{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8L8W5","uniProtkbId":"A0A9W8L8W5_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":10,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750677.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Pentafunctional AROM polypeptide"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-dehydroquinate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"DHQS"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"4.2.3.4"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-phosphoshikimate 1-carboxyvinyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"2.5.1.19"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"5-enolpyruvylshikimate-3-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"EPSP synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"EPSPS"}]}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Shikimate kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"SK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"2.7.1.71"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-dehydroquinate dehydratase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-dehydroquinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"4.2.1.10"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Shikimate dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"1.1.1.25"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750677.1"}],"value":"ARO1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750677.1"}],"value":"GGI19_004965"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-dehydroquinate = 3-dehydroshikimate + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21096"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16630"},{"database":"ChEBI","id":"CHEBI:32364"}],"ecNumber":"4.2.1.10","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21256"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57701"},{"database":"ChEBI","id":"CHEBI:58702"},{"database":"ChEBI","id":"CHEBI:145989"}],"ecNumber":"2.5.1.19","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044633"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:21257"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044633"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21968"},{"database":"ChEBI","id":"CHEBI:32364"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58394"}],"ecNumber":"4.2.3.4","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"shikimate + ATP = 3-phosphoshikimate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13121"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:36208"},{"database":"ChEBI","id":"CHEBI:145989"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.71","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048567"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"shikimate + NADP(+) = 3-dehydroshikimate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17737"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16630"},{"database":"ChEBI","id":"CHEBI:36208"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.1.1.25","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Binds 2 Zn(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004811"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009948"}],"value":"Belongs to the EPSP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the 2nd section; belongs to the EPSP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006477"}],"value":"In the 2nd section; belongs to the type-I 3-dehydroquinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the 3rd section; belongs to the shikimate kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the 4th section; belongs to the type-I 3-dehydroquinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the C-terminal section; belongs to the shikimate dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the N-terminal section; belongs to the dehydroquinate synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009349"}],"value":"In the N-terminal section; belongs to the shikimate kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"In the N-terminal section; belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750677.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01761"}]},{"type":"Domain","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":372,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF24621"}]},{"type":"Domain","location":{"start":{"value":423,"modifier":"EXACT"},"end":{"value":849,"modifier":"EXACT"}},"description":"Enolpyruvate transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00275"}]},{"type":"Domain","location":{"start":{"value":1304,"modifier":"EXACT"},"end":{"value":1384,"modifier":"EXACT"}},"description":"Shikimate dehydrogenase substrate binding N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08501"}]},{"type":"Domain","location":{"start":{"value":1409,"modifier":"EXACT"},"end":{"value":1491,"modifier":"EXACT"}},"description":"Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01488"}]},{"type":"Domain","location":{"start":{"value":1529,"modifier":"EXACT"},"end":{"value":1558,"modifier":"EXACT"}},"description":"SDH C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF18317"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Region","location":{"start":{"value":1299,"modifier":"EXACT"},"end":{"value":1566,"modifier":"EXACT"}},"description":"Shikimate dehydrogenase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"Proton acceptor; for 3-dehydroquinate synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"Proton acceptor; for 3-dehydroquinate synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":837,"modifier":"EXACT"},"end":{"value":837,"modifier":"EXACT"}},"description":"For EPSP synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":1188,"modifier":"EXACT"},"end":{"value":1188,"modifier":"EXACT"}},"description":"Proton acceptor; for 3-dehydroquinate dehydratase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":1218,"modifier":"EXACT"},"end":{"value":1218,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Binding site","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":262,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":283,"modifier":"EXACT"},"end":{"value":283,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":283,"modifier":"EXACT"},"end":{"value":283,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":371,"modifier":"EXACT"},"end":{"value":371,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":883,"modifier":"EXACT"},"end":{"value":890,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0057","category":"Biological process","name":"Aromatic amino acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750677.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750677.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000514","properties":[{"key":"ProteinId","value":"KAJ2750677.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"OrthoDB","id":"204377at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003855","properties":[{"key":"GoTerm","value":"F:3-dehydroquinate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003856","properties":[{"key":"GoTerm","value":"F:3-dehydroquinate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003866","properties":[{"key":"GoTerm","value":"F:3-phosphoshikimate 1-carboxyvinyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004764","properties":[{"key":"GoTerm","value":"F:shikimate 3-dehydrogenase (NADP+) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004765","properties":[{"key":"GoTerm","value":"F:shikimate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009073","properties":[{"key":"GoTerm","value":"P:aromatic amino acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009423","properties":[{"key":"GoTerm","value":"P:chorismate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00502","properties":[{"key":"EntryName","value":"DHQase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08195","properties":[{"key":"EntryName","value":"DHQS"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01556","properties":[{"key":"EntryName","value":"EPSP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01065","properties":[{"key":"EntryName","value":"NAD_bind_Shikimate_DH"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00464","properties":[{"key":"EntryName","value":"SK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1970:FF:000007","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.65.10.10:FF:000007","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1970","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1090.10","properties":[{"key":"EntryName","value":"Dehydroquinate synthase-like - alpha domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.65.10.10","properties":[{"key":"EntryName","value":"Enolpyruvate transferase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.10860","properties":[{"key":"EntryName","value":"Leucine Dehydrogenase, chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00210","properties":[{"key":"EntryName","value":"EPSP_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03143","properties":[{"key":"EntryName","value":"Pentafunct_AroM"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00222","properties":[{"key":"EntryName","value":"Shikimate_DH_AroE"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00109","properties":[{"key":"EntryName","value":"Shikimate_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR046346","properties":[{"key":"EntryName","value":"Aminoacid_DH-like_N_sf"}]},{"database":"InterPro","id":"IPR016037","properties":[{"key":"EntryName","value":"DHQ_synth_AroB"}]},{"database":"InterPro","id":"IPR030960","properties":[{"key":"EntryName","value":"DHQS/DOIS_N"}]},{"database":"InterPro","id":"IPR056179","properties":[{"key":"EntryName","value":"DHQS_C"}]},{"database":"InterPro","id":"IPR001381","properties":[{"key":"EntryName","value":"DHquinase_I"}]},{"database":"InterPro","id":"IPR001986","properties":[{"key":"EntryName","value":"Enolpyruvate_Tfrase_dom"}]},{"database":"InterPro","id":"IPR036968","properties":[{"key":"EntryName","value":"Enolpyruvate_Tfrase_sf"}]},{"database":"InterPro","id":"IPR006264","properties":[{"key":"EntryName","value":"EPSP_synthase"}]},{"database":"InterPro","id":"IPR023193","properties":[{"key":"EntryName","value":"EPSP_synthase_CS"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR008289","properties":[{"key":"EntryName","value":"Pentafunct_AroM"}]},{"database":"InterPro","id":"IPR013792","properties":[{"key":"EntryName","value":"RNA3'P_cycl/enolpyr_Trfase_a/b"}]},{"database":"InterPro","id":"IPR041121","properties":[{"key":"EntryName","value":"SDH_C"}]},{"database":"InterPro","id":"IPR031322","properties":[{"key":"EntryName","value":"Shikimate/glucono_kinase"}]},{"database":"InterPro","id":"IPR013708","properties":[{"key":"EntryName","value":"Shikimate_DH-bd_N"}]},{"database":"InterPro","id":"IPR010110","properties":[{"key":"EntryName","value":"Shikimate_DH_AroM-type"}]},{"database":"InterPro","id":"IPR022893","properties":[{"key":"EntryName","value":"Shikimate_DH_fam"}]},{"database":"InterPro","id":"IPR000623","properties":[{"key":"EntryName","value":"Shikimate_kinase/TSH1"}]},{"database":"InterPro","id":"IPR023000","properties":[{"key":"EntryName","value":"Shikimate_kinase_CS"}]},{"database":"InterPro","id":"IPR006151","properties":[{"key":"EntryName","value":"Shikm_DH/Glu-tRNA_Rdtase"}]},{"database":"NCBIfam","id":"TIGR01356","properties":[{"key":"EntryName","value":"aroA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01357","properties":[{"key":"EntryName","value":"aroB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01093","properties":[{"key":"EntryName","value":"aroD"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01809","properties":[{"key":"EntryName","value":"Shik-DH-AROM"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21090","properties":[{"key":"EntryName","value":"AROM/DEHYDROQUINATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21090:SF5","properties":[{"key":"EntryName","value":"PENTAFUNCTIONAL AROM POLYPEPTIDE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01761","properties":[{"key":"EntryName","value":"DHQ_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF24621","properties":[{"key":"EntryName","value":"DHQS_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01487","properties":[{"key":"EntryName","value":"DHquinase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00275","properties":[{"key":"EntryName","value":"EPSP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF18317","properties":[{"key":"EntryName","value":"SDH_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01488","properties":[{"key":"EntryName","value":"Shikimate_DH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08501","properties":[{"key":"EntryName","value":"Shikimate_dh_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01202","properties":[{"key":"EntryName","value":"SKI"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000514","properties":[{"key":"EntryName","value":"Pentafunct_AroM"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01100","properties":[{"key":"EntryName","value":"SHIKIMTKNASE"}]},{"database":"SUPFAM","id":"SSF51569","properties":[{"key":"EntryName","value":"Aldolase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53223","properties":[{"key":"EntryName","value":"Aminoacid dehydrogenase-like, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56796","properties":[{"key":"EntryName","value":"Dehydroquinate synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55205","properties":[{"key":"EntryName","value":"EPT/RTPC-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00104","properties":[{"key":"EntryName","value":"EPSP_SYNTHASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01128","properties":[{"key":"EntryName","value":"SHIKIMATE_KINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MARALKLAEVERIPILGTESIVCGFHLVDYIWTDIFSSLPAASTYVLITDTNLAKLYLSQYQESFQVAWAHHNQASAAPRLLTHVLPPGELSKSRATKSAIEDWMFSEKCTRDTMVLALGGGVIGDLVGYVAATFMRGVGFIQIPTSLLAMVDSSIGGKTAVDTPAGKNLVGAFWQPKRIYMDMAVLSTLPPREFSNGMAEVIKTAAIWDSAEFDVLESSSVEIRRAVLSGTQDGDAGLTLATRSAEQTLLQRVIAASARVKAYVVTHDERESGMRGLLNFGHTIGHAIEAILSPQVLHGECVAVGCVLEAEVARRMGHLSEVGVARLVRCLRAYGLPTTMDDPLIRGLASSEQLAEVRPQRLMDVMGVDKKTVGTQKRLVVLKQLGATLELKPTNVSDALILEVISAGVLVKPVDDGAVAETVVVPPGSKSISNRALQLAALGKGVCRLRNLLHSDDTQVMMAALQAMGGCEFAWEDGGDTLVVTGGGGALHTPATELYLGNAGTAARFLTTTVNLINSGGESTVLTGNARMKLRPCAPLVDALRANGCTIDYCEKQGSLPLRVSHSGGRGFPGGRIQLAASVSSQYVSSILLCAPYAQEPVRLELVGGKVISQPYIDMTLAMMAQFGCHVQRISETEYLVPLGAYENPAEYVVESDASSATYPLAFAAITGRQCTVPNIGSASLQGDARFAVDVLRPMGCTVEQTATSTTVRGPPRGQLQALGDIDMEPMTDAFLTASVLAAVAPGNGGVTRIRGIANQHVKECDRIQAMCTELARFGVTAVNHADGIDVHARSIDELTRATPSVHCYDDHRVAMSFSVLACVAPGGAELRERRCVGKTWPQWWDVLARDLGAPIAGADPQAEHAEAESVKVSSPSVVVVGMRGAGKSTLSKAAASALGLTFVDMDEYLEQQVGQTIPEIIASEGGWPAFRAHESRLLAQALTKDFATGAIIACGGGVVEAPDNRTLLQRHMSSNGAVICLTPNMDQVAEFLSRDKTRPAYAAGDARDVYERRKPLYKDASNYEMLVDARLPGAWPKIEQEFVRLVSFASGRDCNRVDLAHSSYFVSLTAKDVGEYLENGRLAAVTAGAHAVELRADLLAAIDEEDVLAKVQWQFAMLRHATSLPVVFTVRTVAQGGAFRGSDAQRLSILHAAIRWGAEYVDVEVDTHAAALYAARRNSLIIASHHDPTGQQLRWSQCEFTTEILHRARACGDIVKLISFANQWSDNMDCLEFTRRRHSQETPLIALNMGYEGQMSRVLCPVLTPVTHPLLAAKAAPGQISVQQINVARATAGLLPARKMALCGTPIQHSPSPAMHNAAFSALGLPHVYGLFETAEASELADLFAAPEFGGASVTIPLKQSVISLLDQLTPAARRIGAVNTVIPAGGKLLGDNTDYLGIVGCLRRSQVTAFPKATALVVGAGGTSRAALYALYTLGIGSVMVYNRTAQRANELVAEFSELFTSLVAISDLAAIESPDYVVGTIPASDLVYPDSLFAKVGVALDMAYKPRWTPLLESANRHGWSVVPGVDVLIEQGIHQLEKWTHLTAPTKIMADAVYTKYNADN","length":1566,"molWeight":167496,"crc64":"9F6FD9742230CF87","md5":"BCA21DC14A70E3CFB8F9FBD4B934FED8"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":5,"COFACTOR":1,"PATHWAY":5,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":9,"CAUTION":2},"countByFeatureType":{"Domain":6,"Region":2,"Active site":5,"Binding site":20},"uniParcId":"UPI0022DAB569"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GMI2","uniProtkbId":"A0A9W8GMI2_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":11,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2742692.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00026218"}],"value":"Oxidized purine nucleoside triphosphate hydrolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00026103"}],"value":"3.6.1.56"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031927"}],"value":"2-hydroxy-dATP diphosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030682"}],"value":"7,8-dihydro-8-oxoguanine triphosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030634"}],"value":"8-oxo-dGTPase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032071"}],"value":"Methylated purine nucleoside triphosphate hydrolase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029673"}],"value":"Nucleoside diphosphate-linked moiety X motif 1"}}],"flag":"Fragment"},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2742692.1"}],"value":"GGI19_006785"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00053094"}],"value":"Oxidized purine nucleoside triphosphate hydrolase which is a prominent sanitizer of the oxidized nucleotide pool. Catalyzes the hydrolysis of 2-oxo-dATP (2-hydroxy-dATP) into 2-oxo-dAMP. Also has a significant hydrolase activity toward 2-oxo-ATP, 8-oxo-dGTP and 8-oxo-dATP. Through the hydrolysis of oxidized purine nucleoside triphosphates, prevents their incorporation into DNA and the subsequent transversions A:T to C:G and G:C to T:A. Also catalyzes the hydrolysis of methylated purine nucleoside triphosphate preventing their integration into DNA. Through this antimutagenic activity protects cells from oxidative stress"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-oxo-ATP + H2O = 2-oxo-AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67392"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:71395"},{"database":"ChEBI","id":"CHEBI:172878"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024596"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:67393"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024596"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-oxo-dATP + H2O = 2-oxo-dAMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:31583"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:63212"},{"database":"ChEBI","id":"CHEBI:77897"}],"ecNumber":"3.6.1.56","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024459"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:31584"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024459"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"8-oxo-dATP + H2O = 8-oxo-dAMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65396"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:71361"},{"database":"ChEBI","id":"CHEBI:172871"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024448"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65397"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024448"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:31575"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:63224"},{"database":"ChEBI","id":"CHEBI:77896"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024486"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:31576"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024486"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-methyl-ATP + H2O = N(6)-methyl-AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67608"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:144842"},{"database":"ChEBI","id":"CHEBI:172873"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048002"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:67609"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048002"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-methyl-dATP + H2O = N(6)-methyl-dAMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67604"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:169976"},{"database":"ChEBI","id":"CHEBI:172872"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049032"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:67605"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049032"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"O(6)-methyl-dGTP + H2O = O(6)-methyl-dGMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67600"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:169974"},{"database":"ChEBI","id":"CHEBI:169975"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048894"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:67601"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048894"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005582"}],"value":"Belongs to the Nudix hydrolase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2742692.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"Nudix hydrolase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51462"}]},{"type":"Motif","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"Nudix box","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00794"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2742692.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2742692.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00794"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00794"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2742692.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2742692.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010001777","properties":[{"key":"ProteinId","value":"KAJ2742692.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GMI2","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"447842at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0008413","properties":[{"key":"GoTerm","value":"F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008828","properties":[{"key":"GoTerm","value":"F:dATP diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042262","properties":[{"key":"GoTerm","value":"P:DNA protection"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd03427","properties":[{"key":"EntryName","value":"NUDIX_MTH1_Nudt1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.79.10","properties":[{"key":"EntryName","value":"Nucleoside Triphosphate Pyrophosphohydrolase"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR003563","properties":[{"key":"EntryName","value":"8ODP"}]},{"database":"InterPro","id":"IPR015797","properties":[{"key":"EntryName","value":"NUDIX_hydrolase-like_dom_sf"}]},{"database":"InterPro","id":"IPR020084","properties":[{"key":"EntryName","value":"NUDIX_hydrolase_CS"}]},{"database":"InterPro","id":"IPR000086","properties":[{"key":"EntryName","value":"NUDIX_hydrolase_dom"}]},{"database":"PANTHER","id":"PTHR43758","properties":[{"key":"EntryName","value":"7,8-DIHYDRO-8-OXOGUANINE TRIPHOSPHATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43758:SF2","properties":[{"key":"EntryName","value":"OXIDIZED PURINE NUCLEOSIDE TRIPHOSPHATE HYDROLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00293","properties":[{"key":"EntryName","value":"NUDIX"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01403","properties":[{"key":"EntryName","value":"8OXTPHPHTASE"}]},{"database":"SUPFAM","id":"SSF55811","properties":[{"key":"EntryName","value":"Nudix"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51462","properties":[{"key":"EntryName","value":"NUDIX"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00893","properties":[{"key":"EntryName","value":"NUDIX_BOX"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"ECGLEAKDMQHVGVLLMKSTRSGLMEVFVYTAKEIVGDVIESDEMEPKWFNVADLTYKDTYKEAREWWPTMLEGHTFVAQFEFVDGVITFQEINHVDVKQLALLRSSVKDAEQQAMAHRLYTLVFPMDEQNGRVLLGMKKRGFGRDKLNGFGGKVEVNETIAEGAARELAEESGLEAKSMKQCGLLMFYFENDPVAMEVHVFLVHKYEGTAVESDEMRPQWFGIHDMPFKQMWADDSLWWPYVLKEQKFVGQFWFKADQVTVTREKLSA","length":269,"molWeight":31032,"crc64":"80FF9D9222F15E93","md5":"E8495E5C7CF706D21CCA0FDE9DA7E448"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":7,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Motif":1,"Non-terminal residue":2},"uniParcId":"UPI0022CF356F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GTQ8","uniProtkbId":"A0A9W8GTQ8_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":14,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2751241.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022255"}],"value":"Histone acetyltransferase ESA1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013184"}],"value":"2.3.1.48"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00074445"}],"value":"Histone acetyltransferase esa1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031065"},{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00075313"}],"value":"protein 2-hydroxyisobutyryltransferase ESA1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031553"},{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00076782"}],"value":"protein acetyltransferase ESA1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031133"},{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00077673"}],"value":"protein crotonyltransferase ESA1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2751241.1"}],"value":"ESA1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2751241.1"}],"value":"GGI19_004610"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-butenoyl-CoA + L-lysyl-[protein] = N(6)-(2E)-butenoyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53908"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:13707"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57332"},{"database":"ChEBI","id":"CHEBI:137954"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047752"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:53909"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047752"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24180"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:15921"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:131780"},{"database":"ChEBI","id":"CHEBI:144968"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047557"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:24181"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047557"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21992"},{"database":"Rhea","id":"RHEA-COMP:9845"},{"database":"Rhea","id":"RHEA-COMP:11338"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"ecNumber":"2.3.1.48","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048940"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:21993"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048940"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45948"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:10731"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"ecNumber":"2.3.1.48","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45948"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:10731"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047787"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:45949"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047787"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010107"}],"value":"Belongs to the MYST (SAS/MOZ) family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2751241.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":469,"modifier":"EXACT"}},"description":"MYST-type HAT","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51726"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":374,"modifier":"EXACT"},"end":{"value":374,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602717-51"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]},{"type":"Binding site","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":454,"modifier":"EXACT"},"end":{"value":454,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Modified residue","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"N6-acetyllysine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022990"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0007","category":"PTM","name":"Acetylation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023159"}],"id":"KW-0010","category":"Molecular function","name":"Activator"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2751241.1"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022853"}],"id":"KW-0156","category":"Molecular function","name":"Chromatin regulator"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023015"}],"id":"KW-0805","category":"Biological process","name":"Transcription regulation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0862","category":"Ligand","name":"Zinc"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2751241.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2751241.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000429","properties":[{"key":"ProteinId","value":"KAJ2751241.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GTQ8","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"787137at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0035267","properties":[{"key":"GoTerm","value":"C:NuA4 histone acetyltransferase complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003682","properties":[{"key":"GoTerm","value":"F:chromatin binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0010485","properties":[{"key":"GoTerm","value":"F:histone H4 acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0003712","properties":[{"key":"GoTerm","value":"F:transcription coregulator activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006974","properties":[{"key":"GoTerm","value":"P:DNA damage response"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006357","properties":[{"key":"GoTerm","value":"P:regulation of transcription by RNA polymerase II"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd04301","properties":[{"key":"EntryName","value":"NAT_SF"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.10.10:FF:000526","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.60.60:FF:000001","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.630.30:FF:000002","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.30.140","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.630.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.60.60","properties":[{"key":"EntryName","value":"N-acetyl transferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.10","properties":[{"key":"EntryName","value":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016181","properties":[{"key":"EntryName","value":"Acyl_CoA_acyltransferase"}]},{"database":"InterPro","id":"IPR016197","properties":[{"key":"EntryName","value":"Chromo-like_dom_sf"}]},{"database":"InterPro","id":"IPR002717","properties":[{"key":"EntryName","value":"HAT_MYST-type"}]},{"database":"InterPro","id":"IPR050603","properties":[{"key":"EntryName","value":"MYST_HAT"}]},{"database":"InterPro","id":"IPR025995","properties":[{"key":"EntryName","value":"Tudor-knot"}]},{"database":"InterPro","id":"IPR036388","properties":[{"key":"EntryName","value":"WH-like_DNA-bd_sf"}]},{"database":"InterPro","id":"IPR040706","properties":[{"key":"EntryName","value":"Zf-MYST"}]},{"database":"PANTHER","id":"PTHR10615","properties":[{"key":"EntryName","value":"HISTONE ACETYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10615:SF218","properties":[{"key":"EntryName","value":"HISTONE ACETYLTRANSFERASE ESA1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01853","properties":[{"key":"EntryName","value":"MOZ_SAS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF11717","properties":[{"key":"EntryName","value":"Tudor-knot"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17772","properties":[{"key":"EntryName","value":"zf-MYST"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55729","properties":[{"key":"EntryName","value":"Acyl-CoA N-acyltransferases (Nat)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54160","properties":[{"key":"EntryName","value":"Chromo domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51726","properties":[{"key":"EntryName","value":"MYST_HAT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGGGSRPGTPSSSVSGGGGSGSAGPKPEAVSVEIVTGTAMLSIGCKAFFEKDGEIRQAEILSIRDKAKRQVIQRTADDAPIDNSDGTVEYEFYVHYVEFNKRLDEWVIDTRARLDKPVTFPKKKNKATIAGTQQSVRDKRRKTNIGGSVATGSIPQTPEAIRHDDSVYTAPVETFSKEKEIEKLRTQGSMTQSTSEVARMKNLNVIEMGQYQVEPWYFSPYPLEYAYTPTLYICEFCLCFYANRTQYGRHRTKCSLQHPPGNEIYRKDDISFFEIDGRRQKTYCRNLCLLSKCFLDHKTLYYDVDPFLFYILTKRDERGCHIIGYFSKEKESADNYNLACILTLPQYQRMGFGRVLIQFSYELSKAEGKVGSPEKPLSDLGLLSYRTYWSEILVDVLVGYDGEISIDELSHITSFTTQDIMHALFNLDALRYYHGQHCIVLSERVVEAYERFQKKKHRKIDSGCLKWSPKVFSQAELRYL","length":480,"molWeight":54787,"crc64":"C2071A9D2B76F332","md5":"CF8775B87B74E016AB3D4518535425BB"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":5,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":1,"Active site":1,"Binding site":2,"Modified residue":1},"uniParcId":"UPI0022D0578A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GV40","uniProtkbId":"A0A9W8GV40_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":10,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2752603.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"4: Predicted","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044985"}],"value":"Lysosomal dipeptide transporter MFSD1"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045018"}],"value":"Major facilitator superfamily domain-containing protein 1"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2752603.1"}],"value":"GGI19_003721"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045709"}],"value":"Lysosomal dipeptide uniporter that selectively exports lysine, arginine or histidine-containing dipeptides with a net positive charge from the lysosome lumen into the cytosol. Could play a role in a specific type of protein O-glycosylation indirectly regulating macrophages migration and tissue invasion. Also essential for liver homeostasis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alanyl-L-lysine(out) = L-alanyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79415"},{"database":"ChEBI","id":"CHEBI:192470"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044919"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-arginine(out) = L-alpha-aminoacyl-L-arginine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79367"},{"database":"ChEBI","id":"CHEBI:229968"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044881"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-histidine(out) = L-alpha-aminoacyl-L-histidine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79375"},{"database":"ChEBI","id":"CHEBI:229967"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044884"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-lysine(out) = L-alpha-aminoacyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79383"},{"database":"ChEBI","id":"CHEBI:229966"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044893"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-L-alpha-amino acid(out) = L-arginyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79371"},{"database":"ChEBI","id":"CHEBI:84315"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044899"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-glycine(out) = L-arginyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79391"},{"database":"ChEBI","id":"CHEBI:229955"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044903"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartyl-L-lysine(out) = L-aspartyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79411"},{"database":"ChEBI","id":"CHEBI:229953"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044898"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-L-alpha-amino acid(out) = L-histidyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79379"},{"database":"ChEBI","id":"CHEBI:229964"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044912"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-glycine(out) = L-histidyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79395"},{"database":"ChEBI","id":"CHEBI:229957"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044878"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-alanine(out) = L-lysyl-L-alanine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79399"},{"database":"ChEBI","id":"CHEBI:229954"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044876"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-alpha-amino acid(out) = L-lysyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79387"},{"database":"ChEBI","id":"CHEBI:229965"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044891"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-lysine(out) = L-lysyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79403"},{"database":"ChEBI","id":"CHEBI:229956"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044900"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-glycine(out) = L-lysyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79407"},{"database":"ChEBI","id":"CHEBI:191202"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044924"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00046376"}],"value":"Homodimer. Interacts with lysosomal protein GLMP (via lumenal domain); the interaction starts while both proteins are still in the endoplasmic reticulum and is required for stabilization of MFSD1 in lysosomes but has no direct effect on its targeting to lysosomes or transporter activity"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2752603.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":339,"modifier":"EXACT"},"end":{"value":360,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":372,"modifier":"EXACT"},"end":{"value":391,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":397,"modifier":"EXACT"},"end":{"value":419,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":466,"modifier":"EXACT"},"end":{"value":488,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":536,"modifier":"EXACT"},"end":{"value":555,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":492,"modifier":"EXACT"}},"description":"Major facilitator superfamily (MFS) profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50850"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2752603.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2752603.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000265","properties":[{"key":"ProteinId","value":"KAJ2752603.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GV40","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"424834at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0016020","properties":[{"key":"GoTerm","value":"C:membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0022857","properties":[{"key":"GoTerm","value":"F:transmembrane transporter activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.20.1250.20","properties":[{"key":"EntryName","value":"MFS general substrate transporter like domains"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR011701","properties":[{"key":"EntryName","value":"MFS"}]},{"database":"InterPro","id":"IPR020846","properties":[{"key":"EntryName","value":"MFS_dom"}]},{"database":"InterPro","id":"IPR036259","properties":[{"key":"EntryName","value":"MFS_trans_sf"}]},{"database":"InterPro","id":"IPR052187","properties":[{"key":"EntryName","value":"MFSD1"}]},{"database":"PANTHER","id":"PTHR23512","properties":[{"key":"EntryName","value":"MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23512:SF12","properties":[{"key":"EntryName","value":"TRANSPORTER, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G00260)-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07690","properties":[{"key":"EntryName","value":"MFS_1"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF103473","properties":[{"key":"EntryName","value":"MFS general substrate transporter"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50850","properties":[{"key":"EntryName","value":"MFS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGRPHCLSGSSSTADCDKGIADSGARIPTPDQPLLGSGPSRDPFGEDGRGSLESGSGTMHRRISSSSSSGDMTEFERGLGQHQRGYQVLALACALLISVGSHYSAHTLGALKSTIKKELDITNTQYGALQSTVSAVNTVLPILGGLFIDAFGTTSGSLVATFLIMMGNLIISISTHSRSFSTMVGGRILYGLGSGAITVVQETILGSWFKGKGLAITIAIQITTSRIASFLSMGTAIPVANHFGFYGAAFWANFLVCALSFGINLVYMVTMRRIHRSAPDRIVSRLRSKHRFNPRLVLFFFGLYWLFIVESFTLGGGWNSFLHINSELVKLRFGANDSVAAWSASVSQIMPIFLVPFLGWFFDVFGLRTDMLVMSAGLFTLSMALLGFTMINPLVGLVIFSISLALGPLAEITAISLILPNSSLGTGLGIYKSAMNTGSTIVDIVVGVLQDRGSKTLEETAHSYDYAMAFFVAWGLLSTFVAVTVFFVDRLKWNSLLRSNYNQRREALHAVKDRINRPMVYVAASNWRDYVHPWSYTPLIVLSVTLVISWILFAIKLA","length":558,"molWeight":60534,"crc64":"0D747957FB78DEA2","md5":"6A7ED47B20D807B04385A52829A296BD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":13,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":11,"Domain":1,"Region":1},"uniParcId":"UPI0022D0C49A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GWI3","uniProtkbId":"A0A9W8GWI3_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":12,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753796.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Phosphatidyl-N-methylethanolamine N-methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"2.1.1.71"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Phospholipid methyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"PLMT"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753796.1"}],"value":"OPI3"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753796.1"}],"value":"GGI19_002873"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Catalyzes the second two steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylmonomethylethanolamine (PMME) to phosphatidyldimethylethanolamine (PDME) and of PDME to phosphatidylcholine (PC)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00931"}],"value":"Catalyzes three sequential methylation reactions of phosphatidylethanolamine (PE) by AdoMet, thereby producing phosphatidylcholine (PC)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phosphocholine + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32739"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57643"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:64572"}],"ecNumber":"2.1.1.71","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051252"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32735"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:64572"},{"database":"ChEBI","id":"CHEBI:64573"}],"ecNumber":"2.1.1.71","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052459"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00931"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11164"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:64573"},{"database":"ChEBI","id":"CHEBI:64612"}],"ecNumber":"2.1.1.17","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00931"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005189"}],"value":"Lipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004969"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00931"}],"value":"Phospholipid metabolism; phosphatidylcholine biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Endoplasmic reticulum membrane","id":"SL-0097"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Mitochondrion membrane","id":"SL-0171"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00931"}],"value":"Belongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753796.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Topological domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":7,"modifier":"EXACT"}},"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Intramembrane","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Topological domain","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Transmembrane","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Topological domain","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Transmembrane","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Topological domain","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Transmembrane","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Topological domain","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Domain","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"Phospholipid methyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04191"}]},{"type":"Binding site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022824"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0256","category":"Cellular component","name":"Endoplasmic reticulum"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0594","category":"Biological process","name":"Phospholipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023264"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-1208","category":"Biological process","name":"Phospholipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753796.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753796.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000161","properties":[{"key":"ProteinId","value":"KAJ2753796.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GWI3","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"8300106at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005789","properties":[{"key":"GoTerm","value":"C:endoplasmic reticulum membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0031966","properties":[{"key":"GoTerm","value":"C:mitochondrial membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000773","properties":[{"key":"GoTerm","value":"F:phosphatidyl-N-methylethanolamine N-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004608","properties":[{"key":"GoTerm","value":"F:phosphatidylethanolamine N-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006656","properties":[{"key":"GoTerm","value":"P:phosphatidylcholine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"1.20.120.1630:FF:000005","properties":[{"key":"EntryName","value":"Phosphatidylethanolamine N-methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.120.1630","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03216","properties":[{"key":"EntryName","value":"PLMT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR024960","properties":[{"key":"EntryName","value":"PEMT/MFAP"}]},{"database":"InterPro","id":"IPR007318","properties":[{"key":"EntryName","value":"Phopholipid_MeTrfase"}]},{"database":"PANTHER","id":"PTHR15458","properties":[{"key":"EntryName","value":"PHOSPHATIDYLETHANOLAMINE N-METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR15458:SF5","properties":[{"key":"EntryName","value":"PHOSPHATIDYLETHANOLAMINE N-METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04191","properties":[{"key":"EntryName","value":"PEMT"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005444","properties":[{"key":"EntryName","value":"PEMT"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51599","properties":[{"key":"EntryName","value":"SAM_PEMT_PEM2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLVDFSQASLWLTLACITFNPTAWNVAARREHHTRWLTNLCGGARQGCYAIATAIFSMGIIRDALYNQALNDQPTASLLDNALVRLVAGLLFISGMTFVATSTYALGITGTFLGDYFGILMSERVTGFPFNVLENPMYVGSTMSFLGTALWHAKPAGLLITAYVWLVYWVALQFEGPFTAMIYANASKAKTAGEKQPALISKKKKKL","length":207,"molWeight":22677,"crc64":"310B6EBE4F4F5412","md5":"F7706DCE5440F7BE593C0D98924055D0"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":3,"PATHWAY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Topological domain":5,"Intramembrane":1,"Transmembrane":3,"Domain":1,"Binding site":2},"uniParcId":"UPI0022D009DB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GWM4","uniProtkbId":"A0A9W8GWM4_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":9,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2752223.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"ATP-dependent 6-phosphofructokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"ATP-PFK"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Phosphofructokinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"2.7.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Phosphohexokinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2752223.1"}],"value":"PFK1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2752223.1"}],"value":"GGI19_003975"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6-bisphosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16109"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:32966"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.11","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048070"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000533"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000533"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000533"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade \"E\" sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2752223.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":491,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Domain","location":{"start":{"value":573,"modifier":"EXACT"},"end":{"value":861,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":557,"modifier":"EXACT"}},"description":"N-terminal catalytic PFK domain 1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}]},{"type":"Region","location":{"start":{"value":573,"modifier":"EXACT"},"end":{"value":992,"modifier":"EXACT"}},"description":"C-terminal regulatory PFK domain 2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}]},{"type":"Active site","location":{"start":{"value":332,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}]},{"type":"Binding site","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":367,"modifier":"EXACT"},"end":{"value":367,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":374,"modifier":"EXACT"},"end":{"value":376,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":431,"modifier":"EXACT"},"end":{"value":431,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":459,"modifier":"EXACT"},"end":{"value":459,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":465,"modifier":"EXACT"},"end":{"value":468,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":642,"modifier":"EXACT"},"end":{"value":642,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":699,"modifier":"EXACT"},"end":{"value":703,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":737,"modifier":"EXACT"},"end":{"value":737,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":744,"modifier":"EXACT"},"end":{"value":746,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":803,"modifier":"EXACT"},"end":{"value":803,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":829,"modifier":"EXACT"},"end":{"value":829,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":835,"modifier":"EXACT"},"end":{"value":838,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":927,"modifier":"EXACT"},"end":{"value":927,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2752223.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2752223.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000308","properties":[{"key":"ProteinId","value":"KAJ2752223.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GWM4","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"537915at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005945","properties":[{"key":"GoTerm","value":"C:6-phosphofructokinase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005739","properties":[{"key":"GoTerm","value":"C:mitochondrion"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003872","properties":[{"key":"GoTerm","value":"F:6-phosphofructokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016208","properties":[{"key":"GoTerm","value":"F:AMP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0070095","properties":[{"key":"GoTerm","value":"F:fructose-6-phosphate binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0048029","properties":[{"key":"GoTerm","value":"F:monosaccharide binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0061621","properties":[{"key":"GoTerm","value":"P:canonical glycolysis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030388","properties":[{"key":"GoTerm","value":"P:fructose 1,6-bisphosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006002","properties":[{"key":"GoTerm","value":"P:fructose 6-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.40.50.460:FF:000007","properties":[{"key":"EntryName","value":"ATP-dependent 6-phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.460:FF:000008","properties":[{"key":"EntryName","value":"ATP-dependent 6-phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.450","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.460","properties":[{"key":"EntryName","value":"Phosphofructokinase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_03184","properties":[{"key":"EntryName","value":"Phosphofructokinase_I_E"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR009161","properties":[{"key":"EntryName","value":"6-Pfructokinase_euk"}]},{"database":"InterPro","id":"IPR022953","properties":[{"key":"EntryName","value":"ATP_PFK"}]},{"database":"InterPro","id":"IPR015912","properties":[{"key":"EntryName","value":"Phosphofructokinase_CS"}]},{"database":"InterPro","id":"IPR000023","properties":[{"key":"EntryName","value":"Phosphofructokinase_dom"}]},{"database":"InterPro","id":"IPR035966","properties":[{"key":"EntryName","value":"PKF_sf"}]},{"database":"NCBIfam","id":"TIGR02478","properties":[{"key":"EntryName","value":"6PF1K_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697:SF4","properties":[{"key":"EntryName","value":"ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00365","properties":[{"key":"EntryName","value":"PFK"},{"key":"MatchStatus","value":"2"}]},{"database":"PIRSF","id":"PIRSF000533","properties":[{"key":"EntryName","value":"ATP_PFK_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00476","properties":[{"key":"EntryName","value":"PHFRCTKINASE"}]},{"database":"SUPFAM","id":"SSF53784","properties":[{"key":"EntryName","value":"Phosphofructokinase"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00433","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MSALEAESSLSFSHIALVASTAEQFSETVDFYLSLGLSTVRQTTHDRPQRDIAHNACVVSEAWLHLFADRPENSITLRIIHATGDGIESKGDSNKIRIGMATQEIKTIKEILTSGGHAFTVHADPKVCSDRIATHDPLGNDVFFTLQANSFSIPSSPEVKPLKISEPGTPIEFNLEARTPQKNIGILTSGGDAQGMNPCVRAVVRMAIARNCRPFFIYEGYQGLVDGGAKIKEAKWTDVSGFLALGGTMIGTARCKAFRELEGRRTGVLNLIKNGIDALVVIGGDGSLTGADRLRAEWPEHVQALEQAGLITKENAEKYRTLMIVGMVGSIDNDLASTDMTIGACSALERICESVDAILSTAMSHQRAFVVEVMGRHCGWLALNAAISTGADYLFIPEAPPSKDDWEASMCKTLKASRDAGKRTSLVIVAEGAIDRHLNPIKAEYIKDILSTRLGYDTRVTILGHVQRGGAPAHFDRFLGTMQGAEAIEAILRAKPDTPSLVIGMLENKITTQPLKEAIELTGQVAQSIEGKDFARAITLRSSAFSKQLRSYKEMANFNPDSKMKLPEHMRLRIAILHAGAPAGGMNTATRSAVRLCLNRGHTPLGVHNGFPGLMRGEITEFDWLSVDGWTIAGGSKLGTNRDQPTPQLGAVAYQLQKNGIQALMVIGGFEAYTAVLELARNRSQYPAFNIPMVLIPATVSNNVPGTEFSLGSDTATNVIVQATDMIKQSASSNRRRVFVIEVQGGNCGYLAVVAGLSGGSTTVYTPEEGVDLSRLQRDICHLRSRYIKELGRSEGRITLCNEKASQIYSTDMIAKIYEAESGGFYGARTSVLGHLQQGGTPSPLDRCRANTMAVDSIDWLQSKCWEGMDVPNEDNIRLPADKLKRKYFPPVYSSLSDSAAMLGVIGSEVRFTPVEDLVMQTDFKRRVPRAIWWSAARQLIDILSGVGVDIEHGGCTTVYKSCAIDLTAEDLMRLYGRTRRLSKLGGSPTAV","length":992,"molWeight":107668,"crc64":"D11200952294EFFC","md5":"EFDD2C7353457A0DE2C64FED77D892D4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Active site":1,"Binding site":18},"uniParcId":"UPI0022D72EB9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GXN7","uniProtkbId":"A0A9W8GXN7_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":11,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750976.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044318"}],"value":"Ammonium-dependent carbamoyl phosphate synthetase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013008"}],"value":"2.1.3.2"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044063"}],"value":"6.3.4.16"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012738"}],"value":"6.3.5.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044249"}],"value":"Arginine-specific carbamoyl phosphate synthetase, ammonia chain"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044334"}],"value":"Glutamine-dependent carbamoyl phosphate synthetase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750976.1"}],"value":"URA2_2"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750976.1"}],"value":"GGI19_004782"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"carbamoyl phosphate + L-aspartate = N-carbamoyl-L-aspartate + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20013"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29991"},{"database":"ChEBI","id":"CHEBI:32814"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"}],"ecNumber":"2.1.3.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048859"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18633"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048816"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + NH4(+) + 2 ATP = carbamoyl phosphate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18029"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.16","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047359"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005077"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004852"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044031"}],"value":"Heterodimer composed of 2 chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011643"}],"value":"Homohexamer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750976.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":399,"modifier":"EXACT"},"end":{"value":590,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":595,"modifier":"EXACT"},"end":{"value":740,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00409"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00409"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750976.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750976.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000467","properties":[{"key":"ProteinId","value":"KAJ2750976.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"OrthoDB","id":"1924069at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016597","properties":[{"key":"GoTerm","value":"F:amino acid binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004070","properties":[{"key":"GoTerm","value":"F:aspartate carbamoyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004087","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (ammonia) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004151","properties":[{"key":"GoTerm","value":"F:dihydroorotase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006207","properties":[{"key":"GoTerm","value":"P:'de novo' pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0019240","properties":[{"key":"GoTerm","value":"P:L-citrulline biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006228","properties":[{"key":"GoTerm","value":"P:UTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"FunFam","id":"3.40.50.1370:FF:000002","properties":[{"key":"EntryName","value":"Aspartate carbamoyltransferase 2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1370:FF:000005","properties":[{"key":"EntryName","value":"CAD protein-like isoform X1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000004","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase (glutamine-hydrolyzing)"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.140:FF:000036","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1370","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.1490.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, A domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.140","properties":[{"key":"EntryName","value":"Metal-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00001","properties":[{"key":"EntryName","value":"Asp_carb_tr"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006132","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoyltranf_P-bd"}]},{"database":"InterPro","id":"IPR006130","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoylTrfase"}]},{"database":"InterPro","id":"IPR036901","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoylTrfase_sf"}]},{"database":"InterPro","id":"IPR002082","properties":[{"key":"EntryName","value":"Asp_carbamoyltransf"}]},{"database":"InterPro","id":"IPR006131","properties":[{"key":"EntryName","value":"Asp_carbamoyltransf_Asp/Orn-bd"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR013815","properties":[{"key":"EntryName","value":"ATP_grasp_subdomain_1"}]},{"database":"InterPro","id":"IPR036897","properties":[{"key":"EntryName","value":"CarbamoylP_synth_lsu_oligo_sf"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR005480","properties":[{"key":"EntryName","value":"CPSase_lsu_oligo"}]},{"database":"InterPro","id":"IPR058047","properties":[{"key":"EntryName","value":"CPSase_preATP-grasp"}]},{"database":"InterPro","id":"IPR032466","properties":[{"key":"EntryName","value":"Metal_Hydrolase"}]},{"database":"InterPro","id":"IPR011607","properties":[{"key":"EntryName","value":"MGS-like_dom"}]},{"database":"InterPro","id":"IPR036914","properties":[{"key":"EntryName","value":"MGS-like_dom_sf"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00670","properties":[{"key":"EntryName","value":"asp_carb_tr"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003671","properties":[{"key":"EntryName","value":"carB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002032","properties":[{"key":"EntryName","value":"PRK00856.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF5","properties":[{"key":"EntryName","value":"CAD PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00185","properties":[{"key":"EntryName","value":"OTCace"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02729","properties":[{"key":"EntryName","value":"OTCace_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00100","properties":[{"key":"EntryName","value":"AOTCASE"}]},{"database":"PRINTS","id":"PR00101","properties":[{"key":"EntryName","value":"ATCASE"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53671","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF51556","properties":[{"key":"EntryName","value":"Metallo-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLRTTAVNVIRHLGVVGECNIQYALNPHSREYSIIEVNARLSRSSALASKATGYPLAFVAAKLGLGIPLNEIRNSVTRETTACFEPSLDYVVVKIPRWDLKKFDRVSKNLSSAMKSVGEVMAIGRTFEETMQEAIRSVDTSFDGFSRNTYVPETKEAIEEELTKPTDLRVFAIANAFHMGYTVEEIHQLTAIDRWFLCKLRGLVETERRLQTFAADQSIPRDLLRYAKQQGFSDSGIAHFTKRNEMQVRNTRTGYGITPFVKQIDTVAAEFPAHTNYLYITYNASEHDVQFVDNGVMVLGSGVYRIGSSVEFDWCAVRAIRTLRENQFKTIMADRLYFSNITLERIMDIYEVETSAGVIISMGGQAPNNIALGLQRNKVKIFGTSPENIDGAENRYKFSRMLDQIGVDQPQWRELTQYEDAESFCDEVGYPVLVRPSYVLSGAAMNVVSTSTDLKTYLNQAATMSRDHPVVITKFIEEAKEIDVDAVALDGKLIMHCVSEHVENAGVHSGDATLVQPPQDLDPVTVKKIGDATAAIGQALRVTGPFNIQFMAKNNEIKVIECNVRAARSFPFVSKVTGVDLIEMATKAMLGLPVVPYPNRGQRLNYVGVKVPQFSFSRLQGADPILGVEMASTGEVAAFEHGIDVTALEADKAREGYSLEEYLSSNKIDLYINLPSKNSFRRPATYVSNGYRSRRMAIDFSVPLITNVKCAKMFIEAMARFSMDKWEIESVDYITSHRTTVLPGLVNITALLPGGDGFEQATRAAICGGFTMLGISAHGADAFATTSDQSVSKVKSTGRGHAHTDYVVEIAATEANPTAAAALSADAPILYVSFDRSHPVHVDKYSAVSEHFKAWPQNSAVITNASGNDLATMLLLASLFSRQIHVTDVRTPEDLDLIDLSRARGLCATCDVSVYALFADRLPAIEGLQSNVQPLWSRLSAIDCFTVGVLPAQAAKAAGVKDVNPATLGYQLVLPLLYTAVSEGRLTSADVVERFCNAPRRIFGLPEQPDTYVEIHRDRLVRIPPKSDDAKWFPDILAKPAHCAVHRVVMRGKTLLLDGMFYDQGLAPVGRDLCHVLRTMSSGPSGKQFAQPPAMAAGALSVKTTAEARPPMHARKTSLVMSPAVVPAIEVDTIDEVDAVSASLDVQPPVVEETALTTRIERPLPESRLADVMARHGNQNPFYMKHVLSVRQFTREDLHLLFAVAQEMRTVVQRSGMLPLLTGRVMAAVFYEPSSRTSSSFQTAMLRLGGQVFTANSESSSVAKGETLEDTVRTFGSYADIITLRHPQPGSVQGAARFANIPVLNAGDGIGEHPSQAMLDTFTIREELGTVNGLTITLVGDLKNGRTVHSLARVLSQYKNVTLNYVSPASLAMPESIKRDVALRAPYVEQHEFTELTDAVLAKTDVLYVTRVQKERFENEDEYERTRSAFVIDNEVMRKCKRNMIVMHPLPRVTEIAPEVDTDQRAAYFRQMQYGMFVRMALLALVLCRNF","length":1491,"molWeight":164604,"crc64":"A1E9284AFE820DDB","md5":"24C8D231D2BEC76DB753DC97A0FF9586"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":3,"PATHWAY":2,"SUBUNIT":2,"CAUTION":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI0022DC4BD6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GYA0","uniProtkbId":"A0A9W8GYA0_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":11,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753214.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00039850"}],"value":"Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012046"}],"value":"1.3.8.1"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00039036"}],"value":"1.3.8.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00042821"}],"value":"2-methyl branched chain acyl-CoA dehydrogenase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00041537"}],"value":"2-methylbutyryl-coenzyme A dehydrogenase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753214.1"}],"value":"GGI19_003291"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00094237"}],"value":"Short and branched chain specific acyl-CoA dehydrogenase that catalyzes the proR-proR stereospecific alpha,beta-dehydrogenation of fatty acyl-CoA thioesters using the electron transfer flavoprotein (ETF) as their physiologic electron acceptor, resulting in the formation of trans-2-enoyl-CoA ((2E)-enoyl-CoA). Among the different mitochondrial acyl-CoA dehydrogenases, acts specifically on short and branched chain acyl-CoA derivatives such as (S)-2-methylbutyryl-CoA as well as short straight chain acyl-CoAs such as butyryl-CoA (butanoyl-CoA). Plays an important role in the metabolism of L-isoleucine by catalyzing the dehydrogenation of 2-methylbutyryl-CoA, one of the steps of the L-isoleucine catabolic pathway. Can also act on valproyl-CoA, a metabolite of valproic acid, an antiepileptic drug"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R)-2-methylbutanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = ethylacryloyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65296"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:156439"},{"database":"ChEBI","id":"CHEBI:156440"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048592"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65297"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048592"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2S)-2-methylbutanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:48256"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57337"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:88166"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049552"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:48257"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049552"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-methylbutanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43780"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57336"},{"database":"ChEBI","id":"CHEBI:57337"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"}],"ecNumber":"1.3.8.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048235"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:43781"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048235"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-methylpropanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = 2-methylpropenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:44180"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57338"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:62500"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051903"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:44181"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051903"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a short-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a short-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47196"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:87487"},{"database":"ChEBI","id":"CHEBI:87488"}],"ecNumber":"1.3.8.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051002"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:47197"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051002"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"butanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-butenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24004"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57332"},{"database":"ChEBI","id":"CHEBI:57371"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049096"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:24005"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049096"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hexanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-hexenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43464"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:62077"},{"database":"ChEBI","id":"CHEBI:62620"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049192"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:43465"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049192"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"valproyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-2-propylpent-2-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65344"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:156457"},{"database":"ChEBI","id":"CHEBI:156458"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048307"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65345"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048307"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001974"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00037895"}],"value":"Amino-acid degradation; L-isoleucine degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005198"}],"value":"Lipid metabolism; mitochondrial fatty acid beta-oxidation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011881"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004305"}],"value":"Mitochondrion matrix","id":"SL-0170"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"value":"Belongs to the acyl-CoA dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753214.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02771"}]},{"type":"Domain","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":251,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase middle","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02770"}]},{"type":"Domain","location":{"start":{"value":263,"modifier":"EXACT"},"end":{"value":410,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00441"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022990"}],"id":"KW-0007","category":"PTM","name":"Acetylation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022946"}],"id":"KW-0809","category":"Domain","name":"Transit peptide"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753214.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753214.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000210","properties":[{"key":"ProteinId","value":"KAJ2753214.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GYA0","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"10262177at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005759","properties":[{"key":"GoTerm","value":"C:mitochondrial matrix"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003853","properties":[{"key":"GoTerm","value":"F:short-chain 2-methyl fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046395","properties":[{"key":"GoTerm","value":"P:carboxylic acid catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006631","properties":[{"key":"GoTerm","value":"P:fatty acid metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd01158","properties":[{"key":"EntryName","value":"SCAD_SBCAD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.540.10:FF:000012","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase short/branched chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.140.10:FF:000002","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase short/branched chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.110.10:FF:000001","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.540.10","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase/oxidase, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.110.10","properties":[{"key":"EntryName","value":"Butyryl-CoA Dehydrogenase, subunit A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.140.10","properties":[{"key":"EntryName","value":"Butyryl-CoA Dehydrogenase, subunit A, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006089","properties":[{"key":"EntryName","value":"Acyl-CoA_DH_CS"}]},{"database":"InterPro","id":"IPR046373","properties":[{"key":"EntryName","value":"Acyl-CoA_Oxase/DH_mid-dom_sf"}]},{"database":"InterPro","id":"IPR036250","properties":[{"key":"EntryName","value":"AcylCo_DH-like_C"}]},{"database":"InterPro","id":"IPR009075","properties":[{"key":"EntryName","value":"AcylCo_DH/oxidase_C"}]},{"database":"InterPro","id":"IPR006091","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_M"}]},{"database":"InterPro","id":"IPR013786","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_N"}]},{"database":"InterPro","id":"IPR037069","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_N_sf"}]},{"database":"InterPro","id":"IPR009100","properties":[{"key":"EntryName","value":"AcylCoA_DH/oxidase_NM_dom_sf"}]},{"database":"PANTHER","id":"PTHR43884","properties":[{"key":"EntryName","value":"ACYL-COA DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43884:SF1","properties":[{"key":"EntryName","value":"SHORT_BRANCHED CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00441","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02770","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02771","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF016578","properties":[{"key":"EntryName","value":"HsaA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47203","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56645","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase NM domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00072","properties":[{"key":"EntryName","value":"ACYL_COA_DH_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00073","properties":[{"key":"EntryName","value":"ACYL_COA_DH_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MFRIALTSSRRVAQPMLRRAFTVSAVSKQEDFVSRSLHTMSEDEQMMKDAVSRFARDIVQPHVSAMDESETMEPSVIRGLFDAGLMGVETSVDLGGAGASFTSAIVVVEELAKIDPSVSVLCDVHNTLVNTVFRTYASPELQQQYLPRLSTDALGCFCLSEPTAGSDAFALQTRATAQGSDYIINGAKMWITNSNEADVFLVFATVDPSLGYRGITCFVVDRNTPGLSVAKKEKKLGIRASSTCQVSFDDVRVPATSVVGEVGKGYKIAIEILNEGRIGIAAQMLGLAQGAFDHALPYLFQRKQFGTKIGEFQAMQHQYAQIATEIEAARLLTYNAARMKEEGKPFAKEAAMAKLYASQVAERASSKAVEWMGGVGFTRDMPVEKYYRDCKIGAIYEGTSNIQLQTIAKILAKEYQE","length":417,"molWeight":45596,"crc64":"FF8DB8B7543B5C08","md5":"072CB6DC28819B5E2CD7ABD7727642DC"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":8,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI0022DC9432"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GYF9","uniProtkbId":"A0A9W8GYF9_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":11,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2756285.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"Lon protease homolog, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"3.4.21.53"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2756285.1"}],"value":"PIM1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2756285.1"}],"value":"GGI19_000943"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"3.6.4.10","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050527"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:13066"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050527"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of proteins in presence of ATP.","ecNumber":"3.4.21.53","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10087"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"Homohexamer or homoheptamer. Organized in a ring with a central cavity"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004305"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"Mitochondrion matrix","id":"SL-0170"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01122"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000591"}],"value":"Belongs to the peptidase S16 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2756285.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":455,"modifier":"EXACT"}},"description":"Lon N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51787"}]},{"type":"Domain","location":{"start":{"value":899,"modifier":"EXACT"},"end":{"value":1091,"modifier":"EXACT"}},"description":"Lon proteolytic","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51786"}]},{"type":"Region","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":997,"modifier":"EXACT"},"end":{"value":997,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10087"}]},{"type":"Active site","location":{"start":{"value":1040,"modifier":"EXACT"},"end":{"value":1040,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01122"}]},{"type":"Binding site","location":{"start":{"value":608,"modifier":"EXACT"},"end":{"value":615,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022825"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0720","category":"Molecular function","name":"Serine protease"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2756285.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2756285.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000030","properties":[{"key":"ProteinId","value":"KAJ2756285.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GYF9","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"2411602at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005759","properties":[{"key":"GoTerm","value":"C:mitochondrial matrix"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004176","properties":[{"key":"GoTerm","value":"F:ATP-dependent peptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043565","properties":[{"key":"GoTerm","value":"F:sequence-specific DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003697","properties":[{"key":"GoTerm","value":"F:single-stranded DNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0034599","properties":[{"key":"GoTerm","value":"P:cellular response to oxidative stress"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051131","properties":[{"key":"GoTerm","value":"P:chaperone-mediated protein complex assembly"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0007005","properties":[{"key":"GoTerm","value":"P:mitochondrion organization"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0070407","properties":[{"key":"GoTerm","value":"P:oxidation-dependent protein catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006515","properties":[{"key":"GoTerm","value":"P:protein quality control for misfolded or incompletely synthesized proteins"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd19500","properties":[{"key":"EntryName","value":"RecA-like_Lon"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000021","properties":[{"key":"EntryName","value":"Lon protease homolog"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.5.5270:FF:000001","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.58.1480:FF:000002","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.230.10:FF:000015","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.60","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.5.5270","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.58.1480","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.230.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.130.40","properties":[{"key":"EntryName","value":"LON domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03120","properties":[{"key":"EntryName","value":"lonm_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR003959","properties":[{"key":"EntryName","value":"ATPase_AAA_core"}]},{"database":"InterPro","id":"IPR004815","properties":[{"key":"EntryName","value":"Lon_bac/euk-typ"}]},{"database":"InterPro","id":"IPR054594","properties":[{"key":"EntryName","value":"Lon_lid"}]},{"database":"InterPro","id":"IPR008269","properties":[{"key":"EntryName","value":"Lon_proteolytic"}]},{"database":"InterPro","id":"IPR027065","properties":[{"key":"EntryName","value":"Lon_Prtase"}]},{"database":"InterPro","id":"IPR003111","properties":[{"key":"EntryName","value":"Lon_prtase_N"}]},{"database":"InterPro","id":"IPR046336","properties":[{"key":"EntryName","value":"Lon_prtase_N_sf"}]},{"database":"InterPro","id":"IPR027503","properties":[{"key":"EntryName","value":"Lonm_euk"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR008268","properties":[{"key":"EntryName","value":"Peptidase_S16_AS"}]},{"database":"InterPro","id":"IPR015947","properties":[{"key":"EntryName","value":"PUA-like_sf"}]},{"database":"InterPro","id":"IPR020568","properties":[{"key":"EntryName","value":"Ribosomal_Su5_D2-typ_SF"}]},{"database":"InterPro","id":"IPR014721","properties":[{"key":"EntryName","value":"Ribsml_uS5_D2-typ_fold_subgr"}]},{"database":"NCBIfam","id":"TIGR00763","properties":[{"key":"EntryName","value":"lon"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43718","properties":[{"key":"EntryName","value":"LON PROTEASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43718:SF2","properties":[{"key":"EntryName","value":"LON PROTEASE HOMOLOG, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00004","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05362","properties":[{"key":"EntryName","value":"Lon_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22667","properties":[{"key":"EntryName","value":"Lon_lid"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02190","properties":[{"key":"EntryName","value":"LON_substr_bdg"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00830","properties":[{"key":"EntryName","value":"ENDOLAPTASE"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00464","properties":[{"key":"EntryName","value":"LON"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF88697","properties":[{"key":"EntryName","value":"PUA domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54211","properties":[{"key":"EntryName","value":"Ribosomal protein S5 domain 2-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51787","properties":[{"key":"EntryName","value":"LON_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51786","properties":[{"key":"EntryName","value":"LON_PROTEOLYTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01046","properties":[{"key":"EntryName","value":"LON_SER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSQLSVTFGPAKTRLARGATALSLAYNSCGRHYSSVAAAIDLPQNRLLSLRQTRQSLFASAISPTQYTANGRWHAQQIAALSSLNFASKRTFQTSASARKERDGKSDDNDDPDSSATKKEQEEDEQEADDKDDSKSTSRRRRAPRRSESEKPAAATSAGANGGEQAQTDPLTQLKRAVGVADYAQGQQSFIPDNYPNVMMLPITRRPLFPSLYKSIQVQDPQVIGALKELVERGEPYLATFMLKNDERDVDSIRDMDEVHEIGVFSRIMSIYVSPNPEDKHLTVALYPWRRVRMKRILGTEKDPESTAAAPALDQQELIVPETTEDSAVEEVVSPVANAANVLKAIKLDYNFTALEVENVEDEPYDAKDPTISATMSEIVSVLREITTMNPMFREQIHHFASAQVSKAVFENPSKLADFAAALSGGSSEELQDILSDLNVATRLEKALVVLKKELMNAQLQNKISKDVEAKISKRQRDFYLMEQLKGIKRELGLESDGKDKLIEQFKVKAESLLMPAEVKRVFDEEVGKLAHLEPAASEFNVTRNYLDWLTQIPWGKHSVEDYDLQRAKIVLDEDHYGLEDVKQRILEFIAVGKLRGAVQGKILCFVGPPGVGKTSIGKSIARSLNREFFRFSVGGLTDVAEIKGHRRTYVGAMPGKVVQALKRVQTENPLLLIDEIDKLGRGHQGDPASALLELLDPEQNNAFLDHYMDVPVDLSRVLFVCTANVTDTIPGPLLDRMEVIRLSGYLADEKRAIAQKYLAPQAKEAAGLEGAAVSLQDDAVDALVRNYCRESGVRNLKKHIEKIFRKAALKIVETGVAVEAPSLTPPPTASAVAPEVDTADALAPAPEASTAPATAAPTTAKLPSKMVIPDSYSLDITAGLLKDYVGPPVFESDRLYEHTPAGVVMGLAWTSLGGSALYVESVVEATIASSNSEGEQRNGRLHTTGQLGDVMKESATLAYTYVRSLLNRKHPGNQFFHNNIIHLHVPEGATPKDGPSAGVTMTTALLSLALNRPVRNDVAMTGELTLTGRVLKIGGLKEKTIAARRAGVKRILFPKANMADWDELPANVKEGIEGHPIEWYDQIPALVGLDEPVN","length":1095,"molWeight":120002,"crc64":"20B18032A3533DBF","md5":"03F2A3BF13938CDD44AD61A0BEB4E3B6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":1,"Compositional bias":2,"Active site":2,"Binding site":1},"uniParcId":"UPI0022DC7F3C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GZ61","uniProtkbId":"A0A9W8GZ61_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":12,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753922.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Inosine triphosphate pyrophosphatase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"ITPase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Inosine triphosphatase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"3.6.1.66"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Non-canonical purine NTP pyrophosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Non-standard purine NTP pyrophosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Nucleoside-triphosphate diphosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Nucleoside-triphosphate pyrophosphatase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"NTPase"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"XTP/dITP diphosphatase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753922.1"}],"value":"HAM1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753922.1"}],"value":"GGI19_002789"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054940"}],"value":"Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ITP + H2O = IMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:29399"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58053"},{"database":"ChEBI","id":"CHEBI:61402"}],"ecNumber":"3.6.1.66","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093218"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:29400"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093218"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-hydroxy-dATP + H2O = N(6)-hydroxy-dAMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:83971"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:233529"},{"database":"ChEBI","id":"CHEBI:233530"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093271"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:83972"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093271"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"XTP + H2O = XMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28610"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57464"},{"database":"ChEBI","id":"CHEBI:61314"}],"ecNumber":"3.6.1.66","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dITP + H2O = dIMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28342"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61194"},{"database":"ChEBI","id":"CHEBI:61382"}],"ecNumber":"3.6.1.66","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093255"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:28343"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093255"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008023"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003781"}],"value":"Belongs to the HAM1 NTPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753922.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61402"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"ITP","id":"ChEBI:CHEBI:61402"}},{"type":"Binding site","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61402"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"ITP","id":"ChEBI:CHEBI:61402"}},{"type":"Binding site","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61402"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"ITP","id":"ChEBI:CHEBI:61402"}},{"type":"Binding site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61402"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"ITP","id":"ChEBI:CHEBI:61402"}},{"type":"Binding site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61402"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"ligand":{"name":"ITP","id":"ChEBI:CHEBI:61402"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023080"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0546","category":"Biological process","name":"Nucleotide metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03148"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753922.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753922.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753922.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000152","properties":[{"key":"ProteinId","value":"KAJ2753922.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GZ61","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"6288734at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0035870","properties":[{"key":"GoTerm","value":"F:dITP diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036220","properties":[{"key":"GoTerm","value":"F:ITP diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036222","properties":[{"key":"GoTerm","value":"F:XTP diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009204","properties":[{"key":"GoTerm","value":"P:deoxyribonucleoside triphosphate catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009143","properties":[{"key":"GoTerm","value":"P:nucleoside triphosphate catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00515","properties":[{"key":"EntryName","value":"HAM1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.950.10:FF:000003","properties":[{"key":"EntryName","value":"Inosine triphosphate pyrophosphatase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.950.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03148","properties":[{"key":"EntryName","value":"HAM1_NTPase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR027502","properties":[{"key":"EntryName","value":"ITPase"}]},{"database":"InterPro","id":"IPR029001","properties":[{"key":"EntryName","value":"ITPase-like_fam"}]},{"database":"InterPro","id":"IPR002637","properties":[{"key":"EntryName","value":"RdgB/HAM1"}]},{"database":"NCBIfam","id":"TIGR00042","properties":[{"key":"EntryName","value":"RdgB/HAM1 family non-canonical purine NTP pyrophosphatase"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11067:SF9","properties":[{"key":"EntryName","value":"INOSINE TRIPHOSPHATE PYROPHOSPHATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11067","properties":[{"key":"EntryName","value":"INOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01725","properties":[{"key":"EntryName","value":"Ham1p_like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52972","properties":[{"key":"EntryName","value":"ITPase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSLRKLTFVTGNVNKLREMQELLHGIVDLHNTPVDLEEIQGSTQEVAIAKCRQAAAIIGGPVITEDVGLGFNAMNGLPGAYIKWFLKELKPAGLYKMLHGFEDKSGFAVCTVAYCAGPNHEPILFEGIHHGTIVEPRGPPVFGWNPVFQPDGHNETYAEMSDELKNKCSHRFLAVEKLKAFLSEQQ","length":186,"molWeight":20559,"crc64":"98909378C5FB51F2","md5":"233FBF8EF34BC7F1FD55F4F3D47839C5"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Binding site":7},"uniParcId":"UPI0022D987CD"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8L9C5","uniProtkbId":"A0A9W8L9C5_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":8,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2749884.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Phosphatidylserine decarboxylase proenzyme 1, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"4.1.1.65"}]},"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Phosphatidylserine decarboxylase 1 beta chain"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Phosphatidylserine decarboxylase 1 alpha chain"}}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2749884.1"}],"value":"PSD1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2749884.1"}],"value":"GGI19_005418"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20828"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57262"},{"database":"ChEBI","id":"CHEBI:64612"}],"ecNumber":"4.1.1.65","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyruvate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:15361"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Binds 1 pyruvoyl group covalently per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005189"}],"value":"Lipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","molecule":"Phosphatidylserine decarboxylase 1 alpha chain","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Intermembrane side","id":"SL-9912"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Phosphatidylserine decarboxylase 1 beta chain","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Single-pass membrane protein","id":"SL-9904"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Intermembrane side","id":"SL-9912"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type I sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2749884.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":504,"modifier":"EXACT"}},"description":"Phosphatidylserine decarboxylase 1 beta chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"featureId":"PRO_5041026120"},{"type":"Chain","location":{"start":{"value":505,"modifier":"EXACT"},"end":{"value":540,"modifier":"EXACT"}},"description":"Phosphatidylserine decarboxylase 1 alpha chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"featureId":"PRO_5041026121"},{"type":"Topological domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"Mitochondrial matrix","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Topological domain","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":540,"modifier":"EXACT"}},"description":"Mitochondrial intermembrane","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Region","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Active site","location":{"start":{"value":391,"modifier":"EXACT"},"end":{"value":391,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Active site","location":{"start":{"value":505,"modifier":"EXACT"},"end":{"value":505,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Active site","location":{"start":{"value":505,"modifier":"EXACT"},"end":{"value":505,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Site","location":{"start":{"value":504,"modifier":"EXACT"},"end":{"value":505,"modifier":"EXACT"}},"description":"Cleavage (non-hydrolytic); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Modified residue","location":{"start":{"value":505,"modifier":"EXACT"},"end":{"value":505,"modifier":"EXACT"}},"description":"Pyruvic acid (Ser); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0999","category":"Cellular component","name":"Mitochondrion inner membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0594","category":"Biological process","name":"Phospholipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023264"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-1208","category":"Biological process","name":"Phospholipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023317"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0865","category":"PTM","name":"Zymogen"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2749884.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2749884.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000680","properties":[{"key":"ProteinId","value":"KAJ2749884.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8L9C5","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"4330at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005743","properties":[{"key":"GoTerm","value":"C:mitochondrial inner membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004609","properties":[{"key":"GoTerm","value":"F:phosphatidylserine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006646","properties":[{"key":"GoTerm","value":"P:phosphatidylethanolamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016540","properties":[{"key":"GoTerm","value":"P:protein autoprocessing"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"HAMAP","id":"MF_03208","properties":[{"key":"EntryName","value":"PS_decarb_PSD_B_type1_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003817","properties":[{"key":"EntryName","value":"PS_Dcarbxylase"}]},{"database":"InterPro","id":"IPR033177","properties":[{"key":"EntryName","value":"PSD-B"}]},{"database":"InterPro","id":"IPR033661","properties":[{"key":"EntryName","value":"PSD_type1_euk"}]},{"database":"NCBIfam","id":"TIGR00163","properties":[{"key":"EntryName","value":"PS_decarb"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10067","properties":[{"key":"EntryName","value":"PHOSPHATIDYLSERINE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10067:SF6","properties":[{"key":"EntryName","value":"PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02666","properties":[{"key":"EntryName","value":"PS_Dcarbxylase"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MDIPTIVGVPSFTEFAFKNDTFLIIGLDSAKKIAQVKERTIMRRLDVKYCYADLSQYDLTTDIQFNYDEKYKFKYAYCIDYEPAVLLCHHALRRSPAQLRQFTRLHSSRLPVTLPRIRHYSSGNSNGEKRSGTGEDTSGKDKGSGTGWYWMPVGVGLGYICFQRLTHIKSDISKEQQQAVSGVTVPGPWQLHVLSALPLKAMSRLFGSFNEMEIPRILRKPLLHVYAWTFGCNLGEMKDPDLTHYPNLATFFYRELREDARPVDLHPTAAVVSPSDGKVLHFGVVEQREVEQVKGLTYSLDAFFGKADDPSVEAGIAGSTMVDATLSHSHNAAAEDEFAVVNGIPYTLDSMIGSTGVLEPAVQSLGRQLRDHERLYFCVIYLAPGDYHRFHSPANWVVESRRHFAGELYSVSPYIARTIQNLFVLNERVALLGRWKHGFMSMTAVGATNVGSVVINFDKELRTNLRERSLLPGEFTQLSYKALSSKLHGVPLNKGQEVGGFRLGSTVVLVFSAPNTFQFNVAPDQTVKMGEALGHIPLIE","length":540,"molWeight":60393,"crc64":"807E9CD2327371DF","md5":"7B0D4444A9061778306A59800ED1A3FE"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":2,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Chain":2,"Topological domain":2,"Region":1,"Compositional bias":1,"Active site":4,"Site":1,"Modified residue":1},"uniParcId":"UPI0022D11C7F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8LBP2","uniProtkbId":"A0A9W8LBP2_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":14,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753227.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032195"}],"value":"Alpha-aminoadipate reductase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013073"}],"value":"1.2.1.31"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012913"}],"value":"1.2.1.95"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031335"}],"value":"L-aminoadipate-semialdehyde dehydrogenase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753227.1"}],"value":"LYS2"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753227.1"}],"value":"GGI19_003282"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003499"}],"value":"Catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-2-amino-6-oxohexanoate + AMP + diphosphate + NADP(+) = L-2-aminoadipate + NADPH + ATP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46936"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58321"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:58672"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"1.2.1.95","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048260"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-2-amino-6-oxohexanoate + NAD(+) + H2O = L-2-aminoadipate + NADH + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12308"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:58321"},{"database":"ChEBI","id":"CHEBI:58672"}],"ecNumber":"1.2.1.31","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048414"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-2-amino-6-oxohexanoate + NADP(+) + H2O = L-2-aminoadipate + NADPH + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12304"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58321"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:58672"}],"ecNumber":"1.2.1.31","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049537"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"pantetheine 4'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001957"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00258"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:47942"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004827"}],"value":"Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 1/3"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006432"}],"value":"Belongs to the ATP-dependent AMP-binding enzyme family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010563"}],"value":"Belongs to the XPG/RAD2 endonuclease family. EXO1 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753227.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":880,"modifier":"EXACT"},"end":{"value":956,"modifier":"EXACT"}},"description":"Carrier","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50075"}]},{"type":"Modified residue","location":{"start":{"value":916,"modifier":"EXACT"},"end":{"value":916,"modifier":"EXACT"}},"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00258"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022881"}],"id":"KW-0267","category":"Molecular function","name":"Excision nuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022839"}],"id":"KW-0269","category":"Molecular function","name":"Exonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023154"}],"id":"KW-0457","category":"Biological process","name":"Lysine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022722"}],"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753227.1"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022450"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00258"}],"id":"KW-0596","category":"PTM","name":"Phosphopantetheine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753227.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2753227.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000209","properties":[{"key":"ProteinId","value":"KAJ2753227.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"OrthoDB","id":"329835at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0035312","properties":[{"key":"GoTerm","value":"F:5'-3' DNA exonuclease activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004043","properties":[{"key":"GoTerm","value":"F:L-aminoadipate-semialdehyde dehydrogenase [NAD(P)+] activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0031177","properties":[{"key":"GoTerm","value":"F:phosphopantetheine binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006281","properties":[{"key":"GoTerm","value":"P:DNA repair"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0009085","properties":[{"key":"GoTerm","value":"P:L-lysine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044550","properties":[{"key":"GoTerm","value":"P:secondary metabolite biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd09908","properties":[{"key":"EntryName","value":"H3TH_EXO1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd09857","properties":[{"key":"EntryName","value":"PIN_EXO1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd05235","properties":[{"key":"EntryName","value":"SDR_e1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.300.30:FF:000010","properties":[{"key":"EntryName","value":"Enterobactin synthetase component F"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.150.20:FF:000011","properties":[{"key":"EntryName","value":"exonuclease 1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1010:FF:000002","properties":[{"key":"EntryName","value":"Exonuclease 1, putative"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.300.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.20","properties":[{"key":"EntryName","value":"5' to 3' exonuclease, C-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1010","properties":[{"key":"EntryName","value":"5'-nuclease"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1200.10","properties":[{"key":"EntryName","value":"ACP-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.12780","properties":[{"key":"EntryName","value":"N-terminal domain of ligase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.559.30","properties":[{"key":"EntryName","value":"Nonribosomal peptide synthetase, condensation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036279","properties":[{"key":"EntryName","value":"5-3_exonuclease_C_sf"}]},{"database":"InterPro","id":"IPR010071","properties":[{"key":"EntryName","value":"AA_adenyl_dom"}]},{"database":"InterPro","id":"IPR036736","properties":[{"key":"EntryName","value":"ACP-like_sf"}]},{"database":"InterPro","id":"IPR045851","properties":[{"key":"EntryName","value":"AMP-b_sf"}]},{"database":"InterPro","id":"IPR025110","properties":[{"key":"EntryName","value":"AMP-bd_C"}]},{"database":"InterPro","id":"IPR020845","properties":[{"key":"EntryName","value":"AMP-binding_CS"}]},{"database":"InterPro","id":"IPR000873","properties":[{"key":"EntryName","value":"AMP-dep_synth/lig_dom"}]},{"database":"InterPro","id":"IPR042099","properties":[{"key":"EntryName","value":"ANL_N_sf"}]},{"database":"InterPro","id":"IPR001242","properties":[{"key":"EntryName","value":"Condensation_dom"}]},{"database":"InterPro","id":"IPR037315","properties":[{"key":"EntryName","value":"EXO1_H3TH"}]},{"database":"InterPro","id":"IPR013120","properties":[{"key":"EntryName","value":"FAR_NAD-bd"}]},{"database":"InterPro","id":"IPR008918","properties":[{"key":"EntryName","value":"HhH2"}]},{"database":"InterPro","id":"IPR014397","properties":[{"key":"EntryName","value":"Lys2"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR029060","properties":[{"key":"EntryName","value":"PIN-like_dom_sf"}]},{"database":"InterPro","id":"IPR044752","properties":[{"key":"EntryName","value":"PIN-like_EXO1"}]},{"database":"InterPro","id":"IPR020806","properties":[{"key":"EntryName","value":"PKS_PP-bd"}]},{"database":"InterPro","id":"IPR009081","properties":[{"key":"EntryName","value":"PP-bd_ACP"}]},{"database":"InterPro","id":"IPR006162","properties":[{"key":"EntryName","value":"Ppantetheine_attach_site"}]},{"database":"InterPro","id":"IPR010080","properties":[{"key":"EntryName","value":"Thioester_reductase-like_dom"}]},{"database":"InterPro","id":"IPR006086","properties":[{"key":"EntryName","value":"XPG-I_dom"}]},{"database":"InterPro","id":"IPR006084","properties":[{"key":"EntryName","value":"XPG/Rad2"}]},{"database":"InterPro","id":"IPR006085","properties":[{"key":"EntryName","value":"XPG_DNA_repair_N"}]},{"database":"NCBIfam","id":"TIGR01733","properties":[{"key":"EntryName","value":"AA-adenyl-dom"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR03443","properties":[{"key":"EntryName","value":"alpha_am_amid"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01746","properties":[{"key":"EntryName","value":"Thioester-redct"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR44845","properties":[{"key":"EntryName","value":"CARRIER DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR44845:SF1","properties":[{"key":"EntryName","value":"L-2-AMINOADIPATE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00501","properties":[{"key":"EntryName","value":"AMP-binding"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13193","properties":[{"key":"EntryName","value":"AMP-binding_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00668","properties":[{"key":"EntryName","value":"Condensation"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07993","properties":[{"key":"EntryName","value":"NAD_binding_4"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00550","properties":[{"key":"EntryName","value":"PP-binding"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00867","properties":[{"key":"EntryName","value":"XPG_I"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00752","properties":[{"key":"EntryName","value":"XPG_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00853","properties":[{"key":"EntryName","value":"XPGRADSUPER"}]},{"database":"SMART","id":"SM00279","properties":[{"key":"EntryName","value":"HhH2"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00823","properties":[{"key":"EntryName","value":"PKS_PP"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00484","properties":[{"key":"EntryName","value":"XPGI"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00485","properties":[{"key":"EntryName","value":"XPGN"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47807","properties":[{"key":"EntryName","value":"5' to 3' exonuclease, C-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56801","properties":[{"key":"EntryName","value":"Acetyl-CoA synthetase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47336","properties":[{"key":"EntryName","value":"ACP-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52777","properties":[{"key":"EntryName","value":"CoA-dependent acyltransferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF88723","properties":[{"key":"EntryName","value":"PIN domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00455","properties":[{"key":"EntryName","value":"AMP_BINDING"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50075","properties":[{"key":"EntryName","value":"CARRIER"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00012","properties":[{"key":"EntryName","value":"PHOSPHOPANTETHEINE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTFNTVMTPVASTADLAEVSSRVSRWQDRLRSPTELQLPTDYPRPIPLKVVEAMETFELSPLSSLSVLQLSLYLQQHATDNTASPFTVLLAAFSVLLHRYTAEEDIVVGSSSESLNPLVLRLAVKAEDSFLDVLQMAQRVSMEAAADEVPFAALMSAYQADGGEADASAAPSLFRVRFFNQTDADEATLRRTTTQTTDFTVLVRQKSTGSLRQLHPTIELQIVYNQVLFTAQRMAHMVAQLQMVLATAGETLGKVQAGKEVPAEMQVGRMSIASALDLAAVPDPRADLAWSEFPGSITSIFARNAQAHPDRRFVVENVLRSGVARSFTYMQMLRAARVLSRTLRDGGVVREDVVVVYAYRGVDLVVAILGVLMAGATYSVVDPAYPAARQNVYLGVAQPRGLVVLEHAGKLASEVQAYVDNELQVVCTVAGMELRDDGELVSAGDAMARAARLVDSSEVDSDIVAVGHDSVGTLSFTSGSTGIPKGVRGRHYSLTHFYPWMGAEFGLGASDRFTMLSGIAHDPIQRDVFTPVFFGAELHIPTAEDIGVPGQLAQWMGEHEISVTHLTPAMGQLLSANATSQIGSLRNAFFVGDLLTKRDCHRLQALAANCRIVNMYGTTETQRAVSFCAIPPHSANASFLATAKDVIPAGRGMKDVQLLVVNRHGSGGMCAVGEVGEIYVRSGGLAEGYLQLPEATAEKFVDNWLAAAPSAAAAAAATPSATTPSTEPDGLPYYKGARDRMYRTGDLGRYRADGDVECIGRIDDQVKIRGFRIELGEINNMLSMHPRIRANVTLVRRDKYEEKTLVAYIVPSEEEQRADDPGRQLLIGSVREYLRQKLPAYAVPAVFVPLRRLPLTPNGKIDRAALPFPDTPAPPQQQAGGGSPTERALAAVWADVLGLAHPPAPEASFFDVGGHSVAATRMVFRVRTDFAVDAPLGLVFRCPVLRDMAAAIDALRGELQLPEAAAPEAAPEAEATSEYAADLAELIAQLPLPPAAAPAAVPEDATYLLTGATGFLGAFVLDALLRRHPRASVVCLVRAADSPAAMQRVRQAAVANLVWTDDWARRVRAVAGDLAQPALGLSEADWAACARADVIVHNGALVHWVYPYARLRAANVLSTLEALRLAAAGRPKRLVFVSSTSALDTDHYVQLGCVGESDDLEGARTGLMSGYGQSKWVAERLLMHARQCGWPVAIVRPGYVLGDSRSGATNADDFLWRLAKGCAQLQLSPVMANPVNVCPVDYVADVVAQAASHPRALEHMVYHVFNHAGFRFHDIFDLMRGFGYPMVDAEYMRWRGVLMESTLDEKDSALYPLLHFVLDDLPTSTKSPDLDDKHTRALLEGSGVVCPDIKNLFGLYLAYLIKAGFLDKPEGPAEHALPVLDIEVQGLMGITGLIPLLREAQRSGHVKEFSGQTVGVDSYIWLYKGAFSCASDLALNLPTTKYITFFLSRARMLRHHGIDPLFVFDGGPLPSKLHTELERQRNRSERRQTAVKLWNQSKRKQAYEQFQRCVEVTPMMAKMVIDELRKEGFRCLVAPYEADAQLAYLESQGIITAAISEDSDLIVFGCRNIIFKLDQYGEAVIFDRQKMMDAKAVDIKGWTNEHVRRMCILSGCDYLPSVPGVGLKKAHRYVSRSQDLRAAIQLMRGDKLLVPEEYEAEVERAELTFRYQRVYDPRAKCLAFVTPLDDTAPSIEDMPFIGVQLEPHVAHGIAVAELDPFTYLPFTTQDAVEPPLQPPSPPLVAKPVPVVRGKAAAPVTRARSLQSFWGTPKPAQTRRTPATTTAEQIPGADDCVVVVVAVPPVVPAESNNEVNVKFRGNDQYSKLVSTTQKSRFFAKPPPLATVDTDTTDTTDLSAVSTQVPATVDTPLPHTPLPVSQCETVVDDFNLESSMLSQPRLLRSETAGLQRLPLLPSEADDTRAISLFGQFTNRGAEDIPEYAKLPTYKKSK","length":1947,"molWeight":212167,"crc64":"70598773D833498F","md5":"35457C9BA211B06F0E97C3FF367CCFF2"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":2,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Modified residue":1},"uniParcId":"UPI0022DCCA77"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8LD31","uniProtkbId":"A0A9W8LD31_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":11,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2755174.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00067568"}],"value":"Folic acid synthesis protein FOL1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012458"}],"value":"2.5.1.15"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013253"}],"value":"2.7.6.3"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013043"}],"value":"4.1.2.25"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00068111"}],"value":"Folic acid synthesis protein fol1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2755174.1"}],"value":"FOL1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2755174.1"}],"value":"GGI19_001840"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00058009"}],"value":"Catalyzes three sequential steps of tetrahydrofolate biosynthesis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate = 7,8-dihydropteroate + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19949"},{"database":"ChEBI","id":"CHEBI:17836"},{"database":"ChEBI","id":"CHEBI:17839"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:72950"}],"ecNumber":"2.5.1.15","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000012"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11412"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:44841"},{"database":"ChEBI","id":"CHEBI:72950"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"2.7.6.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000198"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10540"},{"database":"ChEBI","id":"CHEBI:17001"},{"database":"ChEBI","id":"CHEBI:17071"},{"database":"ChEBI","id":"CHEBI:44841"}],"ecNumber":"4.1.2.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001353"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005013"}],"value":"Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005051"}],"value":"Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004763"}],"value":"Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009951"}],"value":"In the C-terminal section; belongs to the DHPS family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009640"}],"value":"In the N-terminal section; belongs to the DHNA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00061548"}],"value":"In the central section; belongs to the HPPK family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2755174.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":520,"modifier":"EXACT"},"end":{"value":816,"modifier":"EXACT"}},"description":"Pterin-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50972"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022909"}],"id":"KW-0289","category":"Biological process","name":"Folate biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2755174.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2755174.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000074","properties":[{"key":"ProteinId","value":"KAJ2755174.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8LD31","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"615426at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005740","properties":[{"key":"GoTerm","value":"C:mitochondrial envelope"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003848","properties":[{"key":"GoTerm","value":"F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004150","properties":[{"key":"GoTerm","value":"F:dihydroneopterin aldolase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004156","properties":[{"key":"GoTerm","value":"F:dihydropteroate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046654","properties":[{"key":"GoTerm","value":"P:tetrahydrofolate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00739","properties":[{"key":"EntryName","value":"DHPS"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00483","properties":[{"key":"EntryName","value":"HPPK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.20:FF:000006","properties":[{"key":"EntryName","value":"Dihydropteroate synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1130.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.70.560","properties":[{"key":"EntryName","value":"7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.20","properties":[{"key":"EntryName","value":"Dihydropteroate synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR045031","properties":[{"key":"EntryName","value":"DHP_synth-like"}]},{"database":"InterPro","id":"IPR006390","properties":[{"key":"EntryName","value":"DHP_synth_dom"}]},{"database":"InterPro","id":"IPR011005","properties":[{"key":"EntryName","value":"Dihydropteroate_synth-like_sf"}]},{"database":"InterPro","id":"IPR006157","properties":[{"key":"EntryName","value":"FolB_dom"}]},{"database":"InterPro","id":"IPR043133","properties":[{"key":"EntryName","value":"GTP-CH-I_C/QueF"}]},{"database":"InterPro","id":"IPR000550","properties":[{"key":"EntryName","value":"Hppk"}]},{"database":"InterPro","id":"IPR035907","properties":[{"key":"EntryName","value":"Hppk_sf"}]},{"database":"InterPro","id":"IPR000489","properties":[{"key":"EntryName","value":"Pterin-binding_dom"}]},{"database":"NCBIfam","id":"TIGR01496","properties":[{"key":"EntryName","value":"DHPS"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00526","properties":[{"key":"EntryName","value":"folB_dom"},{"key":"MatchStatus","value":"2"}]},{"database":"NCBIfam","id":"TIGR01498","properties":[{"key":"EntryName","value":"folK"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20941","properties":[{"key":"EntryName","value":"FOLATE SYNTHESIS PROTEINS"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20941:SF1","properties":[{"key":"EntryName","value":"FOLIC ACID SYNTHESIS PROTEIN FOL1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02152","properties":[{"key":"EntryName","value":"FolB"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF01288","properties":[{"key":"EntryName","value":"HPPK"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00809","properties":[{"key":"EntryName","value":"Pterin_bind"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00905","properties":[{"key":"EntryName","value":"FolB"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF55083","properties":[{"key":"EntryName","value":"6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51717","properties":[{"key":"EntryName","value":"Dihydropteroate synthetase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55620","properties":[{"key":"EntryName","value":"Tetrahydrobiopterin biosynthesis enzymes-like"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00793","properties":[{"key":"EntryName","value":"DHPS_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00794","properties":[{"key":"EntryName","value":"HPPK"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50972","properties":[{"key":"EntryName","value":"PTERIN_BINDING"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSDKIIFRDLQVRTVLGNDSWERKKQQPLLITAEIHTSIASAGKTDKVTESVHYGIACKRATSFAESNHKLHSLEAFAEGIAKACLGVTNRALAVHIIARKPRALLHAEYAGVEIFRTRKEALGSWGDDLAQEGDEADDEFARRKALVDAERAAAEAEAGRLAQEDRIIVKTLSLSTIIGVNLWERHYKQLVHIDLVLHMAKSAGLGAPESDKVPRYRNFRTVVDAVTDLVEKSSYRTVEALATAIARTATKQCKVPKITVRVEKPSALMFAACSAVEITRVLGDYAAMSSAAVSVAPTPRAASPVAAASSDDADKAAKSGTHSAYIALGTNLGNRLENMHQALHRLNTDLPNSHVVESSFLYQTAPMYVTDQPAFLNAACLVKTGLEPLALLDELKRIEAEMGRDFGMYRNGPRIMDLDILFYDEIDMQTERLTIPHALLHERRFQLGPLCDIDSDLMHHRLGKTTGALFRHLTTHSDAPDDIVRVTPLRASTDAGSGAGECNESAILKALSPSSQKETVFMGILNCTPDSFSDGGDFATLDLAVEHAAALTKSGADILDIGGQSTRPGATQVGVDEEIRRVVPVIQRIRELGITTPISIDTFYAEVAAAALDVGADIVNDVSGGSFDAKMLPLVARRQCPYVMMHMRGDPSTMAKMNDYGEYGGDVVRGTRFELAQRVRAALDCGVPRWNIILDPGIGFAKEGAQNFEFLRRLPELTARNIRASAKNATASLATGSAGHEEGEEGFIDEDLATGLANYPVLVGSSRKRFIGQATGKTEAKDRVWGTAATVTAAIQGGASIVRIHDVAEMVDVARVSDHIYRRK","length":825,"molWeight":89402,"crc64":"2D347823A8E1A70D","md5":"FC3142E2E2A14303A9226949487B60AA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"PATHWAY":3,"SIMILARITY":3,"CAUTION":1},"countByFeatureType":{"Domain":1},"uniParcId":"UPI0022D04B58"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GNX6","uniProtkbId":"A0A9W8GNX6_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":13,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2748466.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044078"}],"value":"ATP-dependent RNA helicase DRS1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012552"}],"value":"3.6.4.13"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044094"}],"value":"ATP-dependent RNA helicase drs1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2748466.1"}],"value":"DRS1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2748466.1"}],"value":"GGI19_006103"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043881"}],"value":"ATP-binding RNA helicase involved in ribosome assembly"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"3.6.4.13","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047984"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004604"}],"value":"Nucleus, nucleolus","id":"SL-0188"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043999"}],"value":"Belongs to the DEAD box helicase family. DDX27/DRS1 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2748466.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":449,"modifier":"EXACT"}},"description":"Helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51192"}]},{"type":"Domain","location":{"start":{"value":460,"modifier":"EXACT"},"end":{"value":624,"modifier":"EXACT"}},"description":"Helicase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51194"}]},{"type":"Region","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":665,"modifier":"EXACT"},"end":{"value":709,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Motif","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"Q motif","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00552"}]},{"type":"Compositional bias","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":682,"modifier":"EXACT"},"end":{"value":693,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000492"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022517"}],"id":"KW-0690","category":"Biological process","name":"Ribosome biogenesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2748466.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2748466.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010001069","properties":[{"key":"ProteinId","value":"KAJ2748466.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GNX6","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"10259843at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005730","properties":[{"key":"GoTerm","value":"C:nucleolus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016787","properties":[{"key":"GoTerm","value":"F:hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003676","properties":[{"key":"GoTerm","value":"F:nucleic acid binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003724","properties":[{"key":"GoTerm","value":"F:RNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"CDD","id":"cd17947","properties":[{"key":"EntryName","value":"DEADc_DDX27"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18787","properties":[{"key":"EntryName","value":"SF2_C_DEAD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000842","properties":[{"key":"EntryName","value":"ATP-dependent RNA helicase DRS1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR011545","properties":[{"key":"EntryName","value":"DEAD/DEAH_box_helicase_dom"}]},{"database":"InterPro","id":"IPR014001","properties":[{"key":"EntryName","value":"Helicase_ATP-bd"}]},{"database":"InterPro","id":"IPR001650","properties":[{"key":"EntryName","value":"Helicase_C-like"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR000629","properties":[{"key":"EntryName","value":"RNA-helicase_DEAD-box_CS"}]},{"database":"InterPro","id":"IPR014014","properties":[{"key":"EntryName","value":"RNA_helicase_DEAD_Q_motif"}]},{"database":"PANTHER","id":"PTHR47959:SF1","properties":[{"key":"EntryName","value":"ATP-DEPENDENT RNA HELICASE DBPA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR47959","properties":[{"key":"EntryName","value":"ATP-DEPENDENT RNA HELICASE RHLE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00270","properties":[{"key":"EntryName","value":"DEAD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00271","properties":[{"key":"EntryName","value":"Helicase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00487","properties":[{"key":"EntryName","value":"DEXDc"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00490","properties":[{"key":"EntryName","value":"HELICc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00039","properties":[{"key":"EntryName","value":"DEAD_ATP_HELICASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51192","properties":[{"key":"EntryName","value":"HELICASE_ATP_BIND_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51194","properties":[{"key":"EntryName","value":"HELICASE_CTER"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51195","properties":[{"key":"EntryName","value":"Q_MOTIF"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAIIEDDFIMTIGDDDEVPDLEAVANDAPPQNKRKLNGKQKGGKKAKPQESKDEGDMTKGFLVDLETDGLDAVPQTLDFTLARASLKKRRNPGMYSTLDEKIALSRRAAKIARLAALDKPEEMEVSEEEVEDNVSDDNNDNEDVESASDDDEEEGASDDDEEEDANDSAVEDDSMVDAPVLEGESGSEAESDEEESESEVDSESEESEDGSSSEEESEVDEIEEARKRAYFAKPEEGPAIDIPESFTTMNLSRQIMKGLTKLGFAQPTPIQARTIPLALLGKDICGGAQTGSGKTAAFLVPILERLLYRPKNTTVTRVLILCPTRELAIQCHNVSTKLAGFTDISTCLCVGGLSLKLQESELKLRPDVVIATPGRLIDHLRNSQSFHLDQIEILVMDEADRMLDDGFEDELTEIIKACPQKRQTMLFSATMTDNVDKLIRLSLQKPVRVQIDPPKSAARGLTQEFVRVRTNKDEDRTALLAALCKRHFKSKCIIFFRSKAAAHQMKIIFGLLGMRAGELHGNLSQEGRLQALEQFRDGHVDFLMATDLAARGLDVTGIDTVINYTMPTQFPQYLHRIGRTARAGRTGRAITLIGESDRKMLKLAVKNSPKDKIKQRVVPNETLNKYRTKVDDLVDQVKDIMAEERQEKMLNDAEMQVTRATNLIQHKDEIKNRPRRTWFQSTKDRKEAKDVADRTYAGKIKSKRSYDKN","length":709,"molWeight":79168,"crc64":"D5DBF6D60F4F11F9","md5":"75CF00DFB6E6F99E314E5A46CA30FCE3"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":3,"Motif":1,"Compositional bias":5},"uniParcId":"UPI0022D2FF73"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GP93","uniProtkbId":"A0A9W8GP93_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":9,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2744956.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00071722"}],"value":"tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+]"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00066483"}],"value":"1.3.1.90"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00078338"}],"value":"tRNA-dihydrouridine synthase 4"}}],"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2744956.1"}],"value":"DUS4"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2744956.1"}],"value":"GGI19_006551"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5,6-dihydrouridine(20a) in tRNA + NAD(+) = uridine(20a) in tRNA + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53348"},{"database":"Rhea","id":"RHEA-COMP:13535"},{"database":"Rhea","id":"RHEA-COMP:13536"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:65315"},{"database":"ChEBI","id":"CHEBI:74443"}],"ecNumber":"1.3.1.90","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051779"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:53350"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051779"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5,6-dihydrouridine(20a) in tRNA + NADP(+) = uridine(20a) in tRNA + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53344"},{"database":"Rhea","id":"RHEA-COMP:13535"},{"database":"Rhea","id":"RHEA-COMP:13536"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:65315"},{"database":"ChEBI","id":"CHEBI:74443"}],"ecNumber":"1.3.1.90","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052996"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:53346"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052996"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5,6-dihydrouridine(20b) in tRNA + NAD(+) = uridine(20b) in tRNA + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53352"},{"database":"Rhea","id":"RHEA-COMP:13537"},{"database":"Rhea","id":"RHEA-COMP:13538"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:65315"},{"database":"ChEBI","id":"CHEBI:74443"}],"ecNumber":"1.3.1.90","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051932"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:53354"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051932"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5,6-dihydrouridine(20b) in tRNA + NADP(+) = uridine(20b) in tRNA + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53356"},{"database":"Rhea","id":"RHEA-COMP:13537"},{"database":"Rhea","id":"RHEA-COMP:13538"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:65315"},{"database":"ChEBI","id":"CHEBI:74443"}],"ecNumber":"1.3.1.90","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050434"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:53358"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050434"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 5,6-dihydrouridine in mRNA + NAD(+) = a uridine in mRNA + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:69851"},{"database":"Rhea","id":"RHEA-COMP:14658"},{"database":"Rhea","id":"RHEA-COMP:17789"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:65315"},{"database":"ChEBI","id":"CHEBI:74443"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048342"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:69853"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048342"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 5,6-dihydrouridine in mRNA + NADP(+) = a uridine in mRNA + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:69855"},{"database":"Rhea","id":"RHEA-COMP:14658"},{"database":"Rhea","id":"RHEA-COMP:17789"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:65315"},{"database":"ChEBI","id":"CHEBI:74443"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049447"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:69857"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049447"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001917"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060741"}],"value":"Belongs to the Dus family. Dus4 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2744956.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"DUS-like FMN-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01207"}]},{"type":"Non-terminal residue","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2744956.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022643"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022664"}],"id":"KW-0507","category":"Biological process","name":"mRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2744956.1"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2744956.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2744956.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010001498","properties":[{"key":"ProteinId","value":"KAJ2744956.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GP93","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9977870at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0102266","properties":[{"key":"GoTerm","value":"F:tRNA-dihydrouridine20a synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0102267","properties":[{"key":"GoTerm","value":"F:tRNA-dihydrouridine20b synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd02801","properties":[{"key":"EntryName","value":"DUS_like_FMN"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000159","properties":[{"key":"EntryName","value":"tRNA-dihydrouridine synthase 4"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR035587","properties":[{"key":"EntryName","value":"DUS-like_FMN-bd"}]},{"database":"InterPro","id":"IPR018517","properties":[{"key":"EntryName","value":"tRNA_hU_synthase_CS"}]},{"database":"PANTHER","id":"PTHR11082","properties":[{"key":"EntryName","value":"TRNA-DIHYDROURIDINE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11082:SF31","properties":[{"key":"EntryName","value":"TRNA-DIHYDROURIDINE(20A_20B) SYNTHASE [NAD(P)+]-LIKE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01207","properties":[{"key":"EntryName","value":"Dus"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51395","properties":[{"key":"EntryName","value":"FMN-linked oxidoreductases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01136","properties":[{"key":"EntryName","value":"UPF0034"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVYHGQRRSLLQLFEDQPRLNVCAPMVRYSKGAFREIVRDYNVDIAYTPMILADVFKSSEFARQDYTTNDSDCPVVVQFAAHDPVDLAQAAQLVAPYADGIDLNCGCPQKWAYKERIGAYLSDRPELVRDMVRTVKSAVSIPCSVKIRKHPTDVRQTVELVRRAQMMGVDWITIHGRTRHQRSTEPIDYDVIKLVKESVSVPVLANGSIFTLADAEAMYENTGVDGVMAARGLLQNPALFAGFEHTPLACVEKYVNRAL","length":259,"molWeight":29066,"crc64":"650C14D2BBE25D80","md5":"A8A3C75F6840E58E8846667BEB68EFF9"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":6,"COFACTOR":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Non-terminal residue":1},"uniParcId":"UPI0022D6162D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GPJ7","uniProtkbId":"A0A9W8GPJ7_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":9,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2749826.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00019397"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363013"}],"value":"Triosephosphate isomerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011940"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363013"}],"value":"5.3.1.1"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2749826.1"}],"value":"GGI19_005455"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18585"},{"database":"ChEBI","id":"CHEBI:57642"},{"database":"ChEBI","id":"CHEBI:59776"}],"ecNumber":"5.3.1.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000474"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363013"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004742"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363013"}],"value":"Carbohydrate biosynthesis; gluconeogenesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004680"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363013"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007422"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10127"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363013"}],"value":"Belongs to the triosephosphate isomerase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2749826.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Active site","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"Electrophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10127"}]},{"type":"Active site","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10127"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10127"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10127"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363013"}],"id":"KW-0312","category":"Biological process","name":"Gluconeogenesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363013"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363013"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2749826.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2749826.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000692","properties":[{"key":"ProteinId","value":"KAJ2749826.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GPJ7","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"6715177at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004807","properties":[{"key":"GoTerm","value":"F:triose-phosphate isomerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006094","properties":[{"key":"GoTerm","value":"P:gluconeogenesis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046166","properties":[{"key":"GoTerm","value":"P:glyceraldehyde-3-phosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0019563","properties":[{"key":"GoTerm","value":"P:glycerol catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006096","properties":[{"key":"GoTerm","value":"P:glycolytic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00311","properties":[{"key":"EntryName","value":"TIM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000025","properties":[{"key":"EntryName","value":"Triosephosphate isomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00147_B","properties":[{"key":"EntryName","value":"TIM_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR035990","properties":[{"key":"EntryName","value":"TIM_sf"}]},{"database":"InterPro","id":"IPR022896","properties":[{"key":"EntryName","value":"TrioseP_Isoase_bac/euk"}]},{"database":"InterPro","id":"IPR000652","properties":[{"key":"EntryName","value":"Triosephosphate_isomerase"}]},{"database":"InterPro","id":"IPR020861","properties":[{"key":"EntryName","value":"Triosephosphate_isomerase_AS"}]},{"database":"NCBIfam","id":"TIGR00419","properties":[{"key":"EntryName","value":"tim"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21139","properties":[{"key":"EntryName","value":"TRIOSEPHOSPHATE ISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21139:SF2","properties":[{"key":"EntryName","value":"TRIOSEPHOSPHATE ISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00121","properties":[{"key":"EntryName","value":"TIM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51351","properties":[{"key":"EntryName","value":"Triosephosphate isomerase (TIM)"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00171","properties":[{"key":"EntryName","value":"TIM_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51440","properties":[{"key":"EntryName","value":"TIM_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTRTFWVGGNWKMNGSVASIKDLATTFNAGKTPADVEVVIGAPYVYIPLLADTLRKDWAVAGENCYVHATGAYTGEISPEMLADVGAKWVILGHSERRHILNESSEFTAQKVVKALAAGLKVALCVGELLEEREAGTTQVIVNTQLDAVVSAVSESDWANIVIAYEPVWAIGTGKVASPEQAQEVHAAIREYLKAAVSPKVAEETRIAYGGSVGGKNCKELAQKPDVDGFLVGGASLKPEFLDIVHATQ","length":249,"molWeight":26538,"crc64":"28D6108BC6C0F383","md5":"63FB9D23B5780DC57B8DD3114F8DF66B"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Active site":2,"Binding site":2},"uniParcId":"UPI0022D069A9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GPK8","uniProtkbId":"A0A9W8GPK8_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":12,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2749850.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00017386"}],"value":"ATP-dependent DNA helicase CHL1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044969"}],"value":"5.6.2.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00016387"}],"value":"ATP-dependent DNA helicase chl1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029709"}],"value":"Chromosome loss protein 1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044998"},{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045008"}],"value":"DNA 5'-3' helicase CHL1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2749850.1"}],"value":"CHL1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2749850.1"}],"value":"GGI19_005441"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045702"}],"value":"ATP-dependent DNA helicase important for chromosome transmission and normal cell cycle progression in G(2)/M. May have a role in changing DNA topology to allow the loading of proteins involved in maintaining sister chromatid cohesion in the vicinity of the centromeres. Has a specific role in chromosome segregation during meiosis II"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048954"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction.","ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093875"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001966"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008435"}],"value":"Belongs to the DEAD box helicase family. DEAH subfamily. DDX11/CHL1 sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2749850.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"Helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51193"}]},{"type":"Region","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2749850.1"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2749850.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2749850.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000687","properties":[{"key":"ProteinId","value":"KAJ2749850.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GPK8","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"267079at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0043139","properties":[{"key":"GoTerm","value":"F:5'-3' DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016818","properties":[{"key":"GoTerm","value":"F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0034085","properties":[{"key":"GoTerm","value":"P:establishment of sister chromatid cohesion"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd18788","properties":[{"key":"EntryName","value":"SF2_C_XPD"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"3"}]},{"database":"InterPro","id":"IPR006555","properties":[{"key":"EntryName","value":"ATP-dep_Helicase_C"}]},{"database":"InterPro","id":"IPR045028","properties":[{"key":"EntryName","value":"DinG/Rad3-like"}]},{"database":"InterPro","id":"IPR014013","properties":[{"key":"EntryName","value":"Helic_SF1/SF2_ATP-bd_DinG/Rad3"}]},{"database":"InterPro","id":"IPR006554","properties":[{"key":"EntryName","value":"Helicase-like_DEXD_c2"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR010614","properties":[{"key":"EntryName","value":"RAD3-like_helicase_DEAD"}]},{"database":"InterPro","id":"IPR013020","properties":[{"key":"EntryName","value":"Rad3/Chl1-like"}]},{"database":"NCBIfam","id":"TIGR00604","properties":[{"key":"EntryName","value":"rad3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11472:SF41","properties":[{"key":"EntryName","value":"ATP-DEPENDENT DNA HELICASE DDX11-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11472","properties":[{"key":"EntryName","value":"DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06733","properties":[{"key":"EntryName","value":"DEAD_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13307","properties":[{"key":"EntryName","value":"Helicase_C_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00488","properties":[{"key":"EntryName","value":"DEXDc2"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00491","properties":[{"key":"EntryName","value":"HELICc2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51193","properties":[{"key":"EntryName","value":"HELICASE_ATP_BIND_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVTRILDETAPAECLPTPQTASEFSFPIATPYSIQLDFMQRLFETIEKREFAIFESPTGTGKSLSIICGALTWLKHDTERKARVAPIAADSVLSTTKEDQRPDWVIAYEKKQQLDASNAVGSDSDDAQQKYSRWVANTRRKEAAERKKGMMASRRAAPTDASKKRKPDEDGSTDNDDEMMVVEAYYSGDEDNAQQKSGSKLGDDGEVQYSAAVRKLLERRAGNRPLYDSSDDDNSDNDDSGESAGPPKEPSVTKIIYASRTHSQLQQFVNEIKRTQFASADKVKCVTLGSRMQLCVNDRARQGAQSVHAINERCLEMQTAGSKKSARCGYLPLQHTPMLDFKDATASVIMDIEELAKEGRRRCTCPYYGARASINGAQVVALPYNTLLSRSARQAMGISLTGSVVIVDEAHNLVDTILAIHSIALDWRTVRALLEMVQMYFTKYWRRLKGSNVTYIRQTIALLKALNKFMQSTVADSATRVVSVNEFLTLAHADHINVYKIDRYLRESKLGRKLNMFSDRLAQNNSATSNKRPTTAVRETVAGPAPATAVAAFEAFMECLGKPDRTGSRLVIRTISSNSGTEVELKYLQLDPSEAFGEICAEARAVVLAGGTMKPANDVVEQLLPGRSESQPTPDSKLDPANARLFAWSHVVDRSHICSIVVGSGPTGTALRFAHGDQGDSAKLREAGLALAALCQVIPGGVVAFFPSYALLDRMHRNWTAAGIADRIAKRKPVFVESSTSSGDVLELYSARVRAVGSTGALLLSVVGGRLSEGINFSDDLGRAVVMIGVPFPSLASPELAERLAYYEGMGGAQSTASGVIGSMGPRAKELYESLCMRAVNQSIGRAIRHRNDYAAIVFLDARYAEPRIAHKLPTWIAGSSAPNAASAFGPALAQVSSFFKREFT","length":905,"molWeight":98724,"crc64":"6809E0A2D4D0659A","md5":"B05820A6C0CC69C18CDBED199583F9D2"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Compositional bias":3},"uniParcId":"UPI0022D271C3"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GQ17","uniProtkbId":"A0A9W8GQ17_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":13,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750223.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034808"}],"value":"DNA 3'-5' helicase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034808"}],"value":"5.6.2.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00078607"}],"value":"DNA repair helicase RAD25"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00076598"}],"value":"RNA polymerase II transcription factor B subunit SSL2"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00075489"}],"value":"Suppressor of stem-loop mutation 2"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750223.1"}],"value":"SSL2_1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750223.1"}],"value":"GGI19_005230"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00058901"}],"value":"ATP-dependent 3'-5' DNA helicase/translocase; binds dsDNA rather than ssDNA, unzipping it in a translocase rather than classical helicase activity. Component of the general transcription and DNA repair factor IIH (TFIIH) core complex. When complexed to CDK-activating kinase (CAK), involved in RNA transcription by RNA polymerase II. Also involved in transcription-coupled nucleotide excision repair (NER) of damaged DNA. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATPase activity of XPB/SSL2, but not its helicase activity, is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of XPB/SSL2 is required for promoter opening and promoter escape"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048988"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.","ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034617"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011640"}],"value":"Component of the 7-subunit TFIIH core complex composed of XPB/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is active in NER. The core complex associates with the 3-subunit CTD-kinase module TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006637"}],"value":"Belongs to the helicase family. RAD25/XPB subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750223.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":544,"modifier":"EXACT"}},"description":"Helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51192"}]},{"type":"Domain","location":{"start":{"value":598,"modifier":"EXACT"},"end":{"value":756,"modifier":"EXACT"}},"description":"Helicase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51194"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750223.1"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023015"}],"id":"KW-0805","category":"Biological process","name":"Transcription regulation"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750223.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750223.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000605","properties":[{"key":"ProteinId","value":"KAJ2750223.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GQ17","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"10262986at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0000112","properties":[{"key":"GoTerm","value":"C:nucleotide-excision repair factor 3 complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005675","properties":[{"key":"GoTerm","value":"C:transcription factor TFIIH holo complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0097550","properties":[{"key":"GoTerm","value":"C:transcription preinitiation complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0043138","properties":[{"key":"GoTerm","value":"F:3'-5' DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016787","properties":[{"key":"GoTerm","value":"F:hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006289","properties":[{"key":"GoTerm","value":"P:nucleotide-excision repair"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006367","properties":[{"key":"GoTerm","value":"P:transcription initiation at RNA polymerase II promoter"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd18029","properties":[{"key":"EntryName","value":"DEXHc_XPB"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18789","properties":[{"key":"EntryName","value":"SF2_C_XPB"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000077","properties":[{"key":"EntryName","value":"Probable DNA repair helicase RAD25"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000117","properties":[{"key":"EntryName","value":"Putative DNA repair helicase rad25"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR050615","properties":[{"key":"EntryName","value":"ATP-dep_DNA_Helicase"}]},{"database":"InterPro","id":"IPR032438","properties":[{"key":"EntryName","value":"ERCC3_RAD25_C"}]},{"database":"InterPro","id":"IPR006935","properties":[{"key":"EntryName","value":"Helicase/UvrB_N"}]},{"database":"InterPro","id":"IPR014001","properties":[{"key":"EntryName","value":"Helicase_ATP-bd"}]},{"database":"InterPro","id":"IPR001650","properties":[{"key":"EntryName","value":"Helicase_C-like"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR001161","properties":[{"key":"EntryName","value":"XPB/Ssl2"}]},{"database":"InterPro","id":"IPR032830","properties":[{"key":"EntryName","value":"XPB/Ssl2_N"}]},{"database":"NCBIfam","id":"TIGR00603","properties":[{"key":"EntryName","value":"rad25"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11274:SF0","properties":[{"key":"EntryName","value":"GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11274","properties":[{"key":"EntryName","value":"RAD25/XP-B DNA REPAIR HELICASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16203","properties":[{"key":"EntryName","value":"ERCC3_RAD25_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13625","properties":[{"key":"EntryName","value":"Helicase_C_3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04851","properties":[{"key":"EntryName","value":"ResIII"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00851","properties":[{"key":"EntryName","value":"XRODRMPGMNTB"}]},{"database":"SMART","id":"SM00487","properties":[{"key":"EntryName","value":"DEXDc"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00490","properties":[{"key":"EntryName","value":"HELICc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51192","properties":[{"key":"EntryName","value":"HELICASE_ATP_BIND_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51194","properties":[{"key":"EntryName","value":"HELICASE_CTER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSKWTVNDYEGLEDAEEQQLSPVVCEIASDTERDGYSVPASPAEDAIDGSDRKSDDDEDETNSEDLAQRDISSGLVPKNFVTAFGNSGDDDTDEYDVVRVPKRNLTTGLFGKGDYNYLKLKPDHESRPLWICPHSGHIILEAFSSIAEQAIDFLIAISEPISRPTHIHEYKLTPHSLYAAVSVGLDTNDIIEVLNRLSKVPIPADVIKAINQCTRSYGKVKLVLKHRRYFVESSHPDILQHLLRDPIIAQARILPDEGVDGAGSREGIVIQESSQMRDLNVGSLPKRSARLPSTAASIGPGVDVEGFGALNDDEDDDVENIVHAFEISNTSVENVRKRCNEIDYPMLEEYDFRNDTINPNLDIDLKPATTIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKTLVGITAACTIKKSILCLCTSSVSVMQWKQQFLQWSTIKEEQIAVFTSDQKMPFLGEAGLVISTYAMVANTRKRSPRGQLMMDFISQHEWGMLLLDEVHVAPAAVFRHVVTNVAAHSKLGLTATLVREDDKIDDLSFLIGPKLYEANWMDLANKGHIATVQCAEVWCTMTPEFYKAYLEETSYKRILLYSMNPNKLRTCQYLINFHRNRGDKTIVFIDNVYALRAYAEKLGLPYICGETRQIERMRILHQFQHNPIVNTILLSKVGDTSIDLPEATCLIQVSSHFGSRRQEAQRLGRILRAKRRNDEGFNAFFYSLVSKDTQEMYFSTKRQQFLIDQGYSFKVITHLEGMENCPDLVYGDKDSQKSLLHSVMMAKDADADILEDMPDDLYFDGRIQANAGVRHTAGSLKSLAGSVAKGRVERKKPVEHHPLLKRQFFKKR","length":841,"molWeight":94537,"crc64":"9A6EC5B3DA9D0656","md5":"6AF9044A1FA0FFAEBE9D82164915160F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":1},"uniParcId":"UPI0022D69893"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GQV1","uniProtkbId":"A0A9W8GQV1_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":11,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750411.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Ribokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"RK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"2.7.1.15"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750411.1"}],"value":"RBK1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750411.1"}],"value":"GGI19_005124"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-ribose + ATP = D-ribose 5-phosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13697"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:47013"},{"database":"ChEBI","id":"CHEBI:78346"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.15","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Activated by a monovalent cation that binds near, but not in, the active site. The most likely occupant of the site in vivo is potassium. Ion binding induces a conformational change that may alter substrate affinity"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750411.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":240,"modifier":"EXACT"}},"description":"Carbohydrate kinase PfkB","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00294"}]},{"type":"Active site","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}]},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":338,"modifier":"EXACT"},"end":{"value":338,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":343,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":347,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022958"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0630","category":"Ligand","name":"Potassium"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750411.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750411.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000567","properties":[{"key":"ProteinId","value":"KAJ2750411.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GQV1","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"415590at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004747","properties":[{"key":"GoTerm","value":"F:ribokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046835","properties":[{"key":"GoTerm","value":"P:carbohydrate phosphorylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019303","properties":[{"key":"GoTerm","value":"P:D-ribose catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.40.1190.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01987","properties":[{"key":"EntryName","value":"Ribokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011611","properties":[{"key":"EntryName","value":"PfkB_dom"}]},{"database":"InterPro","id":"IPR002139","properties":[{"key":"EntryName","value":"Ribo/fructo_kinase"}]},{"database":"InterPro","id":"IPR011877","properties":[{"key":"EntryName","value":"Ribokinase"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"PANTHER","id":"PTHR10584:SF166","properties":[{"key":"EntryName","value":"RIBOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10584","properties":[{"key":"EntryName","value":"SUGAR KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00294","properties":[{"key":"EntryName","value":"PfkB"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00990","properties":[{"key":"EntryName","value":"RIBOKINASE"}]},{"database":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MQPRVVSFASINVDEVYSMPRIVRPGETLTSTRRQQNAGGKGANASVAAARAGAPVHVVGKIGSDGLWVRDIIEHAGANVSLVGALDDTATGRAIIQVDANGENAIFLFPGANHRLTETDAHRAFAQFAKGDWLLLTNETTAVAEAITQAHEIGIQVLWNPAPMHDDFLLTNRVVGLVDVLVVNESELLRLAQQISGCDSSDDYEVLARQVMKELGCSVVVATLGSSGCIGLVRRPTSNAHSIPIVGSSTDISIVSGSGGDDTDDIDGIRVISMSCSPIRIDQVIDTTAAGDTWVGYFVAELARAQGESPESIGARAALTPAMVGRAMTIATYASGISVTRMGAVPSIPMREEVEAFIRTKRHE","length":364,"molWeight":38440,"crc64":"3AE2E99C9E18028B","md5":"F4EB3D7B412A0E161E319B015FC0888C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":13},"uniParcId":"UPI0022D29767"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GQZ4","uniProtkbId":"A0A9W8GQZ4_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":13,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750521.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012513"}],"value":"non-specific serine/threonine protein kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012513"}],"value":"2.7.11.1"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750521.1"}],"value":"GCN2_1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750521.1"}],"value":"GGI19_005058"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17989"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048679"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047899"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"value":"Belongs to the protein kinase superfamily. Ser/Thr protein kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750521.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":691,"modifier":"EXACT"}},"description":"Protein kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50011"}]},{"type":"Region","location":{"start":{"value":297,"modifier":"EXACT"},"end":{"value":373,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":423,"modifier":"EXACT"},"end":{"value":479,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":360,"modifier":"EXACT"},"end":{"value":371,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":532,"modifier":"EXACT"},"end":{"value":532,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10141"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Non-terminal residue","location":{"start":{"value":826,"modifier":"EXACT"},"end":{"value":826,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750521.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10141"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750521.1"}],"id":"KW-0396","category":"Molecular function","name":"Initiation factor"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10141"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750521.1"}],"id":"KW-0648","category":"Biological process","name":"Protein biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022527"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"id":"KW-0723","category":"Molecular function","name":"Serine/threonine-protein kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00159"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750521.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750521.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000544","properties":[{"key":"ProteinId","value":"KAJ2750521.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GQZ4","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"341578at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004694","properties":[{"key":"GoTerm","value":"F:eukaryotic translation initiation factor 2alpha kinase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:1990625","properties":[{"key":"GoTerm","value":"P:negative regulation of cytoplasmic translational initiation in response to stress"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"FunFam","id":"3.30.200.20:FF:000379","properties":[{"key":"EntryName","value":"eIF-2-alpha kinase GCN2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.930.10","properties":[{"key":"EntryName","value":"Bira Bifunctional Protein, Domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.200.20","properties":[{"key":"EntryName","value":"Phosphorylase Kinase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.510.10","properties":[{"key":"EntryName","value":"Transferase(Phosphotransferase) domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR045864","properties":[{"key":"EntryName","value":"aa-tRNA-synth_II/BPL/LPL"}]},{"database":"InterPro","id":"IPR050339","properties":[{"key":"EntryName","value":"CC_SR_Kinase"}]},{"database":"InterPro","id":"IPR011009","properties":[{"key":"EntryName","value":"Kinase-like_dom_sf"}]},{"database":"InterPro","id":"IPR000719","properties":[{"key":"EntryName","value":"Prot_kinase_dom"}]},{"database":"InterPro","id":"IPR017441","properties":[{"key":"EntryName","value":"Protein_kinase_ATP_BS"}]},{"database":"InterPro","id":"IPR008271","properties":[{"key":"EntryName","value":"Ser/Thr_kinase_AS"}]},{"database":"PANTHER","id":"PTHR11042:SF136","properties":[{"key":"EntryName","value":"EIF-2-ALPHA KINASE GCN2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11042","properties":[{"key":"EntryName","value":"EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00069","properties":[{"key":"EntryName","value":"Pkinase"},{"key":"MatchStatus","value":"2"}]},{"database":"SMART","id":"SM00220","properties":[{"key":"EntryName","value":"S_TKc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55681","properties":[{"key":"EntryName","value":"Class II aaRS and biotin synthetases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56112","properties":[{"key":"EntryName","value":"Protein kinase-like (PK-like)"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00107","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_ATP"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50011","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_DOM"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00108","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_ST"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVLGLDVLRSVANGHEPDVLEANRDAMPFPLYRVLAMMFTVDHRHRPTAMEVLNDPFFNQGLAGEHSMHRQALDSASRGLTFEMQRTARIADGAEALPPTDNDGVAVADNAAITRPFFSVAQKNIAGEAGPAHAAANFPLPATGAVAANKPPAVLPRQQNQRSPEDLPGVEHFMQPYASRYHTDFEEVEFLGKGGFGSVVKARNKIDGRYYAIKKIKLDARDTEGNKKIFREVTTLSRLHHQNVVRYYTTWVETLDVSEKMEDIPEEDSEGIGGISSGVDASFPSFGASMSNISWSTNDNEFESDSSSSSSSDSASSDSDRGRNDDIETSSSHFISFGDEDESGNDVANSSGVDALDSLSPGTDTDAQAHSKSGRGANVFSAIRFGTMGAGADAPNKRERSRSVALFKPRRELPLRVFGTDLTDDTHATTEEAESEVSEKVPPPKKAPSGLDVREHVGYNRGKLAGSARRKESKQPAPKKQKILYIQMEYCENKTLNDVIKEGLSEKECWQMFGQILDGLNHIHQRGVIHRDLKPVNTFLDGLGDIKIGDFGLATSSFAPIDSSISRHVSLDRSAEDAMTADIGTSTYVAPEVTTKGSGATRYNQKVDMYSLGIIFFEMCYPLNTAMERANVLHNLRRPEIVFPNDFPVEKMQLQYQIIRRLLDHNPRSRLSSAELLESDLMPPKMEDEYIRDTIKTIANPSQPYFAKLLESLFALSTDKHIDATYDYRSNDIQAEQLNTVFLDRIRELMTRVFRTHAAVELSTPALTPKTDLLDMYQRPALYLDPKGNVVQLPYDQTVPFARYVARTKMTEIKRYCFDRYYVANA","length":826,"molWeight":91786,"crc64":"3478BFC380B27816","md5":"97907FBCC8AB5A6F71D552C83C0E9093"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Compositional bias":2,"Active site":1,"Binding site":1,"Non-terminal residue":1},"uniParcId":"UPI0022DA452C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GR42","uniProtkbId":"A0A9W8GR42_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":11,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2743006.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"value":"GTP:AMP phosphotransferase, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"value":"2.7.4.10"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"value":"Adenylate kinase 3"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"value":"AK 3"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2743006.1"}],"value":"ADK2"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2743006.1"}],"value":"GGI19_006745"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"value":"Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'-diphosphate + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13749"},{"database":"ChEBI","id":"CHEBI:57930"},{"database":"ChEBI","id":"CHEBI:61557"},{"database":"ChEBI","id":"CHEBI:456215"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.4.10","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004305"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"value":"Mitochondrion matrix","id":"SL-0170"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"value":"Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon GTP binding. Assembling and disassembling the active center during each catalytic cycle provides an effective means to prevent GTP hydrolysis"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"value":"Belongs to the adenylate kinase family. AK3 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2743006.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"Adenylate kinase active site lid","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF05191"}]},{"type":"Region","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"NMPbind","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}]},{"type":"Region","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"LID","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}]},{"type":"Binding site","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":89,"modifier":"EXACT"},"end":{"value":89,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03169"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2743006.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2743006.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010001732","properties":[{"key":"ProteinId","value":"KAJ2743006.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GR42","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"439792at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005759","properties":[{"key":"GoTerm","value":"C:mitochondrial matrix"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004017","properties":[{"key":"GoTerm","value":"F:AMP kinase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0046899","properties":[{"key":"GoTerm","value":"F:nucleoside triphosphate adenylate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006172","properties":[{"key":"GoTerm","value":"P:ADP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046033","properties":[{"key":"GoTerm","value":"P:AMP metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046039","properties":[{"key":"GoTerm","value":"P:GTP metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046041","properties":[{"key":"GoTerm","value":"P:ITP metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01428","properties":[{"key":"EntryName","value":"ADK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000106","properties":[{"key":"EntryName","value":"Adenylate kinase mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00235","properties":[{"key":"EntryName","value":"Adenylate_kinase_Adk"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03169","properties":[{"key":"EntryName","value":"Adenylate_kinase_AK3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006259","properties":[{"key":"EntryName","value":"Adenyl_kin_sub"}]},{"database":"InterPro","id":"IPR000850","properties":[{"key":"EntryName","value":"Adenylat/UMP-CMP_kin"}]},{"database":"InterPro","id":"IPR033690","properties":[{"key":"EntryName","value":"Adenylat_kinase_CS"}]},{"database":"InterPro","id":"IPR007862","properties":[{"key":"EntryName","value":"Adenylate_kinase_lid-dom"}]},{"database":"InterPro","id":"IPR028586","properties":[{"key":"EntryName","value":"AK3/Ak4_mitochondrial"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"TIGR01351","properties":[{"key":"EntryName","value":"adk"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001381","properties":[{"key":"EntryName","value":"PRK00279.1-3"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011100","properties":[{"key":"EntryName","value":"PRK14527.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23359","properties":[{"key":"EntryName","value":"NUCLEOTIDE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00406","properties":[{"key":"EntryName","value":"ADK"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05191","properties":[{"key":"EntryName","value":"ADK_lid"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00094","properties":[{"key":"EntryName","value":"ADENYLTKNASE"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00113","properties":[{"key":"EntryName","value":"ADENYLATE_KINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLILGAPGAGKGTQSTRIREHFGVTAISSGDVLRRNIAQGTDAGMLAQRAVSRGELVSDELVVELIRSELVTLPQSNWLLDGFPRNIAQAQALDAMLASTNQSLNAVVNLVVPEDVILHRIVERYVHVPSGRVYNLTYNPPKVSGIDDVTGEPLEHRPDDNPESFRRRLQQYHEVTEPLLDYYRRTGVLTSFAGTTSDVIYPMLHAYMDARFD","length":213,"molWeight":23641,"crc64":"7D8363AF3E5B92C7","md5":"0A7FA1D914C3D104504735E8A5E8BE57"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Binding site":11},"uniParcId":"UPI0022D1D735"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GRI1","uniProtkbId":"A0A9W8GRI1_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":12,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750371.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364139"}],"value":"DNA repair protein RAD51 homolog"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750371.1"}],"value":"RAD51"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750371.1"}],"value":"GGI19_005142"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00096208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364139"}],"value":"Homologous DNA recombinase that catalyzes strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single-stranded DNA (ssDNA) in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. RAD51 targeting to ssDNA promotes removal of replication protein-A (RPA) from ssDNA and stabilization of RAD51-ssDNA filaments by blocking ATP hydrolysis. Also required for homologous recombination during meiosis by acting as an non-catalytic accessory factor for DMC1 recombinase, enabling proper chromosome pairing and crossing over"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364139"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007095"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364139"}],"value":"Belongs to the RecA family. RAD51 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750371.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"RecA family profile 1","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50162"}]},{"type":"Domain","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"RecA family profile 2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50163"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":232,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:4705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005856-1"}],"ligand":{"name":"dsDNA","id":"ChEBI:CHEBI:4705"}},{"type":"Binding site","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":235,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:9160"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005856-1"}],"ligand":{"name":"ssDNA","id":"ChEBI:CHEBI:9160"}},{"type":"Binding site","location":{"start":{"value":238,"modifier":"EXACT"},"end":{"value":238,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:4705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005856-1"}],"ligand":{"name":"dsDNA","id":"ChEBI:CHEBI:4705"}},{"type":"Binding site","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:4705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005856-1"}],"ligand":{"name":"dsDNA","id":"ChEBI:CHEBI:4705"}},{"type":"Binding site","location":{"start":{"value":314,"modifier":"EXACT"},"end":{"value":314,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:9160"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005856-1"}],"ligand":{"name":"ssDNA","id":"ChEBI:CHEBI:9160"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005856-1"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364139"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364139"}],"id":"KW-0233","category":"Biological process","name":"DNA recombination"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364139"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005856-1"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364139"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005856-1"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364139"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750371.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750371.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000573","properties":[{"key":"ProteinId","value":"KAJ2750371.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GRI1","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"10251254at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0000794","properties":[{"key":"GoTerm","value":"C:condensed nuclear chromosome"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0140664","properties":[{"key":"GoTerm","value":"F:ATP-dependent DNA damage sensor activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0000150","properties":[{"key":"GoTerm","value":"F:DNA strand exchange activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003690","properties":[{"key":"GoTerm","value":"F:double-stranded DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0003697","properties":[{"key":"GoTerm","value":"F:single-stranded DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0070192","properties":[{"key":"GoTerm","value":"P:chromosome organization involved in meiotic cell cycle"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000730","properties":[{"key":"GoTerm","value":"P:DNA recombinase assembly"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042148","properties":[{"key":"GoTerm","value":"P:DNA strand invasion"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006312","properties":[{"key":"GoTerm","value":"P:mitotic recombination"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:1990426","properties":[{"key":"GoTerm","value":"P:mitotic recombination-dependent replication fork processing"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0007131","properties":[{"key":"GoTerm","value":"P:reciprocal meiotic recombination"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000723","properties":[{"key":"GoTerm","value":"P:telomere maintenance"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd19513","properties":[{"key":"EntryName","value":"Rad51"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.150.20:FF:000008","properties":[{"key":"EntryName","value":"DNA repair protein RAD51 homolog"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000092","properties":[{"key":"EntryName","value":"DNA repair protein Rad51 homolog"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.20","properties":[{"key":"EntryName","value":"5' to 3' exonuclease, C-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR011941","properties":[{"key":"EntryName","value":"DNA_recomb/repair_Rad51"}]},{"database":"InterPro","id":"IPR016467","properties":[{"key":"EntryName","value":"DNA_recomb/repair_RecA-like"}]},{"database":"InterPro","id":"IPR010995","properties":[{"key":"EntryName","value":"DNA_repair_Rad51/TF_NusA_a-hlx"}]},{"database":"InterPro","id":"IPR060101","properties":[{"key":"EntryName","value":"HHH_SAM-like"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR013632","properties":[{"key":"EntryName","value":"Rad51_C"}]},{"database":"InterPro","id":"IPR020588","properties":[{"key":"EntryName","value":"RecA_ATP-bd"}]},{"database":"InterPro","id":"IPR020587","properties":[{"key":"EntryName","value":"RecA_monomer-monomer_interface"}]},{"database":"NCBIfam","id":"NF003301","properties":[{"key":"EntryName","value":"radA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02239","properties":[{"key":"EntryName","value":"recomb_RAD51"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR22942:SF39","properties":[{"key":"EntryName","value":"DNA REPAIR PROTEIN RAD51 HOMOLOG 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR22942","properties":[{"key":"EntryName","value":"RECA/RAD51/RADA DNA STRAND-PAIRING FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14520","properties":[{"key":"EntryName","value":"HHH_5"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08423","properties":[{"key":"EntryName","value":"Rad51"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005856","properties":[{"key":"EntryName","value":"Rad51"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47794","properties":[{"key":"EntryName","value":"Rad51 N-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50162","properties":[{"key":"EntryName","value":"RECA_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50163","properties":[{"key":"EntryName","value":"RECA_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MQAEEFEEQSEAAEVQQGEEDCGPLPIQNLEQVGISAADVKKLTEAGFFTVESVAYTPRKQLLTIKGFAETKVDKILGEAAKLVPMGFTTASDYHQKRSELLHITTGSTELDKLLGGHGIETGSITELFGEFRTGKSQICHTLAVTCQLDEASGGAMGKCLYIDTEGTFRPERLVEIAERYNLDPTEVLENVAYARAFNSDHQTALLNQACLLMTEARFSLLVVDSATSLYRTDYSGRGELSARQMHLARFLRMLLRLADEFGIAVVITNQVVAQVDGGMAMFAADPKKPIGGNIIAHASTTRLSLRKGRGETRVCKIYDSPCLPESEAVFAITAQGIADAKD","length":343,"molWeight":37348,"crc64":"41285768890080D9","md5":"589DE33CCBCB7598528BBB92786D3CAD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":1,"Compositional bias":1,"Binding site":5},"uniParcId":"UPI0022D1E6D4"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GRU9","uniProtkbId":"A0A9W8GRU9_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":10,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2743424.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00018097"}],"value":"Multiple inositol polyphosphate phosphatase 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013040"}],"value":"3.1.3.62"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012976"}],"value":"3.1.3.80"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031642"}],"value":"2,3-bisphosphoglycerate 3-phosphatase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2743424.1"}],"value":"GGI19_006702"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R)-2,3-bisphosphoglycerate + H2O = (2R)-2-phosphoglycerate + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27381"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58248"},{"database":"ChEBI","id":"CHEBI:58289"}],"ecNumber":"3.1.3.80","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043832"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:27382"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043832"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,2,5,6-tetrakisphosphate + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:77115"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57798"},{"database":"ChEBI","id":"CHEBI:195535"}],"ecNumber":"3.1.3.62","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043671"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:77116"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043671"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,2,6-trisphosphate + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:77119"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:195535"},{"database":"ChEBI","id":"CHEBI:195537"}],"ecNumber":"3.1.3.62","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043668"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:77120"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043668"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16989"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57798"},{"database":"ChEBI","id":"CHEBI:58130"}],"ecNumber":"3.1.3.62","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043691"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:16990"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043691"}]}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004236"}],"value":"Cell membrane","id":"SL-0039"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008422"}],"value":"Belongs to the histidine acid phosphatase family. MINPP1 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2743424.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Disulfide bond","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000894-2"}]},{"type":"Disulfide bond","location":{"start":{"value":418,"modifier":"EXACT"},"end":{"value":423,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000894-2"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000894-2"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023180"}],"id":"KW-0325","category":"PTM","name":"Glycoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"}],"id":"KW-0732","category":"Domain","name":"Signal"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2743424.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2743424.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010001669","properties":[{"key":"ProteinId","value":"KAJ2743424.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GRU9","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"6509975at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003993","properties":[{"key":"GoTerm","value":"F:acid phosphatase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0034417","properties":[{"key":"GoTerm","value":"F:bisphosphoglycerate 3-phosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0052745","properties":[{"key":"GoTerm","value":"F:inositol phosphate phosphatase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd07061","properties":[{"key":"EntryName","value":"HP_HAP_like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1240","properties":[{"key":"EntryName","value":"Phosphoglycerate mutase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR033379","properties":[{"key":"EntryName","value":"Acid_Pase_AS"}]},{"database":"InterPro","id":"IPR000560","properties":[{"key":"EntryName","value":"His_Pase_clade-2"}]},{"database":"InterPro","id":"IPR029033","properties":[{"key":"EntryName","value":"His_PPase_superfam"}]},{"database":"InterPro","id":"IPR016274","properties":[{"key":"EntryName","value":"Histidine_acid_Pase_euk"}]},{"database":"PANTHER","id":"PTHR20963:SF8","properties":[{"key":"EntryName","value":"MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20963","properties":[{"key":"EntryName","value":"MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00328","properties":[{"key":"EntryName","value":"His_Phos_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000894","properties":[{"key":"EntryName","value":"Acid_phosphatase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53254","properties":[{"key":"EntryName","value":"Phosphoglycerate mutase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00616","properties":[{"key":"EntryName","value":"HIS_ACID_PHOSPHAT_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MFGNSLSGAERARKRRIYAALAVATIFVMFMWYYSSHKPTVSPGGSRLTNLSLSTKMPYLTPNTTTIRPASSGLELVQVQYVYRHGARYPTQGDMAHIKEVYELDGLSVSRDWINAELIDGDKAGLLAKYGYREMTGIAQRTMQRYPTFLADRLRNPESVRFVSSEYQRSHMSARTFQGVVDPKNHTKPVTVLPLNKDTILAMKAGCSMWEQEKEVATYNAGREVAVFDSIHGQKLRERMSGKLGVKSGMTVAHISTLYTMCGYEISLFAQPDTWCTLFDPDTSALMELRNDIKYSRVYGPFGANINKRMACALFTALFRDIDSALRDPPNAISTFRFGHAETIMFVSTLLSLEQVLGTENSPITGAMPFSLARHRGFKTSVIAPFSTNLGIELYKDQHAQPFFRLLLNERAIRLPECTDEFCSLDVLRNKLGDNIGCDFNSICRITPQ","length":449,"molWeight":50457,"crc64":"B0C7D910224E2C38","md5":"E7936016B83BF734BCE9B7E47FD960B7"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":4,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":1,"Disulfide bond":2},"uniParcId":"UPI0022D1DFFE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GS04","uniProtkbId":"A0A9W8GS04_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":13,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750885.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013824"}],"value":"Eukaryotic translation initiation factor 5B"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011986"}],"value":"3.6.5.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032478"}],"value":"Translation initiation factor IF-2"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750885.1"}],"value":"FUN12_2"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750885.1"}],"value":"GGI19_004840"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + H2O = GDP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19669"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58189"}],"ecNumber":"3.6.5.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048107"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007733"}],"value":"Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750885.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":690,"modifier":"EXACT"},"end":{"value":786,"modifier":"EXACT"}},"description":"DOD-type homing endonuclease","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50819"}]},{"type":"Domain","location":{"start":{"value":855,"modifier":"EXACT"},"end":{"value":1073,"modifier":"EXACT"}},"description":"Tr-type G","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51722"}]},{"type":"Region","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":470,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":323,"modifier":"EXACT"},"end":{"value":367,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":374,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":405,"modifier":"EXACT"},"end":{"value":442,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022540"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750885.1"}],"id":"KW-0396","category":"Molecular function","name":"Initiation factor"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022917"}],"id":"KW-0648","category":"Biological process","name":"Protein biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750885.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2750885.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000481","properties":[{"key":"ProteinId","value":"KAJ2750885.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"OrthoDB","id":"4928at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005739","properties":[{"key":"GoTerm","value":"C:mitochondrion"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004519","properties":[{"key":"GoTerm","value":"F:endonuclease activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003924","properties":[{"key":"GoTerm","value":"F:GTPase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003743","properties":[{"key":"GoTerm","value":"F:translation initiation factor activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030908","properties":[{"key":"GoTerm","value":"P:protein splicing"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd03703","properties":[{"key":"EntryName","value":"aeIF5B_II"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01887","properties":[{"key":"EntryName","value":"IF2_eIF5B"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.30.10:FF:000013","properties":[{"key":"EntryName","value":"eukaryotic translation initiation factor 5B"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.30.10:FF:000026","properties":[{"key":"EntryName","value":"Eukaryotic translation initiation factor 5B"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10050:FF:000002","properties":[{"key":"EntryName","value":"Eukaryotic translation initiation factor 5B"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000112","properties":[{"key":"EntryName","value":"Eukaryotic translation initiation factor 5B"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.170.16.10","properties":[{"key":"EntryName","value":"Hedgehog/Intein (Hint) domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.10.28.10","properties":[{"key":"EntryName","value":"Homing endonucleases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.30.10","properties":[{"key":"EntryName","value":"Translation factors"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.10050","properties":[{"key":"EntryName","value":"Translation initiation factor IF- 2, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036844","properties":[{"key":"EntryName","value":"Hint_dom_sf"}]},{"database":"InterPro","id":"IPR007868","properties":[{"key":"EntryName","value":"Hom_end_hint"}]},{"database":"InterPro","id":"IPR027434","properties":[{"key":"EntryName","value":"Homing_endonucl"}]},{"database":"InterPro","id":"IPR004042","properties":[{"key":"EntryName","value":"Intein_endonuc_central"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR000795","properties":[{"key":"EntryName","value":"T_Tr_GTP-bd_dom"}]},{"database":"InterPro","id":"IPR015760","properties":[{"key":"EntryName","value":"TIF_IF2"}]},{"database":"InterPro","id":"IPR023115","properties":[{"key":"EntryName","value":"TIF_IF2_dom3"}]},{"database":"InterPro","id":"IPR036925","properties":[{"key":"EntryName","value":"TIF_IF2_dom3_sf"}]},{"database":"InterPro","id":"IPR009000","properties":[{"key":"EntryName","value":"Transl_B-barrel_sf"}]},{"database":"NCBIfam","id":"NF003078","properties":[{"key":"EntryName","value":"infB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43381:SF4","properties":[{"key":"EntryName","value":"EUKARYOTIC TRANSLATION INITIATION FACTOR 5B"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43381","properties":[{"key":"EntryName","value":"TRANSLATION INITIATION FACTOR IF-2-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00009","properties":[{"key":"EntryName","value":"GTP_EFTU"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05203","properties":[{"key":"EntryName","value":"Hom_end_hint"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF11987","properties":[{"key":"EntryName","value":"IF-2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51294","properties":[{"key":"EntryName","value":"Hedgehog/intein (Hint) domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55608","properties":[{"key":"EntryName","value":"Homing endonucleases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52156","properties":[{"key":"EntryName","value":"Initiation factor IF2/eIF5b, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50447","properties":[{"key":"EntryName","value":"Translation proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51722","properties":[{"key":"EntryName","value":"G_TR_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50819","properties":[{"key":"EntryName","value":"INTEIN_ENDONUCLEASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGKKKGNKKGGVDDDIWADDLMDDTSAAGAAVIAAAAAGTEAQANAVEEEEGGGGFMSMISRAKKNKNKAKAKVPVPTADDDQASDAEGMPSVAGDAAAAGGDLGDEAGSTIKTAKQKEREKKERAKLQKKQKADEAKAKREAEIRELEASLGTTTIDAAKDGADEDEGEGAAGKKKKTKKKAKKVDDQVDTAPAAEAVAPAAAAAAPAKDDKKKKAKKGAPIAALQKMIEEQRRREEELKRLEEEELKRIEEEERLAAEEEALQNAKREAKREADRLRKEQLKRDGKLLTKKQKEANARREQQLKAMLASGVQVAGLSGESKVTRQDMFQRDAEERQKRAAEKKRREEEAEKKRLEEVEAKLKAAEAAKAASDDEEVDDWEALADATDDEGEAKVDDKAISAAADEEEEEEGSSSEQSEDEDSEESGSDDESDESSSDDELTATQKQEMARKAAATARREQRIQEAMAARSADNLRSPICCILGHVDTGKCWGRNTPILMWDGSSRNVQDVVELDQVMGDDNSPRVVQPGSVIKGEGMLYRVVPDQHDGADSFVCNGEHVLVLTINHKPYVQCDVRMVDGVTETKFIAKSFTIDSAANKPSQLVHGEFESEALALAALPEWQPLTWQCTVLEYLDLVRIDSASADLCSMYKPVNGVEFSASAGQSFTDAISRAFGSVPTSIHELETARFFGVWLGNGANGIPSADAEDTRKALLKEFALTDEKRIPDAIMSASLNHRREFLAGVIESDNASFVAASSAVEEHWEVSSSDEQFLLQLRRLARSIGLHVGPVSQSAAASTISISGEAMCSFGSLIGFEHKRPAERTPESWAVLCSNSWTFAIEEIGHGEYFGFTLDGNSRVLLGDYTVSHNTKLLDKIRQTNVQGGEAGGITQQIGATYFPADAIEKKTAAMYPSSKIDIKVPGLLIIDTPGHESFTNLRSRGSSLCNIAILVVDIMHGLEPQTLESLRLLRDRKTPFIVALNKIDRIYGWNQCPDSPFRDTFKKQPAHAINEFETRAAKVKVEFAEQGLNAELHYKNKNFAKYVSLVPTSAFSGEGIPDLLDLLVTLTQQRMSNQLMYLSELECTVLEVKVIEGLGTTIDVILSNGVLHEGDRIVICGVDGPIVTNVRALLTPQPMRELRVKSAYVHHKSIKAAMGVKISAPDLEKAIAGSRLMVVGPDDDEEELMDEIMSDLARLDDAIDKSGRGVWVQASTLGSLEALLEFLRVSKIPVSGINIGPVHKKDVTRASAMLERAKEYAVMLCFDVKVDKDAEEMAKELDIKVFKADIIYHLFDAFTAHNAQIVEQRRKEQAELAVFPCIMKIISKEHVFNKRSPLLLGVDILDGHLRQGTPICVIKMNHETKVREVVMLGKVTTIKVNDKPVNIVRKANAGAGFTIRIENTVADHDKTYGRHFDENDVLYSRITRRSIDVLKETFRADLTKDEWRLVAKLKSTLGVE","length":1457,"molWeight":159690,"crc64":"352C5193199418F3","md5":"25BB5558FD06C84152959737AEBE9F3D"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Compositional bias":8},"uniParcId":"UPI0022DB5776"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8GS29","uniProtkbId":"A0A9W8GS29_9FUNG","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":11,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Coemansia pectinata","taxonId":1052879,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2751782.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Kickxellomycota","Kickxellomycotina","Kickxellomycetes","Kickxellales","Kickxellaceae","Coemansia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"value":"Alanine--tRNA ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"value":"6.1.1.7"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"value":"Alanyl-tRNA synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"value":"AlaRS"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"value":"ALA1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2751782.1"}],"value":"GGI19_004266"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"value":"Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"tRNA(Ala) + L-alanine + ATP = L-alanyl-tRNA(Ala) + AMP + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12540"},{"database":"Rhea","id":"RHEA-COMP:9657"},{"database":"Rhea","id":"RHEA-COMP:9923"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57972"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78497"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.1.1.7","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"value":"Mitochondrion","id":"SL-0173"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"value":"Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008429"}],"value":"Belongs to the class-II aminoacyl-tRNA synthetase family. Alax-L subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2751782.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":720,"modifier":"EXACT"}},"description":"Alanyl-transfer RNA synthetases family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50860"}]},{"type":"Binding site","location":{"start":{"value":575,"modifier":"EXACT"},"end":{"value":575,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":579,"modifier":"EXACT"},"end":{"value":579,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":677,"modifier":"EXACT"},"end":{"value":677,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":681,"modifier":"EXACT"},"end":{"value":681,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023146"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"id":"KW-0030","category":"Molecular function","name":"Aminoacyl-tRNA synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022917"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"id":"KW-0648","category":"Biological process","name":"Protein biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001140011"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022555"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"id":"KW-0820","category":"Molecular function","name":"tRNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03133"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-7SOR6JG0LLUTG","citationType":"submission","authors":["Reynolds N.K.","Stajich J.E.","Barry K.","Grigoriev I.V.","Crous P.","Smith M.E."],"title":"Phylogenomic reconstructions and comparative analyses of Kickxellomycotina fungi.","publicationDate":"JUL-2022","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2751782.1"}],"value":"BCRC 34297","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ2751782.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JANBUH010000359","properties":[{"key":"ProteinId","value":"KAJ2751782.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8GS29","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"2423964at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001140011","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005739","properties":[{"key":"GoTerm","value":"C:mitochondrion"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004813","properties":[{"key":"GoTerm","value":"F:alanine-tRNA ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0002161","properties":[{"key":"GoTerm","value":"F:aminoacyl-tRNA deacylase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003676","properties":[{"key":"GoTerm","value":"F:nucleic acid binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070143","properties":[{"key":"GoTerm","value":"P:mitochondrial alanyl-tRNA aminoacylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00673","properties":[{"key":"EntryName","value":"AlaRS_core"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.930.10:FF:000004","properties":[{"key":"EntryName","value":"Alanine--tRNA ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.980.10:FF:000004","properties":[{"key":"EntryName","value":"Alanine--tRNA ligase, cytoplasmic"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.30.130","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.54.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.930.10","properties":[{"key":"EntryName","value":"Bira Bifunctional Protein, Domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.980.10","properties":[{"key":"EntryName","value":"Threonyl-trna Synthetase, Chain A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00036_B","properties":[{"key":"EntryName","value":"Ala_tRNA_synth_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR045864","properties":[{"key":"EntryName","value":"aa-tRNA-synth_II/BPL/LPL"}]},{"database":"InterPro","id":"IPR002318","properties":[{"key":"EntryName","value":"Ala-tRNA-lgiase_IIc"}]},{"database":"InterPro","id":"IPR018162","properties":[{"key":"EntryName","value":"Ala-tRNA-ligase_IIc_anticod-bd"}]},{"database":"InterPro","id":"IPR018165","properties":[{"key":"EntryName","value":"Ala-tRNA-synth_IIc_core"}]},{"database":"InterPro","id":"IPR018164","properties":[{"key":"EntryName","value":"Ala-tRNA-synth_IIc_N"}]},{"database":"InterPro","id":"IPR023033","properties":[{"key":"EntryName","value":"Ala_tRNA_ligase_euk/bac"}]},{"database":"InterPro","id":"IPR018163","properties":[{"key":"EntryName","value":"Thr/Ala-tRNA-synth_IIc_edit"}]},{"database":"InterPro","id":"IPR009000","properties":[{"key":"EntryName","value":"Transl_B-barrel_sf"}]},{"database":"InterPro","id":"IPR012947","properties":[{"key":"EntryName","value":"tRNA_SAD"}]},{"database":"NCBIfam","id":"TIGR00344","properties":[{"key":"EntryName","value":"alaS"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11777:SF9","properties":[{"key":"EntryName","value":"ALANINE--TRNA LIGASE, CYTOPLASMIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11777","properties":[{"key":"EntryName","value":"ALANYL-TRNA SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01411","properties":[{"key":"EntryName","value":"tRNA-synt_2c"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07973","properties":[{"key":"EntryName","value":"tRNA_SAD"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00980","properties":[{"key":"EntryName","value":"TRNASYNTHALA"}]},{"database":"SMART","id":"SM00863","properties":[{"key":"EntryName","value":"tRNA_SAD"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55681","properties":[{"key":"EntryName","value":"Class II aaRS and biotin synthetases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF101353","properties":[{"key":"EntryName","value":"Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55186","properties":[{"key":"EntryName","value":"ThrRS/AlaRS common domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50447","properties":[{"key":"EntryName","value":"Translation proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50860","properties":[{"key":"EntryName","value":"AA_TRNA_LIGASE_II_ALA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSASDIRQRYTDYFVKNGHTLMPSADIVPRNDATLLFSSAGMVPFKQFFLNPATAPHKMVTTVQKCVRAGGKHNDLDQVGFTPRHHTFFEMLGNFSFGAYSKREIIHMAWKFVRQELKMPEDRLRVTVLETDDEAYDIWKNEVGVDPRRIVRCGAEDNFWSMGSEGPCGPSSEIFWDTRDPRYMESDDERWLEFWNLVFMQFHRGADGKLRPLDTPCVDTGMGLERVASILQGKVNNFDTDEFQVIIRDIDARCSPGQSSGNVDLAKALACKRIIADHLRASAFLISEGVFPSNIGRGYVLRRIIRRAVRAGRLLGINDSVLSALYPSLELAMGAAYPELMERRQLIVSVLESEEKMFLRTLDKGLVLLEGIFASGNSQRLVSGADAFSLYDTHGFPLDLTEIIARDSGWTVDVEAFAKIQRQSRERNKASWKGKLTKQDSVAREIEATCLEWEEAGVSSQFSGYDVDPEAKPTAAACRVIAFKSLSNGDGLLVIDPCPFYATGGGQEADTGVITIGDSEGSHEFAVSDAVAMPSGQATVLRLTATSDKQHLFRGGQMIYATVDEARRLGSAVHHTATHLLNAALRKTVGVSVMQAGSLVQAEGLRFDFTSGALSSEQLREIEGLVNKAALDNIDITTARMPLDQAKAQGAVALFSEKYDAASVRVVNVAGLSMELCGGTHLRSTRAVFPFHITSEGSIGAGTRRIEAKAGAAASVWLQQQLEYGRATAQTLGAAQLGVMDKKAQQLVDRNRALREEADRWLRAAAVNAEAVATHSTALGERGVPAAFHILAPLPFNARLVAERACHLRDTEPSLVHVVIQGRAIALSVNAEQLPGEHAAALLSSVLGKLPGKGGGQASLAQGQLETAVAELAQVAHL","length":878,"molWeight":95626,"crc64":"7A568CBD64B80E03","md5":"E4347BE168A4C1B6BFF6604B877EB305"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":4},"uniParcId":"UPI0022D02DB6"}}]}