRFKCYNHIWQKEKEDTIMTFIAQNPLLSEFESRILYFQSLEQEINAEPEYICVGSIALYTADLKFSLTAETKAWMMVLGRHCNRKYRSEMENIFTVVEEFQKKLNRPIKDLDDIRIAMAALKEIREQQISTDFQVGPIEESYALLNKYGLLVAKEEMDKVDTLRYAWEKLLARASDVQNELGALQPSFRKELISTVEVFLQDCQQFYLDYDLNGPMVSGLKPQEASDRLIIFQNQFDNIYRKYITYTGGEELFGLPVTQYPQLLEIKKQLNLLQKIYSLYNNVIETVNSYQDTLWSEVNIEKINSELLEFQNRCRKLPRALKDWQAFLDMKKTIDDFSECCPLLEYMASNAMVERHWQRITTLTGHSLDVGNETFKLRNIMEVPLLKYKEEIEDICISAVKERDIEQKLKQVINEWDNKTLTFSSFKTRGELLLRGDSTSEVIASMEDSLMLLGSLLSNRYNMPFKAQIQNWVQCLSNSTDIIENWMTVQNLWIYLEAVFVGGDIAKQLPKEAKRFSNIDKSWVKIMTRAHEIPNVVQCCVGDETMGQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFFFVSDPALLEILGQASDSHTIQAHLLNVFDNIKTVKFHDKIYDRILSISSREGETIELDKPVMAEGNVEVWLNSLLEESQSSLHLVIRQAAANIQESGFQLIEFLSSFPAQVGLLGIQMLWTRDSEEALQNAKFDKKIMQKTNQSFLELLNMLIEMTTKDLSSMERVKYETLITIHVHQRDIFDDLCHMHVKSPTDFEWLKQCRFYFKEDSDKTMIHITDVAFTYQNEFLGCTDRLVITPLTDRCYITLAQALGMSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKGLAQSGSWGCFDEFNRIDLPVLSVAAQQISIILTCKKEHKKSFIFTDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINFRSVAMMVPDRQIIIRVKLASCGFIDNVVLARKFFTLYQLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRASHTDTESTIVMRVLRDMNLSKLIDEDEPLFLSLIEDLFPNILLDKAGYPELETAISKQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTLGPSGSGKTSCIHTLMKAMTDCGKPHREMRMNPKAITAPQMFGRLDVATNDWTDGIFSTLWRKTLKAKKGEHIWIVLDGPVDAIWIENLNSVLDDNKTLTLANGDRIPMAPNCKIVFEPHNIDNASPATVSRNGMVFMSSSVLDWSPILEGFLKRRSPQEAEILRQLYAETFPDLYRFSIQNLEFKMEILEAFVITQSTHMLQGLIPTKEQAGDVDPEHLGRLFVFAMMWSVGAVLELEGRRRMELWLRSREGPTLHLPQLTDPGDTMFDYYVAPDGTWRHWSMCIPEYVYPPDTTPEYGSILVPNVDNVRTDFLIKTIAKQGKAVLLIGEQGTAKTVIIKGFMSKFDPESHTVKNLNFSSATTPLMFQRTIESYVDKRMGTTYGPPAGKKMAVFIDDLNMPVINEWGDQVTNEIVRQLMEQNGFYNLEKPGEFTSIVDIQFLAAMIHPGGGRNDIPQRLKRQFSIFNCTLPSDASMDKIFGVIGEGYYCAQRGFSKEVQDAVIKLVPLTRRLWQMTKLKMLPTPAKFHYVFNLRDLSRIWQGMLNITSEVIKDTDELLRLWKHECKRVIADRFSMSSDVTWFDKAVVSLVEEEFGEEKTPVVDCGVDAYFVDFLRDAPEATGETPEETDAEMPKLYEPIASLNHLQERLSVFLQLYNESIRGTGMDMVFFRDAMVHLVKISRVIRTPRGNALLVGVGGSGKQSLTRLASFIAGYTSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNEIKEESFLEYMNNVLSSGEVSNLFARDEIDEINSDLTSIMKKEHPKRPPTNDNLYEYFMSRVRGNLHIVLCFSPVGEKFRNRALKFPALISGCTIDWFSRWPKDALVAVSEHFLSSYNIDCTAEIKKELVQCMGSFQDGVAEKCADYFQRFRRSTHVTPKSYLSFIQGYKFIYEEKHVEVQSLANRMNTGLEKLKEASESVAALSQELAVKEKELQVANEKADMVLKEVTMKAQAAEKVKAEVQKVKDKAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIKPSDIATVRTLGRPPHLIMRIMDCVLLLFHRRVNAVKIDLDKSCTVPSWQESLKLMTAGNFLQNLQQFPKDTINEEVIEFLSPYFEMSDYNIETAKRVCGNVAGLCSWTKAMASFFSINKEVLPLKANLIVQENRHALAMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQ | 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 motility [GO:0030317]; heart development [GO:0007507]; lateral ventricle development [GO:0021670]; outer dynein arm assembly [GO:0036158] | 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. {ECO:0000250|UniProtKB:Q8TE73}. | 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 exocytosis [GO:0045921]; positive regulation of smooth muscle cell migration [GO:0014911]; positive regulation of smooth muscle cell proliferation [GO:0048661]; postsynaptic neurotransmitter receptor internalization [GO:0098884]; receptor internalization [GO:0031623]; regulation of endosome size [GO:0051036]; regulation of filopodium assembly [GO:0051489]; regulation of long-term neuronal synaptic plasticity [GO:0048169]; regulation of synaptic vesicle exocytosis [GO:2000300]; synaptic vesicle endocytosis [GO:0048488]; synaptic vesicle recycling [GO:0036465]; vesicle-mediated transport [GO:0016192] | 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 [GO:0012505]; endosome [GO:0005768]; endosome membrane [GO:0010008]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; melanosome [GO:0042470]; membrane raft [GO:0045121]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; phagocytic vesicle [GO:0045335]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; postsynaptic early endosome [GO:0098842]; postsynaptic endocytic zone membrane [GO:0098844]; protein-containing complex [GO:0032991]; recycling endosome [GO:0055037]; ruffle [GO:0001726]; somatodendritic compartment [GO:0036477]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]; terminal bouton [GO:0043195]; zymogen granule membrane [GO:0042589] | 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 vesicle {ECO:0000250|UniProtKB:P20339}. Cell projection, ruffle {ECO:0000250|UniProtKB:P18066}. Membrane {ECO:0000250|UniProtKB:P20339}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P20339}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9CQD1}. Endosome membrane {ECO:0000250|UniProtKB:P20339}. Note=Enriched in stage I melanosomes. Alternates between membrane-bound and cytosolic forms. {ECO:0000250|UniProtKB:P20339}. | 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|UniProtKB:P20339}; | 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 form is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB5A is required for the fusion of plasma membranes and early endosomes. Contributes to the regulation of filopodia extension. Required for the exosomal release of SDCBP, CD63, PDCD6IP and syndecan. Regulates maturation of apoptotic cell-containing phagosomes, probably downstream of DYN2 and PIK3C3. {ECO:0000250|UniProtKB:P18066, ECO:0000250|UniProtKB:P20339, ECO:0000250|UniProtKB:Q9CQD1}. | 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 formation (PubMed:26765567). {ECO:0000250|UniProtKB:P38182, ECO:0000269|PubMed:26765567, ECO:0000305|PubMed:26765567}. | 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, PubMed:29932422). {ECO:0000269|PubMed:26765567, ECO:0000269|PubMed:29932422, ECO:0000305|PubMed:26765567, ECO:0000305|PubMed:29932422}. | 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 initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses such as the plum pox virus (PPV) strain D (PubMed:23382802). {ECO:0000250|UniProtKB:Q66WU1, ECO:0000269|PubMed:23382802}.; FUNCTION: (Microbial infection) Susceptibility host factor required for viral infection by recruiting viral RNAs to the host ribosomal complex via an interaction with viral genome-linked protein (VPg). {ECO:0000269|PubMed:23382802}. | 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-inhibitory molecules and the anti-inflammatory cytokine interleukin-10 (PubMed:23825947). It has a pocket to accomodate cholesterol, which may have immune-modulatory roles, either directly or through interactions with the host gut microbiota (Probable). {ECO:0000269|PubMed:23825947, ECO:0000305|PubMed:29167574}. | Rhipicephalus appendiculatus (Brown ear tick) |
M1RNJ8 | ATH1_CANGB | MGFKDKILFWKDEVQYRTLAVADQVANRFLHSFENVYQGDESVEDADSRPVGLTNETLSHSSDFFVLPEERISTRVKIRRQNILNTTLILGMLIALVIWTAILSTNSYFSSSLASASPLFNKEGRVVRPMRESNLGLHADPQTRKSSKTLYDLLSDFDNAFYDDENMILGSLAFGENTYSRQPYVANGYIGSRIPNIGFGYALDTLNLYADAPGALNNGWPLRNRRFAGSFVSDFYSLQAKLNSTNFPELDEKGYTTVISSIPEWTDLQFTVDLNGTKWFNPQSVLIDDVINYNQNLSMKDGIVSTNMDWLNGMINIKSEVWAHRKIHSLGITRLEISLNLDALPDEFTELPVTVYDIIDLNTSHRTTLYEKGQDEDNKAIYMIVNPDNVPYSNAVVYSTCTIKGTENNFSPYNFTSDDRIARNYMTNLTEENPKVVIYKYTSVVSSEYNNDEPNPNVNLKFASNIANTAKGNYKSLLSNHKRAWYDLYNDAFIEIPSDSLLEMTARSSLFHLLANTRQYNVSTTRGLPVGVGGLSSDSYGGMVFWDADVWMAPALLPFFPNIAMNMNNYRNATHQQAIENAKQYNYPGAVYPWTSGRYANCTSTGPCIDYEYHINVDIALASFSIYMNGAEGADEDYLRFTTWPMVKDAAVFFKAYVKYNETLGEYETYNLTDPDEFANHVNNGAFTNAGIKTLLKWATDIGTHLGEEVDPKWMEIADNIHIPRSDSNITLEYSGMNSSVEIKQADVTLMVYPLGYINDESILNNAIKDLYYYSERQSASGPAMTYPVFVAAAASLLNHGSSSQSYLYKSVLPYLRSPFAQFSEQSDDNFLTNGLTQPAFPFLTANGGFLQSILFGLTGLRYSYEVTPRTKKISRLLKFDPVKLPLLPGGIAIRNFKYMGQVLDIIIDDNNGTIAHKGGDKPIRIKVPNRDILHDRNITSALYSKRDDDLSATDDYYGTYFTLYPNEELVIPLYDTKLNIDGNIAESKQITNLTAGVPGDVGFSALDGNNYTHWQPFDKSDNAKLLIDLGFNSTHVIKKGIILWGQRPAKNISLSVLPHSERIEQLFANITDLLETSSITKGGLPLNQMLGQTQSNVTAEIDDDILALLNWKGDDLDQLIPYLPDMHLLQEKFIPILKDYPIKPNQRYYEEIIDDDIIKLLPSNTTEFTIDYNSIPGGEKRARYVVLTVHGTYDDDDDLKGATIREIVLQE | 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:33146242}. | Candida glabrata (Yeast) (Torulopsis glabrata) |
M1T7M3 | HOG1B_WALI9 | MADFVNASIFGTLFQITSRYVNLEPVGMGAFGLVCSAKDQLTSSPVAIKKIMKPFSTPVLSKRTYRELKLLKHIRHENIISLSDIFISPSEDIYFVTELLGTDLHRLLTARPLEKQFIQYFLYQILRGLKYVHSAGVVHRDLKPSNILVNENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVAVDIWSTGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVIQTICSENTLRFVQSLPKKPRIPFNEKFKTNDPLALDLVEKMLSFDPRTRITASQALAHPYLAPYHDPNDEPVAAEQFDWSFNDADLPIDTWKVMMYSEILDFHHISQDGDQFLNANGPGTEQASDSSFTV | 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-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; | 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 | MSNETLSADVVIIGAGICGSLLAHKLVRNGLSVLLLDAGPRRDRSQIVENWRNMPPDNKSQYDYATPYPSVPWAPHTNYFPDNNYLIVKGPDRTAYKQGIIKGVGGTTWHWAASSWRYLPNDFKLHSTYGVGRDYAMSYDELEPYYYEAECEMGVMGPNGEEITPSAPRQNPWPMTSMPYGYGDRTFTEIVSKLGFSNTPVPQARNSRPYDGRPQCCGNNNCMPICPIGAMYNGVYAAIKAEKLGAKIIPNAVVYAMETDAKNRITAISFYDPDKQSHRVVAKTFVIAANGIETPKLLLLAANDRNPHGIANSSDLVGRNMMDHPGIGMSFQSAEPIWAGGGSVQMSSITNFRDGDFRSEYAATQIGYNNTAQNSRAGMKALSMGLVGKKLDEEIRRRTAHGVDIYANHEVLPDPNNRLVLSKDYKDALGIPHPEVTYDVGEYVRKSAAISRQRLMDIAKAMGGTEIEMTPYFTPNNHITGGTIMGHDPRDSVVDKWLRTHDHSNLFLATGATMAASGTVNSTLTMAALSLRAADAILNDLKQG | 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 | MGSQHQSQHNSALIQAARDGEATLSVAFGGQGPSNLNCFNDLLELNKTYGSTLRPLIHTADATLSELASLPHRSGFHEDEGFETLDWLQDPKQAPSREYLALSPMSFPINTLLSLCNYCVTLRALRLDPGQFRSSLHNVVGHSQGIFAAAAIAKADSWESFLEAAEIALKISFWVGLESHTAAPPSHISAAAVQDCVEHGEGQPSSMLGITGLNRAQVEMLVERVNKSLSDDDRHVCLALANSRDKYTIAGPPHSLRAVCVQIREIRAADGVDQSRILFNKRKQEVDALFLPISAPYHSQYLKQVSNNVLDALDVDLVGSELGIPLLHTQSGQNLQDWKSKSIIKAIVCAVTTDMVEWPDVCQRLGSSYILGFGPGNIGNLIHESTEGTGVRVIQMNDRSPGSRGIGARAELFSEEMPPQALDWKQTFGPRLVLDHRGDVQIQTRMTQLLNAPPVMVAGMTPTTVTWDFVSCVMQAGYHVELAGGGYSSEARFEEALRRLAASIPIYRGITCNLLYANPQTIAWQVAVLRRLIKEGISIEGVTIGAGVPSPDVIKEYIAIGLKHISFKPGSIAAIDEVIEIAQAHPQFPIGLQWTGGRAGGHHSHEDLHLPILKTYARIRRCSNIVLIAGSGFGGGSDTYPYISGDWSKSLSYPPMPFDGILLGSRVMVAKEAHTSPQAKQLIVQTEGVGDNDWHTSFETPTGGVITITSEHGQPIHMLATRGVMLWKEFDKRIFSIKDAAKRLSYIRAHREEIITRLNKDYQKPWFGVNGDGQNVDLDRMTYREVLGRMCQLMSRGDNGWTDPSWLAMVKDFVEIAGERFGCQVDAHATKAPEVRTAFEATLGGSVDETLYPEDVALVLELLRRRGRKPPPFVPALDENFETWCKKDSLWQSEDVDSLVGKDVQRACIIQGPVAVRHSTIHDEPVQDILDNICNFHIESLLQSGETPGVARKQDLGRPNSIKKSVPGVQITTEKTTIRYQVHKTDKLPPEMDTLIEHIVGPAADCWTHHCLKDEWVFRDQARLRNPIRAAFLRQIQPGEVIEVRLSRDGNTQAIALKTALFGKSSLQTVLRIASTDGKSIKVALTPPSFLSDKPLGLQFAYQLSRKSRGSKLVEVTPNRLDAIKGFYAQLWVDSNQDVKEAGLNSEFWGEPTTLLAQDVQNYTAVVSRSTSPQLQAWNPTGSVPVDYCIVLAWTALTKPLTIPALQCDLLNLLHRSVNFKYAANARPLRLGDVTQTVSRITSLTIQPTGKLVEVSAELRRNDETVVTITTEFFIVGQFEDYETQFKSFEEPLFEVRVHSVTRQALLQSRKWLVLDDPSMDLAGLTLAFKLNTHTTFDHEGKVGALQVTGSVSRVESTGFDTRIGKVYFKKDSCNGNPVVDFLNRHGYPRVTRQPLENPGWNEGSTVLMKAPAKSNQYAMASKDTNPLHVCGVFARYAGLPDTVVHGMHTSAIVRRAVEWAVGDSDRSRFKKWQVSFEGMVRPNDRLKIQLQHTAMEHGRMIMKVQAFNDETGDKVIEAEAEVEQPRTGYVFCGQGSQEKGMGMSLYNARPEAKALWDRGDQFLREQYGFSLLSLVRENPTTLTINFGGRRGKRIRDNYLAMTKKTSLKADAKDVCIVQGLTPTSTSHTFSETKGLLFSTQFSQPAIALMEMVEHEHLFAKGVVQPSALFAGHSLGEYAALGACTTFMPFESLLTLIFYRGLKMQNALERDANGRTDYSMMAADPSRVGKAGFDERAFQCLVELVNEETGLLMEIVNHNVRSQQYVCAGHFRALWILGKVCDDLAKHPKIHLLSMQDLKDMVTTHVPAAGKLTNDIVLTRGKATIPLNGIDIPFHSTMLRGEIEHFRRYLLTKVNVPDIKPNELVGKWIPNVVGRPFSLDRSYIEHVQSVTGSEPLQKMLKAMA | 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:0004312]; fatty acyl-[ACP] hydrolase activity [GO:0016297]; fatty-acyl-CoA synthase activity [GO:0004321] | 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, ChEBI:CHEBI:83139; EC=2.3.1.86; Evidence={ECO:0000250|UniProtKB:Q8TGA1}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA; Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479, ChEBI:CHEBI:78446; EC=2.3.1.38; Evidence={ECO:0000250|UniProtKB:Q8TGA1}; CATALYTIC ACTIVITY: Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP]; Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449; EC=2.3.1.39; Evidence={ECO:0000250|UniProtKB:Q8TGA1}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000250|UniProtKB:Q8TGA1}; CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9; Evidence={ECO:0000250|UniProtKB:Q8TGA1}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) + holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14; Evidence={ECO:0000250|UniProtKB:Q8TGA1}; | 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 step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits hexA and hexB, as well as the polyketide synthase pksA (PubMed:16649078, PubMed:23207690). PksA combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR (By similarity). The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by the fungal fatty acid synthase hexA/hexB (By similarity). The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase nor1, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin (PubMed:23207690). The cytochrome P450 monooxygenase avnA then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN) (PubMed:23207690). The next step is performed by adhA that transforms HAVN to averufin (AVF) (PubMed:23207690). Averufin might then be converted to hydroxyversicolorone by cypX and avfA (PubMed:23207690). Hydroxyversicolorone is further converted versiconal hemiacetal acetate (VHA) by moxY (PubMed:23207690). VHA is then the substrate for the versiconal hemiacetal acetate esterase est1 to yield versiconal (VAL) (PubMed:23207690). Versicolorin B synthase vbsA then converts VAL to versicolorin B (VERB) by closing the bisfuran ring (PubMed:16649078, PubMed:23207690). Then, the activity of the versicolorin B desaturase verB leads to versicolorin A (VERA) (PubMed:23207690). DotB, a predicted chloroperoxidase, may perform epoxidation of the A-ring of VERA (PubMed:23207690). Alternatively, a cytochrome P450, such as cypX or avnA could catalyze this step (PubMed:23207690). It is also possible that another, uncharacterized, cytochrome P450 enzyme is responsible for this step (PubMed:23207690). Opening of the epoxide could potentially be achieved by the epoxide hydrolase epoA (PubMed:23207690). However, epoA seems not to be required for DOTH biosynthesis, but other epoxide hydrolases may have the ability to complement this hydrolysis (PubMed:23207690). Alternatively, opening of the epoxide ring could be achieved non-enzymatically (PubMed:23207690). The next step is the deoxygenation of ring A to yield the 5,8-dihydroxyanthraquinone which is most likely catalyzed by the NADPH dehydrogenase encoded by ver1 (PubMed:23207690). The last stages of DOTH biosynthesis are proposed to involve hydroxylation of the bisfuran (PubMed:23207690). OrdB and norB might have oxidative roles here (PubMed:23207690). An alternative possibility is that cytochrome P450 monoogenases such as avnA and cypX might perform these steps in addition to previously proposed steps (PubMed:23207690). {ECO:0000250|UniProtKB:Q8TGA1, ECO:0000269|PubMed:12039746, ECO:0000269|PubMed:16649078, ECO:0000303|PubMed:22069571, ECO:0000305|PubMed:17683963, ECO:0000305|PubMed:23207690, ECO:0000305|PubMed:23448391}. | Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight fungus) (Mycosphaerella pini) |
M2YJJ3 | HEXA_DOTSN | MGQKTIKRKIQSAERPAEADVAFLASTQHSKDLCYEYDAPEEVAVEEPVDETPAPETAPERPPLSRAKTAAVKPQETAAPTTATIADVPLSAEEIVRALVARKLKKPILSIPTSKSVKELCNGKSTLQNEIVGDFHSEFTNLPDRPEDIPLKELVPASQSLMLGRVSSALLSKLVSSKMPARFNADAIGKYLASKWGLGPLRSVAVMLFAIAAEPEARLGSVAAAEKYLDDTAAKYAEWAGITLQERSTQSSAGGGGSSGTVDPTVLAELTKTNTRLAKRQFQALAEYLQVDLMKPSSEQESEALAVELQQKLDAWTAEFSEEFLAGVAPTFSEKKSRRYNAWWNAARQDVLALFSGNLQEDLSRDAAALEAFLDRLSNRAGESLLAMTRSLSRRNQANAIPGLTDIARRAEKAISSCIDRPATAKVHLPATRPRTTVSDEGDIKFNEVPRPDVSGHAAYADVLQAKDLNGHPAAARFVSLKSAHSHTDLTNGMLDRIRTALDSGMSFAGKNILITGAGQGSIGAEVVRILLTGGARVIVTTSREPSSTAKYFQQMYEESGAKGSELILTRFNQASAKDCENLVDHIYDSSGLDRDLDAVLPFAAAPEGGTEIQDVGAKNELVHRLMLASVFRMLGRVIKNKRDRSIDCHPTQVLLPLSPNHGTFGGDGMYAESKLGLESLVNRVQSESWSDELAICGVKIGWTRGTGLMNANDIVAEAIEDHGVLTFSVQEMAFNIAMLMTPELVDLCENAPLMADFGGGLSALEDCAKILSAARTEINTAADVARAVKAEDDLERAASRTLPAPSSTSPVAKKSMLRIGFPRLPDFELELSPLEHLRDIKDPSETVVVVGFSELGPWGSARLRWEIESKGDFSQVGYMEMAWMMDLIKHVDGPTKNGYYVGWVDSKTGESVHDAEIEARYGEVIRKHSGIRFVDPEGSAGYDPSKKEYLHEVAVEEDLPEFEASSATAEAFRLRHGTNVSISPIEGTENCRVQVKRGASIKIPKSVPFTWGSVAGQLPKGWSPKKYGIPEDLIPQLDPVSLYTICCVAEAFYSAGITDPLEIFKYIHLSEIGNFLGSSMGGALKTRQMYRDIYLDKDIQSDVLQETYLNTTGAWVNMLLLGSTGPIKTPMGACATGVESIDSAFESIMSDKTRMCIVGGFDDFHEDESYGFSTMKATVNVEEELAKGRLPSEMSRPTAESRSGFVEAHGCGVQILCRGDVALEMGLPVYGIIAGSTMAADKVGRSVPAPGQGILTFARETGQAQLDKSSPSTNTTSRTSSVSLARRGATVSPLRASLDAWGLTIDDLDVASLHGTSTKANDLNEPEVICKQMDHLGRTPGRPLWAICQKSVTGHPKAPAAAWMLNGCLQVMDSRTIPANRNADNVDPALQTATHLCFPTRPVRVQDVRAFILTSFGFGQKGGQVVGVAPKYFFATLDEEVYKDYSVRVTKRSKTADRAYAKALMSNAIVKVQDHSPYEQEDQSRIFMDPLSRITEDAETGSYHFDTKDIRNVADVKARLTRLVRGERLNARPDAASGLAQAARSAQAWIEKQTGGRSSVDTSTVGIDLVDLSAFSAHENETFIERNFTEQEKAFAKQSLDQKMAFASRWAAKEAVFKCLHTQTKGAGAAMKDIEIVKSDNAPKVKLHNDCIKAGRKAGLEDIQLSISHGEDCLIAVAIGIAGNGPAKYTL | 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:0000287] | 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, ChEBI:CHEBI:83139; EC=2.3.1.86; Evidence={ECO:0000250|UniProtKB:P19097}; CATALYTIC ACTIVITY: Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651; EC=2.3.1.41; Evidence={ECO:0000255|PROSITE-ProRule:PRU10022}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100; Evidence={ECO:0000250|UniProtKB:P19097}; | 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 step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits hexA and hexB, as well as the polyketide synthase pksA (PubMed:16649078, PubMed:23207690). PksA combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR (By similarity). The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by the fungal fatty acid synthase hexA/hexB (By similarity). The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase nor1, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin (PubMed:23207690). The cytochrome P450 monooxygenase avnA then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN) (PubMed:23207690). The next step is performed by adhA that transforms HAVN to averufin (AVF) (PubMed:23207690). Averufin might then be converted to hydroxyversicolorone by cypX and avfA (PubMed:23207690). Hydroxyversicolorone is further converted versiconal hemiacetal acetate (VHA) by moxY (PubMed:23207690). VHA is then the substrate for the versiconal hemiacetal acetate esterase est1 to yield versiconal (VAL) (PubMed:23207690). Versicolorin B synthase vbsA then converts VAL to versicolorin B (VERB) by closing the bisfuran ring (PubMed:16649078, PubMed:23207690). Then, the activity of the versicolorin B desaturase verB leads to versicolorin A (VERA) (PubMed:23207690). DotB, a predicted chloroperoxidase, may perform epoxidation of the A-ring of VERA (PubMed:23207690). Alternatively, a cytochrome P450, such as cypX or avnA could catalyze this step (PubMed:23207690). It is also possible that another, uncharacterized, cytochrome P450 enzyme is responsible for this step (PubMed:23207690). Opening of the epoxide could potentially be achieved by the epoxide hydrolase epoA (PubMed:23207690). However, epoA seems not to be required for DOTH biosynthesis, but other epoxide hydrolases may have the ability to complement this hydrolysis (PubMed:23207690). Alternatively, opening of the epoxide ring could be achieved non-enzymatically (PubMed:23207690). The next step is the deoxygenation of ring A to yield the 5,8-dihydroxyanthraquinone which is most likely catalyzed by the NADPH dehydrogenase encoded by ver1 (PubMed:23207690). The last stages of DOTH biosynthesis are proposed to involve hydroxylation of the bisfuran (PubMed:23207690). OrdB and norB might have oxidative roles here (PubMed:23207690). An alternative possibility is that cytochrome P450 monoogenases such as avnA and cypX might perform these steps in addition to previously proposed steps (PubMed:23207690). {ECO:0000250|UniProtKB:Q12437, ECO:0000269|PubMed:12039746, ECO:0000269|PubMed:16649078, ECO:0000303|PubMed:22069571, ECO:0000305|PubMed:17683963, ECO:0000305|PubMed:23207690, ECO:0000305|PubMed:23448391}. | Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight fungus) (Mycosphaerella pini) |
M3TYT0 | ROCK2_PIG | MSRPPPTGKMPGAPEAVSGDGAGASRQRKLEALIRDPRSPINVESLLDGLNSLVLDLDFPALRKNKNIDNFLNRYEKIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKHGHLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLCFPEDAEISKHAKNLICAFLTDREVRLGRNGVEEIKQHPFFKNDQWNWDNIRETAAPVVPELSSDIDSSNFDDIEDDKGDVETFPIPKAFVGNQLPFIGFTYYRENLLLSDSPSCKENDSIQIRKNEESQEIQKKLYTLEEHLSTEIQAKEELEQKCKSVNTRLEKVAKELEEEIALRKNVESALRQLEREKALLQHKNAEYQRKADHEADKKRNLENDVNSLKDQLEDLKKRNQNSQISTEKVNQLQRQLDETNALLRTESDTAARLRKTQAESSKQIQQLESNNRDLQDKNCLLETAKLKLEKDFINLQSVLESERRDRTHGSEIINDLQGRISGLEEDLKNGKILLTKVEMEKRQLQERFTDLEKEKNNMEIDMTYQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSILDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMSLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLCKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDTTIASLEETNRTLTSDVANLANEKEELNNKLKDAQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDMRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHIGLDSSSIGSGPGDAEADDGFPESRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKLFHVRPVTQTDVYRADAKEIPRIFQILYANEGESKKEQEFPVEPVGEKSNCICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYDISSAKNLLLLANSTEEQQKWVSRLVKKIPKKPPAPDPFARSSPRTSMKIQQNQSIRRPSRQLAANKPS | 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 biomineral tissue development [GO:0070168]; phosphorylation [GO:0016310]; positive regulation of centrosome duplication [GO:0010825]; positive regulation of protein localization to nucleus [GO:1900182]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell junction assembly [GO:1901888]; regulation of circadian rhythm [GO:0042752]; Rho protein signal transduction [GO:0007266]; rhythmic process [GO:0048511]; smooth muscle contraction [GO:0006939] | 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 and membrane blebbing (By similarity). {ECO:0000250}. | 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-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; | 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, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1-p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus. Plays an important role in generating the circadian rhythm of the aortic myofilament Ca(2+) sensitivity and vascular contractility by modulating the myosin light chain phosphorylation. {ECO:0000269|PubMed:23172836}. | Sus scrofa (Pig) |
M3W955 | APOA4_FELCA | MFLRAVVLTLALVAVTGARAEVSPDQVATVVWDYFSQLSNNAKEAVEHLQQSELTQQLNALFQDKLGQVNTYADNLQKKLVPFATELHERLTKDSEKLKEEIRKELEELRARLLPHANEVSQKIGDNVRELQQRLGPYADELRTQVNTHAEHLRRHLTSHAQRMEAVLRENVDNLQSSLTPYADEFKAKIDQNIEELKGHLTPYADELKVKIDQNVEELRRSLAPYAQDVQEKLNHQLEGLAFQMKKNAEELKAKITANADELRQRLAPVAEDVRSKLRDNAKGLQESLAQLNSHLDRQVEEFRRNLGPYGDTFNRALVQQVEELRQKLGPYAGGMEDHLSFLEKDLRDKVNSFFITLKEKENQDRPLALPEQEQAPGPLES | 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 biosynthetic process [GO:0045723]; positive regulation of triglyceride catabolic process [GO:0010898]; regulation of intestinal cholesterol absorption [GO:0030300]; reverse cholesterol transport [GO:0043691]; triglyceride homeostasis [GO:0070328]; very-low-density lipoprotein particle remodeling [GO:0034372] | 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]; positive regulation of protein phosphorylation [GO:0001934]; regulation of cell migration [GO:0030334] | 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 regression phase (By similarity). {ECO:0000250|UniProtKB:P12034, ECO:0000250|UniProtKB:Q20FD0}. | Felis catus (Cat) (Felis silvestris catus) |
M3XFH7 | AMPQ_FELCA | MGPPSSSGFYVSRAVALLLAALAAALLLALAVLAALYGRCARVQPSDLHHSGVPDAASSPRGTQEEPLPTWPPRPTREPAGTATPGHWRPPGPWDQLRLPPWLVPLHYELELWPRLRPNEFQSPTLSFTGRVNITVRCAAATARLLLHSLFLDCESAEVRGPLSSGPRDGALGRVPVDDVWFAFDMQYMVLELGATLQPGSRYELQLSFSGLVYRDLREGLFFSIYTDQGERRALLASQMEPTFARSVFPCFDEPALKATFNITIIHHPSYGALSNMPKLGQSEKRDVNGSVWTVTTFSTTPHMPTYLVALAICDYDHVSRTERGQEIRIWARKDAIANGNAAFALNITGPIFSFLEDLFNISYPLPKTDIIALPTFDNSAMENWGLLIFDESLLLMQPNDQVTDKKAVISFILSHEIGHQWFGNLVTMNWWNDIWLKEGFASYFEFGVINYFNPKFRRNEVFFSNILHHVLSEDHALVSRAVSLKVENFTETSEINELFDLFTYNKGASLARMLSSFLNENVFISALKSYLKTFSYSNAEQDDLWRHFQMVVDNQSKILLPAPVKSIMDRWTHQSGFPVITLNVSTGAMKQEPFYLGKVQNQTLLTHNDTWIVPILWIKNGITQSLVWLDKSSEIFPEMQVSDSDHDWVILNLNMTGYYRVNYDKVGWKKLKQQLEKDPKAIPVIHRLQMIDDAFSLSKNNYVEIETALDLTKYLAEEDEIIVWYAVLVNLVTKDLVFDVNNYDMYPLLKKYLLKRLISIWNMYSTVIRENVAALQDDYLALVALEKLFETACWLGLEDCLQLSRELFKNWTNHPENEIPYPIKSVVLCYGVAFGSDEEWDFLLNMYSNKTKEEERIQLTYAMSCSKDPWILHRYLEYAVTAAPFTFNETNIMEVVAESEVGRYIVKDFLINNWQAVSERYGTQSLVNLMYIIGRTISTDLQITELQQFFGNMLEEHQKLTVRAKLQTIKNKNLENKKRNARMTAWLRKNT | 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 at or before hair follicle development (PubMed:22997338). {ECO:0000250|UniProtKB:Q6Q4G3, ECO:0000269|PubMed:22997338}. | Felis catus (Cat) (Felis silvestris catus) |
M4DUF2 | ASO_BRARP | MGMWWIVAVAILAHTASAAVREYAWEVEYKFGWPDCKEGMVMAVNGQFPGPTIHALAGDTIVVHLTNKLATEGLVIHWHGIRQLGSPWADGAAGVTQCAISPGETFTYNFTVDKPGTHFYHGHYGMQRSAGLYGSLIIDVAKGKKEPLRYDGEFNLLLSDWWHEDVLSQEIGLSSRPMRWIGEAQSILINGRGQFNCSLAAQFSSTSLPTCTFKEGDQCAPQRLHVEPNKTYRIRLASSTALASLNFAVQGHKLVVVEADGNYITPFTTDDIDIYSGETYSVLLTTDQDPSQNYYITAGVRGRKPNTPPALTVLNYVTAPSSQLPTSPPPETPRWNDFDRSKNFSKKIFAAMGSPSPPETFDERLILLNTQNLIEGFTKWAINNVSLAVPGTPYLGSVKYNLRTGFNRSSPPKDYPVDYDIMTPPRNRNAKQGNVSCVFPFNVTVDVILQNANGLNANASEIHPWHLHGHDFWVLGYGEGKFKPGVDEKTYNLKNPPLRNTVALYPYGWTALRFVTDNPGVWFFHCHIEPHLHMGMGVVFAEGLNRIGKVPDEALGCGLTKQFLMNRNNP | 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 incompatible Turnip mosaic virus (TuMV strain UK1) by preventing jasmonic acid (JA)- dependent accumulation of ascorbic acid (AsA, AS) and dehydroascobic acid (DHA) (PubMed:27255930). {ECO:0000250|UniProtKB:Q8LPL3, ECO:0000269|PubMed:27255930}. | Brassica rapa subsp. pekinensis (Chinese cabbage) (Brassica pekinensis) |
M4GGR9 | LYR_PROMI | MSLGIRYLALLPLFVITACQQPVNYNPPATQVAQVQPAIVNNSWIEISRSALDFNVKKVQSLLGKQSSLCAVLKGDAYGHDLSLVAPIMIENNVKCIGVTNNQELKEVRDLGFKGRLMRVRNATEQEMAQATNYNVEELIGDLDMAKRLDAIAKQQNKVIPIHLALNSGGMSRNGLEVDNKSGLEKAKQISQLANLKVVGIMSHYPEEDANKVREDLARFKQQSQQVLEVMGLERNNVTLHMANTFATITVPESWLDMVRVGGIFYGDTIASTDYKRVMTFKSNIASINYYPKGNTVGYDRTYTLKRDSVLANIPVGYADGYRRVFSNAGHALIAGQRVPVLGKTSMNTVIVDITSLNNIKPGDEVVFFGKQGNSEITAEEIEDISGALFTEMSILWGATNQRVLVD | 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|PubMed:23118975, ECO:0000269|Ref.1}; | 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|PubMed:23118975, ECO:0000269|Ref.1}. | Proteus mirabilis |
M4IQQ5 | CCL4_HUMLU | MEDLKPRPASSSPLTPLGFLERAATVYGDCTSVVYDAVSYTWSQTHRRCLCLASSIASLGIENGHVVSVLAPNVPQMYELHFAVPMAGAILNAVNLRLDARTISILLHHSESKLIFVDHLSRDLILEAIALFPKQAPVPRLVFMADESESGNSSELGKEFFCSYKDLIDRGDPDFKWVMPKSEWDPMILNYTSGTTSSPKGVVHCHRGIFIMTVDSLIDWGVPKQPVYLWTLPMFHANGWSYPWGMAAVGGTNICLRKFDSEIIYDMIKRHGVTHMCGAPVVLNMLSNAPGSEPLKTTVQIMTAGAPPPSAVLFRTESLGFAVSHGYGLTETAGLVVSCAWKKEWNHLPATERARLKSRQGVGTVMQTKIDVVDPVTGAAVKRDGSTLGEVVLRGGSVMLGYLKDPEGTAKSMTADGWFYTGDVGVMHPDGYLEIKDRSKDVIISGGENLSSVEVESILYSHPDILEAAVVARPDEFWGETPCAFVSLKKGLTKKPTEKEIVEYCRSKLPRYMVPKTVVFKEELPKTSTGKVQKFILRDMARGMGSATAGASRSRM | 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; Xref=Rhea:RHEA:46177; Evidence={ECO:0000269|PubMed:23300257}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA; Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:456215; EC=6.2.1.17; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374; Evidence={ECO:0000269|PubMed:23300257}; CATALYTIC ACTIVITY: Reaction=ATP + butanoate + CoA = AMP + butanoyl-CoA + diphosphate; Xref=Rhea:RHEA:46172, ChEBI:CHEBI:17968, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173; Evidence={ECO:0000269|PubMed:23300257}; CATALYTIC ACTIVITY: Reaction=2-methylbutanoate + ATP + CoA = 2-methylbutanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:46180, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:48946, ChEBI:CHEBI:57287, ChEBI:CHEBI:57336, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46181; Evidence={ECO:0000269|PubMed:23300257}; | 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 10.5 min(-1) with 2-methylbutanoate as substrate (PubMed:23300257). kcat is 167 min(-1) with CoA as substrate (PubMed:23300257). {ECO:0000269|PubMed:23300257}; | 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-methylbutanoyl-CoA, respectively (PubMed:23300257). Can also use propanoate and butanoate as substrates with a lower efficiency (PubMed:23300257). {ECO:0000269|PubMed:23300257, ECO:0000305|PubMed:30468448}. | Humulus lupulus (European hop) |
M4IRL4 | CCL2_HUMLU | MDNYRRLHTPVALCVASPPAPPTTSWKSMEGLVQCSANHVPLSPITFLERSSKAYRDNTSLVYGSVRYTWAQTHHRCLKLASALTTHLGISPGDVVATFSYNLPEIYELHFAVPMAGGILCTLNARNDSAMVSTLLAHSEAKLIFVEPQLLETARAALDLLAQKDIKPPTLVLLTDSESFTSSSYDHYNHLLANGSDDFEIRRPKNEWDPISINYTSGTTARPKAVVYSHRGAYLNSIATVLLHGMGTTSVYLWSVPMFHCNGWCFPWGAAAQGATNICIRKVSPKAIFDNIHLHKVTHFGAAPTVLNMIVNSPEGNLHTPLPHKVEVMTGGSPPPPKVIARMEEMGFQVNHIYGLTETCGPAANCVCKPEWDALQPEERYALKARQGLNHLAMEEMDVRDPVTMESVRADGATIGEVMFRGNTVMSGYFKDLKATEEAFEGGWFRSGDLGVKHEDGYIQLKDRKKDVVISGGENISTVEVETVLYSHEAVLEAAVVARPDKLWGETPCAFVTLKEGFDNDVSADQIIKFCRDRLPHYMAPKTVVFEELPKTSTGKIQKYILKEKAMAMGSLS | 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; Xref=Rhea:RHEA:46185; Evidence={ECO:0000269|PubMed:23300257}; CATALYTIC ACTIVITY: Reaction=ATP + butanoate + CoA = AMP + butanoyl-CoA + diphosphate; Xref=Rhea:RHEA:46172, ChEBI:CHEBI:17968, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173; Evidence={ECO:0000269|PubMed:23300257}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA; Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741; Evidence={ECO:0000269|PubMed:23300257}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + pentanoate = AMP + diphosphate + pentanoyl-CoA; Xref=Rhea:RHEA:46168, ChEBI:CHEBI:30616, ChEBI:CHEBI:31011, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57389, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46169; Evidence={ECO:0000269|PubMed:23300257}; CATALYTIC ACTIVITY: Reaction=3-methylpentanoate + ATP + CoA = 3-methylpentanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:66992, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:167610, ChEBI:CHEBI:167613, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66993; Evidence={ECO:0000269|PubMed:23300257}; CATALYTIC ACTIVITY: Reaction=4-methylpentanoate + ATP + CoA = 4-methylpentanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:66988, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:74904, ChEBI:CHEBI:131445, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66989; Evidence={ECO:0000269|PubMed:23300257}; | 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:23300257}; | 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, 3-methylpentanoate and 4-methylpentanoate as substrates with a lower efficiency (PubMed:23300257). {ECO:0000269|PubMed:23300257, ECO:0000305|PubMed:30468448}. | Humulus lupulus (European hop) |
M4IS88 | CCL3_HUMLU | MGMVGRDIDDLPKNAANYTALTPLWFLERAATVHPTRTSVIHGSRHYTWLQTYHRCRQFASALNNHSIGLGSTVAVIAPNVPALYEAHFAVPMAGAVVNCVNIRLNASTIAFLLGHSSAAAVMVDQEFFSLAEEALKILAQESKSHYKPPLLVVIGDESCDPKTLEYALKTGAIEYEKFLEGGDPEFDWKPPEDEWQSISLGYTSGTTASPKGVVLSHRGAYLMSLSASVVWGINEGAIYLWTLPMFHCNGWCYTWGMAAFCGTNICLRQVTAKGVYSAIAKYGVTHFCAAPVVLNTIVNAPPEEAIIPLPHLVHVMTAGAAPPPSVLFAMSEKGFKVAHTYGLSETYGPSTICAWKPEWDSLPPIKQARLNARQGVRYIALEGLDVVDTKTMKPVPADGTTMGEIVMRGNAVMKGYLKNPKANEESFADGWFHSGDLAVKHPDGYIEIKDRSKDIIISGGENISSLEVENTLYLHPAVLEVSVVARPDERWGESPCAFVTLKPNIDKSNEQVLAEDIIKFCKSKMPAYWVPKSVVFGPLPKTATGKIQKHVLRAKAKEMGALKKSNL | 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:RHEA:23177; Evidence={ECO:0000269|PubMed:23300257}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA; Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:456215; EC=6.2.1.17; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374; Evidence={ECO:0000269|PubMed:23300257}; CATALYTIC ACTIVITY: Reaction=ATP + butanoate + CoA = AMP + butanoyl-CoA + diphosphate; Xref=Rhea:RHEA:46172, ChEBI:CHEBI:17968, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173; Evidence={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; Xref=Rhea:RHEA:46185; Evidence={ECO:0000269|PubMed:23300257}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + pentanoate = AMP + diphosphate + pentanoyl-CoA; Xref=Rhea:RHEA:46168, ChEBI:CHEBI:30616, ChEBI:CHEBI:31011, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57389, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46169; Evidence={ECO:0000269|PubMed:23300257}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA; Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741; Evidence={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; Xref=Rhea:RHEA:46177; Evidence={ECO:0000269|PubMed:23300257}; CATALYTIC ACTIVITY: Reaction=2-methylbutanoate + ATP + CoA = 2-methylbutanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:46180, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:48946, ChEBI:CHEBI:57287, ChEBI:CHEBI:57336, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46181; Evidence={ECO:0000269|PubMed:23300257}; CATALYTIC ACTIVITY: Reaction=2-methylpentanoate + ATP + CoA = 2-methylpentanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:66996, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:167611, ChEBI:CHEBI:167615, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66997; Evidence={ECO:0000269|PubMed:23300257}; CATALYTIC ACTIVITY: Reaction=3-methylpentanoate + ATP + CoA = 3-methylpentanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:66992, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:167610, ChEBI:CHEBI:167613, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66993; Evidence={ECO:0000269|PubMed:23300257}; CATALYTIC ACTIVITY: Reaction=4-methylpentanoate + ATP + CoA = 4-methylpentanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:66988, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:74904, ChEBI:CHEBI:131445, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66989; Evidence={ECO:0000269|PubMed:23300257}; | 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), acetate, butanoate, isovalerate, pentanoate, hexanoate, 2-methylbutanoate, 2-methylpentanoate, 3-methylpentanoate and 4-methylpentanoate as substrates with a lower efficiency (PubMed:23300257). Triggers the formation of very short chain acyl-CoAs from the corresponding fatty acids, including acetic acid, propanoic acid, butyric acid and its isomer (PubMed:23300257). {ECO:0000269|PubMed:23300257, ECO:0000305|PubMed:30468448}. | Humulus lupulus (European hop) |
M4QN28 | WBDA_ECOLX | MHILIDVQGYQSESKVRGIGRSTPAMSRAIIENAGEHRVSILINGMYPIDNINDVKMAYRDLLTDEDMFIFSAVAPTAYRHIENHGRSKAAQAARDIAIANIAPDIVYVISFFEGHSDSYTVSIPADNVPWKTVCVCHDLIPLLNKERYLGDPNFREFYMNKLAEFERADAIFAISQSAAQEVIEYTDIASDRVLNISSAVGEEFAVIDYSAERIQSLKDKYSLPDEFILSLAMIEPRKNIEALIHAYSLLPAELQQRYPMVLAYKVQPEQLERILRLAESYGLSRSQLIFTGFLTDDDLIALYNLCKLFVFPSLHEGFGLPPLEAMRCGAATLGSNITSLPEVIGWEDAMFNPHDVQDIRRVMEKALTDEAFYRELKAHALAQSAKFSWANTAHLAIEGFTRLLQSSQETDAGQAESVTASRLQMMQKIDALSEVDRLGLAWAVARNSFKRHTRKLLVDISVLAQHDAKTGIQRVSRSILSELLKSGVPGYEVSAVYYTPGECYRYANQYLSSHFPGEFGADEPVLFSKDDVLIATDLTAHLFPELVTQIDSMRAAGAFACFVVHDILPLRRPEWSIEGIQRDFPIWLSCLAEHADRLICVSASVAEDVKAWIAENRHWVKPNPLQTVSNFHLGADLDASVPSTGMPDNAQALLAAMAAAPSFIMVGTMEPRKGHAQTLAAFEELWREGKDYNLFIVGKQGWNVDSLCEKLRHHPQLNKKLFWLQNISDEFLAELYARSRALIFASQGEGFGLPLIEAAQKKLPVIIRDIPVFKEIAQEHAWYFSGEAPSDIAKAVEEWLALYEQNAHPRSENINWLTWKQSAEFLLKNLPIIAPAAKQ | 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-(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 + 2 H(+); Xref=Rhea:RHEA:13789, Rhea:RHEA-COMP:9558, Rhea:RHEA-COMP:14053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:74010, ChEBI:CHEBI:138439; EC=2.4.1.371; Evidence={ECO:0000269|PubMed:22875852, ECO:0000269|PubMed:22989876, ECO:0000269|PubMed:25422321}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13790; Evidence={ECO:0000269|PubMed:22875852, ECO:0000269|PubMed:22989876, ECO:0000269|PubMed:25422321}; CATALYTIC ACTIVITY: Reaction=alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[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->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)](n+1)-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 + 2 H(+); Xref=Rhea:RHEA:54980, Rhea:RHEA-COMP:9558, Rhea:RHEA-COMP:14055, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:74010, ChEBI:CHEBI:138439; EC=2.4.1.371; Evidence={ECO:0000269|PubMed:22875852, ECO:0000269|PubMed:22989876, ECO:0000269|PubMed:25422321}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54981; Evidence={ECO:0000269|PubMed:22875852, ECO:0000269|PubMed:22989876, ECO:0000269|PubMed:25422321}; | 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 mannopyranose residues (PubMed:22875852, PubMed:22989876, PubMed:25422321). Extension is terminated by the action of the chain terminator bifunctional methyltransferase/kinase WbdD (PubMed:19734145). {ECO:0000269|PubMed:19734145, ECO:0000269|PubMed:22875852, ECO:0000269|PubMed:22989876, ECO:0000269|PubMed:25422321}. | Escherichia coli |
M5A7P9 | SL9A3_TRISC | MGRNRSGCVARCVSLTALVLLLCCPVVRSSEAETDPDSHTEHGDSHGGSREGNDTGFQIVTFRWEHVQTPYVIALWILVASLGKIVFHLSEKVTSVVPESALLIVLGLILGGIVWAADHSASFTLTPTVFFFYLLPPIVLDAGYFMPNRHFFGNLGTILTYAVIGTVWNAATTGLSLYGVFLLGLMGDLKAGLLEFLLFGSLIAAVDPVAVLAVFEEVHVNEVLFIIVFGESLLNDAVTVVLYNVFNSFVEVGAGNVQGLDYFKGIVSFFVVSLGGTAVGIIFAFILSLVTRFTKHVRVIEPGFVFVISYLSYLTADMLSLSAILAITFCGICCQKYVKANLCEQSITTVRYAMKMLASGAETIIFMFLGISAVNPTIWTWNTAFILLTLVFISVYRVIGVVIQTWILNHYRVVQLEIIDQVVMSYGGLRGAVAFALVVLLDSNYVGERRLFVSTTIIVVYFTVIFQGLTIKPLVKWLKVKRSQHKEPLLNEKLHGRAFDHILSAIEDISGQIGHNYLRDKWTNFDRKYLSKIMMRKSAQISRDKILSVFRELNLKDAISYVSEGERKGSLAFIRSSSDVNVDFTGPRHSVVDSSVSAVLRESTSEVCLDMHAVENRAKSPKDREEIVTHHMLQQHLYKPRKRYRLNYSRHKLARSEGEKQDKEIFQRTMKKRLENFKPTKLGTNYTTKFRNMKKERAAKKKHSDAVPNGRLATHSVSFHVNKDSEVEDPADGGISFLITPASNDADETGTGIDNPSFSNEEDQSIYQMIPPWISNEETVIPSQRARLQIPRSPTNFRRLTPLQLSNRSIDAFLLADISDEHPLSFLPESSM | 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 protein {ECO:0000250|UniProtKB:P48764}. Early endosome membrane {ECO:0000250|UniProtKB:P48764}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P48764}. Note=In intestinal epithelial cells, localizes to the ileal brush border. Phosphorylation at Ser-663 by SGK1 is associated with increased abundance at the cell membrane. Angiotensin-2 enhances apical expression (By similarity). {ECO:0000250|UniProtKB:Q28362}. | 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 and blood pressure regulation. {ECO:0000250|UniProtKB:P48764}. | Triakis scyllium (Banded houndshark) (Hemigaleus pingi) |
M5AAG8 | POL_BPNNR | MIMEIPAIKALSRYAQWVIWKKERDTKIPYNPNNGKKASSTDPLAWGDIDEAQAGLVRYGANGLGFVLTKSDPFVFIDLDHVLDENKRVKCEWARQLLKEIKSYTEISPSGDGLHVVVSGKLPDYIKHKTKFDDGSALEVYESGRYMTITGEVFDGRDDIKELDLSILGEFAEHKIETKNAPVQIESATTLDDEAIIDLMKRKGQWPDAPKDGDDWSSLDMSFANRLAFWCGKDIERMDRIFRQSPLMRQKWDRPTAGSTYGRITLKKACDFVDSVYDPALRNESDCPFEPYNEEGGPRNDKEEKDPLWLYKVLLTKGIEVWFDIKLEKYGIKRNNRVDYIAKSSLQQIVFEIIGKTPKNIAVPTYIGAYEPSKPEKWEEEGIKYINLFKPTPLMKVKPVKEMPEIVKNLLLNLFDYDAKSMGLFINWLAFIYQYKERTGVAWIFMGKQGTGKGLLVDLLKKIFEEHMSSNITDANLDSQFNPYLYNKLIVHLNEVSADNRKSRMLVKNRLKTWITDETLYINRKNMKEVEIKNFCNFIINSNETIPVDIEDSDRRFNVIECNNVLKEQEWWTTESYQEILNNAEGFAKYLAGIKVDRSKVNEVVMSEKKKAIVETTESVLKQIAKALTDRDIEWFLDNGLEGVVEKNIVNDFQWEELQEAITTGVIPNKYLMIIVEQILGDSKTITWIKRNIITPYQVGETTVVKMAGKPIRAIVVG | 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 ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000269|PubMed:32016421}; | 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 | MADSGGPGSKHMDPTTIDAGGGGAGAAGGDDVPPVPAVRRRRAHEQKSSREQVLEEEKSQQLETSTVTRTYMKTITTSLTTSSSSNVEEFILGEHAAGAAAAPSPNQQRLRQKVAQYEKVWSDGSSPVKRPAEQSSDELRLTDDQDEYDAENPFEIDVHEIERRLRQERQRGLAEAEAAKLAFQQVQLRHTTPPRRVEVTSDQVASPFNVTLRTTSRMSPGAEHGNVEEHLAPFNVTLRTTRRTKKKEFKELENFLEGERTVREVPSADGVRTIITSSMTSDGGYAEEKIYRHGEGYVSPRDSPSWSRSSYSSERSSVTPPRSVDLTAGGRRILIKLEQESELTEENQTRDETDLSFGRQEVAMATGNIDITVGGSNPRRRLYQQTTVQVGGGNRTSPQDSTPQRPRDLDLAGTTKTMLTSTPIGTKEQPQTGPKTLVSPAATCQLRGSSTEEPRKIVSHKTITSTTTKSTSSSTSATSSSSTSRKLIETSPVVVGKIAQIRTGKSNASDNDIDIDNDSDTEGRPASSIVIVSTPTRPTTPATASVSASAVTPSASISATAAHALSGIGTFSKSLRQDYQTLATQSGRSNESPSDQEYQEFQSTMASINYARSNSQYDSHIKEKREEQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTIILYFQIEENSRNLEYLGHGIGGSVSSLDSVGNQKHGDLKAEKWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDVDVPKPDEKSIMTYVAQFLHKYPEPKGASRDQSHVQQEADELRRFLVEKTTEYEPMVMMSSFPRDFGEYLLARSEVDAHLAAYNRLKQLIESQSGFLQVSRQSWEEINELWQRLQYQMMYWLWLLDSELPGDFGTVGKWLAEAEKLLMDNDIPNAMNEETAAVISRKLEEHKLFFADLPRILAMFDNAKRSPVAQQIPLEQLRNMERRLQEVGPKAAERRIRLKFLEHKCCLIAFLNLVENKMRGWTGKYGHEEKVAQQLEQYKNFVSRNKIFQEFQKAFVDMQQVVEEYKRDGNVPRKEINDIDRFMYETEERWKRVSMELKCCQNSLEEVVNCWRSWNQLAPTCEEWLQLAEQKVNQSEDERLDFFQDIPVWKDKFDALASSANYLIASCEEPIAQQLRQRHGALSERFERLFANTKQYMHAGDIIRSRQEYKSGIEQLSRWLRGAESVLDQRQVLGNSEQVKEYGQQLQQLASEIDDNEELFKTISRNFQSLIQDLSRDEVDKMMKLLKQEKESLVRIRAQLPAKLHLFHQLQIQQESLEAGQKEIHQWLSEAEQLLGTHNLSGGRDAINEQLHKHKTYFSRTVYYRSMLESKNKVFQNLLKAVSSDDKIDTAPASQQMQQLNERFNYVIQNAQQWEQRLDSAAGGWSNFKDNERVVSEWLTQAESMLVEKHIESKTTIETQKYFFEQVNDRWMNDLVQSAQQLLTTLPAQEQPAVVHSVEQLQSRWKNVLSQAPLHLLKLEFRLDENAFYQSLKDVEKELQLEQQALNRNEDVDSILQRNQQFLLQQDVVPRLERCLQNMQRLAQAHRQQQPGDISLDQAYDNAKSQWQLLSNKLGDMRQTLQQIPAQWQGYHLKFNDMVDWMNGVDQSLKNIVNEVNTMEEFEKEKVVFQKICQDADNKREDMKWLVKTLDSLLSYATEDEANLEQKKLEDLIARYKNLIPTIEITMVKTEVFSKCYTYRREVHEVVCLLSKVKDQTANIPAPDSLDRVNRLIEEQQYAINQLDHQRPHIMSMLQRGRDLIKDVHAPAFVNAEVKNLETGWNQAYTETSDKLQALKGTQAVWSEFVDQKNDIFSMLQTAETELRSLTPLQTDPKNVSQDLKSKRDLNVQLQQASHQLLPKLHALKSELAPLAAPDKRPILEKEVTEVEKMFFNTMEHVKDRVGYLEDYSAKWNNYKTRLAELQEWANKVAPKNIEALQSEDLTPEERVVKVQAFKRILGDRMKQLDLLAADASELAPKEGNIAEAKRLKGEITKLQEVLSAINRNVDHQAQAVQEDLVNWQQFQAGLQQIKPAVEQSEVKVNNVVSKPISLEEAVAMQQNAQQFETQCQEQLDKLHGISNISHKMLCKTNAPDELDAMHSRWTAVHENAKQASAKLEKLVANWKSFDADAAKLEDWVGQGEQQMSRRPAVLNTPHIDKLEKELVKLKSFNNEISQQQAKLVTLGQNADQISLHLAPEGAAALKDRVNQMKGKLQKLSEATRGHINEVSDAIISRQDFNAKLVNFSNWMEQLRNQVTQVEEINPERVETSLHVIHALLQEHADKKPSFNAIYDEVKQLALGATPEESNALNDAYTALVVNYQNLETNMLQKKAALEKWTELLGWKNDTESHLNYLKHQLDKPEGPAAEELSKVIDEIDNLGQGIGYWKGQAKEIDENPAIQLRDALSRRPLIATQIVNDVENKLENLKLRSQSQQQQIQQMTVRKDKFHALEHNFGQALQENRAKLDEILRQHPTLNNIDQIIADLVALNDALKYQADLKNRIHDEGSLLMREDIASMPAIQESLLIMDKNYDSLQNEIADRIQKYNLISQALREYADSKDKFSKELKKAEDLYNAIPQQPRDETELHQASEKTRKTMEQLRKSKLSLDELERRGNNVGKLFSAIGEPIPQEVPQEVTAAKQHWQDLHDKTAKNAHVYETEAVIWSQIEDAKKDLLPWLSETNQGLCDAADNSIEIEFGPMRLSKYRTELPSYQALKDSIVEKTNDLVKINKGAEIPALSALNKLLSEQFAEVNNNADRLSAITTSFNDQEQELRRRSKEAGERVSKLREQLIKCDDMSGDNNKIMERLQQCRALRGELDNSGNEIDNIKQKVDELRNLYPTFSESIIPKELNNVQKRYENVDLYAKKIESSLLQFLKKFHADKVGMLKRIIATQREKVAWCQPESSSDKYNLDVKKSSLQEVSKSIDDCKARHAETLKSLEMLKAVESPQNLAELTSDAELLRKDMQALQDSFDQIKGILDENVDLWSQYEQSNEQISNWLRDVEGRVKAETSSQVNLSEVPQKLQELSILQQDVLAHEPIINNLEQTSQQLIEKNPEARIGQFVTHLVQRYQAVSKALTSYIDKIRGAQLSNANFAKAAKDFNEWFGDAKIEFQELARMGSPGSSSATAQQLQTVKNYIKTFDNGQILLNNAVDIGEALYPVVSPDNRERIRADLRQMREKFDYLRDEANAFMQQVEGVLIQKTSIEESYTQVSHYLNESKAKVPTTDELYPTLATKKAALQNYKTQLQEITLHKNALKQLHDKAVTLCDDESERKTDESIQEYNTLSKKISDRITTVGNHVVKHEAYDQVLEKAQDWLNTIKSEAIDILNETTFEKEGAEEKLLVVENLLQHKPEGDSIFDTCHKLLETVLTQTHPSGHPALLKGFEEPKQSWEDFMTLCQDSLVKLKQLCSKWDEFDTIIEELDNWMKNVEAVVKNQNLKSTAEAKNAHLKQLQDISKDIERRGAAINELMDQGREIEGETDLNLKLSRLNTRYQTLKNLCKESIAKYVNYVKDHESFDKDFDSFKQNLQSSVDELAKTNEIVGDQSVLQDQQNKLREMSDKRILDSTLFEGLIDRGEKLYGHTSPEGREIIRQQLRALRTLWDNYTDDLNSATQKIDQCLLQFNEFSIAQDQLTKWLKDVDKAMQSHTEPKTTLQEKRAQLQNHKLLHQEITTHNVLVDNVCDKAQILVDQIKDNSLNVYLTSIKQLFQSIVQKSDEILHNLDDCVQKHNELNNALSSAKTWISNEKAKLLECDDAYGEKADIKRKIETLGQLAQNKPQAMKIISDIRDLFEKVKATTSEKGNEVLDKEIEELETTMKSHFDDIEGIEGKQKDVLAQWDKFEKALEELTKWCRSAEAVFREQQLQSTLHEKVEQLEKYKIQRELILQKEKEIDAFGDAAHALLNNCGADRLKTLTTQITNRYQLLQVLSKEVVNRWSNLVDDHQFYQDKYNEVDLWLQPIESQMAKVLLDEPTQSSNILQVLLSEKEQAESLFAALNAAGEKALPETSTQGREKIRKDLRDIRDRWDKLDEGIRNLEKRQEAQGVQLSSYQDILNQTVNWLDQVEKLIHNENPASWTSAQEIRSKLYKYKATNQDINSHKRIVEAVNEKAAALLGSAAPANADEISKAVAEVNKRYDQVGQDCAKLVADLDGAFDVYQQFSELQKAQQDYQKNLWDRLTGYSDYSGNKAALQARLQKINEIQDALPEGVAKLKSLEDHIEQQASNIPARSKEVMARDLANLHADFEKFGASLSDVKSGLENRLQQWNDYEINLDRLITWLGEAENSLKNYNLKSSFEEKEEQLNGFQSLAQNLRQNEADFDKVKDDTSELVQSSGETRIAVNVQQVSSRFQSIQATAKEILKKCEQAVQDHGHFNDKYKQCADWLANAQARYDDCCDLSTVASRDDLLKKQVVIQELLAQQPTATQLLNSTVELGEKCYGSTATEGREAIRSQLDDLTFDQLFDNIAITARKIQDKIAKWSGFDEIADSLKSWLDETENALPADIELKTTLDEKRNKLQTYRDILNDINNHQVELGNLQEIAANLPEKTELVDQIIKDISDRFGKLQKRAQNYVERYEGIVSAHQQYSKAVMDAQEFIDATLNTVHYWGDLDLEQISLHTNLDRLKNLKASLADEFPRVDQVRALGEKVIPGTVDVGQVNIKSQIDTTQQEWESLLTTISSTIEAIEARLQHWSEYEQLRDQCLAWIRDTDNNLHAIDLKEDLPKKRAQLDALKALQGDVRAKELEVDNVTEKAQTLLKGPSSNRASGPELVTKYQQIFHKVKELNNRWQQYVTSHEDFDNAISDCSSWINEIKEKLDYCSDMSSMSPKELDKKLATIQDVILLKDEGSARVLKILEQAQHVLANTAPGGHEAINKELTDLQDLWSGIALRIMDVKSNLDDSITQWSGFLDQVQNVRKFNEWLDGQVKELSEHQTTMTEKRAQLDRVKSTEEKVRVEKIDVDALKIQAKEMIASGQQSQAAFQAQKVLDTFDELFAKTQKLLSHRQDQYRDHRLFKEAYDDLVSWIGRAREKFPSLKQSSLSDKLAIENAVQATEALLNKQAQGELLVEHLVHTGEVVLASTSAQGQEIIRNDIRALRDSFEGLFREINQQKENLEVTMVQWRAYKEEYERLMEWLQQIDILVKNHKLNLCPNLPEKEKQVADMKEVMSRLEKGKDDIDKFNASAASLLKSHLDTYVNNQLRHLSSVYQVQVNLAKDVLKKVETNRDQHREYDANMKSAKDWIANAKATIQSAGEGAGSKEALQRRLEQIQDLIRNRELGQNLVHTAINNGEKIIRNTRSDGRDAINTEMKELQTEWDRLVKKMSTAKVQLETNLLQWADYSSSYSQLQQWITDREAKLQQACEQKIVKSKRGQPGLSSGLSERKANLRQTNNIVQDIVSFEPMIQSVTSKASVLQQGAPGTEISDKYENLTKQAKDLYEKQKNTIESYQSLIDAGNEFATWLRNAKERLSKCSEPTGDKQALAEKTHQLKILQGELPEGAQKLKNALEQGEIACRSAEPEDCEIIEQEVALLQEEFDAYREALNKAKDYLEVGIVKWSDYQDQYTEALEWLSKTEALVQSYNKLQDSLIQKKVVLEQFQGHLQTLFDWQKTLDDLNMKAQVLLETCSDTRISNAIMQLTTKYNALLTLAKEVMRRLEMHYQEHQQHHSLYEECQSWIEKTREKLSECEQIPGTLNEVQIKLNTVKNLRQGFETGQNKLRYLLELKEKVIMNTEQNGAAKIQEDTEALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDVEPSVKTSDEFLNDLSEKRAALEKFRVIQRDINGHNDIVEKINQRLKEDNSLDLKDFQPGLTKFDDLQTQVNKIIESLENQVNSHEKYKQAYNELQDWLRRTRIEVEQCADCHGEKDQVESRLNRLGDIQSSSLEGKALLEACEELSQAVIATSGSEGQDNVAQEIKHLTSEWETLQTISRDARSSLESCLAAWQTFLQKFNKINLWIETMNKRVTKSQEGENKTPEDLVNAKKLLEEVLAEKDNVEDLNDNCELLMEQSACTRIRDQTIETQANYTKLLTSAQGLVAKIEKNLSDHTEFLNYKKEMDAWIEKAQQVLDDCSTDGDAAIIAQKLDTVNSLASRLPEGQHLLALVQDAYSKASNITPEDKQEKLRELMTKVREDWDALGLAVKQKLSDLKQAQNRWNDFAANKDKLEKWLNETETTLKVAPETKGELSEMKTLLERYKTLSNELKLKGNELEQLQSEARDLGTEVDAVNRLQSRCDKLKNDCSAHITALEQEMFDYNAYHQSLQDVEKWLLQISFQLMAHNSLFISNREQTQEQIKQHEALLVEIQKYQTNLDDLNAKGQAQIKRYESSTPAIRPTVESQLKNIQDSYNSLLQTSVQIKNRLLESLAKFQEYEDTLDSIMRNLETYEPIIQTELDAPATSLELAQNQLRCAQEMQNKLNNEKSRLAAAVQACEAATASISRPSSPLETAMQAIPERELIVRAKLEDLLDQKPPPKTRSSTGGVSTDDDKDEADVEIQVELSDVNEALLDPIAHERVKNYRRIVRLNSAHVGKLNELVAKVQSHLGGLTASVSELEQQQKQRAELQDWVKKQQSSVSDWMMRPCKLRPEAAQQELVSMNDLLNSIGDKRSQLMLEMTGSLGDEDTDLDDNIDKLESELMDAIAKKQAGQNVIDGYRQGMADVQNWFDTLIKRMDVLDRGSGLNCAQKMAAINEIKNEYELQGHPKIQELKGKAAQVAEVISNLDGQQVEEQMKSLDRRFADLGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNWVKQQIEELQAPKPLGYTPKDAEARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELEPVEYSQLESALRNLNTENRNLSGVLKAELDRALEASKARKSLENDLDKARQWLKTKISEVRKLPVYHPLTSAEIEKKIQENRKYDDDAKQFNDSVLTDVQRQAANIMKDCDDADKAALQQILDEIAADYQTLKDESSKRGKSLDDLLQGRKAFEDSMKNMGDWLNEMETATEGELRTTSLPVLEEQLAHYKKLLSDAENKGGLINDVSEQGKSILPTLSNADKLKLNDDIKNMKDRYGRIKNTIDDRVNALGDHIKKYKDAKSRLAECSQFLGNIQQKLRELNRPIGSRIEDVQDLLGAYEGILKELKDSKSKMGDMQMDDLPELQSILAQQDDMIKLIEDQLAHLRQLLLLREQFIALINEIIAFIMKYTDVIIDIENSPDSLEDKINKYDDVIVKIQECEGVLASANDKGQKIASEGNAADKNSITEQLQSLKNQLQNLRKAVESQRQKHQLQLESHKKMAAELSEILDWLHSHEGAAKSRPLLDRDPESVERELQKHQSLSQDIESYLNKFNKINDGVKTEIGMPSSLLEMLSEGRSLVASLPHELEEREKYLKNNRDSRLEYMQLVAKFNDWVHEAELRLQNSQHGIDYEHLVQDLDEHKIFFGNEAPIRNLVHKQIQEAADKIWSSLNNYEQSELSAELAQFQTKLTNTLANAKTQQSELEKEAERWREYQQSIDRVKATIERTKFVDEPVQNLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIRQADARNRQLIEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKSSHKEIEALSKSILTFLGEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVHVYDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAHYQAKQNQLPSDIAQEFTALELLAERVQVTMETKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELLQRINHEITAIYERFTLVKTNGQLIIENCRNSEEKTLVQTTIDQLAASLAQVRGWLDEKKQAVGDSLDAWTRFMNLYQIVMSWASEKRNFIDQTIELRTLPEARNKLNDYVTSVKSIKPIVKHLSEMDKELEHIGQVTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEACEEWDQCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQLGFCEKTLADINVQKTKLRLSIEKLEVHFRNGMGGDPRLSENVDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRLVMAPTYLPHDRERALAEQQDLITQELDELLQSLSSVEDGIANMNQSSLDGMLHGLKLIQSNLEVHERDAIELKNQAKKLPTDPATERLLNDTVDRIDLLLRRTQQGITMIANAMHGQKKRQQEIDEYQQHLLELEQWIIEVSAELASFEPTSDSSTDEQVLKSQVERSQQLLRTLKDRQQSMEDLVEQTRQLQSHPDVSPLADTLMEQLQSIITILREQVTVATKRIFTIEKRIVDLRKAKSEEAQRQRVLADSLIKPPTEAPASPEAHESIESNENTIDSSSMPEEEIKPTGVYVETQTSLSLQQPPVQVVTTTTVEAQTSFKEPAVETAEVALQTQKERSPTENIMVTQTVHHGQETIQIDTTRNKDVPDEPEDVQIEARYHQRPKGDVDRATELILKNVPQAFETTFVEPDETTTEVIVGPDGTKHIVLKKVTRTRQQVVQQQQISSIETISDSDGNIEVHSTGQINLENVHTTDTKADPEEGSVHTVITQQTRGAVVDSTQPEGVILQEFETEPTIETYEEVIAPGSQAQLIPMQPGDVQTQGTIRAVVQQVTRKVIRKTRKIIKRVVIIDGKEHITEEVVEEPEEVEITEEETAPHINVNIVRTVDGKVVSEEEFQRMMQEPGVLIEEVATDLQKPTAEPQQEVFDIESTQVTTTTRTTTATTQEQEQPEQQTQPTTTETTKEAPVELPAPQVDVEQPVVVATTSPVHVPTADVVEPKDSSPTSTTAAVVDVEAVVEDINEIWPLEHHLKPTNIDFSQHVEELAAPAAVTAETEASMPVEEIWPTSPETGNSLTLEQYEFEPQSPHEESTKSDLVKPQETEPQVVAETKPEGITTGSITITKTTTTITSSTEVPEETLVQNVPADEQQPPANKIKTDIQSFLEAEQTLAAALKEQSSTPTGASVAEDVQTQPEEIVLEERTVEISTIKTEENQQEPVIVEEVKSLPVEPEPVEPELEEVAIAIVEQTEEKPEEPVIEKQPASGPIDLRAATQLFISGEAAASTAPQKTFQISAPSLEDNGAGVLKVVLGKESTNEEDTAAPTTGKVSMTIIETAAAPAADAKRRRKKKKRRDTKHEEELEQEQETEPEPVAAVKEPEVSSDVPVSPEDSPRDTVRHESIVEISPDSDLSSIEIDTKVKIVEDAVVSSPSESPRTPMVELVIPTEVVELALVEDEEQQTTPRIPSPTEKSEVEQDIKSVQTSPQHQPKLDETAVQTSLEVQPDNQENESQTLIVEITETEAQTTPRSEEQSVAVEISTTEIQTDVSGQPAETVEISSQTTVTTTIEKELQTTPKDSPRAPEAGSSDVVESLVQDLVKDMTTDLPVRTSEQSTVTETTTTTETHVQTTTPEPREQTEVIKPETAHEETSTVELVQFADGEMQTTPPGDQQPASLDDSSLTATSISVSEPYELEVKTTVAIPADSDTSVAEPTVYEYTQTMQLPKQEKKSKKDKKKKQKNVPEVEQQLPEDQQISVTVEIAPELLSESGIVVSTNQQIEDVPHVTPVVDTPIESEEVETPKAQRVQLQITKTTVYDEYPDLPVHITEQNKVLIASQQSKRSGAGPTSSAVTIEEVGSPTEELVVPITPGPDNLSGEPHNIWFSATTSVDKTPIELSQALIMSESLQHYPGQQKLTQEPILISTKEAIGDRIKQLKQASPQQATPLSNVLHLATLSEQIKELPTEQRILEVNEGLKDLDVAIKNGDKTVIQTTVITVIEKVSTWLETIEYRVYLIRQNSNEGPSEEKLDNYNQLNDELSTIKQNVVQLERQLSKAEPEPQLLQCVDSLKEHVDAVEQVTQQNQVQDSNDLDKWHNFEVLLYNVSSVLADLQQSYDLLINQEYPLSAKLAQLDELEQQHEAAQQQLAHLCQNARAFQRDFPGKKMPQDVHNAFETSKNIANNIQAERERVLQLQSLAEEYEQTLKEFTKITVLADKLVESPIVSSSLEQLNNEVQKQRKFFVNLSHCRAMLESLEENIDSETREKHSELHKELYNRATSLLDKASERSSKLVQAASRWTVLEKGMRDELQWLQVAQQRVPDLSAVTSADYDQYTTLYQSLSNDISHHYVKMTQLSGIANKLQLLVQAPNLVEETNEALIVLLKLREEVALYLHRLLVFKEIWVQYEQQTDKLEAFVREAEQELRNIQIPSQPTHQPIEHMRQFWEIKARFELHNNVRTDTGLSFEKSLQVIPLADEMLQRQFHAQLEDRWQAVAQAIELIQHNIVECLSSEDVPADEKLKMVERELQEIYLTMTSMKGVIKNEEELCLYIERVQVLRTRVGFIGNELGRIGLQEPAIEPEKVGELFSLSHKISTQIAEELEGASVLRDQLQAIQEGISNQRKHQAKISVILDECEAAERQGADVLEKAVADCQAAGEELVISWQEIMRIRQMLHTLPMRLKMSVSPVKLERDISQLQDDHAFLESKCTNIMAILRSRLAVWLRYERQLELVHGSVQETDFMMELIRVHGQVDYERLRKATERLEGLAGDLHNREQLIDELKGAAKPLIESCDVQIVEQIESAVQEAVVAWNDTSENLQQLRTRYQRAVELWDKYRNASAAVKNSIDQQMDAVKSLEQPLDALQHAKVCQDNLTTQNDRILELRDIVAKIAADVGLDASALMQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQHVQSFLSCAIPEDYSSLREQQQLCAIHQNLLISQQSVLSETPLESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALATAMRMEQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELKECISPHDMKTIRQRNWLLWQQHADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQRLEQRVEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWLLSTSRELLTLYSEPEVRSQVQQQSDSLIDRWQRLKYLAKQKATKIGELKMTLLRLEERIALIRAWLFEVESQLDKPLNFESYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDADSWRTQVNTSGLAASAQNLEQRWKNVCSQSAERKARILTIWNLLQQLIKLTAEHKNWLGKQESQIAGFERDQKSHSKHKLEERQMELRAKLEELESQSVNLRQLEQIYAKLAMSAGVEPENIQKLTLPTKVMVSMWRQLTPRCHALLDAIDKDAKLMREFNNAQLEATNSLNAIQKALEQLPSAENQQTSKAEPKAVLQRLESLEKKLQDAQQHVQQADNLAQEAKTRTKQQPQLKQLLELVSAYTTLWQTVQTRIVTLKTTWLTRAAQAAASLPVSEAANAAVQVNTLSQRKLRQAQQMQRETSITAKDAYIMELQTAITECQNNLDELQRTVVDKTRKPGPQKIAKLLGNAQSSTELVKHLSHLLLTECKADDQAAEVDTVAELTLRFDTLQSQWKARQQHDQNASEVGRLTCPLCTQRNWQQIDNDLWRLEQWLQFAESTQKAQSAPPSNIELLEDVTQDHREFLLDLESHKSIISSLNVVGDHLATHTLDTEKARQLRSRLEADNERWNNVCINATKWQGLLQTALMGNSEFHQTIGELVEWLQRTEQNIKASEPVDLTEERSVLETKFKKFKDLRAELERCEPRVVSLQDAADQLLRSVEGSEQQSQHTYERTLSRLTDLRLRLQSLRRLSGIYIVKLGAVLGYEGDNLGVPLHMLSSELLDNTTLSTSSMQAAAPNTENANNTDGGDAVDGDVINTTVLARGARFLGRVARASLPIQALMLLLLGVATLVPHGEDYTCMFSNTFARSLEPMLSYPHGPPPT | 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 anchoring [GO:0034453]; mitochondrion localization [GO:0051646]; nuclear migration [GO:0007097]; nucleus localization [GO:0051647]; nucleus organization [GO:0006997]; ovarian nurse cell to oocyte transport [GO:0007300] | 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-disks is mediated by interaction with sls (PubMed:22927463). In the fat body, localizes to a perinuclear non-centrosomal microtubule-organizing centers (ncMTOCs) (PubMed:32066907). {ECO:0000269|PubMed:22927463, ECO:0000269|PubMed:32066907}. | 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 between a nuclear ring structure of Msp300 and the plus ends of a unique astral MT network (PubMed:22927463). In addition, is essential for anchoring nuclei, mitochondria and endoplasmic reticulum (ER) structures to the Z-disks (PubMed:22927463). In fat body cells, part of perinuclear non-centrosomal microtubule-organizing centers (ncMTOCs) which function to accommodate the organization of microtubule (MT) networks to control nuclear positioning and dynein motor-based retrograde endosomal trafficking (PubMed:32066907). Functions as the primary organizer of the ncMTOC by recruiting Patronin, shot and msps to the organizing centre (PubMed:32066907). Within the ncMTOC, Msp300 and shot anchors the ncMTOC at the nuclear surface and recruits the MT minus-end regulators Patronin and Nin for assembly, anchoring and/or stabilization of circumferential and radial MTs at the ncMTOCs (PubMed:32066907). Patronin, and perhaps Nin, recruits msps to the ncMTOC for the gamma-tubulin-independent elongation of radial MTs (PubMed:32066907). {ECO:0000250|UniProtKB:Q8NF91, ECO:0000269|PubMed:22927463, ECO:0000269|PubMed:32066907}. | Drosophila melanogaster (Fruit fly) |
M9MRI4 | TRIM9_DROME | MEDELRCPTCKQLYANPVLLPCFHALCLGCALDIQTPYSPGSALPGAVNGAGAASAAGHNGLHGNGGGAGGGAAAPVTNPNGPGTRHSSHSSAASTASSNTGSESVTSDQDQSDKVSIFSEADSGVVCCSNTSRPVSYAGTGLLPGVGNVVAPPGAAYCLTCPLCRKLVFFDDGGVRNLPTYRAMEAIVDRFCAREALRCQMCETDPKVASLICEQCEIRYCDACRELTHPARGPLAKHTLVKPRGAAQQRESVCGEHEETLSQYCLSCKAPACGLCIGELRHQAHDVQSINVTCKAQKTELSHNLQQLSEKARSTTEFIQRLKGMSDKVTESCMEFERLVHAQCEALIQAIHDRREYLLEAIRMDKDTKIRILKDQQSNCTGKLQQTTGLIQFCIEALKETDSAAFLQVGSMLINRVTNTDMTWHQEVTNAAPRVSPIVDLTLDDAALARAIDNLNFIQMRAVKDGDERCPAAPMTPTILPSDCSAENNSVTVAWQPPNHSFVEGYVLELDDGSGGEFREVYCGKETICTVDGLHFNSMYNARVKAFNSAGEGEYSELIGLQTAEVAWFTFDPVLSGGAGSGLIFSKNNATVSVEGWEHRVALGSVGFSRGVHYWEFTIDNYTADTDPAFGVARIDVARNKMLGKDEKSFAMYIDRQRSWFQHNSIHERRVEGGITTGSTIGVLLDLERHTLSFLVNEMPQGSVAFRDLYGVFYPAVSINRGVTLTMHTAMDAPKMDYF | 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]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]; regulation of axonogenesis [GO:0050770]; regulation of locomotion involved in locomotory behavior [GO:0090325] | 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 upon neuronal activity (PubMed:24746793). During eye development, consolidates the attachment of R8 photoreceptor growth cones to the target medulla layer, probably downstream of fra (PubMed:27743477). {ECO:0000250|UniProtKB:Q9C026, ECO:0000269|PubMed:21338947, ECO:0000269|PubMed:22084112, ECO:0000269|PubMed:24746793, ECO:0000269|PubMed:27743477}. | Drosophila melanogaster (Fruit fly) |
M9MSG8 | PIEZO_DROME | MVFSYACMVLQRIVVPAVLVLAALMRPVGISFVYLLMFFVSPFVPLATRRNFKGSVTAFFIILLTLSTLVLLGHITLQILAVSLTLPIYNCSFSERLLRHIGFVSFIDLQPFAIIEWLVPEVLVFATSLGSYLTVKRVASQPVGAEQLENGEVVDGQAENAQTSSQPSAADANGGDVQQATVTTPLQQQQQQLRKRVSMISQHIHFEGLVKISPLFCLATLFFAAVLRPSVPGGFYFLIFLLSGTYWATCQTLQRGFALLLRCVMVVLVLHSLSIVSYQTPWMQSHLNHTTLTARLIGLEPLIESYCSPDIRVFLYNNKLSLDSYLNPFALFFAYFALALTTKHLIKPRLVRQSTRKARTPQPLESGSSVAPSVTQRGNDMQLESMEQRSEQENTTTSILDQISYGFVSVGGFIYQNSYIFTNILMMAWSIVYHSWLTFVLLLSANVLWMIPNQRKAMMRSSPFIVLYAEALLIAQYIYGMDLNNEELPTSVPTAGINLQQIGFERPIENQMRPCVPLIVKTAFVLMFWVTSRQFFKEKRDRRRDSTLADFIAPLQITVGSAGSSYLINDGKKTSKFLKKAGDVIKNLLVRLWIWLLVLVIFLCAITGENMTGFRICYMALFLFFLLVFQSSSKAWVKIMYGFWLFLIFYAMSILILIYTYQFDKFDTYWSDYLNVSATLQKDIGLKRYQTKDLFLHLVSPTIIVILTVIQVHYFHKRFIASLQQQPLAGGSAQQKPTETTALEPAPSKRRGSAGSLRKSQGPSAEAAPGATTDFETSVRDLVRISFRKIKNKSEYIFKNFKDVFWRFLELHIMKAVYIAAFVCSVSEVCVLHIIFVGFCVLGATSRKAVQVVISRLISFIVTVIVLSKMIYQIEYLSHSQHNVVCSDNRTANNAEWIGLTKADKVTGGLMSLLRTYIIYMVIVTMHAVISLRQLQMRVKIGALNAPPTKLLFPNIIRADAEKDLVGLVKYLLNFGFYKFGIEISLIALVSTITYRQDIVAVVYALWLVVLLLLRRSQCAKIWGVFQAFFAISILTQYIVLVGLPPSSCLVFPWDEGPFGEGIQRWAMLPGALHFNHVPKLIFDFIVLVILNRQKSIFCIEQRYASNDDYPGGSNRSVIADIAQLGRVPFDNPTHDFCSYIRNYSDILKNGVLCGFYWFTLAVVFLAGTNIADLLALGYLIGAFIFLWQGSDFYLRPIHTIIFRWKWLLAFNVANILIKTSFQMAGCLFMTQLTKDCCWLVHMLGITCTSNVLTEQIMLPEEAELALKPGECPKITHQVVLLWDTICFAFIIFQLRIFKSHYFCHIITDTKANNILASRGADIIESLRHKQIAHRHDHEKQVLHKIKRKMERIRATQQKMLRPLDKQTHFDEHGYPLPAPTVRRRKEIKLHPHATRAGDYYMFEEMDDKFELDLIHDEIDFLEEENITESEMKMQRRKTLYDKSKDAPTGEFPSTSKGISKERDAATASSSASPAPTRDVGDLPVIPPPSTGLGREQTSKETSDSKSKMEVDSGEVTAKDSDEDFDTNPIIRLLEGFLVTLTIRLNRFSRNYRFVNRILAGEKKTLKESSSLNRLGLSSAAAMFHFLKSNLESDESEPPASSSTPRRVVIAPPNATEHSDPTSTTLNTNTTTTPLSPPEPLQPLQPLQPNTTSTPQQQHQHIRAAEEIIELPVDTVDGVAHRKQSINSSPPAKGAGEFNLEEENFAQRDHHIIVEVLISSWYALLANTDLICYIVVFINQVVNASLISLPLPIMVFLWGTLSLPRPTKTFWVTLIAYTQAIVLIKCIFQFKLIWSNYHQLPNQPLTPAKIFGVENKAHYAIYDLILLLVLFLHRYLLKSQGLWKSGYKDTDNQFTKPTASIDERDDSDNLSQPDSRQLNDDAAQKLSLQVSQASLPGSPEFSKTGINQLERTKYTSSLYKFFFSLVHKSRLATDVYALMFLCDFVNFFVLLFGFTAFGTQQTESDEGVQTYLAENKVPIPFLIMLLVQFLLIVIDRALYLRKALVNKIIFHFFSVIGIHIWMFFVVPAVTERTFNSLAPPIIFYVIKCFYMLLSSYQIKSGYPKRILGNFFTKGFSMVNMIAFKVYMQIPFLYELRTILDWVCIDSTMTIFDWLKMEDIFSNIYLIRCTRQSETDFPAMRAQKKASLSKLIMGGTIVLLIVICIWGPLCLFALGNAVGTSNVPFHVSLSIRIGPYDPIYTTNNYDSIFEINPEMYSQMTNAYIKEKQALTFIAGYDATDVAAVRLAGNSPSLWNIAPPDRQRLLNDLRNNHTLKARFSYSLTRKAPAKGLKENVGDEHAISLDESFEGRAALIHMLSETHDVEPIYSNGTTNGTTPEVEEVVVIPGMIPKFIKVLNSGDAAVVSVLSPKHYDYRPLVIKMHRDNETNGLWWEIRDYCNDTFYNETLSKFAYSNCTSGIVMYTFNDKKFPSTFSFLTAGGIIGLYTTFVLLASRFMKSFIGGQNRKIMFEDLPYVDRVLQLCLDIYLVREALEFALEEDLFAKLLFLYRSPETLIKWTRPKEEYVDDDGDTDSIPSRMSVRRPEQLQPQQPQ | 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 transport [GO:0034220]; regulation of membrane potential [GO:0042391] | 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 mechanosensors (PubMed:32649914). During their evalulation of potential egg-laying sites, females determine the softest substrate for their eggs first by making a coarse evaluation of substrate hardness using mechanosensitive channels nan and Piezo in the leg tarsal bristles, followed by a much finer assessment using nan, iav and Tmc mechanosensitive channels on the labellum (PubMed:32649914). Acts in the nompC- and nan-expressing neurons of the female leg tarsals, to sense the mild differences in egg-laying substrate stiffness (PubMed:32649914). {ECO:0000269|PubMed:22343891, ECO:0000269|PubMed:22343900, ECO:0000269|PubMed:32649914}. | Drosophila melanogaster (Fruit fly) |
M9NDE3 | BARK_DROME | MKLQHHKTNRQRISKPHRDPKWASICLWLLVTLAFSTHLARSQESRQTEDSKEVELLQDNDIEFASLDGASQLLPATRHSGADVTVAPQGSTPSMTSSSSYTELQGGEILSDRILRRSESPYLARDDIEVLRGARLTIEPGVTIEFAPTKGLKINGVLQAVGTPTSRIVLKSQSNTANYKLELPDDQEKGIRLVDGPTPVEGRLQLFHKGAWRSVCSNSRNWTLADYGVACKQLGYRGGRFWNWVERTPGYYPRLLYEQPKCKGGEGSLQDCAWTSRQMGAGACDYHNDLGIQCLPVHSETLGHWRGIYFDNAPSTKALGRDNIVYAAQSESRLKYVDIIRAGSGAGFNAKSAVEVQGLPPQMEHVVISHSAYTGFNSTRPWAGFQLQNVTVRKCNGIGVFVNSSQGAVQLDGCSIVDNAGDGIKYVGHDLRGTERKDRASIYDFCTLPTTSGQTYPISLSFTQKYYAGSGKECGKYFFTRPGYLLTLHFENFVLMQNETATVEIYDGASTNDRLLFEWKARNFTRPQSVTSTREKMFVRIRADARQELNGFFRMTSGDSVAYDLKVSQSTVEDNGGRGVAIDNIRSKLHVHSSSVSGNGHVAGVHVTSGAGDVNITSSNISFNNGAGVNITYYGGNRNISRSALTANKGYGVATWLNQTSDVNRMEYIPFNQTSVVEYSQIGGNLETGVFHGNFCRPIWVNITGNSFNGSQQNDIFIESCYQATANGRPNMQLQLGHNQFKYSQANSIYLSPALNLQGRIEYNMFRFGSYGCLFINNDYIYPEFNYFPVKLIIQSNYFMRNSGVHVVSLGLSPYSRAEVQYILFTRNFVRGNNITEAFGPLIAGSEGSDGAGRLNPRSRVAAPVVVGSSNVDIFRNILHNLDSMYEIGSQLTDQSKIINATCNWLGHTDENKIYARLFHRNDRYNLAKINYLPYLLHSSNPGSTAMITVSTVVPRFFHEGSDVIGGEVDGQDMVPAGTYTVTKDINIRPGGKLILQPGTTLKFEPSVGMMVAGKLEARGRRPDDILFTLKRETIMGESNDTETIDLDSETEAIDMETEVIPADGVPRVPVRLVGGAGANEGRLQVYLKGRWGTVCDYGWNVLNAALVCHQLGYSLNPQDWRLLRSQLPNAGTSEDILMANVRCTLQDRDVTKCRAEYEFENTCSHENDVGLRCYEGAWAGVRFSMLAERADLQYVTVEKAGLFDYTTNAFKPAVQMDHARHNLENVRIVNNLQDGLGIIYADIYAGKSVNNIKNSEFSGNKGSGISLKQLDFRVSGSIIKDNKGSGVSHDAVISALDQKEIGGWFNMATDFNSFDTDYDPYLLPREISNIDLGTFEHKYIRTEELLGQNINRKIVVQCPAGYVIGIQLLNPIHNLSTESINILNARTENIRSDLWQVKRDLNVFPVTSSSYGIIIYYESGLQALGGAVLMLSTVTAPVQNIRNRIVSGAVPTLTIRSTKIQKNLRGITGIYYNRYIGDNGEYYLRKANESIKLINSELSYNEREAILIRSPFWDVISSNLSEVTLHVNGSLITQNGLGIRQMSKDLRSSNNLFHYVIQDTTFEQNTHGGFQVSLPYVWQYNENFTHSIYFGNSTWQRNRDFRISVSGHYTVFNITSNVFRENNCPGALISLDGMEKRLRFDNNRFESNNAKFVLLFKADSLSEIIGQVPASIEFNSFKGNNIVTMTANYRNHYMKVARRIRKQHKIPTAVIRLDGVQNVRLYRNLIAENEMDYNLVAGVRSARLNNYFEARENWWGTKDTAFIEAKIFDFDNWNDHADVIYQPFLIEDSYDASVSVVVPFNQDQEIDLTNYKGGRVYKDLLLTKQSTPYYISSDITVMPGKTLTINHGVTMEFEPNVGILVLGTLVAIGYRESPIVMRPFRNATRESLIDVQPKKRALEDMSAPLTEFDSIRLCTSANNCTGDADGLFGLNEGFLEYFNHTTLQWVPICDSRFTERNAQVVCRELGYDPLNVYYGHDRRIEFHTNSLTRIWSWVQPLECRGDEERMEDCAERLNGQLYGHRHECRWDDVFVFVSCNGIADDEVYWGGIRFANSKFEEIQYEHRLHNTRSHARLPLRESQLEFVRIEQAGILHNHKAAAIQAIHKNPSITSVSIENSANHGINMIAPSGKLNLNHLNINNTLGTGISIVSLSGEGRDSDESSFTPLKKLDLPYKLFSLVDICDPQKVLTIEERMLIYYKYDNNPVNCVKIFTSAFRAKPIGFRLLQSNLFNHSKLYGRTDFIKLYDGDIYNVTATYLGKIESDTDNQRSFFKTKGPTMSLQLVASGAPETHGFIAEVVTVPISTLGQYRDALHNITDTHISGAIKGAVTYSSAGEVTPTLTLIGNRIEKNCRQLYGNFSTCTSALNLDVQNMNSLYFMNNLITENQGGLRIRADSRGSATSLRGFVHHNLFMRNRNRPALYVEGRQSSPYQEVELYRNYFAQNMAGYEDVIRLCQVVSNFSYNYVHSNVGGRIMEVSGFEKVRLQIYQTTAHNGFYRNFATNWMTRATIVAGTAGQQYVDNIFENHENDYELLTVNNSILSFDYENRTFETWSSKIDARHNYWSYNNTISVQSRIRDKSDDPMLLEVLAVPFQMNNETILDGKCPPGWALVHDTCFIYVGAPMTFHEARDFCRSENSTMPFIRTDKTTLWKYLQSQMRHLKYPDKVWIQDYNHIDRCTSFVFGEIEIEDCNKERGFICESDPRVIIDPLSWRADIFAISIISAFVLAIILLILVAFCWFAKSKHRHTQRLQRRNSIRQSLRSLNSIDPQGSLRRRPNYNMSSNGTLSKGQDYKQMVANGSIDSMDKSVLSSEAGSFEGYEQKPHYNEYVNQNALRPAHPAQDHQSHKVATISKASGHRARAAAAAAAALEPDAFELSYRNEGFRDNSTYGDNTRANSISTSVAEDTPIIHHTDQEIDEGGSDYYGNASTLPLRTEGGTPAGRRGQPGLAFLSELKQNLPEYQRSSHSSFMPHRSSGDSLPFDQKLDQFNYSTESSLYRPAPAVPSSQQATPADMRRPDSYYTAVRSSKAPVSHYRTPRPLAQPPAAPNVAPAGGPAQRRPKTVYQTASEESSPTTPSPLTNQYHRSKSEALLETDFDGDGGSVGLQPLQTNGRSHSQPLETAM | 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 as tricellular junctions (TCJs), that mediate cell contacts at three-cell vertices. {ECO:0000269|PubMed:25982676}. | 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 Nrg during late embryogenesis (PubMed:25704509). Involved in the formation of tricellular junctions which mediate cell contact where three epithelial cells meet but not of bicellular junctions (PubMed:25982676). Required for the accumulation of Gli at tricellular junctions. {ECO:0000269|PubMed:25704509, ECO:0000269|PubMed:25982676}. | Drosophila melanogaster (Fruit fly) |
M9NEY8 | TET_DROME | MASSILAQSSTGATVDSSNLGATAAAATSVEATVSSLHNTHLNQLSSLSQHYTTPYHHPHSHSHPHHHYQQHYPQQQHLQQQQQQQHHAQQQHQQQQQQQQQQQQQHWDYYARQQQQHQQQQQQQQQPAAATGNTNGNSSNNGNNGNNGNNSNPDGSNTTVPAPLGSSNNSSSNHANAASGGNSGQRHGDANANAISAASAAVGNPGNQQPNNSAGNANSNSNSNSNSNGSYTRPWEMESKDNGPQPPQTQPHLQLKSGFEPFSKLPSFQSQFHGFNEQLLPDGTPMPVPIGAGVPPGSAAAVAAATGSIPPGSVGPNSVAGPVGPTAMSSLQTVAMSPASISVSSPGMMSVGSPLTQLSSLQTSITPPSAGSFPAPPPPNAFAHHHALNPHHHHRGASGYPTPYAELPLYPGFTPLSVKKEPISGGSDFEMLLKKEDFDLSNSGGAGLIHHPLQHGQPHPIPMGMHTPTSYDGNNSNNSYPQAAGGGSGSHTPHTTTTQPTPTTTTPVKVEKLLQSPIARLEARKKERRKQRPNSLESSAESEASGMDVDPSNPGQVDAVSSTANFKSPLSALGMGDSNDANASGCDKQSKKKRKRCGECVGCQRKDNCGECAPCRNDKSHQICKQRRCEKLTEKKIVFGADGQPVRPDSKRGRGKGKSSGSGNGTVNATGIAAGNGTPTTGQSRARKNSTKANKLNAAAASATSPRLSPVPAATLLPQQSPNTTSATGNLQQQQQQQQQQYQQHQQLLSQQQLLSQQQQQYQQPQQQQQHFQQQQQQHLQQQHAQQQHLPQQQHQITAQIQTMKDQPQQPMAPMAFYPTWQADPSQGWQNQFIQQIPQNTPAITSLNSLDFQTQSYAYPSNGYVQSGLGFDPNYGRSPYAAPVQRYDFQSQQLSTAPSAINQVGLQSVAGFAPSYAGQVSAAPVPPSQQQQQQQQQQQQQHLGADLNKTMSGNDTPGYPRVSSVPPRSLNCNGYSGDYSGSPATNSNSNNNSSSNTSNTNNSNASNNNATTVVSGGTTTPAPPPTVVAQPASSPMQPPNQAVPQSPTRSNMLQQQQQQHQSPTGNGLQPYVAPQQQQQQQQQQHLSSPPMQDWNWQQQQQQQQSLGGEGYAQGERLHLNTRIKSMIMRKSDPKDPPPDLQQQPQQVQQQQQTGHFLSYSHHLRPEAALSANGPSSATPTHPLPNLQQQQQQVQQVQQVQQQQQQQQAVGGQVAAEPIGGGGDHIWKPHHANSFKKPSVVSGYPASQDAQLQLQLQQHQPGQHTTINHSVDPPVVPPQQHPPVAAAQPKKSRSRSKASRAAAAAAAAAEAAAEIDRDRNSTDPGGGGLKPLSAHYPPHPHAAGGPPPGQDYHSQYIKTEPGLLGPPQPNKMEGYERNYQNFIQYADFCQNDGQGQPVQQHHGHGQQDYAGYHHNSAYYGAGASSFQQNFQQNFVPGYQHSTYGARGKPPANQPHQIHGHGQSLMELDRKPDTNSIIPLPTNYEKDIPAYPIPPHRYALGHGAPPHLSHHGMLEPKIEDMGMLGHGGGYAYLGSEGKPLNNGFSCCRQGGTRPPTAEHLKDGTCLGLGIQPKEELIDEDELIDTHGNGLKPIGGVGKAKGKQKPDEIPEIVVKHEKINPMFDTTDRLEKGNKTEIPECECFQSDKNPPEPGTYYTHLGTASSLMDLRREFEERCNLTGRQLRIEKIVYTGKEGKTSQGCPVAKWVIRRADLEEKILVVVKKRPGHRCIAAYIVVCMVAWDGMPRLEADNAYKNLIPKLNKYGLPTTRRCATNENRTCACQGLDPESSGASYSFGCSWSMYYNGCKYARSKTVRKFRLSVKSEEAAIEDHMNLIATLLAPVFKQVCPRSYDNQTKYEHEASDCRLGLEPGKPFSGVTACLDFCAHSHRDLHNMQDGCTVHVALLKPGNRDTRLPDDEQFHVLPLYTMDGTDEFESVEGQRDKHRTGAVQMLDKFPCEVRVRSTPLIPCRRHGKKRKDGDEAAPPDGDQDAVGDANSQSSSSNGAQSQTQANNQQSSPPALGTAHIKKENGNGVNANGASSKSKGKGKSNQSNNSSASTPGSAPPSTPSPRCQTPVTNNPSPAGSAFSTPPVHGSNANPQSNGGQGTGNQPGQLMSSNSSLMNMATMIDTFTDAQLQSNQISSTVLDSPYSYDYQTASYIDSRNYYGQWPTPHAPMGMQAQVGGLGGGGPGGTVAGVPPLTPSTPTAQPQLGVPPATSIAGGTTTGAPTGALPATAPPTATPTQLETSNGYGPGNYQTLVSNPASNLTNPGGVTTEVQQQHQQAQQQSALTGGVGPGGLPVVGGAPGDLKGRLVSEENPDSTTLVNHHHHHHNLTESKLTALTAMQPMTNLAPLTTSHHPQEGFVKPKPPPSDYTAQYTAQYPNNYQMYPPPPPPPHSAYSAYDAYQNMNYNYGYHQAYSPYGMYPQQTPPPTPPPPSPNWNMYGHHQTGSVNSGYGSANPAAGAGSLISSHGSVASAGVGLQKAMVPVPGPLHHQQQQVLQQQQQQQQQQQQQQQQQQQQQQQQVQQLQQEAPQTILPDLSNGQTNSDTVATPTPTGDSSSNDAGPGNPGAGNQAPASGAGAATTAPPIASPGSTNSTKIEPIGEVAEINENIEAFQDPQMGGVAIALNHGSVLIECAKHEMHATTAVRRPDRHHPTRMTLIFYQHRNLNRCRHGIDEWEEKMRVKKINTDLDNKAKEERERLIKKAAGEDMDELDEDALMQDEPVPIKKESSANGQQLKNGASGSKKKKSSDSKKSQANEQSKNEKVALHAPTLTTTSWTTLFPTHPCVVSGKYPEGNSSPTSSTNNAPNGGGCPAQQQQHLPPPPGSGLIHPPPGTPTGTAAPPPLPTPHQQLPQQQQT | 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. {ECO:0000250|UniProtKB:Q6N021}; | 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:CHEBI:90615, ChEBI:CHEBI:90616; EC=1.14.11.51; Evidence={ECO:0000269|PubMed:30078725, ECO:0000305|PubMed:25936838}; 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:CHEBI:136731; EC=1.14.11.80; Evidence={ECO:0000305|PubMed:25936838}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-hydroxymethyl-2'-deoxycytidine in DNA + O2 = a 5-formyl-2'-deoxycytidine in DNA + CO2 + H2O + succinate; Xref=Rhea:RHEA:53828, Rhea:RHEA-COMP:13315, Rhea:RHEA-COMP:13656, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:136731, ChEBI:CHEBI:137731; EC=1.14.11.80; Evidence={ECO:0000305|PubMed:25936838}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-formyl-2'-deoxycytidine in DNA + O2 = a 5-carboxyl-2'-deoxycytidine in DNA + CO2 + H(+) + succinate; Xref=Rhea:RHEA:53832, Rhea:RHEA-COMP:13656, Rhea:RHEA-COMP:13657, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:137731, ChEBI:CHEBI:137732; EC=1.14.11.80; Evidence={ECO:0000305|PubMed:25936838}; | 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 may act as a regulator of gene expression (PubMed:25936838). Promotes differentiation of early germ cells in ovary (PubMed:25936838). Contributes to neuronal morphology, development, and function in the brain (PubMed:30078725). By interacting with histone modifier wds, binds to a specific set of genes, modulates intragenic (N(6)-methyladenosine) DNA levels and thereby maintains transcriptional activation (PubMed:30078725). Also able to catalyze the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) (PubMed:25936838). {ECO:0000269|PubMed:25936838, ECO:0000269|PubMed:30078725}. | Drosophila melanogaster (Fruit fly) |
M9PBE2 | HAKAI_DROME | MDTEEVKRGRGRGRGTRARGRGRGRGRGRGKKIDDSSIADAAALAASSCAALEDSPGRLDASEDSVMQELDKDGELETPGALEEPLPHGALGAVAASGNMTPATQQPQVLQQVPPPVMSQTTISLSLARAVDMEADISQLEAPTFTTLSRGPPEPMLRLKWNHKVSLIGEKVLNPMIHCCDQCDKPILVYGRMIPCKHVFCLKCARAEPIKSCPRCTDKVLRVEQSGLGTVFMCTHGGSRYGSSGCRRTYLSQRDLQAHINHRHVAPQPPPLQPQPQLSAMAEQPKMTDLGGVGLGLELHKQRKLSESSVPISVSASIASRPVLSRLPLTGGVGNIGSIGSIPPPGSAAAAQNAIHGGHSTLTLANLTRINNANAQECHQGKASLHHTLKKGTPHQSESVADASYYSSVLASFGSAAGNPGSGPPGGGATAAAQPANPSGSHSAVGPGALIGGSTDAPTGGSSGNWQQSQYYR | 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]; protein ubiquitination [GO:0016567]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of cell adhesion [GO:0030155]; segmentation [GO:0035282] | 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 mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29535189). Its function in the WMM complex is unknown (PubMed:29535189). {ECO:0000250|UniProtKB:Q75N03, ECO:0000250|UniProtKB:Q9JIY2, ECO:0000269|PubMed:19682089, ECO:0000305|PubMed:29535189}. | Drosophila melanogaster (Fruit fly) |
M9PE65 | AXO_DROME | MAFPYIWALLPLICSASGLSLPNMTSTDAVVAGGGILPILVAGNPGNLGSSNMSLSGGGGLAGSSTGGQSLPDTGGGNSAGGSPAGGSSGTGGGGSNSGISGNNSAMIQGQKSNQYEKCAGPGDPGPCKQYIYKWRYEPTTNECTNFIWGGCEGNPQNRFGTEAECLFHCIGGPHTLPPFLQSTTREPSTTESSMLLGLPYTQSPAQSPDGMGGAEGGDGTTPVPIEQRGPELTFAETGQGKTFIFAKNNTFIQMDGDIIQTFQLRLCREISFQFRTRLPHGLLVYHNVKNPDRINLDPYALYVIVEKGQLKVVHVFGKHSTSVTVGESLNRDEWHSVMVRIDVHGARLIARVDNSQEEVYLKGLNHEYNYGVSTNLPSVVLVGGLSSEEKLHGVKYITESFVGCIRNVVLSSGKAASDLLPIAPLVATKHENVNEGCSDMCESRHNLCFVGSRCINHYGGISCDCFGTHYEGEHCDIYTATIITLRGASYVSYRIYDWKDRVHSSTRRISLMFRTNFDDSALFYASGESLKHQYIAASIKNQSVHVEMDFGDNVMSTVLTDDLTRGYWHNLTILHEQRTVSIILDQQQKVLELPATASGNMLFDPEIYFGGGPELHKKKGLASHNNFVGSLKYVYYNDISILYELQRGNPKVHYHGVLEAEFVENEVNVIPITYPFATSHIWWPINHAEEFNIKFDFRSSRPGAVLAYSDVTTSAGNGFWEIRLTSDKLSFDLVPDVNNNVTHSTTIKINRATSWHSVELDYKLGEIRFTVDYRHTLSQMYGLTFNIGDKLIIGSSLKSAAMGLVGCIRDIEINGHLIEPRHVVKTERVVGEVALDNCNYIDPCKRPNTCEHGGKCFVKDDRVTCDCKHTGYIGKNCHFTKYRKTCEELALLGFTKSDVYLIDIDGNGVFPPAHVKCDFQSLENATKTIVEHNLPSQVDVRSARESDFSFNIRYREFSPHMLQELISHSLYCTQYIKYDCYRAQLELHSATWFTSSAKNLTVDFLGNVKRGACPCSVNKTCVDPNQSCNCDVKENKWNSDEGYYQDPQSLGITNMYFLQQKDMDDEAQGRITLGPLECVETNTQKYVVTFTTSQSYIEVPGWRKGDIAFSFRTTGEKAILLFQPPIRPHYPSFMVALTGDDQLTFTFTLSTGTTRELVINSHRRLNGGEWHKIWIDYNQYHVRFMINTDYQMLDLLPEEEFGPFEGSMYIGGATFDLLKKLSVKAGLIGCFRGLVVNGEILDIYSYMSVHLSEIIKDCKPSCVPSPCRNGAQCKELWSSFKCVCNNPWAHIGEFCETNINEKALTFINRESFLMRNYLSVGATPVILMHGINGERDVLKGILNQDLLINLRTYDTNALVLYANDHYNNFVHLYISLNREIVFLYNYGDEIVNLTLLDDTLMASLKSIQVAIVRGEQETRMHVNEHSVSIDRGTLLLDEYANKPWSNPEKEVLSPHRPPAPPTEYFQFHVGGYDPANLLRPNVDAPALEGYIGCVRGLKIGAQLIDLADINERNIAPTQEGVLPNCQIKCDAEPCKNGGTCQEHFAEQLSTCDCEHTSFLGEFCSEEKGADFSGESTLQRKFELPGTGRVDYVRLQLAFSSFDLRRANRIMLLMQTEAERSYYLLLAITSDGYLQLEEDRDNGQTVGARIDRNFLNSARHSVYYVRNGTQSQLFIDREQVPLSEFAARVLTTGGDAGSNRVQIGGINSTDSRFAVFKSYSGCLSNIYIQVNGHVMKPLEEYMLFTKSGADNITVINPQGVRSAQCNAKFDVSEQPTQEPMVNVSMIPEPWVEEPPARVPYIPRFVYDENKQEDSTQVVFLTLTSVFVIIVICCLLEVYRSHLAYKKRIERETDEDIIWSKEQATKMHESPGVKAGLLGGVTAGSGNGLPPYTYKALPQEDKKPGNGAPLVGILKNGSATPSQPGTPTALSKNGDIASRIEEEEEEEDEAPAQKAAEKSGENEEPPAKDTTASEIKESQAQPPEQLAKDTTDASAAPKASKETEAQAEPSEPSSQLNSAQNGQLAQMEQAARGDEVQVPSLPHPIQPPDAIFMPNLPQKAQQRQPQEHKSRHKATDDTEAPKQQQQQQQQQQSFDVATNANGSSLPASRVKNPEEPGGKSPLVPMRQHHSKVTRPPPPPTLFLENSLLQRQFANPISYLGGPRLQPRSNRTSIDSILSLD | 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:10037607, ECO:0000305|PubMed:10037607}. | 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 | MDATSIITQVSRDDEQLNVYPSYPNDKDAWLGFSGSVWLPDCPADHAQLTHDVDRLKPQKRGLFHSLLCCWRRNRTKTNQNGTQIDGSTTPPPLPDQQRYLLPQVRLTDMHRKCMVIDLDETLVHSSFKPIPNADFIVPVEIDGTVHQVYVLKRPHVDEFLQKMGELYECVLFTASLAKYADPVADLLDKWNVFRARLFRESCVYYRGNYIKDLNRLGRDLQKIVIVDNSPASYIFHPDNAVPVKSWFDDVTDCELRELIPLFEKLSKVDSVYSVLCNSNQPLNNQTNQQQHPQELQQAPNQLHQQLQQQQQQQTISATTVITQATTLSAPTMLNQQQTSPPSPQSELLQKT | 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 | MGQTLCDFVRQQEVVPANRARKGSAISEDGTTSCTTQPQRNTSISSEEQTVQGANIQKSGHRSFNRSASSRQKPNPTSKLKDTLNRKPTCKQGTLSAHTSTSSTTSIQSSPIEPASSLPTLNTTPTPPAASKSNLFVRVLRRFSNNTLPGKTASSPKNVDDVPKVNDNNNGDLGKQQSTDVEVLCSQDNQSREQNEDEMDSKIEPADAISNQKAGLTSGKPKKDKSVKGTSQAVVSDTKKMEARKSSSDTVIEPLIKQQAPLHSSKTTPTTLTANFVQNIRFVRKNVEQSGRNTNPLQFVELETEFPRDYDDNIEMLSREAEHLEEQFRTPTRSNATDATSHHVAGIIDNIITEASRSLTIEKTEDDVPLKSSTKHSSGVKRVGFQVEDKDDTEVQSEKQAKSFDDITKKAESSEASAEEAAVTGSSTDASASPLPSTSLVSTTSSATSITKSKSDEDDDPVAMSPCGRFFKYDKEVGRGSFKTVYRGLDTLTGVPVAWCELLDKQVKKSERTRFREEADMLKKLQHPNIVRFYTYWEFPIGRKKNIVLVTELMLSGTLKSYLKRFKKIHPKVLKSWCRQILKGLNFLHTRQFPIIHRDLKCDNIFITGTTGSVKIGDLGLATLKNRSHAKSVIGTPEFMAPEMYEEHYDESVDVYAFGMCMLEMAISEYPYSECKGPAQIYKKVISGIKPAALAKVEDPNVRDIIERCIELKKEDRPSCNELLESEFFDEDIGIRVEPTASEQFLSDPSISIIEFRLRFMDPKKRSSRHKENEAIQFEYNIRHDEYEQIAQEMMKENIISEDDSRAVARLLKVQVVSLLKERAQRQTQIKLQNEKSRLEKLALQKQRESLPTNVDEDEEEEEESEDEEDGVKWNQRLQLRYDLLNTDSETSLALSTNSVEPQQLSTRSNTSIPNSGIQQPVQVPGQVPVSQLISVQPQAIPSPAIPMQQKPTVHYIQPPQLASYQNSNASMQEMTNNQVISPTGSQQMQQQQPVVAPTVNHQVMPQQQVNQQQQQPQMMQQIPQQVQVQQPQTVLPPQPHEQQPQQQQQPLQQQLQQLMHTNVQAPDLTQQQQMAQQQAQQYFQQQQQQPQQAVNMQQAYAMQQAGQQQQLSQPLQIQQQILQQQQVAVSHQQQIMQQQLAQHQLQQLQQQQLQQQQLQQQQQIQQQQLQQQQLQQQQFVQQYAQAMPQQQHQQLVTGSQVMAPHQHQQPIQIPVQMQVPPTSVAPPIQHTYNQQGGQVTLSDAQQQQHPGFSAVPQQAAPFIQQPTQQPIQLSMPLEQQLQQLLHSQPAQQQQAMSQQQQQPLVQQQQLPLVQQQPPLVQQQQPLVQHQQPSVQHQQPLVQQPQQQQPQPQNQQPQPQTQQTHVVQQQPPQQQPAVEQISQISSQVPVQQENLQPIQVNKDANVATDAMSLNSAHGALEPAPKTEPQNSADAEKQQKQTGTGTRSQKPRRSNRSGNERIPKLSVTSVDEGSVINCHMENKLKTITFKFDIGDVNPVEIANKLIAQDLLSNCQSTVFVEMINEIVDQVKQNPNQIPIPTNYRRNIEKVRHASLTRQRSTFRSHQRHRSRDETASDITKMFEPTIHGVETLPSGGGGAEQSNCNLTLEARSHLSNIPNAKEPQLNVSTPPTTTSTMSSSSTASRDAPNSSNDVTIGSGSVSRKTSTASEYTSLSIDYMPDSNITPTGPEPPLDDGKDKKPCSLAIARMQKLLESAGNGAPRSLNLPLNRHLKIQEDLKHTRSLDDLTAVKITFDMPNKAALDTSENAQQATEAEAEKPKDKSGQAVGNQGTGAANTLEQLKIELENITHAHAFASAVVASINNRAPHQASPAMSSLKATSGQPQTQEITKPNNGAGPSVPSVGQNTPTAALTSARGSGSSVYNSRRTSIDNSVGSDMHLHTATNLEGTVSNPDPIPTEASVGITIATGHEKQLSKQPSLEKPSATSILTNNSDPPQRNPSNGSINQNSIADLEKKLAALRNTENTEESATATLSVVPKQVEEVVNPSARKISRFSVSRVQEQKTSTGVEEPAQGQLKIDLQVAGPGGQVQTNNSVQNGSVVNTPTEVISSPIQNVPLAINGIQLMYQQPQQIHQLPGGTSTTTSGAGTQCIVVPQVVNQNGTHVQQPSNLQPQQQSVHPNMTQQPQQTPLNGHPSMVNTLQQQPPQQSLPMQTIQSQQQQHNQMPIISQQQQQQILMQQQQQQGSQQGSQQFNLPGTQQTHPQHQFIQSQPNQLHSLPPQVVSMAQGNLPHQLPPMQTMGAQQQMISQQQHQLQMQSHMHQQNVPGMYNQQTGARVAAPQNFAGAVPNHLLQQSPLMASQQPAQPMQHVMQPIFNATSGEVTEEPVSLAATHPHLLPSDIQSDIKHNLDSLVNQLCNTRLGTNQHQRLLLLRQRQLIEEDELRLKHYVEYEKFQKALRQSISTNVPANAAYYSAAAAQLPTNLAAPAAPSSSNPTSTSSANT | 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 signaling pathway [GO:0090263]; positive regulation of potassium ion import across plasma membrane [GO:1903288]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; wing disc development [GO:0035220] | 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:0000269|PubMed:25086033}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:23797875, ECO:0000269|PubMed:25086033}; | 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 increase in response to hyperosmotic stress by acting as a molecular crowding sensor, which senses cell shrinkage and mediates formation of a membraneless compartment by undergoing liquid-liquid phase separation (PubMed:36318922). The membraneless compartment concentrates Wnk with its substrate Fray, promoting Wnk-dependent phosphorylation and activation of downstream kinase Fray. Following activation, Fray catalyzes phosphorylation of ion cotransporters Ncc69 and Irk1, regulating their activity (PubMed:25086033, PubMed:35303418, PubMed:36318922). Phosphorylation of Na-K-Cl cotransporter Ncc69 promotes its activation and ion influx (PubMed:25086033). Involved in circadian rhythms in small ventral lateral (sLNv) pacemaker neurons: in the morning, Wnk activity is repressed by high levels of intracellular chloride; in contrast Wnk activation in the evening promotes the activation of the inwardly rectifying potassium channel Irk1 via Fray (PubMed:35303418). Acts as a positive regulator of the canonical Wnt signaling pathway during wing disk development (PubMed:23797875). {ECO:0000269|PubMed:23797875, ECO:0000269|PubMed:25086033, ECO:0000269|PubMed:35303418, ECO:0000269|PubMed:36318922}. | Drosophila melanogaster (Fruit fly) |
M9Z1G5 | MOMT3_SOLHA | MALSMDNIVISNEEEIYMMKAMHIPCGLYLNMVLKAAIELDLFEIIAKSTTQKLSSYEIASQIPTKNPNASSLVLERILRFLASQSFLTCNITKNDDGIVHTSYNLTPLSQSLISDKDGSSIAPFLLLATDPVAVNSWFHFKDAILEGEIPFNKAHGVHAFEYHGKDSRMNGLFNRAMQNVTCTEMKRIVECYNGFQGVKEIIDVGGGLGISLATIISKYPNIKGINFDLPHVIKDAPTYEGIEHVGGDMFKSVPQRELILLKAILHDWDDEYCVKILKNCWRALPKDGKVVVIEQMQPEYPETNLISKNSSSVDMLMMTMLDGGKERTKQQFEDLAKQAGFTVFKIVARAYYCWVIELYK | 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; Xref=Rhea:RHEA:74744; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=quercetin + S-adenosyl-L-methionine = 3',4',5,7-tetrahydroxy-3-methoxyflavone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17673, ChEBI:CHEBI:15378, ChEBI:CHEBI:57694, ChEBI:CHEBI:57856, ChEBI:CHEBI:57928, ChEBI:CHEBI:59789; EC=2.1.1.76; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17674; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=myricetin + S-adenosyl-L-methionine = 3-O-methylmyricetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74747, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58395, ChEBI:CHEBI:59789, ChEBI:CHEBI:194072; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74748; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=kaempferide + S-adenosyl-L-methionine = 3,4'-O-dimethylkaempferol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74755, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58925, ChEBI:CHEBI:59789, ChEBI:CHEBI:194074; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74756; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=isorhamnetin + S-adenosyl-L-methionine = 3,3'-O-dimethylquercetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74759, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:144055, ChEBI:CHEBI:194063; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74760; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=rhamnetin + S-adenosyl-L-methionine = 3',4',5-trihydroxy-3,7-dimethoxyflavone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74763, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:77710, ChEBI:CHEBI:192706; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74764; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=laricitrin + S-adenosyl-L-methionine = 3,3'-O-dimethylmyricetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74779, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:60006, ChEBI:CHEBI:194066; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74780; Evidence={ECO:0000269|PubMed:22711283}; CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + syringetin = 3,3',5'-O-trimethylmyricetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:74767, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58412, ChEBI:CHEBI:59789, ChEBI:CHEBI:194075; Evidence={ECO:0000269|PubMed:22711283}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74768; Evidence={ECO:0000269|PubMed:22711283}; | 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-adenosylmethionine) {ECO:0000269|PubMed:22711283}; KM=0.55 uM for S-adenosyl-L-methionine (in the presence of myricetin) {ECO:0000269|PubMed:22711283}; Note=kcat is 0.82 sec(-1) with myricetin as substrate (in the presence of S-adenosylmethionine) (PubMed:22711283). kcat is 1.66 sec(-1) with 3'-methyl myricetin as substrate (in the presence of S-adenosylmethionine) (PubMed:22711283). kcat is 0.39 sec(-1) with 7-methyl quercetin as substrate (in the presence of S-adenosylmethionine) (PubMed:22711283). kcat is 2.94 sec(-1) with S-adenosyl-L-methionine as substrate (in the presence of myricetin) (PubMed:22711283). {ECO:0000269|PubMed:22711283}; | 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-atherosclerotic, and anti-inflammatory effects (PubMed:22711283). Catalyzes S-adenosylmethionine-dependent regioselective 3-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates (PubMed:22711283). Active with myricetin, quercetin, kaempferol, 4'-methyl kaempferol (kaempferide), 3'-methyl quercetin (isorhamnetin), 7-methyl quercetin (rhamnetin), 3'-methyl myricetin (laricitrin) and 3',5'-dimethyl myricetin (syringetin), thus producing 3-methyl myricetin, 3-methyl quercetin, 3-methyl kaempferol, 4',3-methyl kaempferol, 3',3-methyl quercetin, 7,3-dimethyl quercetin, 3',3-dimethyl myricetin and 3',5',3-dimethyl myricetin, respectively (PubMed:22711283). Inactive with flavonol substrates methylated at the 3-hydroxyl position such as 3-O-methyl quercetin (PubMed:22711283). {ECO:0000269|PubMed:22711283}. | Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum) |
N0A3C0 | POLG_FCV | MSQTLSFVLKTHSVRKDFVHSVKRTLARRRDLQYLNNKLSRSMRAEACPSCASYDVCPNCTSGDIPDDGSSTMTIPSWEEITKTSTYSLLLSEDTSDELCPDDLVNVAAHIRKALSTQSHPANVEMCKEQLTSLLVMAEAMLPQRSRSMIPLHQQHQTARLEWREKFFSKPIDFLLERIGVSKDILQITAIWKIILEKACYCKSYGEEWFNIAKQKLREIKCFEGNTLKPLVGAFIDGLRLMTVDNPNPMAFLPKLIGLIKPLNLAMIIDNHENTTSGWIITLTAIMELYGITECTIDIITSLITTFYDKLAKATKFYSQVKALFMGFRSEDVANSFWYMAAAILCYLITGLIPNNGKFSKIKACLSGATTLVSGIIATQKLAAMFATWNSESIVNELSARTVAISELNNPTTTSDTDSVERLLELAKILHEEIKVHTLNPIMQSYNPILRNLMSTLDGVITSCNKRKAIARKRQVPVCYILTGPPGCGKTTAAQALAKKLSDQEPSVINLDVDHHDTYTGNEVCIIDEFDSSDKVDYANFVIGMVNSAPMVLNCDMLENKGKLFTSKYIIMTSNSETPVKPSSKRAGAFYRRVTIIDVTNPLVESHKRARPGTSVPRSCYKKNFSHLSLAKRGAECWCKEYVLDPKGLQHQTIKAPPPTFLNIDSLAQTMKQDFTLKNMAFEAEEGCSDHRYGFVCQQSEVETVRRLLNAIRVRLNATFTVCVGPEASNSVGCTAHVLTPDEPFNGKKFVVSRCNEASLSALEGNCVQSALGVCMSNKDLVHLCHFIRGKIVNDSVRLDELPANQHVVTVNSVFDLAWALRRHLSLTGQFQAIRAAYDVLTVPDKIPAMLRHWMDQTSFSDEHVVTQFVTPGGIVILESCGGARIWALGHNVIRAGGVTATPTGGCVRLMGLSAQTMPWCEIFRELFSLLAKIWSSVKVSTLVLTALGMYASRFRPKSEAKGKTKSKIGPYRGRGVALTDDEYDEWKEHNASRKLDLSVEDFLMLRHRAALGADDADAVKFRSWWNSRSKLADDYEDVTVIGKGGVKHERIRTSTLKAVDRGYDVSFAEESGPGTKFHKNAIGSVTDVCGEHKGYCVHMGHGVYASVAHVVKGDSFFLGERIFDLKTNGEFCCFRSTKILPSAAPFFSGKPTRDPWGSPVATEWKAKAYTTTSGKIVGCFATTSTETHPGDCGLPYIDDNGRVTGLHTGSGGPKTPSAKLVVPYVHIDMRTKAVTAQKYDVTKPDISYKGLICKQLDEIRIIPKGTRLHVSPAHTEDYEECSHQPASLGSGDPRCPKSLTAIVVDSLKPYCEKVEGPPHDILHRVQKMLIDHLSGFVPMNISSETSMLSAFHKLNHDTSCGPYLGGRKKDHMTNGEPDKTLLDLLSSKWKLATQGISLPHEYTIGLKDELRPVEKVAEGKRRMIWGCDVGVATVCAAAFKAVSDAITANHQYGPVQVGINMDSPSVEALYQRIKSAAKVYAVDYSKWDSTQSPRVSAASIDILRYFSDRSPIVDSAANTLKSPPVAIFNGVAVKVTSGLPSGMPLTSVINSLNHCLYVGCAIMQSLEARNIPVTWNLFSSFDVMTYGDDGVYMFPTMFASISDQIFGNLSAYGLKPTRVDKSIGAIEPIDPDSVVFLKRTITRTPQGIRGLLDRSSIIRQFYYIKGENSDDWKTPPKTIDPTSRGQQLWNACLYASQHGSEFYNKVYRLAVRAVEYEELHFEPPTYSSALEHYNSQFNGVEARSDQINMSDGTALHCDVFEV | 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 the polyadenylated genomic and subgenomic RNAs. This uridylylated form acts as a nucleotide-peptide primer for the polymerase. | 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 ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: [Protease-polymerase p76]: Reaction=Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-|-Xaa and the P1' position is occupied by Gly-|-Yaa.; EC=3.4.22.66; Evidence={ECO:0000255|PROSITE-ProRule:PRU01242}; | 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 subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation. {ECO:0000250|UniProtKB:Q66914}.; FUNCTION: [Protease-polymerase p76]: The protease activity processes the polyprotein: Pro-Pol is first released by autocleavage, then all other proteins are cleaved (By similarity). Cleaves host translation initiation factor eIF4G1, eIF4G2 and PABP1 thereby inducing a shutdown of host protein synthesis (By similarity). This shutdown may not prevent viral mRNA from being translated since viral Vpg replaces the cap (By similarity). May cleave host polyadenylate-binding protein thereby inhibiting cellular translation (By similarity). Seems to act as a RNase and degrades host Pol II-driven mRNAs with the help of host XRN1 (PubMed:33853967). Inhibits the integrated stress response (ISR) in the infected cell by cleaving host G3BP1 and G3BP2 (By similarity). Stress granule formation is thus inhibited, which allows protein synthesis and viral replication (By similarity). The RNA-directed RNA polymerase activity replicates genomic and antigenomic viral RNA by recognizing specific signals. Transcribes also a subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This sgRNA codes for structural proteins. Catalyzes the covalent attachment VPg with viral RNAs. {ECO:0000250|UniProtKB:Q66914, ECO:0000269|PubMed:33853967}.; FUNCTION: [Protein p30]: Selectively decays the mRNA of host interferon receptor IFNAR1. {ECO:0000269|PubMed:33075108}. | 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 for 30 min. {ECO:0000269|PubMed:27666486}; | 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 thrombosis. Does not have hemorrhagic activity (PubMed:27666486, PubMed:28579355). Reduces the motility of human liver cancer HepG2 cells in a wound-healing assay (PubMed:28579355). {ECO:0000269|PubMed:27666486, ECO:0000269|PubMed:28579355}. | Gloydius halys (Chinese water mocassin) (Agkistrodon halys) |
N1NVB7 | GCY6_CAEEL | MIGVYLRSVIFPLLFVIQTICQPPGNVFHLGFLHCDVLENNVEGSTTYINYRTSASAASIAIDKIKREGLLLGYDFKFTILYDQCDENIAAGNAIKLFAEHNVDVLFGPTTNNAAMPVFILATYYNIPLITWGITSSATLDDESRFPTAGMLSIGSRSLAVTFREVMKEYGWDQFVFAYSLEMNDEKCETLRDDFQNMVAYYGDIVLSYAVQIMDHSEEGLLAILKDVSTRGRIIVPCFHEGNSRGLHRRWMLVAARNGFVNDEYVYIFPSLRSRGYAVPQADGTFRYPWTEATGPQPGDQEALLGFQKSIFIVDMQGQGNVGSNYTQFEHEIIQRMKEPPYNCTDACASPEYQTAATYAGQLHDSVYIYGVVMDQIMKTVPNQYKNGTAFPRKMAGVFNGVGGTVAIDEGGGLQPTLFVLTLDSNNNSSLIMTVDVDQQEAVVTKHYTNEATALWSHRKGIRPPDQPICGYTGSLCPANVFFQYIGWFIAAIIIIFFTIMGAILAFIYLCHAKQQEVERQNALWQIPFKSMMTVTKKGKGEHSMRSISSVPSTISSTRSSTLSEVGETRNYLFFQIQNDVEMERVAAKKHSIRMVFDNKTCATMRQMRLIDHANLNKFIGMSLDAPQLYSVWRFCSRGSLADVIRKASMQMDGFFIYSLMKDIINGLTWIHESSHEFHGMLTSKNCLLNDRWQLKITDFGLRIFRTHDQYNKSDRLWTSPELLRTDDILGSREGDIYSFGIISAELITRSSVFDLENRKEDAEEIIYMLKKGGLQSPRPSLEHDESIEINPALLHLVRDCWTERPSERPDIKQVASQLRSMNTNRNDNLMDHVFNVLESYASTLEDEVAERMKELVEEKKKSDVLLYRMLPRQVADKLKLGQTVEPETFDIVTLFFSDVVSFTTLAGKCTPLQVVNLLNGLYTIFDGIIEQHDVYKVETIGDGYFVASGVPRRNGNEHTRNIASMSINFVKSLADFSIPHLPGEKIKIRVGFHCGSVVAGVVGLTMPRYCLFGDAVNTASRMESNSKPGQIHLSEEANQMLMRLGGFTTEPRGEVIIKGKGVMATYWLLKMDESAAPKILKKKQD | 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]; response to magnesium ion [GO:0032026]; response to salt [GO:1902074] | 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 | MKRIRSLWFNAEASYSNLNNSPSLRNKNSTGNNSRSKNYRSFSRFDLINSILLLMMLFLLAIFVTALYLTKSSRLTYSHASRAALFNPLGVISPSLGNHTLNYDPEARESSKKLYELLSDFNTAYYDDENMILGSNLFSKNTYSRQPYVANGYIGSRIPNIGFGYALDTLNFYTDAPGALNNGWPLRNHRFAGAFVSDFYCLQPKLNSTNFPELDDVGYSTVISSIPQWTNLQFSLVNDSKWFNPQNVTLDDVTNYSQNLSMKDGIVTTELDWLNSQIHVKSEIWAHRHIHPLGVVSLEISLNTDHLPSDFDSLDVNIWDILDFNTSHRTVLHSTGTDEKNNAVFMIVQPDNVPSSNCAIYSTCTVKYENSTNPINSSESFEEKDVSSNIYNVILTEDQPKIIVHKYVGIMSTEFNKNKEQQDNTNIGLAKMIALNSKGNYEKLLSSHKRAWYDLYNDAFIEIPSDSLLEMTARSSLFHLLANTRDYNVSSDRGLPVGVSGLSSDSYGGMVFWDADIWMEPALLPFFPNVAQNMNNYRNATHSQAKLNAEKYGYPGAIYPWTSGKYANCTSTGPCVDYEYHINVDVAMASFSIYLNGHEGIDDEYLRYTTWPIIKNAAQFFTAYVKYNSSLGLYETYNLTDPDEFANHINNGAFTNAGIKTLLKWATDIGNHLGEVVDPKWSEISKDIYIPRSSSNITLEYSGMNSSVEIKQADVTLMVYPLGYINDESILNNAIKDLYYYSERQSASGPAMTYPVFVAAAAGLLNHGSSSQSYLYKSVLPYLRAPFAQFSEQSDDNFLTNGLTQPAFPFLTANGGFLQSILFGLTGIRYSYEVDPDTKKINRLLRFNPIELPLLPGGIAIRNFKYMNQVLDIIIDDHNGTIVHKSGDVPIHIKIPNRSLIHDQDINFYNGSENERKPNLERRDVDRVGDPMRMDRYGTYYLLKPKQELTVQLFKPGLNARNNIAENKQITNLTAGVPGDVAFSALDGNNYTHWQPLDKIHRAKLLIDLGEYNEKEITKGMILWGQRPAKNISISILPHSEKVENLFANVTEIMQNSGNDQLLNETIGQLLDNAGIPVENVIDFDGIEQEDDESLDDVQALLHWKKEDLAKLIEQIPRLNFLKRKFVKILDNVPVSPSEPYYEASRNQSLIEILPSNRTTFTIDYDKLQVGDKGNTDWRKTRYIVVAVQGVYDDYDDDNKGATIKEIVLND | 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). Vacuolar localization appears to be associated with its degradation (By similarity). {ECO:0000250|UniProtKB:P48016, ECO:0000269|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 | MTTIWEHCVDVDGEVAASTGCFTTLPIRIHRRNDIADDATKQSIHDWGAYVGDGWEQRSGSSWSPVGNWGAFIFPESLPDRLGVITYLANMGNIHDDLCDELPFEEALKEHSNLSQAMEVSNSDTRQCSKASDRSMKMKKYISKCLLEAMEIDRARALRMINSYRSKWLDVMESQNVNDMQTLEEYLAFRNLNGGMEAFWSMVEFGMAIDISESEKTHTRPLFQAAESALVLTNDYWSWDREWRLAQRTQDPRIVNAVHLFMRTEGLSVDQAREKVRERIVDYEREYLRLKEEFYTQNPNLPLYLRRYVEVCGVITAGNHYWCANCPRHHAWRDEESSPSERSFSPSNEGIEDPRLSPGASTTSSMSQKSSPATEITLSDVLGFMAINDNHKPQRSSDMALMAPVQYIRSMPSKGLRSLMVEALDQWLLVDDPELEQIKNIIDLLHNSSLILDDIEDDSPLRRGLPATHTVFGQAQSINSANFMFVQAVQMTQKLNNPASLDTLLDELECLFIGQSWDLYWKFHLQVPTEKEYLEMVDCKTGAMFRLLARLMFHESSVVSGTQVLQLLDEMCRLFGRFFQIRDDFMNLYSTEYSDQKGFCEDLDEGKMSYPLIMLLWQNPGQRDQIMGIFRQQASNTSRGPTSDRSRLPLETKRYVMSLLKGSDIMASTLRKLRDLEAAVDYSISGLEKALGDANPVMRIVLSRLSVRDVSL | 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; Xref=Rhea:RHEA:17654; Evidence={ECO:0000269|Ref.3}; CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:25694, ChEBI:CHEBI:33019, ChEBI:CHEBI:57907, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769; EC=2.5.1.81; Evidence={ECO:0000269|Ref.3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25695; Evidence={ECO:0000269|Ref.3}; | 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) domain of btcA catalyzes formation of GFPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of GFPP into betaestacin I (Ref.3). The cytochrome P450 monooxygenase btcB oxidizes the C25 methyl group of betaestacin I to yield the carboxylic acid betaestacin IV via the alcohol betaestacin III (Ref.3). The cytochrome P450 monooxygenase btcC further catalyzes the multistep oxidation of betaestacin IV to produce several compounds, including betaestacins Va, Vb, Vc and VI (Ref.3). {ECO:0000269|Ref.3}. | Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum lagenarium) |
O00085 | PHYA1_ASPTE | MGFLAIVLSVALLFRSTSGTPLGPRGKHSDCNSVDHGYQCFPELSHKWGLYAPYFSLQDESPFPLDVPEDCHITFVQVLARHGARSPTHSKTKAYAATIAAIQKSATAFPGKYAFLQSYNYSLDSEELTPFGRNQLRDLGAQFYERYNALTRHINPFVRATDASRVHESAEKFVEGFQTARQDDHHANPHQPSPRVDVAIPEGSAYNNTLEHSLCTAFESSTVGDDAVANFTAVFAPAIAQRLEADLPGVQLSTDDVVNLMAMCPFETVSLTDDAHTLSPFCDLFTATEWTQYNYLLSLDKYYGYGGGNPLGPVQGVGWANELMARLTRAPVHDHTCVNNTLDASPATFPLNATLYADFSHDSNLVSIFWALGLYNGTAPLSQTSVESVSQTDGYAAAWTVPFAARAYVEMMQCRAEKEPLVRVLVNDRVMPLHGCPTDKLGRCKRDAFVAGLSFAQAGGNWADCF | 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}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16990; Evidence={ECO:0000269|PubMed:9025298, ECO:0000269|PubMed:9925555}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,2,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77115, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, ChEBI:CHEBI:195535; Evidence={ECO:0000269|PubMed:9925555}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77116; Evidence={ECO:0000269|PubMed:9925555}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,2,6-trisphosphate + phosphate; Xref=Rhea:RHEA:77119, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195535, ChEBI:CHEBI:195537; Evidence={ECO:0000269|PubMed:9925555}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77120; Evidence={ECO:0000269|PubMed:9925555}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,6-trisphosphate + H2O = 1D-myo-inositol 1,2-bisphosphate + phosphate; Xref=Rhea:RHEA:77131, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195537, ChEBI:CHEBI:195539; Evidence={ECO:0000269|PubMed:9925555}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77132; Evidence={ECO:0000269|PubMed:9925555}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2-bisphosphate + H2O = 1D-myo-inositol 2-phosphate + phosphate; Xref=Rhea:RHEA:77135, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:195539; Evidence={ECO:0000269|PubMed:9925555}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77136; Evidence={ECO:0000269|PubMed:9925555}; | 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-monophosphate is the end product (PubMed:9925555). Has a broad substrate specificity and is also able to dephosphorylate other classic acid phosphatase substrates such as p-nitrophenyl phosphate, phenyl phosphate, fructose 1,6-bisphosphate, glucose 6-phosphate, 3-phosphoglycerate, as well as ADP and ATP (PubMed:9925555). {ECO:0000269|PubMed:9025298, ECO:0000269|PubMed:9925555}. | Aspergillus terreus |
O00092 | PHYA_ASPFU | MVTLTFLLSAAYLLSGRVSAAPSSAGSKSCDTVDLGYQCSPATSHLWGQYSPFFSLEDELSVSSKLPKDCRITLVQVLSRHGARYPTSSKSKKYKKLVTAIQANATDFKGKFAFLKTYNYTLGADDLTPFGEQQLVNSGIKFYQRYKALARSVVPFIRASGSDRVIASGEKFIEGFQQAKLADPGATNRAAPAISVIIPESETFNNTLDHGVCTKFEASQLGDEVAANFTALFAPDIRARAEKHLPGVTLTDEDVVSLMDMCSFDTVARTSDASQLSPFCQLFTHNEWKKYNYLQSLGKYYGYGAGNPLGPAQGIGFTNELIARLTRSPVQDHTSTNSTLVSNPATFPLNATMYVDFSHDNSMVSIFFALGLYNGTEPLSRTSVESAKELDGYSASWVVPFGARAYFETMQCKSEKEPLVRALINDRVVPLHGCDVDKLGRCKLNDFVKGLSWARSGGNWGECFS | 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=Rhea:RHEA:16990; Evidence={ECO:0000269|PubMed:9143104, ECO:0000269|PubMed:9925555}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,2,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77115, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, ChEBI:CHEBI:195535; Evidence={ECO:0000269|PubMed:9925555}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77116; Evidence={ECO:0000269|PubMed:9925555}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,2,6-trisphosphate + phosphate; Xref=Rhea:RHEA:77119, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195535, ChEBI:CHEBI:195537; Evidence={ECO:0000269|PubMed:9925555}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77120; Evidence={ECO:0000269|PubMed:9925555}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,6-trisphosphate + H2O = 1D-myo-inositol 1,2-bisphosphate + phosphate; Xref=Rhea:RHEA:77131, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195537, ChEBI:CHEBI:195539; Evidence={ECO:0000269|PubMed:9925555}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77132; Evidence={ECO:0000269|PubMed:9925555}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2-bisphosphate + H2O = 1D-myo-inositol 2-phosphate + phosphate; Xref=Rhea:RHEA:77135, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:195539; Evidence={ECO:0000269|PubMed:9925555}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77136; Evidence={ECO:0000269|PubMed:9925555}; | 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-monophosphate is the end product (PubMed:9143104, PubMed:9925555). Has a broad substrate specificity and is also able to dephosphorylate other classic acid phosphatase substrates such as p-nitrophenyl phosphate, phenyl phosphate, fructose 1,6-bisphosphate, fructose 6-phosphate, glucose 6-phosphate, ribose 5-phosphate, alpha-glycerophosphate, beta-glycerophosphate, 3-phosphoglycerate, phosphoenolpyruvate, as well as ADP and ATP (PubMed:9143104, PubMed:9925555). {ECO:0000269|PubMed:9143104, ECO:0000269|PubMed:9925555}. | Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) |
O00093 | PHYA_EMENI | MAFFTVALSLYYLLSRVSTQAPVVQNHSCNTADGGYQCFPNVSHVWGQYSPYFSIEQESAISEDVPHGCEVTFVQVLSRHGARYPTESKSKAYSGLIEAIQKNATSFWGQYAFLESYNYTLGADDLTIFGENQMVDSGAKFYRRYKNLARKNTPFIRASGSDRVVASAEKFINGFRKAQLHDHGSKRATPVVNVIIPEIDGFNNTLDHSTCVSFENDERADEIEANFTAIMGPPIRKRLENDLPGIKLTNENVIYLMDMCSFDTMARTAHGTELSPFCAIFTEKEWLQYDYLQSLSKYYGYGAGSPLGPAQGIGFTNELIARLTQSPVQDNTSTNHTLDSNPATFPLDRKLYADFSHDNSMISIFFAMGLYNGTQPLSMDSVESIQEMDGYAASWTVPFGARAYFELMQCEKKEPLVRVLVNDRVVPLHGCAVDKFGRCTLDDWVEGLNFARSGGNWKTCFTL | 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}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16990; Evidence={ECO:0000269|PubMed:9349716, ECO:0000269|PubMed:9925555}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,2,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77115, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, ChEBI:CHEBI:195535; Evidence={ECO:0000269|PubMed:9925555}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77116; Evidence={ECO:0000269|PubMed:9925555}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,2,6-trisphosphate + phosphate; Xref=Rhea:RHEA:77119, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195535, ChEBI:CHEBI:195537; Evidence={ECO:0000269|PubMed:9925555}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77120; Evidence={ECO:0000269|PubMed:9925555}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,6-trisphosphate + H2O = 1D-myo-inositol 1,2-bisphosphate + phosphate; Xref=Rhea:RHEA:77131, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195537, ChEBI:CHEBI:195539; Evidence={ECO:0000269|PubMed:9925555}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77132; Evidence={ECO:0000269|PubMed:9925555}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2-bisphosphate + H2O = 1D-myo-inositol 2-phosphate + phosphate; Xref=Rhea:RHEA:77135, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:195539; Evidence={ECO:0000269|PubMed:9925555}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77136; Evidence={ECO:0000269|PubMed:9925555}; | 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-monophosphate is the end product (PubMed:9925555). Has a broad substrate specificity and is also able to dephosphorylate other classic acid phosphatase substrates such as p-nitrophenyl phosphate, phenyl phosphate, fructose 1,6-bisphosphate, fructose 6-phosphate, glucose 6-phosphate, ribose 5-phosphate, alpha-glycerophosphate, beta-glycerophosphate, 3-phosphoglycerate, as well as ADP and ATP (PubMed:9925555). {ECO:0000269|PubMed:9349716, ECO:0000269|PubMed:9925555}. | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
O00100 | PHYA2_ASPTE | MGVFVVLLSIATLFGSTSGTALGPRGNHSDCTSVDRGYQCFPELSHKWGLYAPYFSLQDESPFPLDVPDDCHITFVQVLARHGARSPTDSKTKAYAATIAAIQKNATALPGKYAFLKSYNYSMGSENLNPFGRNQLQDLGAQFYRRYDTLTRHINPFVRAADSSRVHESAEKFVEGFQNARQGDPHANPHQPSPRVDVVIPEGTAYNNTLEHSICTAFEASTVGDAAADNFTAVFAPAIAKRLEADLPGVQLSADDVVNLMAMCPFETVSLTDDAHTLSPFCDLFTAAEWTQYNYLLSLDKYYGYGGGNPLGPVQGVGWANELIARLTRSPVHDHTCVNNTLDANPATFPLNATLYADFSHDSNLVSIFWALGLYNGTKPLSQTTVEDITRTDGYAAAWTVPFAARAYIEMMQCRAEKQPLVRVLVNDRVMPLHGCAVDNLGRCKRDDFVEGLSFARAGGNWAECF | 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=Rhea:RHEA:16990; Evidence={ECO:0000269|PubMed:9925555}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,2,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77115, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, ChEBI:CHEBI:195535; Evidence={ECO:0000269|PubMed:9925555}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77116; Evidence={ECO:0000269|PubMed:9925555}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,2,6-trisphosphate + phosphate; Xref=Rhea:RHEA:77119, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195535, ChEBI:CHEBI:195537; Evidence={ECO:0000269|PubMed:9925555}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77120; Evidence={ECO:0000269|PubMed:9925555}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,6-trisphosphate + H2O = 1D-myo-inositol 1,2-bisphosphate + phosphate; Xref=Rhea:RHEA:77131, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195537, ChEBI:CHEBI:195539; Evidence={ECO:0000269|PubMed:9925555}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77132; Evidence={ECO:0000269|PubMed:9925555}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2-bisphosphate + H2O = 1D-myo-inositol 2-phosphate + phosphate; Xref=Rhea:RHEA:77135, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:195539; Evidence={ECO:0000269|PubMed:9925555}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77136; Evidence={ECO:0000269|PubMed:9925555}; | 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 product (PubMed:9925555). Has a broad substrate specificity and is also able to dephosphorylate other classic acid phosphatase substrates such as p-nitrophenyl phosphate, phenyl phosphate, fructose 1,6-bisphosphate, glucose 6-phosphate, 3-phosphoglycerate, as well as ADP and ATP (PubMed:9925555). {ECO:0000269|PubMed:9925555}. | 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|PROSITE-ProRule:PRU10133}; | 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 of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains, and of the hrd1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M) (By similarity). Together with hrd1, required for the degradation of the transcription factor sre1 precursor in the absence of its binding partner scp1. Has a role in the formation of chromatin structures that influence the localization of transcriptional silencing factors. {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:12456009, ECO:0000269|PubMed:19520858}. | 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 mitotic metaphase/anaphase transition [GO:0030071]; ubiquitin-dependent protein catabolic process [GO:0006511] | 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|PROSITE-ProRule:PRU10133}; | 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 | MIPLLLAALLCVPAGALTCYGDSGQPVDWFVVYKLPALRGSGEAAQRGLQYKYLDESSGGWRDGRALINSPEGAVGRSLQPLYRSNTSQLAFLLYNDQPPQPSKAQDSSMRGHTKGVLLLDHDGGFWLVHSVPNFPPPASSAAYSWPHSACTYGQTLLCVSFPFAQFSKMGKQLTYTYPWVYNYQLEGIFAQEFPDLENVVKGHHVSQEPWNSSITLTSQAGAVFQSFAKFSKFGDDLYSGWLAAALGTNLQVQFWHKTVGILPSNCSDIWQVLNVNQIAFPGPAGPSFNSTEDHSKWCVSPKGPWTCVGDMNRNQGEEQRGGGTLCAQLPALWKAFQPLVKNYQPCNGMARKPSRAYKI | 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 fetal liver and bone marrow, where it degrades nuclear DNA expelled from erythroid precursor cells (PubMed:29259162). {ECO:0000269|PubMed:29259162, ECO:0000269|PubMed:31775019}. | Homo sapiens (Human) |
O00116 | ADAS_HUMAN | MAEAAAAAGGTGLGAGASYGSAADRDRDPDPDRAGRRLRVLSGHLLGRPREALSTNECKARRAASAATAAPTATPAAQESGTIPKKRQEVMKWNGWGYNDSKFIFNKKGQIELTGKRYPLSGMGLPTFKEWIQNTLGVNVEHKTTSKASLNPSDTPPSVVNEDFLHDLKETNISYSQEADDRVFRAHGHCLHEIFLLREGMFERIPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADETRTIISLDTSQMNRILWVDENNLTAHVEAGITGQELERQLKESGYCTGHEPDSLEFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRGIIEKSCQGPRMSTGPDIHHFIMGSEGTLGVITEATIKIRPVPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNKQFQFGHALKPQVSSIFTSFLDGLKKFYITKFKGFDPNQLSVATLLFEGDREKVLQHEKQVYDIAAKFGGLAAGEDNGQRGYLLTYVIAYIRDLALEYYVLGESFETSAPWDRVVDLCRNVKERITRECKEKGVQFAPFSTCRVTQTYDAGACIYFYFAFNYRGISDPLTVFEQTEAAAREEILANGGSLSHHHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNIFGNRNLL | 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:8399344, ECO:0000269|PubMed:9553082}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36172; Evidence={ECO:0000305|PubMed:8399344, ECO:0000305|PubMed:9553082}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoylglycerone 3-phosphate + hexadecan-1-ol = 1-O-hexadecylglycerone 3-phosphate + H(+) + hexadecanoate; Xref=Rhea:RHEA:40659, ChEBI:CHEBI:7896, ChEBI:CHEBI:15378, ChEBI:CHEBI:16125, ChEBI:CHEBI:58303, ChEBI:CHEBI:77429; Evidence={ECO:0000269|PubMed:9553082}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40660; Evidence={ECO:0000305|PubMed:9553082}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoylglycerone 3-phosphate + a long-chain fatty acid = a 1-acylglycerone 3-phosphate + hexadecanoate; Xref=Rhea:RHEA:40727, ChEBI:CHEBI:7896, ChEBI:CHEBI:57534, ChEBI:CHEBI:57560, ChEBI:CHEBI:58303; Evidence={ECO:0000250|UniProtKB:Q8C0I1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40728; Evidence={ECO:0000250|UniProtKB:Q8C0I1}; | 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:9553082}. | 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 | MATANFGKIQIGIYVEIKRSDGRIHQAMVTSLNEDNESVTVEWIENGDTKGKEIDLESIFSLNPDLVPDEEIEPSPETPPPPASSAKVNKIVKNRRTVASIKNDPPSRDNRVVGSARARPSQFPEQSSSAQQNGSVSDISPVQAAKKEFGPPSRRKSNCVKEVEKLQEKREKRRLQQQELREKRAQDVDATNPNYEIMCMIRDFRGSLDYRPLTTADPIDEHRICVCVRKRPLNKKETQMKDLDVITIPSKDVVMVHEPKQKVDLTRYLENQTFRFDYAFDDSAPNEMVYRFTARPLVETIFERGMATCFAYGQTGSGKTHTMGGDFSGKNQDCSKGIYALAARDVFLMLKKPNYKKLELQVYATFFEIYSGKVFDLLNRKTKLRVLEDGKQQVQVVGLQEREVKCVEDVLKLIDIGNSCRTSGQTSANAHSSRSHAVFQIILRRKGKLHGKFSLIDLAGNERGADTSSADRQTRLEGAEINKSLLALKECIRALGRNKPHTPFRASKLTQVLRDSFIGENSRTCMIATISPGMASCENTLNTLRYANRVKELTVDPTAAGDVRPIMHHPPNQIDDLETQWGVGSSPQRDDLKLLCEQNEEEVSPQLFTFHEAVSQMVEMEEQVVEDHRAVFQESIRWLEDEKALLEMTEEVDYDVDSYATQLEAILEQKIDILTELRDKVKSFRAALQEEEQASKQINPKRPRAL | 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]; regulation of cell migration [GO:0030334] | 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]; spindle pole [GO:0000922] | 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 and spindle poles requires the kinase activity of PLK1. Recruited to mitotic spindles by interaction with PSRC1. | 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. Promotes spindle turnover. Implicated in formation of bipolar mitotic spindles. Has microtubule depolymerization activity. {ECO:0000269|PubMed:15843429, ECO:0000269|PubMed:17538014, ECO:0000269|PubMed:18411309}. | Homo sapiens (Human) |
O00141 | SGK1_HUMAN | MTVKTEAAKGTLTYSRMRGMVAILIAFMKQRRMGLNDFIQKIANNSYACKHPEVQSILKISQPQEPELMNANPSPPPSPSQQINLGPSSNPHAKPSDFHFLKVIGKGSFGKVLLARHKAEEVFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTADKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEHNSTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDRTKRLGAKDDFMEIKSHVFFSLINWDDLINKKITPPFNPNVSGPNDLRHFDPEFTEEPVPNSIGKSPDSVLVTASVKEAAEAFLGFSYAPPTDSFL | 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 [GO:0006468]; regulation of apoptotic process [GO:0042981]; regulation of blood pressure [GO:0008217]; regulation of catalytic activity [GO:0050790]; regulation of cell growth [GO:0001558]; regulation of cell migration [GO:0030334]; regulation of cell population proliferation [GO:0042127]; regulation of DNA-binding transcription factor activity [GO:0051090]; regulation of gastric acid secretion [GO:0060453]; regulation of signal transduction by p53 class mediator [GO:1901796]; renal sodium ion absorption [GO:0070294]; sodium ion transport [GO:0006814] | 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 activity [GO:0004712]; sodium channel regulator activity [GO:0017080] | 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). Phosphorylation on Ser-397 and Ser-401 are also essential for its activity (PubMed:19068477). Phosphorylation on Ser-78 by MAPK7 is required for growth factor-induced cell cycle progression (PubMed:11254654). {ECO:0000269|PubMed:10191262, ECO:0000269|PubMed:11096081, ECO:0000269|PubMed:11254654, ECO:0000269|PubMed:18925875, ECO:0000269|PubMed:19068477, ECO:0000269|PubMed:20338997, ECO:0000269|PubMed:36373794}.; PTM: Ubiquitinated by NEDD4L; which promotes proteasomal degradation. Ubiquitinated by SYVN1 at the endoplasmic reticulum; which promotes rapid proteasomal degradation and maintains a high turnover rate in resting cells. Isoform 2 shows enhanced stability. {ECO:0000269|PubMed:15576372}. | 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 in synchrony with the cell cycle, and in serum/growth factor-stimulated cells it resides in the nucleus. In contrast, after exposure to environmental stress or treatment with glucocorticoids, it is detected in the cytoplasm and with certain stress conditions is associated with the mitochondria. In osmoregulation through the epithelial sodium channel, it can be localized to the cytoplasmic surface of the cell membrane. Nuclear, upon phosphorylation.; SUBCELLULAR LOCATION: [Isoform 2]: Cell 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-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; | 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. Contributes to regulation of renal Na(+) retention, renal K(+) elimination, salt appetite, gastric acid secretion, intestinal Na(+)/H(+) exchange and nutrient transport, insulin-dependent salt sensitivity of blood pressure, salt sensitivity of peripheral glucose uptake, cardiac repolarization and memory consolidation. Up-regulates Na(+) channels: SCNN1A/ENAC, SCN5A and ASIC1/ACCN2, K(+) channels: KCNJ1/ROMK1, KCNA1-5, KCNQ1-5 and KCNE1, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channels: BSND, CLCN2 and CFTR, glutamate transporters: SLC1A3/EAAT1, SLC1A2 /EAAT2, SLC1A1/EAAT3, SLC1A6/EAAT4 and SLC1A7/EAAT5, amino acid transporters: SLC1A5/ASCT2, SLC38A1/SN1 and SLC6A19, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, glutamate receptor: GRIK2/GLUR6. Up-regulates carriers: SLC9A3/NHE3, SLC12A1/NKCC2, SLC12A3/NCC, SLC5A3/SMIT, SLC2A1/GLUT1, SLC5A1/SGLT1 and SLC15A2/PEPT2. Regulates enzymes: GSK3A/B, PMM2 and Na(+)/K(+) ATPase, and transcription factors: CTNNB1 and nuclear factor NF-kappa-B. Stimulates sodium transport into epithelial cells by enhancing the stability and expression of SCNN1A/ENAC. This is achieved by phosphorylating the NEDD4L ubiquitin E3 ligase, promoting its interaction with 14-3-3 proteins, thereby preventing it from binding to SCNN1A/ENAC and targeting it for degradation. Regulates store-operated Ca(+2) entry (SOCE) by stimulating ORAI1 and STIM1. Regulates KCNJ1/ROMK1 directly via its phosphorylation or indirectly via increased interaction with SLC9A3R2/NHERF2. Phosphorylates MDM2 and activates MDM2-dependent ubiquitination of p53/TP53. Phosphorylates MAPT/TAU and mediates microtubule depolymerization and neurite formation in hippocampal neurons. Phosphorylates SLC2A4/GLUT4 and up-regulates its activity. Phosphorylates APBB1/FE65 and promotes its localization to the nucleus. Phosphorylates MAPK1/ERK2 and activates it by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. Phosphorylates FBXW7 and plays an inhibitory role in the NOTCH1 signaling. Phosphorylates FOXO1 resulting in its relocalization from the nucleus to the cytoplasm. Phosphorylates FOXO3, promoting its exit from the nucleus and interference with FOXO3-dependent transcription. Phosphorylates BRAF and MAP3K3/MEKK3 and inhibits their activity. Phosphorylates SLC9A3/NHE3 in response to dexamethasone, resulting in its activation and increased localization at the cell membrane. Phosphorylates CREB1. Necessary for vascular remodeling during angiogenesis. Sustained high levels and activity may contribute to conditions such as hypertension and diabetic nephropathy. Isoform 2 exhibited a greater effect on cell plasma membrane expression of SCNN1A/ENAC and Na(+) transport than isoform 1. {ECO:0000269|PubMed:11154281, ECO:0000269|PubMed:11410590, ECO:0000269|PubMed:11696533, ECO:0000269|PubMed:12397388, ECO:0000269|PubMed:12590200, ECO:0000269|PubMed:12634932, ECO:0000269|PubMed:12650886, ECO:0000269|PubMed:12761204, ECO:0000269|PubMed:12911626, ECO:0000269|PubMed:14623317, ECO:0000269|PubMed:14706641, ECO:0000269|PubMed:15040001, ECO:0000269|PubMed:15044175, ECO:0000269|PubMed:15234985, ECO:0000269|PubMed:15319523, ECO:0000269|PubMed:15496163, ECO:0000269|PubMed:15733869, ECO:0000269|PubMed:15737648, ECO:0000269|PubMed:15845389, ECO:0000269|PubMed:15888551, ECO:0000269|PubMed:16036218, ECO:0000269|PubMed:16443776, ECO:0000269|PubMed:16982696, ECO:0000269|PubMed:17382906, ECO:0000269|PubMed:18005662, ECO:0000269|PubMed:18304449, ECO:0000269|PubMed:18753299, ECO:0000269|PubMed:19447520, ECO:0000269|PubMed:19756449, ECO:0000269|PubMed:20511718, ECO:0000269|PubMed:20730100, ECO:0000269|PubMed:21865597}. | 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:19130; Evidence={ECO:0000269|PubMed:11687801, ECO:0000269|PubMed:9989599}; CATALYTIC ACTIVITY: Reaction=2'-deoxycytidine + ATP = ADP + dCMP + H(+); Xref=Rhea:RHEA:46040, ChEBI:CHEBI:15378, ChEBI:CHEBI:15698, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:456216; EC=2.7.1.74; Evidence={ECO:0000269|PubMed:11687801, ECO:0000305|PubMed:9989599}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46041; Evidence={ECO:0000269|PubMed:11687801, ECO:0000305|PubMed:9989599}; CATALYTIC ACTIVITY: Reaction=2'-deoxyuridine + ATP = ADP + dUMP + H(+); Xref=Rhea:RHEA:28206, ChEBI:CHEBI:15378, ChEBI:CHEBI:16450, ChEBI:CHEBI:30616, ChEBI:CHEBI:246422, ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:9989599}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28207; Evidence={ECO:0000305|PubMed:9989599}; | 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 chemotherapeutic agents (PubMed:9989599). {ECO:0000269|PubMed:11687801, ECO:0000269|PubMed:9989599}. | Homo sapiens (Human) |
O00144 | FZD9_HUMAN | MAVAPLRGALLLWQLLAAGGAALEIGRFDPERGRGAAPCQAVEIPMCRGIGYNLTRMPNLLGHTSQGEAAAELAEFAPLVQYGCHSHLRFFLCSLYAPMCTDQVSTPIPACRPMCEQARLRCAPIMEQFNFGWPDSLDCARLPTRNDPHALCMEAPENATAGPAEPHKGLGMLPVAPRPARPPGDLGPGAGGSGTCENPEKFQYVEKSRSCAPRCGPGVEVFWSRRDKDFALVWMAVWSALCFFSTAFTVLTFLLEPHRFQYPERPIIFLSMCYNVYSLAFLIRAVAGAQSVACDQEAGALYVIQEGLENTGCTLVFLLLYYFGMASSLWWVVLTLTWFLAAGKKWGHEAIEAHGSYFHMAAWGLPALKTIVILTLRKVAGDELTGLCYVASTDAAALTGFVLVPLSGYLVLGSSFLLTGFVALFHIRKIMKTGGTNTEKLEKLMVKIGVFSILYTVPATCVIVCYVYERLNMDFWRLRATEQPCAAAAGPGGRRDCSLPGGSVPTVAVFMLKIFMSLVVGITSGVWVWSSKTFQTWQSLCYRKIAAGRARAKACRAPGSYGRGTHCHYKAPTVVLHMTKTDPSLENPTHL | 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 pathway [GO:1901029]; negative regulation of necroptotic process [GO:0060546]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of skeletal muscle acetylcholine-gated channel clustering [GO:1904394]; nervous system development [GO:0007399]; neuroblast proliferation [GO:0007405]; non-canonical Wnt signaling pathway [GO:0035567]; ossification [GO:0001503]; positive regulation of apoptotic process [GO:0043065]; positive regulation of bone mineralization [GO:0030501]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of neural precursor cell proliferation [GO:2000179]; postsynapse organization [GO:0099173]; regulation of cell cycle [GO:0051726]; regulation of cytosolic calcium ion concentration [GO:0051480]; regulation of postsynaptic cytosolic calcium ion concentration [GO:0099566]; regulation of skeletal muscle acetylcholine-gated channel clustering [GO:1904393]; release of cytochrome c from mitochondria [GO:0001836] | 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 [GO:0005886]; postsynapse [GO:0098794] | 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 negatively regulating the clustering of acetylcholine receptors (AChR) through the beta-catenin canonical signaling pathway (By similarity). May play a role in neural progenitor cells (NPCs) viability through the beta-catenin canonical signaling pathway by negatively regulating cell cycle arrest leading to inhibition of neuron apoptotic process (PubMed:27509850). During hippocampal development, regulates neuroblast proliferation and apoptotic cell death. Controls bone formation through non canonical Wnt signaling mediated via ISG15. Positively regulates bone regeneration through non canonical Wnt signaling (By similarity). {ECO:0000250|UniProtKB:Q8K4C8, ECO:0000250|UniProtKB:Q9R216, ECO:0000269|PubMed:27509850}. | Homo sapiens (Human) |
O00148 | DX39A_HUMAN | MAEQDVENDLLDYDEEEEPQAPQESTPAPPKKDIKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQIEPVNGQVTVLVMCHTRELAFQISKEYERFSKYMPSVKVSVFFGGLSIKKDEEVLKKNCPHVVVGTPGRILALVRNRSFSLKNVKHFVLDECDKMLEQLDMRRDVQEIFRLTPHEKQCMMFSATLSKDIRPVCRKFMQDPMEVFVDDETKLTLHGLQQYYVKLKDSEKNRKLFDLLDVLEFNQVIIFVKSVQRCMALAQLLVEQNFPAIAIHRGMAQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIVFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSDENDAKILNDVQDRFEVNVAELPEEIDISTYIEQSR | 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 | MTTQQIDLQGPGPWGFRLVGGKDFEQPLAISRVTPGSKAALANLCIGDVITAIDGENTSNMTHLEAQNRIKGCTDNLTLTVARSEHKVWSPLVTEEGKRHPYKMNLASEPQEVLHIGSAHNRSAMPFTASPASSTTARVITNQYNNPAGLYSSENISNFNNALESKTAASGVEANSRPLDHAQPPSSLVIDKESEVYKMLQEKQELNEPPKQSTSFLVLQEILESEEKGDPNKPSGFRSVKAPVTKVAASIGNAQKLPMCDKCGTGIVGVFVKLRDRHRHPECYVCTDCGTNLKQKGHFFVEDQIYCEKHARERVTPPEGYEVVTVFPK | 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 II [GO:0006357]; response to hypoxia [GO:0001666]; response to oxidative stress [GO:0006979]; stress fiber assembly [GO:0043149] | 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 and in maintaining cell polarity of fibroblasts (By similarity). {ECO:0000250|UniProtKB:P52944, ECO:0000269|PubMed:10861853}. | Homo sapiens (Human) |
O00154 | BACH_HUMAN | MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVPLSLKNVDKVLEVPPVVYSRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHAEPQP | 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 biosynthetic process [GO:1900535] | 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|PubMed:12435388}. | 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={ECO:0000305|PubMed:10578051}; CATALYTIC ACTIVITY: Reaction=H2O + octanoyl-CoA = CoA + H(+) + octanoate; Xref=Rhea:RHEA:30143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386; Evidence={ECO:0000305|PubMed:10578051}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144; Evidence={ECO:0000305|PubMed:10578051}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+); Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375; Evidence={ECO:0000305|PubMed:10578051}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000305|PubMed:10578051}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000305|PubMed:10578051}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence={ECO:0000305|PubMed:10578051}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate; Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385; Evidence={ECO:0000250|UniProtKB:Q64559}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence={ECO:0000250|UniProtKB:Q64559}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+); Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430; Evidence={ECO:0000250|UniProtKB:Q64559}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence={ECO:0000250|UniProtKB:Q64559}; CATALYTIC ACTIVITY: Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate; Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394; Evidence={ECO:0000250|UniProtKB:Q64559}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140; Evidence={ECO:0000250|UniProtKB:Q64559}; | 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 an important physiological function in brain (PubMed:10578051). {ECO:0000269|PubMed:10578051}. | Homo sapiens (Human) |
O00155 | GPR25_HUMAN | MAPTEPWSPSPGSAPWDYSGLDGLEELELCPAGDLPYGYVYIPALYLAAFAVGLLGNAFVVWLLAGRRGPRRLVDTFVLHLAAADLGFVLTLPLWAAAAALGGRWPFGDGLCKLSSFALAGTRCAGALLLAGMSVDRYLAVVKLLEARPLRTPRCALASCCGVWAVALLAGLPSLVYRGLQPLPGGQDSQCGEEPSHAFQGLSLLLLLLTFVLPLVVTLFCYCRISRRLRRPPHVGRARRNSLRIIFAIESTFVGSWLPFSALRAVFHLARLGALPLPCPLLLALRWGLTIATCLAFVNSCANPLIYLLLDRSFRARALDGACGRTGRLARRISSASSLSRDDSSVFRCRAQAANTASASW | 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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