{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6T6H6","uniProtkbId":"A0AAD6T6H6_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":10,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7040729.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Pentafunctional AROM polypeptide"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"3-dehydroquinate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"DHQS"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"4.2.3.4"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"3-phosphoshikimate 1-carboxyvinyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"2.5.1.19"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Shikimate kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"SK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"2.7.1.71"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"3-dehydroquinate dehydratase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"3-dehydroquinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"4.2.1.10"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Shikimate dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"1.1.1.25"}]}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7040729.1"}],"value":"C8F04DRAFT_1177714"}]}],"comments":[{"texts":[{"evidences":[{"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":"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":"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":"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":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Binds 2 Zn(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"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":"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":"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":"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":"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":"PIRNR","id":"PIRNR000514"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"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":"PIRNR","id":"PIRNR000514"}],"value":"In the 2nd section; belongs to the EPSP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"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":"PIRNR","id":"PIRNR000514"}],"value":"In the 4th section; belongs to the type-I 3-dehydroquinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"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:0000313","source":"EMBL","id":"KAJ7040729.1"}],"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":81,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01761"}]},{"type":"Domain","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF24621"}]},{"type":"Domain","location":{"start":{"value":418,"modifier":"EXACT"},"end":{"value":829,"modifier":"EXACT"}},"description":"Enolpyruvate transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00275"}]},{"type":"Domain","location":{"start":{"value":1253,"modifier":"EXACT"},"end":{"value":1323,"modifier":"EXACT"}},"description":"Shikimate dehydrogenase substrate binding N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08501"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023141"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"id":"KW-0057","category":"Biological process","name":"Aromatic amino acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"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":"ARBA00022857"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7040729.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7040729.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000020","properties":[{"key":"ProteinId","value":"KAJ7040729.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001218188","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-EC"}]},{"database":"GO","id":"GO:0003856","properties":[{"key":"GoTerm","value":"F:3-dehydroquinate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0003866","properties":[{"key":"GoTerm","value":"F:3-phosphoshikimate 1-carboxyvinyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004764","properties":[{"key":"GoTerm","value":"F:shikimate 3-dehydrogenase (NADP+) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004765","properties":[{"key":"GoTerm","value":"F:shikimate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0009073","properties":[{"key":"GoTerm","value":"P:aromatic amino acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009423","properties":[{"key":"GoTerm","value":"P:chorismate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"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":"cd00464","properties":[{"key":"EntryName","value":"SK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.1090.10:FF:000007","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"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":"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":"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":"IPR031322","properties":[{"key":"EntryName","value":"Shikimate/glucono_kinase"}]},{"database":"InterPro","id":"IPR013708","properties":[{"key":"EntryName","value":"Shikimate_DH-bd_N"}]},{"database":"InterPro","id":"IPR000623","properties":[{"key":"EntryName","value":"Shikimate_kinase/TSH1"}]},{"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":"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":"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":"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"}]}],"sequence":{"value":"MADADILKVSILGRESIHCGFHLVPYIASTVISTLHSSTYVLITDSNVAKHHLAAFEAEFQSALSIAQPNGITPKSRFLSLVIPPGETSKSRDGKANIEDFLLLNRCTRDTVIMALGGGVVGDLVGFVSATFMRGVRVVQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGSFWQPQYIFIDAAFLETLPSREFSNGMAEVVKTAAIWNETEFAALESRAAEIFTAIQSPSLNFSGRTKKTRSVAQDLLLSVIVGSISVKAHIVTVDELETGLRNIVNFGHTIGHAIEAVLTPTILHGECVSVGMILEAEISRQMGILSQVGVGRLTRCLKAYNLPISLTDPRIANLPAAKQLTVGRLLDIMRIDKKNSGDEKKVVILSRIGATYEPKATVIRDAVIAKTLSDAAKVVAGIPTHHPVKMATPGSKSISNRALVLAALAKGTCHDGRTHRAQGREFLLGRRRRDIGCSRRGWIARSASEGKEIYLGNAGTAARFLTTVCTLVQTSAPADHTTVITGNARMKQRPIGPLVDALRANGSKIDFLESAGCLPLSIAPQGLKGGTIQLAASVSSQYVSSVLLCAPYAAQPVTLELTGGQVISQPYIDMTIAMMRTFGVDVVRRVDKATGKALDIYDIPVGVYTNPADYSIESDASSATYPLAIAAITGTTCTIDNIGSSSLQGDARFAKEVLEGMGCTGGADRDGDNAIEEIDMEVMTDAFLTATVLAAVARGKTRILGIANQRVKECNRIRAMMDQLVPQRRSQRNSESRTIELDDGLEIIGKPFRELATGVSVHCYDDHRVAMAFSVLGTVIPETILEEKRCVEKTWPNWWDDLGEQGLSYQYIGLKVQGVELECVGVVGSPSGTITQDVSASIILIGMRGSGKTFTGHLASTALSWTCLDADAYFQVKHQIGVRQFVAENGWPAFRAAETAILEELLTTNDKNHVISLGEPKGPVVHIMRPIDEVVAYLGVESARPAYGEPITDVFNRRAPWFKDCATHEFVNHVGVDTSLANKSGTRHEVIRFFKHITGQQPNLAPNLATGKRSYFLALTFPDLTPALHHIDDLTQGVDAMELRLYPLGALCQGANRGLASLDLPAPHLYHQNLYRKEARSRTPPRTRAFDLLKLALALGIEYIDVEITLPEPMIRELISRKGHSKIIASWHDWSGAMKWDGAVVQEKTTLLSTISSKANSQPNAKPILAINMGLEGQISRILNPTFSPVSHPLLPVKAAPGQLSFAEIQKALHLIGQLPSQRFVLFGNPISYSMSPTLHNTAFDETTDVGQEIKATITAPDFGGASVTIPFKLDVIPLLDKLSPAAEAIGAVNTIIPVRTDGTNRILYGENTDWLGIRHLHSLSRTFRIHPRCPARAAIYALQSLGAAKVYIYNRTRKNAQALAEAFPHAHVEILESLNEWPSGIVPPNVIVSTVPAAAAATSDVPDALQLSSNLFLYRDGPAVVIDMAYKPAETALLALAKQAGGNWELVRGTGRPSGARDVLWRSVFGRDTRKR","length":1504,"molWeight":162580,"crc64":"14C3F33651CE606D","md5":"F4CB5FB50A2AE3C768BB1C22B266983C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":5,"COFACTOR":1,"PATHWAY":5,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":6,"CAUTION":1},"countByFeatureType":{"Domain":4},"uniParcId":"UPI002971FC83"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6RYB3","uniProtkbId":"A0AAD6RYB3_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":8,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7017088.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Phosphatidylserine decarboxylase proenzyme 2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"4.1.1.65"}]},"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Phosphatidylserine decarboxylase 2 beta chain"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Phosphatidylserine decarboxylase 2 alpha chain"}}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"PSD2"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7017088.1"}],"value":"C8F04DRAFT_980034"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"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_03209"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyruvate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:15361"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"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_03209"}],"value":"Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Golgi apparatus membrane","id":"SL-0134"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Endosome membrane","id":"SL-0100"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"The C2 domains have an essential, but non-catalytic function. They may facilitate interactions with other proteins and are required for lipid transport function"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"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_03209"}],"value":"Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type II sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7017088.1"}],"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":1079,"modifier":"EXACT"}},"description":"Phosphatidylserine decarboxylase 2 beta chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"featureId":"PRO_5041752037"},{"type":"Chain","location":{"start":{"value":1080,"modifier":"EXACT"},"end":{"value":1124,"modifier":"EXACT"}},"description":"Phosphatidylserine decarboxylase 2 alpha chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"featureId":"PRO_5041752038"},{"type":"Domain","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"C2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50004"}]},{"type":"Domain","location":{"start":{"value":386,"modifier":"EXACT"},"end":{"value":508,"modifier":"EXACT"}},"description":"C2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50004"}]},{"type":"Region","location":{"start":{"value":227,"modifier":"EXACT"},"end":{"value":300,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":321,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":632,"modifier":"EXACT"},"end":{"value":665,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":701,"modifier":"EXACT"},"end":{"value":738,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":258,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":364,"modifier":"EXACT"},"end":{"value":374,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":632,"modifier":"EXACT"},"end":{"value":641,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":935,"modifier":"EXACT"},"end":{"value":935,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Active site","location":{"start":{"value":993,"modifier":"EXACT"},"end":{"value":993,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Active site","location":{"start":{"value":1080,"modifier":"EXACT"},"end":{"value":1080,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Active site","location":{"start":{"value":1080,"modifier":"EXACT"},"end":{"value":1080,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Site","location":{"start":{"value":1079,"modifier":"EXACT"},"end":{"value":1080,"modifier":"EXACT"}},"description":"Cleavage (non-hydrolytic); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Modified residue","location":{"start":{"value":1080,"modifier":"EXACT"},"end":{"value":1080,"modifier":"EXACT"}},"description":"Pyruvic acid (Ser); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10142"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0967","category":"Cellular component","name":"Endosome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0333","category":"Cellular component","name":"Golgi apparatus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"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_03209"}],"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_03209"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10142"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"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_03209"}],"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_03209"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0865","category":"PTM","name":"Zymogen"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7017088.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7017088.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000435","properties":[{"key":"ProteinId","value":"KAJ7017088.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6RYB3","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0010008","properties":[{"key":"GoTerm","value":"C:endosome membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000139","properties":[{"key":"GoTerm","value":"C:Golgi membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005795","properties":[{"key":"GoTerm","value":"C:Golgi stack"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005509","properties":[{"key":"GoTerm","value":"F:calcium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"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":"CDD","id":"cd04039","properties":[{"key":"EntryName","value":"C2_PSD"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.150","properties":[{"key":"EntryName","value":"C2 domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.238.10","properties":[{"key":"EntryName","value":"EF-hand"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00663","properties":[{"key":"EntryName","value":"PS_decarb_PSD_B_type2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000008","properties":[{"key":"EntryName","value":"C2_dom"}]},{"database":"InterPro","id":"IPR035892","properties":[{"key":"EntryName","value":"C2_domain_sf"}]},{"database":"InterPro","id":"IPR011992","properties":[{"key":"EntryName","value":"EF-hand-dom_pair"}]},{"database":"InterPro","id":"IPR018247","properties":[{"key":"EntryName","value":"EF_Hand_1_Ca_BS"}]},{"database":"InterPro","id":"IPR003817","properties":[{"key":"EntryName","value":"PS_Dcarbxylase"}]},{"database":"InterPro","id":"IPR033177","properties":[{"key":"EntryName","value":"PSD-B"}]},{"database":"InterPro","id":"IPR033179","properties":[{"key":"EntryName","value":"PSD_type2_pro"}]},{"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:SF17","properties":[{"key":"EntryName","value":"PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00168","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02666","properties":[{"key":"EntryName","value":"PS_Dcarbxylase"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00239","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF49562","properties":[{"key":"EntryName","value":"C2 domain (Calcium/lipid-binding domain, CaLB)"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF47473","properties":[{"key":"EntryName","value":"EF-hand"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50004","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00018","properties":[{"key":"EntryName","value":"EF_HAND_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTATKHPKLRRALKLPFNGRGGTTAVARNTFVPRQGEQPIVFLRVQVLSGNKLLAKDRNGFSDPFVVASLLQTRHHTPVAKKTVNPVYAPKDATWDFPIYLSLAEKLGVVELVVWDKDVLRKDYLGEAGLAVEDWFADARPKAWDAPGNVPFTLPLVSTRPNTPSQGTIQLRVGFVLPRAPTAQNQAEMDLDALYSNLVKNTRKSLVSAPPTEGVGTIRSHIGPAFAEFEDDGGLSSASDECSDNEEGEGDSEEEDDGSEYHVIPGSPASEVGVGGTGSKTPTGPSPLTTPTPSSSGGIVSAVPLGSTLASSAATIVPSASAGAVGGEKEKKGKPSFIALPLPKKFLSRSRPTTPGEGKDAMKEQQQQQKESAGNGNGKKRFRRSWSGAGTTASTGNDIVGIVMLEIASAVDLPRLKNMTRTSFDMDPFVVISFGKKVFRTRVIRHSLNPVWDEKLLFHVRRYEIGYEVRLTVLDWDKLSSNDYIGEASFNVSELDAAAAERGTRIPLYAETEGGDHPMKEFKLKLETGAAGGREPVIWESKHSPVLSFRAKYQPYSLLRQRFWRQYLKQYDTDDTKTLSHIEITSMLDSLGSTLTADTIDSFFTRFGKDPQHDDLTVEEAIRCLETEVLRPESERRRVDEESSGAGTGLPSTSASPAPERGLGGELRLGEMDFAGPALDVDFITGERKGYVTEPSEMVLLTPGQATPGTHPHSRHPTSESSSDADLEEDSSGSSEESFERVINVKNCPLCHRPRLNSKAEVDIITHIAVCASQDWNIVDRIVVGNFVTASQAQRKWYTKIIGKISSGDYRLGANSANIIVQNRLTGQLEEEKMQVYVRLGIRLLYKGMKSRMEGGRARRLLKSLSIKQGVKYDSPESARDIPTFIEFHQLKVEDILEPLSSFKTFNQFFYRKLKPSARPTEHPEDPYRLVSAADCRLMAFESVTEATRLWIKGREFTVGRLLGDAYKHEAERYSGGALAIFRLAPQDYHRFHSPVDGTIGNMTYIAGEYYTVNPQAIRTALDVYGENARKIVPIDSPQFGRVMAVCVGAMMVGSIETTVKEGETVKRGQEFGYFAFGGSTIVLLFEKDVVEWDEDLLVNGKASLETLVQVGMGIGNGTRKPGR","length":1124,"molWeight":123425,"crc64":"9F79C8FB9589D49C","md5":"8E2F17956E747A6CF1A45F9B6B03861E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Chain":2,"Domain":2,"Region":4,"Compositional bias":3,"Active site":4,"Site":1,"Modified residue":1},"uniParcId":"UPI00297410DD"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6STK3","uniProtkbId":"A0AAD6STK3_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2024-05-29","entryVersion":10,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7033450.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"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":"KAJ7033450.1"}],"value":"C8F04DRAFT_1210909"}]}],"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":"KAJ7033450.1"}],"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":44,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02771"}]},{"type":"Domain","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase middle","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02770"}]},{"type":"Domain","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":413,"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":"UP001218188"}],"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-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7033450.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7033450.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000065","properties":[{"key":"ProteinId","value":"KAJ7033450.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6STK3","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","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":"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":"MLRTGIIRSLSAARTRPVLPARLFTTSRCIRSDAAPLNSLDVYTEEETMLREAVQRFATDIVGPKVREMDENEQMDPAIIKGLFDQGLMGIETSGDHGGAESSFTSAIIVIEELAKVDPSVSVLCDVHNTLVNTIFRKYGSKEQQDKWLPQLAESKLGSFCLSEPASGSDAFALQTRAKKDGDSWIINGSKMWITNSYEAEIFLIFANIDPSKGYKGITCFVATKDMGIQIAKKEQKLGIRASSTCTLNFDDLKVPAENIIGGEGKGYKIAIEILNEGRIGIAAQMLGLAQGAFNKAVPYTYSRSQFGQPVGTFQGMAFQIAQAAIEIESARLLTYNAARRKEEGKSFAKEAAMAKYWSSVVAQKVSGQAIEWAGGVGFTRETGIEKFWRDSKIGAIYEGTSNIQLQTIAKFIQKEHS","length":418,"molWeight":45777,"crc64":"A905E3FF0FDB9846","md5":"09C91903F79F16B743CCB1809FC5F083"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":8,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI00297574E6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6SVW2","uniProtkbId":"A0AAD6SVW2_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":12,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7034664.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0008006","source":"Google","id":"ProtNLM"}],"value":"Aspartate carbamoyltransferase"}}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7034664.1"}],"value":"C8F04DRAFT_1100552"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"ecNumber":"3.5.1.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049534"}]}},{"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"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001947"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004812"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3"}],"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":"ARBA00043998"}],"value":"In the 2nd section; belongs to the CarB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043968"}],"value":"In the 3rd section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043979"}],"value":"In the C-terminal section; belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043984"}],"value":"In the N-terminal section; belongs to the CarA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7034664.1"}],"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":597,"modifier":"EXACT"},"end":{"value":789,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":1132,"modifier":"EXACT"},"end":{"value":1323,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":1388,"modifier":"EXACT"},"end":{"value":1569,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":337,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":421,"modifier":"EXACT"},"end":{"value":421,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":423,"modifier":"EXACT"},"end":{"value":423,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]}],"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":"PROSITE-ProRule","id":"PRU00605"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"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"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00409"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"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-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7034664.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7034664.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000055","properties":[{"key":"ProteinId","value":"KAJ7034664.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001218188","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:TreeGrafter"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase 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: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:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006228","properties":[{"key":"GoTerm","value":"P:UTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01744","properties":[{"key":"EntryName","value":"GATase1_CPSase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01423","properties":[{"key":"EntryName","value":"MGS_CPS_I_III"},{"key":"MatchStatus","value":"1"}]},{"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":"3.40.50.1380:FF:000005","properties":[{"key":"EntryName","value":"CAD protein-like isoform X1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000011","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":"3.50.30.20:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase 1, mitochondrial"},{"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":"3.30.470.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000002","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":"2"}]},{"database":"Gene3D","id":"3.40.50.880","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":"3.50.30.20","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase small subunit, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"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":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00001","properties":[{"key":"EntryName","value":"Asp_carb_tr"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01209","properties":[{"key":"EntryName","value":"CPSase_S_chain"},{"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":"IPR006274","properties":[{"key":"EntryName","value":"CarbamoylP_synth_ssu"}]},{"database":"InterPro","id":"IPR002474","properties":[{"key":"EntryName","value":"CarbamoylP_synth_ssu_N"}]},{"database":"InterPro","id":"IPR036480","properties":[{"key":"EntryName","value":"CarbP_synth_ssu_N_sf"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR035686","properties":[{"key":"EntryName","value":"CPSase_GATase1"}]},{"database":"InterPro","id":"IPR006275","properties":[{"key":"EntryName","value":"CPSase_lsu"}]},{"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":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"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":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01368","properties":[{"key":"EntryName","value":"CPSaseIIsmall"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002032","properties":[{"key":"EntryName","value":"PRK00856.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009475","properties":[{"key":"EntryName","value":"PRK12838.1"},{"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":"2"}]},{"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":"PF00988","properties":[{"key":"EntryName","value":"CPSase_sm_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"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":"PRINTS","id":"PR00099","properties":[{"key":"EntryName","value":"CPSGATASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01097","properties":[{"key":"EntryName","value":"CPSase_sm_chain"},{"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":"SSF52021","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, small subunit N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"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":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00097","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSNPAVPLPFRPLLSRLNSALNDPTAPVSASAETADLEDAVLELSDGSAFRGISFGAQGKSVAGECVFQTGMVGYTESLTDPSYEGQILVLTYPIVGNYGVPERPENPLDALPVAFESSKIHVSAIVIGYHSEDYSHFLAKSSLGAWLKENDVPAIYGVDTRALTKKIREKGSMLGKILARRSGAPAGRARSLIPSSQAPSRAPSRASSPPSTQSWREDYDDIPFLDPNQINLVAAVSIAAPRLYKSTITPRLHPTGRPLRVLAIDVGMKYNQIRCFIERGMELKVVPWDYDFLAEPEPYDGIFVSNGPGDPAMVTSTTSRLAVALQKADRPIFGICLGHQLLALAAGASTSKMKYGNRGHNIPCTDALSGRCYITSQNHGFEVDTATLPAGWKELFRNANDGSNEGIYCEDKPFFSVQFHPESTPGPRDTEFLFDVFIQNVADCAATNALVPIVMPGGKKEDNDKRVPRATVSKVVILGSGGLSIGQAGEFDYSGSQAIKALKEEGIYTIMVNPNIATIATSKGLADKVYFLPVTPEFVRKIIKYEKPDGIYVTFGGQTALNVGIKLKDEFEALGVKVLGTPIETIITTEDRQLFASAMEEIGEKCAESNTATNQEEAIAAAQAIGFPVIVRAAYALGGLGSGFAQNEAQLKALCSKAFATSPQVLVEKSMKGWKEIEYEVVRDCRDNCITVCNMENFDPLGIHTGDSIVIAPSQTLSDSDYNMLRTTAINVIRHLGVVGECNIQYALNPVSQEYCIIEVNARLSRSSALASKATGYPLAFIAAKLGLGIPLNEIKNSVTKVTSACFEPSLDYVVVKIPRWDLTKFNRVSRLLSSSMKSVGEVMSIGRTFEETFQKAIRAIDDHFLGFAKNDFVENIDEELVNPTDKRIFAISTAFHRGYSVDKIWQMTNIDKWFLTKLQYIFNMELRLSDCNVSTIAPTLLKQAKQLGFSDRQLAICMGSTELAVRRLRQETGIAPFVKQIDTVAAEFPAFTNYLYTTYNAIEHDVLFDDRGIMVLGSGVYRIGSSVEFDWCAVRAIRTLREQGLQTIMVNYNPETVSTDYDEADRLYFENISLETILDIYDTERSRGVILAMGGQTPNNIALPLYRQNVKIYGTSPEMIDTAENRYKFSRLLDEIGVDQPLWKELTSFEEAEKFCEKVGYPVLVRPSYVLSGAAMNVVSTGDDLSNYLTQATAVSRDHPVVITKYIEQAKEIEMDAVAKDGKMVMHFISEHVENAGVHSGDATLIHPPQDLDPQTVRQIEEATAKIGNALNVTGPFNIQFIAKNNEIKVIECNLRAARSFPFVSKVTGIDAIEMATKVMLGFPVEPYPDPGLPPDYVGIKVPQFSFSRLSGADPVLGVEMASTGEVACFGHDKYEAYLKALISTGIVPPKKNILFSIGSYREKLEILPSVQKLSAAGYNIFATSGTADFLTEHNVPCKYLETLGEDNRDKQKSEYSLTQHLANNLIDMYINLPSKNHYRRPASYSSKGYHTRRMAVDFAVPLITNIKNAKLLAEALVRKMPLEVSSIDSKSSHRTHTFPGLINIAAFVPSLVAENSPDLVEVTKASISAGFTTSVIIPLDLKGSISDRASLERAKANVAGAAHCNFALSIAASADNVQSLDEELQAEAKALFIPFDASTTSTPLSVVAAHFTSWPAEKPVVTDAKGSDLACILLLASLHNRSVHITDVRSKDDLLLISLSKAKHLKVTCDVSVYALFFSREEFPKCTFLPSADDQKSLWQKLELIDAFSVGATPYRLALEVGETASASSGMEETLPLLLTAVQDGRLSLDDIRVRLHDNPVHIFGLPDQAQTHVEVVIGRKARFGKRETCWSPLEPKFVTGAIHRVVVHGHTAFLDGSLFSAPLGKDISSATINHPPVLGPVALKEPEASMSSSNIMALTSMGSSQSSGGPFHATPGVHLSSHTLAHPAFHRRHILSVKQFTHRDMYDLFSLAHEMRLQVERNGTLDILKGRVLCTLFYEPSTRTSSSFDAAMKRCGGEVVQIAADNSSVVKGESLPDTIRTLGCYGDAIVIRHPDVGSAQLAAKFSPVPIINAGDGIGEHPTQALLDVYTIRSELGTVNGRTITLLGDLKNGRTVHSLVTLLSLYSVRLNFVSPRSLAMPASVIAVARKAGIPVTQCESLNEVLADTDVLYVTRIQKERFESETEWTQVKDAYRVDHAVLSRAKEEMIVMHPLPRVNEIDPEVDFDSRRAVYFRQMRYGLFIRMALLASVMG","length":2236,"molWeight":244714,"crc64":"4C01721EC8575197","md5":"66989A5B87733319DD42664F49419392"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":4,"COFACTOR":1,"PATHWAY":2,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Domain":3,"Region":1,"Compositional bias":1,"Active site":3},"uniParcId":"UPI00297632DD"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6T3I9","uniProtkbId":"A0AAD6T3I9_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2024-05-29","entryVersion":7,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7038171.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"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":"KAJ7038171.1"}],"value":"C8F04DRAFT_951456"}]}],"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":"KAJ7038171.1"}],"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":71,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":236,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":312,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":349,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":376,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":480,"modifier":"EXACT"},"end":{"value":501,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":565,"modifier":"EXACT"},"end":{"value":587,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":506,"modifier":"EXACT"}},"description":"Major facilitator superfamily (MFS) profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50850"}]},{"type":"Region","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":53,"modifier":"EXACT"}},"description":"Polar residues","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":"UP001218188"}],"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-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7038171.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7038171.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000033","properties":[{"key":"ProteinId","value":"KAJ7038171.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6T3I9","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","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":"1"}]},{"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":"1"}]},{"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":"MLRTPSPSEHRRSSCDELLVSADSDGDDLEFLSDADSISTLRVANSDHPSTESTPPPAPRRRRLNENQRAFLIRSLALFCACWLSVGSHYASYVLGPLKSRISRDLGTGHAEYSLLISALSLNSTWTPLVGGILAGTLGTTFTSILATGVVFIGTAFLLAGDVWGDVRIMAAGMFIFGLGVSPLAVVQETIIVRFFKSHGLGVSMAFGLVVGKGSSFVSARTSYPLTERFGPRAPFYVACLLAGMSVVINLAYIAASRWLIDGAGAELEAVDINEEAQRRSVINMSEAQALEKVAAKRRVHLREITKLGDVFWAYIAVNIFCGTIWAPFTHLAANIIELRYQMTERDAANTASYVLVGSIFLYPMCGYIVDRFKRKPIVIILLVLSSVFTLGAYTWLALPSSWTRTAKPAVAAFGFGHGFSPLLLVLLVPKIVPLKFISTALGAHKSLEQTGATIFQTLAGLAMDKAKKDHPDGSSTQGIINAFLFLNFLQLLSILGVAYLQHRREKILSRKVRRGSSVSARPVLPDDPSQPLLGVSSLQNRRYSTGSRVVNEEISKKEVRRGDVFATISGTLIISAWILFLGTAWFKLGMKKNSGN","length":597,"molWeight":64923,"crc64":"C2960754B32BEB33","md5":"400FDE25F3C32F6CD3C5B89314D8F383"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":13,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":11,"Domain":1,"Region":1,"Compositional bias":1},"uniParcId":"UPI00297322B7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6T6Q7","uniProtkbId":"A0AAD6T6Q7_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":11,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7039911.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"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"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7039911.1"}],"value":"C8F04DRAFT_1085308"}]}],"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":"KAJ7039911.1"}],"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":26,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"Nudix hydrolase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51462"}]},{"type":"Motif","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"Nudix box","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00794"}]}],"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":"UP001218188"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7039911.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7039911.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000025","properties":[{"key":"ProteinId","value":"KAJ7039911.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6T6Q7","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","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":"1"}]},{"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":"1"}]},{"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":"MPPPGLPNNLKEVHSSGSGDWFPEAEIRYYTNVFVVQDGKLLLGYKKRGLGIHRYNGFGGKVEAEESTLDAALRELKEEAGITAPLVHAGTLLFVVPGEKWAHIDIFRADKYTGTITESDEMRPEWFPTTDIPFDNMWESDRYWLPLLLSKQHFSARADFNREGEKHIPMKWWIGTASKAVSQSN","length":185,"molWeight":21009,"crc64":"BC760774F70C49F3","md5":"57E2D3D9A55651EA1242EC60E6D6873D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":7,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Motif":1},"uniParcId":"UPI00297AA369"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6TCH5","uniProtkbId":"A0AAD6TCH5_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2024-05-29","entryVersion":9,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7041808.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"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"}],"value":"PIM1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7041808.1"}],"value":"C8F04DRAFT_994533"}]}],"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":"Hydrolysis of proteins in presence of ATP.","ecNumber":"3.4.21.53","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}]}},{"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"}],"value":"Belongs to the peptidase S16 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7041808.1"}],"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":142,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"Lon N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51787"}]},{"type":"Domain","location":{"start":{"value":875,"modifier":"EXACT"},"end":{"value":1063,"modifier":"EXACT"}},"description":"Lon proteolytic","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51786"}]},{"type":"Region","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":776,"modifier":"EXACT"},"end":{"value":850,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1072,"modifier":"EXACT"},"end":{"value":1096,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":83,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"Pro residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":798,"modifier":"EXACT"},"end":{"value":817,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1075,"modifier":"EXACT"},"end":{"value":1084,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":968,"modifier":"EXACT"},"end":{"value":968,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01122"}]},{"type":"Active site","location":{"start":{"value":1011,"modifier":"EXACT"},"end":{"value":1011,"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":552,"modifier":"EXACT"},"end":{"value":559,"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":"UP001218188"}],"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"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022946"}],"id":"KW-0809","category":"Domain","name":"Transit peptide"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7041808.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7041808.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000015","properties":[{"key":"ProteinId","value":"KAJ7041808.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6TCH5","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","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":"3.30.230.10:FF:000019","properties":[{"key":"EntryName","value":"Lon protease homolog 2, peroxisomal"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.8.60:FF:000184","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"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":"2.30.130.40:FF:000010","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":"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"}]}],"sequence":{"value":"MNRLGQGIRRAAVASGKSLLWRPVASSSRVTLDSRHFSVSIPSYAQPTRLLKYPRWINPKGGADEQDVPAPAQNIELEAPENDSPGDSASNGSAASSSSSESAPPASSGGDNPDAPPPPKDPPPPSTGTIAKQSVPELYPHVLALPIARRPLIPGFYKAVVVKNPDVVAAIKDMMKRGQPYLGAFLLKDENTDSDVITDINAVHPVGVFAQITSVFTATGRGDDEPEEGLTAVLYPHRRVKITELLQASVVKVEGVSPEQPQTVLEPPEPEPAPVVEQKPPPPGPVQTSFLHTHPIAIVAIENITTLPFNKDDQHVRAFMAEIISVFKDIAQLNPMFRDQITNFTMNQVTSSIFDEPDKLADFAAAVCSGDVRELQDVLESLEVTDRLQKALLVLKKELINAQLQSKLARDVDSKIAKRQREYYLMEQLKGIKKELGMESDGKDRILDKFRERAAGLKMPEPVRKVFDEELSKLAGLEPAASEANVTRNYLEWLTQIPWGQHSPENFSIAHAQTVLDADHYGLSDVKDRILEFLAVGKLRGTVQGKIVCLVGPPGVGKTSIGKSIARALGRQFFRFSVGGLTDVAEIKGHRRTYVGALPGKIIQALKRVGTENPLVLIDEVDKIGRGINGDPASALLEMLDPEQNNGFLDHYMDVPVDLSRVLFVCTANTLDTIPAPLLDRMEVLEVSGYVSEEKAQIASRYLGPQAKEASGLKDADVLLDERAVDMLIKYYCRESGVRGLKKHIEKIYRKAALSLVKELGEEVFPEPAAAAAAETEVVKSVESQEPPSNEPAVEEVASTTGSSSTSPPADSTSTADNTVETEDASSTPDRKPVTTQERQPMPIPDSVHVRITPDNLKDYVGPPVYQKDRLYARAPPPGVSTGLGYLGNGSGAVMPVEVISMPGKGGLQLTGKLGEVIRESAHIGLSWVKSHASELGITSVSGDGGLLDARDIHVHMPEGSIGKEGPSAGTAIVAAFVSLFTKTRISPDIAMTGEISLVGQVLPVGGLKEKILAAHRAGITTILAPAANRADIEENVPASVKDGIRFVYVEDVREVLHEVFKGSAVAERWKETLPLEDGEPLESESEHEPLPVAAP","length":1096,"molWeight":118157,"crc64":"AF3E4F56B70AE412","md5":"2169A6EEF1030AE7D877C39325DFADCA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":4,"Compositional bias":4,"Active site":2,"Binding site":1},"uniParcId":"UPI002971B130"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6TEM0","uniProtkbId":"A0AAD6TEM0_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":10,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7043916.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012429"}],"value":"protein kinase C"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012429"}],"value":"2.7.11.13"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7043916.1"}],"value":"C8F04DRAFT_1070927"}]}],"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":"2.7.11.13","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047470"}]}},{"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":"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":"2.7.11.13","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047272"}]}},{"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":"PROSITE-ProRule","id":"PRU10027"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005490"}],"value":"Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily"}],"commentType":"SIMILARITY"},{"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:0000256","source":"PROSITE-ProRule","id":"PRU00618"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7043916.1"}],"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":112,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"REM-1","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51860"}]},{"type":"Domain","location":{"start":{"value":203,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"C2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50004"}]},{"type":"Domain","location":{"start":{"value":428,"modifier":"EXACT"},"end":{"value":476,"modifier":"EXACT"}},"description":"Phorbol-ester/DAG-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50081"}]},{"type":"Domain","location":{"start":{"value":495,"modifier":"EXACT"},"end":{"value":545,"modifier":"EXACT"}},"description":"Phorbol-ester/DAG-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50081"}]},{"type":"Domain","location":{"start":{"value":754,"modifier":"EXACT"},"end":{"value":1013,"modifier":"EXACT"}},"description":"Protein kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50011"}]},{"type":"Domain","location":{"start":{"value":1014,"modifier":"EXACT"},"end":{"value":1081,"modifier":"EXACT"}},"description":"AGC-kinase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51285"}]},{"type":"Zinc finger","location":{"start":{"value":428,"modifier":"EXACT"},"end":{"value":476,"modifier":"EXACT"}},"description":"Phorbol-ester/DAG-type","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}]},{"type":"Zinc finger","location":{"start":{"value":495,"modifier":"EXACT"},"end":{"value":545,"modifier":"EXACT"}},"description":"Phorbol-ester/DAG-type","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}]},{"type":"Region","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":565,"modifier":"EXACT"},"end":{"value":584,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":589,"modifier":"EXACT"},"end":{"value":746,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Coiled coil","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Compositional bias","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":617,"modifier":"EXACT"},"end":{"value":632,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":633,"modifier":"EXACT"},"end":{"value":645,"modifier":"EXACT"}},"description":"Pro residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":685,"modifier":"EXACT"},"end":{"value":696,"modifier":"EXACT"}},"description":"Pro residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":714,"modifier":"EXACT"},"end":{"value":726,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":879,"modifier":"EXACT"},"end":{"value":879,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]},{"type":"Binding site","location":{"start":{"value":783,"modifier":"EXACT"},"end":{"value":783,"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":"Modified residue","location":{"start":{"value":1055,"modifier":"EXACT"},"end":{"value":1055,"modifier":"EXACT"}},"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00618"}]},{"type":"Modified residue","location":{"start":{"value":1073,"modifier":"EXACT"},"end":{"value":1073,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00618"}]}],"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:0000256","source":"PROSITE-ProRule","id":"PRU01207"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"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":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"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:0000256","source":"ARBA","id":"ARBA00022553"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00618"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"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":"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"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}],"id":"KW-0862","category":"Ligand","name":"Zinc"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022771"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00226"}],"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7043916.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7043916.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000008","properties":[{"key":"ProteinId","value":"KAJ7043916.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6TEM0","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019992","properties":[{"key":"GoTerm","value":"F:diacylglycerol binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004697","properties":[{"key":"GoTerm","value":"F:diacylglycerol-dependent serine/threonine kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0009272","properties":[{"key":"GoTerm","value":"P:fungal-type cell wall biogenesis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0007165","properties":[{"key":"GoTerm","value":"P:signal transduction"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd20822","properties":[{"key":"EntryName","value":"C1_ScPKC1-like_rpt1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd20823","properties":[{"key":"EntryName","value":"C1_ScPKC1-like_rpt2"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd11620","properties":[{"key":"EntryName","value":"HR1_PKC-like_2_fungi"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd05570","properties":[{"key":"EntryName","value":"STKc_PKC"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.287.160:FF:000004","properties":[{"key":"EntryName","value":"Protein kinase C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.510.10:FF:000101","properties":[{"key":"EntryName","value":"Protein kinase C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.200.20:FF:000103","properties":[{"key":"EntryName","value":"Protein kinase C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.60.20:FF:000014","properties":[{"key":"EntryName","value":"Protein kinase C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.60.20:FF:000034","properties":[{"key":"EntryName","value":"Protein kinase C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.60.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"2.60.40.150","properties":[{"key":"EntryName","value":"C2 domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.287.160","properties":[{"key":"EntryName","value":"HR1 repeat"},{"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":"IPR000961","properties":[{"key":"EntryName","value":"AGC-kinase_C"}]},{"database":"InterPro","id":"IPR046349","properties":[{"key":"EntryName","value":"C1-like_sf"}]},{"database":"InterPro","id":"IPR000008","properties":[{"key":"EntryName","value":"C2_dom"}]},{"database":"InterPro","id":"IPR035892","properties":[{"key":"EntryName","value":"C2_domain_sf"}]},{"database":"InterPro","id":"IPR011072","properties":[{"key":"EntryName","value":"HR1_rho-bd"}]},{"database":"InterPro","id":"IPR036274","properties":[{"key":"EntryName","value":"HR1_rpt_sf"}]},{"database":"InterPro","id":"IPR011009","properties":[{"key":"EntryName","value":"Kinase-like_dom_sf"}]},{"database":"InterPro","id":"IPR037312","properties":[{"key":"EntryName","value":"PKC-like_HR1"}]},{"database":"InterPro","id":"IPR002219","properties":[{"key":"EntryName","value":"PKC_DAG/PE"}]},{"database":"InterPro","id":"IPR017892","properties":[{"key":"EntryName","value":"Pkinase_C"}]},{"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":"PTHR24351","properties":[{"key":"EntryName","value":"RIBOSOMAL PROTEIN S6 KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00130","properties":[{"key":"EntryName","value":"C1_1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02185","properties":[{"key":"EntryName","value":"HR1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF00069","properties":[{"key":"EntryName","value":"Pkinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00433","properties":[{"key":"EntryName","value":"Pkinase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00109","properties":[{"key":"EntryName","value":"C1"},{"key":"MatchStatus","value":"2"}]},{"database":"SMART","id":"SM00742","properties":[{"key":"EntryName","value":"Hr1"},{"key":"MatchStatus","value":"2"}]},{"database":"SMART","id":"SM00133","properties":[{"key":"EntryName","value":"S_TK_X"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00220","properties":[{"key":"EntryName","value":"S_TKc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF49562","properties":[{"key":"EntryName","value":"C2 domain (Calcium/lipid-binding domain, CaLB)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF57889","properties":[{"key":"EntryName","value":"Cysteine-rich domain"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF46585","properties":[{"key":"EntryName","value":"HR1 repeat"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56112","properties":[{"key":"EntryName","value":"Protein kinase-like (PK-like)"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51285","properties":[{"key":"EntryName","value":"AGC_KINASE_CTER"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50004","properties":[{"key":"EntryName","value":"C2"},{"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"}]},{"database":"PROSITE","id":"PS51860","properties":[{"key":"EntryName","value":"REM_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00479","properties":[{"key":"EntryName","value":"ZF_DAG_PE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50081","properties":[{"key":"EntryName","value":"ZF_DAG_PE_2"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MAELDQKIQDVYKHIQTERKILEACQSLAKATTNPDVLRRNDAKIRETERSLLYFEATLRELQTRKMQQSQQDSSGSAAPQVPPKIDPRTGRASTQGPPGAAPKYSNLDLIKAETPHTPTKISRMLHQLEFKLRVEMQYKEGIEKMAKLYQADGDKKSRADAETKKVESEKKIQLLQTALKQYKNLHILDDVVEEEDTNNNGPPGTDTERKDNLRAKPLSGTLQVTVQGARELDHAPVVSNKSRSASKQVTETVVSLKVEGTQLARSHPSRTDRWNEDFEITVDKANEVEIVVADKQVADTQGVPIGLLWIRISDLVEALRRQKVGQDSGQGWVTAGAMPGNPMMPNGGNMNSPLGYRDGGTGSMIGMAPTADGIDAWFAVEPAGAILLHLNFIKENVRKRPMDAPLGGLGRQGAVRKRKDEIHEMNGHKFVQRQFYQLMLCAFCSEFLLNAVGYQCEDCRYTCHKKCYEKVVTKCISKSISGEGDEEKINHRIPHRFEPLTNIGANWCCHCGYMLPLGRKNSRKCSECNITCHANCVHLVPDFCGMSMETANILLRDWRDINKSRSDKTHSAPRKQLSMAVESPTVAMGNMRLGGPDTAPPDYGRPPPGGTDPRHQQLPQQPTHPQHMQPPGQVPYSPPGPAARPPGGARVSIPPSYDSTQQGQQGRPPPGAYDPASALGPDGYPAPYPGPPKSPQPGARPVKQGGLPPSPNPMRQSTGPPQMQMTIPPVRPHPQQQPVRQPTRKRKVGLDDFNFLAVLGKGNFGKVMLAEEKKTNGLYAIKVLKKEFIIDNDEVESTRSEKRVFLAAARERHPFLLGLHSCFQTETRVYFVMEYVSGGDLMLHIQRKQFSLRQAKFYASEVLLALEYFHKNGIIYRDLKLDNILLTVEGHVKVADYGLCKEEMWYGKTTSTFCGTPEFMAPEILLEQRYGRAVDWWAFGVLTYEMLLGQSPFRGDDEDEIFDAILEDEPLYPITMPRDAVSILQKLLNRDPLRRLGAGEEDAEEIKRQPFFKDVNFDDVLNKRIPPPYFPTINGSADTSNFDEEFTKEQPTLTPVHGQLSSRDQQEFSGFSWVANWADV","length":1081,"molWeight":120944,"crc64":"143881E693004BC9","md5":"716D40602AC8BEAC735C21D4BA5539A6"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":4,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":6,"Zinc finger":2,"Region":4,"Coiled coil":1,"Compositional bias":5,"Active site":1,"Binding site":1,"Modified residue":2},"uniParcId":"UPI0029744AE1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6THI5","uniProtkbId":"A0AAD6THI5_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":12,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7045782.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013184"}],"value":"histone acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013184"}],"value":"2.3.1.48"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7045782.1"}],"value":"C8F04DRAFT_1066152"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045805"}],"value":"Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac. The NuA4 complex is involved in the DNA damage response and is required for chromosome segregation. The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) through homologous recombination. Recruitment to promoters depends on H3K4me. Also acetylates non-histone proteins. In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-hydroxyisobutyrylation and crotonylation, respectively"}],"commentType":"FUNCTION"},{"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":"ARBA00011353"}],"value":"Component of the NuA4 histone acetyltransferase complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004286"}],"value":"Chromosome","id":"SL-0468"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"}],"value":"Nucleus","id":"SL-0191"}}]},{"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":"KAJ7045782.1"}],"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":263,"modifier":"EXACT"},"end":{"value":534,"modifier":"EXACT"}},"description":"MYST-type HAT","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51726"}]},{"type":"Region","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":439,"modifier":"EXACT"},"end":{"value":439,"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":443,"modifier":"EXACT"},"end":{"value":443,"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":452,"modifier":"EXACT"},"end":{"value":452,"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":363,"modifier":"EXACT"},"end":{"value":363,"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:0000256","source":"ARBA","id":"ARBA00022853"}],"id":"KW-0156","category":"Molecular function","name":"Chromatin regulator"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022454"}],"id":"KW-0158","category":"Cellular component","name":"Chromosome"},{"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:0000256","source":"ARBA","id":"ARBA00023242"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"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-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7045782.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7045782.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000004","properties":[{"key":"ProteinId","value":"KAJ7045782.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6THI5","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0000785","properties":[{"key":"GoTerm","value":"C:chromatin"},{"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:0003682","properties":[{"key":"GoTerm","value":"F:chromatin binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004402","properties":[{"key":"GoTerm","value":"F:histone acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003712","properties":[{"key":"GoTerm","value":"F:transcription coregulator activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"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:000022","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":"MSPSTTEEVLLSPPPITAGGTYTIQTVSVGCKIYIRRPGPDGQTEERLAEILSIRDKPVNAYTQRNKDIKQEDSDGSNPADKWEYFVHWDTFNKRLDDWVPGSRLILSRDLEWPRPKASPVKKVTPAAKKAPGKAPRPTSQNLLKKATSNAAFAASPALPATPSAFGGFSASPSPGPSTLKRKLPHDEEEEEEEEEPEDEDADAEGEMDVDGEGETETFDLSLTEPAAETEVPPPPLSAFSKEQEIEKLRTSGSMTQSISEIARVKNLNRLQIGKHEVDAWYFSPYPKEYAHLPILYICEFCLSFFPSPMMLSRHRLRCNILHPPGNEIYRSEDISFYEIDGKRQLTWCRNLSLLSKCFLDHKTLYYDVTPFMYYVMAQRDSTGCHVIGYFSKEKESAENYNVACILTLPQHQRFGYGKLLIEFSYELSKKEGKLGSPEKPLSDLGLLGYRSYWADTILELLMSSGEEMSIDDIAQKTSITHADVTNTCATLGLFKHYKGSHIICLNNAVLERIEKSRNKRKRRINPEHLRWKPPVFTRDQLRFGF","length":546,"molWeight":61829,"crc64":"5F1885C6D3C5B217","md5":"563BEE7726F07170FDF355326F101604"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":5,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":3,"Compositional bias":3,"Active site":1,"Binding site":2,"Modified residue":1},"uniParcId":"UPI002976A941"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6XD93","uniProtkbId":"A0AAD6XD93_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":11,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7045727.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Sulfate adenylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"2.7.7.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"ATP-sulfurylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Sulfate adenylate transferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"SAT"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"MET3"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7045727.1"}],"value":"C8F04DRAFT_1065958"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24152"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58243"},{"database":"ChEBI","id":"CHEBI:58339"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001823"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"sulfate + ATP + H(+) = adenosine 5'-phosphosulfate + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18133"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16189"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58243"}],"ecNumber":"2.7.7.4","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Allosterically inhibited by 3'-phosphoadenosine 5'-phosphosulfate (PAPS)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00062002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Homohexamer. Dimer of trimers"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"The adenylyl-sulfate kinase (APS kinase) is non-functional. It is involved in allosteric regulation by PAPS. PAPS binding induces a large rotational rearrangement of domains lowering the substrate affinity of the enzyme"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"In the C-terminal section; belongs to the APS kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"In the N-terminal section; belongs to the sulfate adenylyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7045727.1"}],"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":14,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"ATP-sulfurylase PUA-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF14306"}]},{"type":"Domain","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":398,"modifier":"EXACT"}},"description":"Sulphate adenylyltransferase catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01747"}]},{"type":"Domain","location":{"start":{"value":406,"modifier":"EXACT"},"end":{"value":562,"modifier":"EXACT"}},"description":"APS kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01583"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"N-terminal","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Region","location":{"start":{"value":406,"modifier":"EXACT"},"end":{"value":585,"modifier":"EXACT"}},"description":"Allosteric regulation domain; adenylyl-sulfate kinase-like","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Active site","location":{"start":{"value":209,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Active site","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Active site","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16189"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"sulfate","id":"ChEBI:CHEBI:16189"}},{"type":"Binding site","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16189"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"sulfate","id":"ChEBI:CHEBI:16189"}},{"type":"Binding site","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16189"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"sulfate","id":"ChEBI:CHEBI:16189"}},{"type":"Binding site","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":445,"modifier":"EXACT"},"end":{"value":448,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58339"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"3'-phosphoadenylyl sulfate","id":"ChEBI:CHEBI:58339","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":530,"modifier":"EXACT"},"end":{"value":530,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58339"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"3'-phosphoadenylyl sulfate","id":"ChEBI:CHEBI:58339","note":"allosteric inhibitor"}},{"type":"Site","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Site","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Site","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"Induces change in substrate recognition on ATP binding","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0198","category":"Biological process","name":"Cysteine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"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_03106"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7045727.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7045727.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000004","properties":[{"key":"ProteinId","value":"KAJ7045727.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6XD93","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","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:0004020","properties":[{"key":"GoTerm","value":"F:adenylylsulfate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004781","properties":[{"key":"GoTerm","value":"F:sulfate adenylyltransferase (ATP) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070814","properties":[{"key":"GoTerm","value":"P:hydrogen sulfide biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000103","properties":[{"key":"GoTerm","value":"P:sulfate assimilation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02027","properties":[{"key":"EntryName","value":"APSK"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00517","properties":[{"key":"EntryName","value":"ATPS"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.400.10:FF:000003","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000802","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000052","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"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":"3.10.400.10","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03106","properties":[{"key":"EntryName","value":"Sulf_adenylyltr_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002891","properties":[{"key":"EntryName","value":"APS"}]},{"database":"InterPro","id":"IPR059117","properties":[{"key":"EntryName","value":"APS_kinase_dom"}]},{"database":"InterPro","id":"IPR025980","properties":[{"key":"EntryName","value":"ATP-Sase_PUA-like_dom"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR015947","properties":[{"key":"EntryName","value":"PUA-like_sf"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"InterPro","id":"IPR027535","properties":[{"key":"EntryName","value":"Sulf_adenylyltr_euk"}]},{"database":"InterPro","id":"IPR050512","properties":[{"key":"EntryName","value":"Sulf_AdTrans/APS_kinase"}]},{"database":"InterPro","id":"IPR024951","properties":[{"key":"EntryName","value":"Sulfurylase_cat_dom"}]},{"database":"InterPro","id":"IPR002650","properties":[{"key":"EntryName","value":"Sulphate_adenylyltransferase"}]},{"database":"NCBIfam","id":"TIGR00455","properties":[{"key":"EntryName","value":"apsK"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004040","properties":[{"key":"EntryName","value":"PRK05537.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00339","properties":[{"key":"EntryName","value":"sopT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42700","properties":[{"key":"EntryName","value":"SULFATE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42700:SF1","properties":[{"key":"EntryName","value":"SULFATE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01583","properties":[{"key":"EntryName","value":"APS_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01747","properties":[{"key":"EntryName","value":"ATP-sulfurylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14306","properties":[{"key":"EntryName","value":"PUA_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52374","properties":[{"key":"EntryName","value":"Nucleotidylyl transferase"},{"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"}]}],"sequence":{"value":"MFDDLQLRRYAGNPPHGGVLQDLLARDEFIADKLREEAETLPDIILTERQLCDLELLTNGGFSPLEGFMNEADYTSVVDNLRLANGVLFPMPITLDVSQASIDALSIVPGARIALRDFRDDEPLAIITVEDIYKPDQVKEAVQVFGADDPAHPAVAYLRNKIHAFYVGGKVQAIQAPSHFDYVALRYTPAELRSHFKKLAWRKVVAFQTRNPMHRAHRELTVRAARQRHANVLIHPVVGLTKPGDVDAFTRVRVYQSIMEKYPNGMGHLALLPLAMRMAGPREAVWHAIIRKNFGATHFIVGRDHAGPGKNSQGKDFYGPYDAQELVTKYRDELQIDMVPFQQMSYIPATDEYQPADEIPAGVQTLDISGTELRRRLKTGAPIPDWFSYDAVVKTLRESYPPRNKQGFVLFLTGLWNSGKDNIARALQVTLNEQGGRSVTLLLGETVRQELSAELGFSREDRHTNTQRIAFVAAELTRAGAGVIAAPIAPHELSREAARETVLSSGGAGGNFFLIHVATPLAYCEKKDRKGVYAKARRGEIKGFTGVDDPYEVPKKADLTVDVSTQSIPEIVHSIVLLLETNGLL","length":585,"molWeight":64973,"crc64":"175F7F338DE9B629","md5":"D2E9ED7C3EB327839872CADF02C84907"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":3,"Region":2,"Active site":3,"Binding site":8,"Site":3},"uniParcId":"UPI0029779EE5"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6XDD1","uniProtkbId":"A0AAD6XDD1_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":10,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7041139.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"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":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7041139.1"}],"value":"C8F04DRAFT_170430"}]}],"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"}],"evidences":[{"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-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":"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:0000256","source":"HAMAP-Rule","id":"MF_03216"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7041139.1"}],"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":18,"modifier":"EXACT"}},"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Intramembrane","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Transmembrane","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Topological domain","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":51,"modifier":"EXACT"}},"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Transmembrane","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":72,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Topological domain","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Topological domain","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03216"}]},{"type":"Domain","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"Phospholipid methyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04191"}]},{"type":"Binding site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":104,"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":184,"modifier":"EXACT"},"end":{"value":185,"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":"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":"UP001218188"}],"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-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7041139.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7041139.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000018","properties":[{"key":"ProteinId","value":"KAJ7041139.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6XDD1","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","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":"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":"MSLPRGIDDIPTIVDWSQTSLYVSLFSIAASPLLWNLIGRNEYKNRTLTKLIGARTACFILGVSIFLAGLLRDVLYRIALHDQPRYPLPYEIQAILAWIIFGAGNFLVVSAYFQLGFWGTFCGDYFSILQEKRVTGFPFSILDNPMYFGAEMCFVGAALWYERPAGLLVALYVHLTYAVALRFEGPFTAMVYANHKSPGIQKHE","length":204,"molWeight":23005,"crc64":"AC14F59BA4076258","md5":"C8AD4031ED16184B346D73B19F7625DE"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":3,"PATHWAY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Topological domain":4,"Intramembrane":1,"Transmembrane":3,"Domain":1,"Binding site":2},"uniParcId":"UPI00297AE189"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6RWE4","uniProtkbId":"A0AAD6RWE4_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2024-05-29","entryVersion":10,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7016424.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"4: Predicted","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012462"}],"value":"tripeptidyl-peptidase II"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012462"}],"value":"3.4.14.10"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7016424.1"}],"value":"C8F04DRAFT_1161823"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002451"}],"value":"Secreted tripeptidyl-peptidase which degrades proteins at acidic pHs and is involved in virulence"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Release of an N-terminal tripeptide from a polypeptide.","ecNumber":"3.4.14.10","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001910"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Ca(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01032"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01032"}],"value":"Binds 1 Ca(2+) ion per subunit."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004239"}],"value":"Secreted, extracellular space","id":"SL-0112"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7016424.1"}],"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":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":579,"modifier":"EXACT"}},"description":"tripeptidyl-peptidase II","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5042001237"},{"type":"Domain","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":579,"modifier":"EXACT"}},"description":"Peptidase S53","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51695"}]},{"type":"Region","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"Gly residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":207,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":300,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01032"}]},{"type":"Active site","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01032"}]},{"type":"Active site","location":{"start":{"value":498,"modifier":"EXACT"},"end":{"value":498,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01032"}]},{"type":"Binding site","location":{"start":{"value":539,"modifier":"EXACT"},"end":{"value":539,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01032"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108"}},{"type":"Binding site","location":{"start":{"value":540,"modifier":"EXACT"},"end":{"value":540,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01032"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108"}},{"type":"Binding site","location":{"start":{"value":558,"modifier":"EXACT"},"end":{"value":558,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01032"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108"}},{"type":"Binding site","location":{"start":{"value":560,"modifier":"EXACT"},"end":{"value":560,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01032"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01032"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023180"}],"id":"KW-0325","category":"PTM","name":"Glycoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01032"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01032"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01032"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022525"}],"id":"KW-0964","category":"Cellular component","name":"Secreted"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022825"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01032"}],"id":"KW-0720","category":"Molecular function","name":"Serine protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"id":"KW-0732","category":"Domain","name":"Signal"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023026"}],"id":"KW-0843","category":"Biological process","name":"Virulence"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023145"}],"id":"KW-0865","category":"PTM","name":"Zymogen"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7016424.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7016424.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000509","properties":[{"key":"ProteinId","value":"KAJ7016424.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6RWE4","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion 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:0008240","properties":[{"key":"GoTerm","value":"F:tripeptidyl-peptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd04056","properties":[{"key":"EntryName","value":"Peptidases_S53"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd11377","properties":[{"key":"EntryName","value":"Pro-peptidase_S53"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.200:FF:000015","properties":[{"key":"EntryName","value":"Tripeptidyl peptidase A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.200","properties":[{"key":"EntryName","value":"Peptidase S8/S53 domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000209","properties":[{"key":"EntryName","value":"Peptidase_S8/S53_dom"}]},{"database":"InterPro","id":"IPR036852","properties":[{"key":"EntryName","value":"Peptidase_S8/S53_dom_sf"}]},{"database":"InterPro","id":"IPR015366","properties":[{"key":"EntryName","value":"S53_propep"}]},{"database":"InterPro","id":"IPR030400","properties":[{"key":"EntryName","value":"Sedolisin_dom"}]},{"database":"InterPro","id":"IPR050819","properties":[{"key":"EntryName","value":"Tripeptidyl-peptidase_I"}]},{"database":"PANTHER","id":"PTHR14218","properties":[{"key":"EntryName","value":"PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14218:SF15","properties":[{"key":"EntryName","value":"TRIPEPTIDYL-PEPTIDASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00082","properties":[{"key":"EntryName","value":"Peptidase_S8"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF09286","properties":[{"key":"EntryName","value":"Pro-kuma_activ"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00944","properties":[{"key":"EntryName","value":"Pro-kuma_activ"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54897","properties":[{"key":"EntryName","value":"Protease propeptides/inhibitors"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52743","properties":[{"key":"EntryName","value":"Subtilisin-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51695","properties":[{"key":"EntryName","value":"SEDOLISIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVATVLLCLFSLAAASPVINRRVVLERRDVPSSFASLGAASKTDSIKLRFALASQDIPGLQKALLDVSTPSSANYGKHLTLDEVNAYAAPSAAALTAVQNWLSSNNVNATSSGSGDWLTATVSIAQANTLLGTTYQTFQHSSGRTYARTLSYSLPAEVVQYIDEVHPSTTFNSPISLQPVVSMPQPDSRRHRKGNKGGKGGGGSSGSSGNSATNSTAADSCDTDVTPECLQTLYNIPATPATQASNSIAVAGFIDQFAQKADLQQFLTALRPDLSPQTTFSLETLDGGSNTQGAAEAGVEANLDVQYTVGVATKVPVVFVSVGEQSQDGDLGGFLDIVNFISGQKTIPQVMTTSYGENEADISPALATKLCNAYMALGARGTSVLFASGDGGVEGGSAQSCTTFQAAFPAGCPYLTAVGAVHGTAPETASTFSSGGFSNVFGVADYQKDAVAGYLTALGNTNKGLFNVSGRGYPDVAAQGENVQIVSGGTTQGVAGTSCSSPIFASVVALINDQLIAAGKSPLGFLNPFLYENAAALNDVTTGSNPGCGTQGFPAKTGWDPVTGLGTPNFAALKKAAGL","length":579,"molWeight":59178,"crc64":"502A45791715FE43","md5":"B478596CE067231A2F2F920AAE9C849D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"CAUTION":1},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":1,"Region":1,"Compositional bias":2,"Active site":3,"Binding site":4},"uniParcId":"UPI0029728573"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6RWL4","uniProtkbId":"A0AAD6RWL4_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2024-05-29","entryVersion":8,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7016699.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"value":"Double-strand break repair protein"}}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7016699.1"}],"value":"C8F04DRAFT_499916"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"value":"Core component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases. The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage. Within the MRN complex, MRE11 possesses both single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity. MRE11 first endonucleolytically cleaves the 5' strand at DNA DSB ends to prevent non-homologous end joining (NHEJ) and licence HR. It then generates a single-stranded DNA gap via 3' to 5' exonucleolytic degradation, which is required for single-strand invasion and recombination"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004286"}],"value":"Chromosome","id":"SL-0468"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009028"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003447"}],"value":"Belongs to the MRE11/RAD32 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7016699.1"}],"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":316,"modifier":"EXACT"},"end":{"value":499,"modifier":"EXACT"}},"description":"Mre11 DNA-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM01347"}]},{"type":"Region","location":{"start":{"value":437,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":547,"modifier":"EXACT"},"end":{"value":713,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":445,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":547,"modifier":"EXACT"},"end":{"value":561,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":575,"modifier":"EXACT"},"end":{"value":587,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":603,"modifier":"EXACT"},"end":{"value":614,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":623,"modifier":"EXACT"},"end":{"value":635,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":639,"modifier":"EXACT"},"end":{"value":656,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":661,"modifier":"EXACT"},"end":{"value":677,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000882-1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022454"}],"id":"KW-0158","category":"Cellular component","name":"Chromosome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022759"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"id":"KW-0255","category":"Molecular function","name":"Endonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022839"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"id":"KW-0269","category":"Molecular function","name":"Exonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023254"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"id":"KW-0469","category":"Biological process","name":"Meiosis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022722"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7016699.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7016699.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000471","properties":[{"key":"ProteinId","value":"KAJ7016699.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6RWL4","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0030870","properties":[{"key":"GoTerm","value":"C:Mre11 complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0035861","properties":[{"key":"GoTerm","value":"C:site of double-strand break"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008296","properties":[{"key":"GoTerm","value":"F:3'-5'-DNA exonuclease activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000014","properties":[{"key":"GoTerm","value":"F:single-stranded DNA endonuclease activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000724","properties":[{"key":"GoTerm","value":"P:double-strand break repair via homologous recombination"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006303","properties":[{"key":"GoTerm","value":"P:double-strand break repair via nonhomologous end joining"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042138","properties":[{"key":"GoTerm","value":"P:meiotic DNA double-strand break formation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0097552","properties":[{"key":"GoTerm","value":"P:mitochondrial double-strand break repair via homologous recombination"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0007095","properties":[{"key":"GoTerm","value":"P:mitotic G2 DNA damage checkpoint signaling"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0031573","properties":[{"key":"GoTerm","value":"P:mitotic intra-S DNA damage checkpoint signaling"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000723","properties":[{"key":"GoTerm","value":"P:telomere maintenance"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00840","properties":[{"key":"EntryName","value":"MPP_Mre11_N"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.60.21.10:FF:000011","properties":[{"key":"EntryName","value":"Double-strand break repair protein"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.60.21.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.110.110","properties":[{"key":"EntryName","value":"Mre11, capping domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004843","properties":[{"key":"EntryName","value":"Calcineurin-like_PHP"}]},{"database":"InterPro","id":"IPR029052","properties":[{"key":"EntryName","value":"Metallo-depent_PP-like"}]},{"database":"InterPro","id":"IPR003701","properties":[{"key":"EntryName","value":"Mre11"}]},{"database":"InterPro","id":"IPR038487","properties":[{"key":"EntryName","value":"Mre11_capping_dom"}]},{"database":"InterPro","id":"IPR007281","properties":[{"key":"EntryName","value":"Mre11_DNA-bd"}]},{"database":"InterPro","id":"IPR041796","properties":[{"key":"EntryName","value":"Mre11_N"}]},{"database":"NCBIfam","id":"TIGR00583","properties":[{"key":"EntryName","value":"mre11"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10139","properties":[{"key":"EntryName","value":"DOUBLE-STRAND BREAK REPAIR PROTEIN MRE11"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10139:SF1","properties":[{"key":"EntryName","value":"DOUBLE-STRAND BREAK REPAIR PROTEIN MRE11"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00149","properties":[{"key":"EntryName","value":"Metallophos"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04152","properties":[{"key":"EntryName","value":"Mre11_DNA_bind"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000882","properties":[{"key":"EntryName","value":"DSB_repair_MRE11"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01347","properties":[{"key":"EntryName","value":"Mre11_DNA_bind"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56300","properties":[{"key":"EntryName","value":"Metallo-dependent phosphatases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSDDEGPGTGPAIRNRDEFPNDTIRIMLATDNHIGYMERDPVRGQDSINTFREILQLAVKHDVDFILLAGDLFHENKPSRDCLYKTIALLREYTLGDKPVQVELLSDPDEGKADGFSFPAVNYEDPNFNVSIPVFSIHGNHDDPQGAGSEGALCALDVLSVTGLINYMGKIDLPVGDAEANNTGIAVRPILLRKGNTHLGLYGIGNVKDQRMHFELRSNRVRMFMPRNKQEWFNIMLLHQNRVKHGPQEFVPESLFDDSVDLVIWGHEHDCRIVPEPVAGKQYYISQPGSSVATSLADGEALEKHVALLQIQGKEFEMTPIPLRTVRPFVIESLVLSEIAEEEGLNLSDQMEITKYLKNKVNSLIAQANAQWEERNARAAEEGEEPLEPMLPLVRLKVDTTGVSEMSNPIRFGQEFQGQLANPRDVLVFHRAKKSAARGGKVNAEEPDLEEGDDGGDADLTSDEKLARVRVATLVKKYLEAQELQLLGEMEMSDAIAMFVEKDDTHAIQSYVTKAFKKLTKSAQATGDDDDIGEEELDEMLAKAKAEQDKNYADKVKDTQAARKAKGKGKAAAVEESDDSMMVDEPMDGGGDGSDFDSDPVPVKKKAAAAKPKKAAPVAKAKAAPKKAPAKRGKKAVSESEDDEDVIEIDSDDSDEPPAKATKKTAAAKKAPAKKKAAPAAQSQLTFAPAGRSSRVAATKARGKMVVEDDSDD","length":713,"molWeight":78036,"crc64":"0F5B4786949F6D8B","md5":"464F930679141CE6026114E8246653F0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Compositional bias":7,"Active site":1},"uniParcId":"UPI0029736BEB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6RX11","uniProtkbId":"A0AAD6RX11_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":10,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7016890.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038999"}],"value":"mitogen-activated protein kinase kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038999"}],"value":"2.7.12.2"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7016890.1"}],"value":"C8F04DRAFT_1158957"}]}],"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":"PROSITE-ProRule","id":"PRU10027"}]}},{"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":"2.7.12.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049014"}]}},{"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":"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":"2.7.12.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049299"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10596"},{"database":"Rhea","id":"RHEA-COMP:10136"},{"database":"Rhea","id":"RHEA-COMP:20101"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:61978"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.12.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051693"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038035"}],"value":"Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily"}],"commentType":"SIMILARITY"},{"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":"KAJ7016890.1"}],"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":126,"modifier":"EXACT"},"end":{"value":440,"modifier":"EXACT"}},"description":"Protein kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50011"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":332,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"Pro residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":89,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]},{"type":"Binding site","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":155,"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"}}],"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: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":"Proteomes","id":"UP001218188"}],"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-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7016890.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7016890.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000454","properties":[{"key":"ProteinId","value":"KAJ7016890.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6RX11","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004674","properties":[{"key":"GoTerm","value":"F:protein serine/threonine kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004712","properties":[{"key":"GoTerm","value":"F:protein serine/threonine/tyrosine kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0000165","properties":[{"key":"GoTerm","value":"P:MAPK cascade"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"FunFam","id":"3.30.200.20:FF:000040","properties":[{"key":"EntryName","value":"Dual specificity mitogen-activated protein kinase kinase"},{"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":"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":"PTHR47448","properties":[{"key":"EntryName","value":"DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE DSOR1-LIKE PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR47448:SF1","properties":[{"key":"EntryName","value":"SERINE_THREONINE-PROTEIN KINASE STE7 HOMOLOG"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00069","properties":[{"key":"EntryName","value":"Pkinase"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00220","properties":[{"key":"EntryName","value":"S_TKc"},{"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":"MATPIRKKRNFKGIQLVMPPAVSPPPPLEPEPVPIRQAPVAGGAPGGKRRPPPMTLKAPKLPANTTSATPVENNTLLSVSNGDSTSPHTASPHANRRNTYHTALSNTLATLEIKNEIKFELRNEDLKDLHELGQGNGGSVKKVEHIPTGKFMAKKIVLIDAKPAVRKQILRELQILHDCNSKYIISFWGAFLADPNICICMEFADKGSLDGIYKKIGPIEIDVVGKVALAVLEGLTYLYDVHRIIHRDIKPSNILFNSEGEVKICDFGVSGELVNSIADTFVGTSTYMSPERIQGSPYTVKSDVWSLGISLIEIALGRFPFSESLSDDSDLSDFEGTLSPARPGSMNSLAALGLPPSRKRSSAAATSKKDKRKSKGVSLQGGAMTMSILELLQHIVNEPAPRLTPEGRFPEEAETFVDSCLLKDPEERKTPKDLLKDDWIMYSKTSPVDLKVWASTF","length":457,"molWeight":49897,"crc64":"D8F39A0E19370909","md5":"440A75F1FEABA680789478D25E3EAD22"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":5,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Compositional bias":3,"Active site":1,"Binding site":1},"uniParcId":"UPI002976F8F1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6RX92","uniProtkbId":"A0AAD6RX92_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":10,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7017044.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038999"}],"value":"mitogen-activated protein kinase kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038999"}],"value":"2.7.12.2"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7017044.1"}],"value":"C8F04DRAFT_1158259"}]}],"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":"PROSITE-ProRule","id":"PRU10027"}]}},{"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":"2.7.12.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049014"}]}},{"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":"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":"2.7.12.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049299"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10596"},{"database":"Rhea","id":"RHEA-COMP:10136"},{"database":"Rhea","id":"RHEA-COMP:20101"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:61978"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.12.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051693"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038035"}],"value":"Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily"}],"commentType":"SIMILARITY"},{"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":"KAJ7017044.1"}],"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":92,"modifier":"EXACT"},"end":{"value":401,"modifier":"EXACT"}},"description":"Protein kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50011"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]},{"type":"Binding site","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":121,"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"}}],"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: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":"Proteomes","id":"UP001218188"}],"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-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7017044.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7017044.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000441","properties":[{"key":"ProteinId","value":"KAJ7017044.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6RX92","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004674","properties":[{"key":"GoTerm","value":"F:protein serine/threonine kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004712","properties":[{"key":"GoTerm","value":"F:protein serine/threonine/tyrosine kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0000165","properties":[{"key":"GoTerm","value":"P:MAPK cascade"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"FunFam","id":"3.30.200.20:FF:000040","properties":[{"key":"EntryName","value":"Dual specificity mitogen-activated protein kinase kinase"},{"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":"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":"PTHR47448","properties":[{"key":"EntryName","value":"DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE DSOR1-LIKE PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR47448:SF1","properties":[{"key":"EntryName","value":"SERINE_THREONINE-PROTEIN KINASE STE7 HOMOLOG"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00069","properties":[{"key":"EntryName","value":"Pkinase"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00220","properties":[{"key":"EntryName","value":"S_TKc"},{"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":"MSIRKKRNFRDLQLPAAALGPNEGDPVPARLAPSGPRQRPHPLREHGPNGSLGPHSPPPSGSLHDQASLSSTIASLDPKPQYKEFDLQNDDFTNLQELGQGNGGSVMKVQHVPTGTIMAKKIVLIDAKPAERKKILLELQIMHDCDSPYIISSYGAYLAEPNICICMEFMDKGSFDGIYKRIGAIEIKVVGKVAVAVLEGLRYLYDVHRIIHRDIKPSNILCNSSGDIKLCDFGVSGELVNSIANTFVGTSIYMSPERIQGATYSVKSDIWSLGITLIELTVGQFPFSGSFSDDEDSDLEPNGINGDGETTPSHRDSLQVPAPTDAASKRRSRRRSKGVSLHGGGMTMSIIELMHQIVNEPSPRLPSGKFGREAEEFINGCLEKDLDARRTPAQLFDYAWILYSRQNGVDMKAWAATF","length":418,"molWeight":45802,"crc64":"2423FC642085D94A","md5":"8C215F136F257671A7FFF2552B954247"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":5,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Active site":1,"Binding site":1},"uniParcId":"UPI00297A5C3B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6RYU0","uniProtkbId":"A0AAD6RYU0_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":7,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7017820.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Acireductone dioxygenase"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Acireductone dioxygenase (Fe(2+)-requiring)"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"ARD'"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Fe-ARD"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"1.13.11.54"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Acireductone dioxygenase (Ni(2+)-requiring)"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"ARD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Ni-ARD"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"1.13.11.53"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"ADI1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7017820.1"}],"value":"C8F04DRAFT_1154246"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3-(methylsulfanyl)propanoate + CO + formate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14161"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:17245"},{"database":"ChEBI","id":"CHEBI:49016"},{"database":"ChEBI","id":"CHEBI:49252"}],"ecNumber":"1.13.11.53","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-methylsulfanyl-2-oxobutanoate + formate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24504"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:16723"},{"database":"ChEBI","id":"CHEBI:49252"}],"ecNumber":"1.13.11.54","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000428"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29033"}},{"name":"Ni(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49786"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes an acireductone dioxygenase reaction producing 2-keto-4-methylthiobutyrate, while nickel-binding promotes an acireductone dioxygenase reaction producing 3-(methylsulfanyl)propanoate."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 5/6"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"value":"Belongs to the acireductone dioxygenase (ARD) family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7017820.1"}],"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":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29033"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"ligand":{"name":"Fe(2+)","id":"ChEBI:CHEBI:29033","note":"for iron-dependent acireductone dioxygenase activity"}},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786","note":"for nickel-dependent acireductone dioxygenase activity"}},{"type":"Binding site","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29033"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"ligand":{"name":"Fe(2+)","id":"ChEBI:CHEBI:29033","note":"for iron-dependent acireductone dioxygenase activity"}},{"type":"Binding site","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786","note":"for nickel-dependent acireductone dioxygenase activity"}},{"type":"Binding site","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29033"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"ligand":{"name":"Fe(2+)","id":"ChEBI:CHEBI:29033","note":"for iron-dependent acireductone dioxygenase activity"}},{"type":"Binding site","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786","note":"for nickel-dependent acireductone dioxygenase activity"}},{"type":"Binding site","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29033"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"ligand":{"name":"Fe(2+)","id":"ChEBI:CHEBI:29033","note":"for iron-dependent acireductone dioxygenase activity"}},{"type":"Binding site","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786","note":"for nickel-dependent acireductone dioxygenase activity"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022964"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"id":"KW-0223","category":"Molecular function","name":"Dioxygenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023167"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022596"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"id":"KW-0533","category":"Ligand","name":"Nickel"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03154"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7017820.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7017820.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000377","properties":[{"key":"ProteinId","value":"KAJ7017820.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6RYU0","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","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:0010308","properties":[{"key":"GoTerm","value":"F:acireductone dioxygenase (Ni2+-requiring) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0010309","properties":[{"key":"GoTerm","value":"F:acireductone dioxygenase [iron(II)-requiring] activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016151","properties":[{"key":"GoTerm","value":"F:nickel cation binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0033353","properties":[{"key":"GoTerm","value":"P:L-methionine cycle"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02232","properties":[{"key":"EntryName","value":"cupin_ARD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.120.10:FF:000099","properties":[{"key":"EntryName","value":"1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.120.10","properties":[{"key":"EntryName","value":"Jelly Rolls"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03154","properties":[{"key":"EntryName","value":"Salvage_MtnD_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004313","properties":[{"key":"EntryName","value":"ARD"}]},{"database":"InterPro","id":"IPR027496","properties":[{"key":"EntryName","value":"ARD_euk"}]},{"database":"InterPro","id":"IPR014710","properties":[{"key":"EntryName","value":"RmlC-like_jellyroll"}]},{"database":"InterPro","id":"IPR011051","properties":[{"key":"EntryName","value":"RmlC_Cupin_sf"}]},{"database":"PANTHER","id":"PTHR23418","properties":[{"key":"EntryName","value":"ACIREDUCTONE DIOXYGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23418:SF0","properties":[{"key":"EntryName","value":"ACIREDUCTONE DIOXYGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03079","properties":[{"key":"EntryName","value":"ARD"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51182","properties":[{"key":"EntryName","value":"RmlC-like cupins"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRAYYFDNIPGDQRLPHDYAPSRPVAPDVLTALNVLSWTIPVDGYENSVNSIAKERGYKNRDTIDVSKEGMGEIYETKIKGFFEEHMHEDEEIRYILSGSGFFDIRETPTDAWIRLAVEPGDLIVLPAGIYHRFTLDEANRIKALRLFQDEPKWIPHNRSSDTDVNPHRLGYLKEIGVGA","length":180,"molWeight":20621,"crc64":"1745A8153326F1E2","md5":"7FA801B950175D5B6C2C2A884CCD7F4C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Binding site":8},"uniParcId":"UPI0029774F4F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6RYW4","uniProtkbId":"A0AAD6RYW4_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":10,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7017908.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038999"}],"value":"mitogen-activated protein kinase kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038999"}],"value":"2.7.12.2"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7017908.1"}],"value":"C8F04DRAFT_1153828"}]}],"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":"PROSITE-ProRule","id":"PRU10027"}]}},{"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":"2.7.12.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049014"}]}},{"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":"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":"2.7.12.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049299"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10596"},{"database":"Rhea","id":"RHEA-COMP:10136"},{"database":"Rhea","id":"RHEA-COMP:20101"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:61978"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.12.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051693"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038035"}],"value":"Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily"}],"commentType":"SIMILARITY"},{"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":"KAJ7017908.1"}],"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":88,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"Protein kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50011"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":294,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"Pro residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]},{"type":"Binding site","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":117,"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"}}],"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: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":"Proteomes","id":"UP001218188"}],"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-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7017908.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7017908.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000371","properties":[{"key":"ProteinId","value":"KAJ7017908.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6RYW4","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004674","properties":[{"key":"GoTerm","value":"F:protein serine/threonine kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004712","properties":[{"key":"GoTerm","value":"F:protein serine/threonine/tyrosine kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0000165","properties":[{"key":"GoTerm","value":"P:MAPK cascade"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"FunFam","id":"3.30.200.20:FF:000040","properties":[{"key":"EntryName","value":"Dual specificity mitogen-activated protein kinase kinase"},{"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":"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":"PTHR47448","properties":[{"key":"EntryName","value":"DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE DSOR1-LIKE PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR47448:SF1","properties":[{"key":"EntryName","value":"SERINE_THREONINE-PROTEIN KINASE STE7 HOMOLOG"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00069","properties":[{"key":"EntryName","value":"Pkinase"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00220","properties":[{"key":"EntryName","value":"S_TKc"},{"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":"MATPIRKKRNFKGIQLVMPPAVSPPPPLEPEPVPIRQAPVAGGAPGGKRRPPPMTLKAPKLPANTTSATPVENNTLLSIKFELRNEDLKDLHELGQGNGGSVKKVEHIPTGKFMAKKIVLIDAKPAVRKQILRELQILHDCNSKYIISFWGAFLADPNICICMEFADKGSLDGIYKKIGPIEIDVVGKVALAVLEGLTYLYDVHRIIHRDIKPSNILFNSEGEVKICDFGVSGELVNSIADTFVGTSTYMSPERIQGSPYTVKSDVWSLGISLIEIALGRFPFSESLSDDSDLSDFEGTLSPARPGSMNSLAALGLPPSRKRSSAAATSKKDKRKSKGVSLQGGAMTMSILELLQHIVNEPAPRLTPEGRFPEEAETFVDSCLLKDPEERKTPKDLLKDDWIMYSKTSPVDLKVWASTF","length":419,"molWeight":45809,"crc64":"0ABBE2C13B86053F","md5":"2304A7DBB9A120EB641B2C47D2A2E22C"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":5,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Compositional bias":2,"Active site":1,"Binding site":1},"uniParcId":"UPI002971C420"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6RZT7","uniProtkbId":"A0AAD6RZT7_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2024-05-29","entryVersion":9,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018345.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362021"}],"value":"Nicotinamide-nucleotide adenylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362021"}],"value":"2.7.7.1"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362021"}],"value":"2.7.7.18"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018345.1"}],"value":"C8F04DRAFT_392195"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093425"}],"value":"Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Can also use GTP and ITP as nucleotide donors. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, can use NAD(+), NADH, NaAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide (NGD) as substrates. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+). Protects against axonal degeneration following injury. May be involved in the maintenance of axonal integrity. Also functions as a stress-response chaperone protein that prevents toxic aggregation of proteins; this function may be independent of its NAD(+) synthesis activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-nicotinamide D-ribonucleotide + ATP + H(+) = diphosphate + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21360"},{"database":"ChEBI","id":"CHEBI:14649"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57540"}],"ecNumber":"2.7.7.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049001"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362021"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"nicotinate beta-D-ribonucleotide + ATP + H(+) = deamido-NAD(+) + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22860"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57502"},{"database":"ChEBI","id":"CHEBI:58437"}],"ecNumber":"2.7.7.18","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048721"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362021"}]}},{"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":"ARBA00004658"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362021"}],"value":"Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005019"}],"value":"Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1"}],"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":"ARBA00004173"}],"value":"Mitochondrion","id":"SL-0173"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007064"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362021"}],"value":"Belongs to the eukaryotic NMN adenylyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018345.1"}],"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":37,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"Cytidyltransferase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01467"}]},{"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":"Region","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":273,"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":"RuleBase","id":"RU362021"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362021"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362021"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362021"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022642"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362021"}],"id":"KW-0662","category":"Biological process","name":"Pyridine nucleotide biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362021"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018345.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018345.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000344","properties":[{"key":"ProteinId","value":"KAJ7018345.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6RZT7","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005759","properties":[{"key":"GoTerm","value":"C:mitochondrial matrix"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0000309","properties":[{"key":"GoTerm","value":"F:nicotinamide-nucleotide adenylyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004515","properties":[{"key":"GoTerm","value":"F:nicotinate-nucleotide adenylyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0009435","properties":[{"key":"GoTerm","value":"P:NAD+ biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd09286","properties":[{"key":"EntryName","value":"NMNAT_Eukarya"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000221","properties":[{"key":"EntryName","value":"Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004821","properties":[{"key":"EntryName","value":"Cyt_trans-like"}]},{"database":"InterPro","id":"IPR051182","properties":[{"key":"EntryName","value":"Euk_NMN_adenylyltrnsfrase"}]},{"database":"InterPro","id":"IPR005248","properties":[{"key":"EntryName","value":"NadD/NMNAT"}]},{"database":"InterPro","id":"IPR045094","properties":[{"key":"EntryName","value":"NMNAT_euk"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"TIGR00482","properties":[{"key":"EntryName","value":"nicotinate (nicotinamide) nucleotide adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12039","properties":[{"key":"EntryName","value":"NICOTINAMIDE MONONUCLEOTIDE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12039:SF0","properties":[{"key":"EntryName","value":"NICOTINAMIDE-NUCLEOTIDE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01467","properties":[{"key":"EntryName","value":"CTP_transf_like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52374","properties":[{"key":"EntryName","value":"Nucleotidylyl transferase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAAHSARDFTNPPNYEFPHHRLSPTLRDPEKTPIVLVACGSFSPVTYLHLRMFEMAKDYVRQNTDFEIVGGYLSPVSDMYKKPGLLSAQHRVNMCTLGAEDTSSWLMVDPWEAFQDYQRTAVVLDHFDYHINTVLGGAKTPDGEQRNIRIMLLAGSDLISTMSEPGVWSYSDLDHILGRYGTFIVERAGSGMDQATDSLARWRNNIHLISQLIQNDVSSTKVRLFIRRGLSVRYLLPANVVEYIEQNGLYLEDGASPNIPEKEPVADGSKKDSPASSLRS","length":280,"molWeight":31423,"crc64":"75EC5932ED3DAC5E","md5":"BF923C156C2D5BB3FF555FF22EE83D09"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Compositional bias":1},"uniParcId":"UPI00297A762E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6S049","uniProtkbId":"A0AAD6S049_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2024-05-29","entryVersion":8,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018374.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361156"}],"value":"Carboxypeptidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361156"}],"value":"3.4.16.-"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018374.1"}],"value":"C8F04DRAFT_1151751"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00037042"}],"value":"Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Preferential release of a C-terminal arginine or lysine residue.","ecNumber":"3.4.16.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001003"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Release of a C-terminal amino acid with broad specificity.","ecNumber":"3.4.16.5","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10075"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004393"}],"value":"Golgi apparatus, trans-Golgi network membrane","id":"SL-0267"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004393"}],"value":"Single-pass type I membrane protein","id":"SL-9905"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009431"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361156"}],"value":"Belongs to the peptidase S10 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018374.1"}],"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":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361156"}]},{"type":"Chain","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":640,"modifier":"EXACT"}},"description":"Carboxypeptidase","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361156"}],"featureId":"PRO_5041766032"},{"type":"Transmembrane","location":{"start":{"value":535,"modifier":"EXACT"},"end":{"value":559,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Region","location":{"start":{"value":599,"modifier":"EXACT"},"end":{"value":640,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":604,"modifier":"EXACT"},"end":{"value":613,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10074"}]},{"type":"Active site","location":{"start":{"value":462,"modifier":"EXACT"},"end":{"value":462,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10075"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022703"}],"id":"KW-0053","category":"Biological process","name":"Apoptosis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022645"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361156"}],"id":"KW-0121","category":"Molecular function","name":"Carboxypeptidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023180"}],"id":"KW-0325","category":"PTM","name":"Glycoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023034"}],"id":"KW-0333","category":"Cellular component","name":"Golgi apparatus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361156"}],"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:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361156"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361156"}],"id":"KW-0732","category":"Domain","name":"Signal"},{"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-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018374.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018374.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000343","properties":[{"key":"ProteinId","value":"KAJ7018374.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6S049","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005802","properties":[{"key":"GoTerm","value":"C:trans-Golgi network"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004185","properties":[{"key":"GoTerm","value":"F:serine-type carboxypeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.40.50.1820:FF:000121","properties":[{"key":"EntryName","value":"Carboxypeptidase D"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1820","properties":[{"key":"EntryName","value":"alpha/beta hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029058","properties":[{"key":"EntryName","value":"AB_hydrolase_fold"}]},{"database":"InterPro","id":"IPR001563","properties":[{"key":"EntryName","value":"Peptidase_S10"}]},{"database":"InterPro","id":"IPR033124","properties":[{"key":"EntryName","value":"Ser_caboxypep_his_AS"}]},{"database":"InterPro","id":"IPR018202","properties":[{"key":"EntryName","value":"Ser_caboxypep_ser_AS"}]},{"database":"PANTHER","id":"PTHR11802:SF190","properties":[{"key":"EntryName","value":"PHEROMONE-PROCESSING CARBOXYPEPTIDASE KEX1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11802","properties":[{"key":"EntryName","value":"SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00450","properties":[{"key":"EntryName","value":"Peptidase_S10"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00724","properties":[{"key":"EntryName","value":"CRBOXYPTASEC"}]},{"database":"SUPFAM","id":"SSF53474","properties":[{"key":"EntryName","value":"alpha/beta-Hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00560","properties":[{"key":"EntryName","value":"CARBOXYPEPT_SER_HIS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00131","properties":[{"key":"EntryName","value":"CARBOXYPEPT_SER_SER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIRSRCLAVLWTLVFALKSTYAAPTDLPSAASFYVPFLPDIHQDPEHPLTIFAGHLPSDPNASKYDAKTVTAHLFFVMIKNRRMADKQRIMFWFNGGPGCSSFDGLMMEVGPWRMDGKGGFKVAEGGWEEYTTMVYVDQPAGTGFSYTSTDKYVHTLDEAATQLLEFMGNFYKVFPEYKHMDTFLGGESYAGQWIPYFADAILNSKIGTNLRGAAIGNGWIDARRQYASYIDFAVKTGILEENSDAWKHAKERTDECMADIAKITSPEPITAPRCEGLLLDVTSVREKVYVCSWAEAGYRFDSIFDFSCSVDGKQMCINIYDIRFDDFAPACGMNWPPDIKPVTTYLDRKDVVRALHAEKNPVSWVECRGRIHQEIHERLSDSAITKLPKVLERIPVLIFAGDQDLICNYVGLESMIQAMEWNGEKGLGTVQTQSWSVSGAPAGTWVSSRNLTYTKIFNASHMAPFDLPHVSHDMILRFMGVNFSEIVGGSARIPSSVGSVVKPHLLEDVPTAATATAVADAGKSPQQAKAMWEAYYNAGSAAVVLTLIFAAIGIFVCYRRRRASGPRLPVNQHGEDIPLNAHSDDDLNGEMAQVEGDDEAFRQRQRRAKGKGKAVDVGPPIFDVGDSDEEEFGMGIRAD","length":640,"molWeight":70964,"crc64":"3F78483D1B167559","md5":"2313124389ABDE2EC47384BB45BA5862"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Signal":1,"Chain":1,"Transmembrane":1,"Region":1,"Compositional bias":1,"Active site":2},"uniParcId":"UPI002971C92E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6S068","uniProtkbId":"A0AAD6S068_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2024-05-29","entryVersion":10,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018826.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"value":"3-hydroxyanthranilate 3,4-dioxygenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"value":"1.13.11.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"value":"3-hydroxyanthranilate oxygenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"value":"3-HAO"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"value":"3-hydroxyanthranilic acid dioxygenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"value":"HAD"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"value":"Biosynthesis of nicotinic acid protein 1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"value":"BNA1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018826.1"}],"value":"C8F04DRAFT_976648"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"value":"Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17953"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:36559"},{"database":"ChEBI","id":"CHEBI:77612"}],"ecNumber":"1.13.11.6","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001954"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29033"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"value":"Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"value":"Belongs to the 3-HAO family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018826.1"}],"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":46,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:15379"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"ligand":{"name":"O2","id":"ChEBI:CHEBI:15379"}},{"type":"Binding site","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022964"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"id":"KW-0223","category":"Molecular function","name":"Dioxygenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022642"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03019"}],"id":"KW-0662","category":"Biological process","name":"Pyridine nucleotide biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018826.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018826.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000321","properties":[{"key":"ProteinId","value":"KAJ7018826.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6S068","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","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:0000334","properties":[{"key":"GoTerm","value":"F:3-hydroxyanthranilate 3,4-dioxygenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008198","properties":[{"key":"GoTerm","value":"F:ferrous iron binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0034354","properties":[{"key":"GoTerm","value":"P:'de novo' NAD+ biosynthetic process from L-tryptophan"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006569","properties":[{"key":"GoTerm","value":"P:L-tryptophan catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019805","properties":[{"key":"GoTerm","value":"P:quinolinate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06123","properties":[{"key":"EntryName","value":"cupin_HAO"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.120.10:FF:000131","properties":[{"key":"EntryName","value":"3-hydroxyanthranilate 3,4-dioxygenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.120.10","properties":[{"key":"EntryName","value":"Jelly Rolls"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00825","properties":[{"key":"EntryName","value":"3_HAO"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR010329","properties":[{"key":"EntryName","value":"3hydroanth_dOase"}]},{"database":"InterPro","id":"IPR014710","properties":[{"key":"EntryName","value":"RmlC-like_jellyroll"}]},{"database":"InterPro","id":"IPR011051","properties":[{"key":"EntryName","value":"RmlC_Cupin_sf"}]},{"database":"NCBIfam","id":"TIGR03037","properties":[{"key":"EntryName","value":"anthran_nbaC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR15497","properties":[{"key":"EntryName","value":"3-HYDROXYANTHRANILATE 3,4-DIOXYGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR15497:SF1","properties":[{"key":"EntryName","value":"3-HYDROXYANTHRANILATE 3,4-DIOXYGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06052","properties":[{"key":"EntryName","value":"3-HAO"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51182","properties":[{"key":"EntryName","value":"RmlC-like cupins"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPLALPLNFPAWLKDKSHLLKPPVNNFCLYQGQDFVVMAVGGPNERIDYHLNETEEWFYQYKGGMLLRTVDEGSFRDIRIEEGEMFLLSANTPHNPVRYADTIGIVMERVRPEKSRDHLRWYCPSDVHKEPTIIYEETFHVTDLGTQLKPVIQRWQENEQLRTCKSCGFVADPK","length":174,"molWeight":20340,"crc64":"22A171C46C4E0C34","md5":"29A2D5B85A4D7C5D97DC69609341BF7C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Binding site":7},"uniParcId":"UPI00297210CF"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6S0K0","uniProtkbId":"A0AAD6S0K0_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":9,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018056.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"}],"value":"Very-long-chain 3-oxoacyl-CoA reductase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"}],"value":"1.1.1.330"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"}],"value":"3-ketoacyl-CoA reductase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"}],"value":"3-ketoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"}],"value":"KAR"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"}],"value":"Microsomal beta-keto-reductase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018056.1"}],"value":"C8F04DRAFT_1214763"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"}],"value":"Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-long-chain 3-oxoacyl-CoA + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:48680"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:85440"},{"database":"ChEBI","id":"CHEBI:90725"}],"ecNumber":"1.1.1.330","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005194"}],"value":"Lipid metabolism; fatty acid biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"}],"value":"Endoplasmic reticulum membrane","id":"SL-0097"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"}],"value":"Single-pass membrane protein","id":"SL-9904"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000363"}],"value":"Belongs to the short-chain dehydrogenases/reductases (SDR) family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018056.1"}],"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":201,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10001"}]},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022824"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"}],"id":"KW-0256","category":"Cellular component","name":"Endoplasmic reticulum"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023160"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"}],"id":"KW-0275","category":"Biological process","name":"Fatty acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"}],"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_03107"}],"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_03107"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"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_03107"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03107"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018056.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7018056.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000362","properties":[{"key":"ProteinId","value":"KAJ7018056.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6S0K0","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","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:0045703","properties":[{"key":"GoTerm","value":"F:ketoreductase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0141040","properties":[{"key":"GoTerm","value":"F:very-long-chain 3-oxoacyl-CoA reductase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0030497","properties":[{"key":"GoTerm","value":"P:fatty acid elongation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd05356","properties":[{"key":"EntryName","value":"17beta-HSD1_like_SDR_c"},{"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":"HAMAP","id":"MF_03107","properties":[{"key":"EntryName","value":"3_ketoreductase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR027533","properties":[{"key":"EntryName","value":"3_ketoreductase_fungal"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR020904","properties":[{"key":"EntryName","value":"Sc_DH/Rdtase_CS"}]},{"database":"InterPro","id":"IPR002347","properties":[{"key":"EntryName","value":"SDR_fam"}]},{"database":"PANTHER","id":"PTHR43086:SF2","properties":[{"key":"EntryName","value":"HYDROXYSTEROID DEHYDROGENASE-LIKE PROTEIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43086","properties":[{"key":"EntryName","value":"VERY-LONG-CHAIN 3-OXOOACYL-COA REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00106","properties":[{"key":"EntryName","value":"adh_short"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000126","properties":[{"key":"EntryName","value":"11-beta-HSD1"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00081","properties":[{"key":"EntryName","value":"GDHRDH"}]},{"database":"PRINTS","id":"PR00080","properties":[{"key":"EntryName","value":"SDRFAMILY"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00061","properties":[{"key":"EntryName","value":"ADH_SHORT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDVLQDLAKGFALGALTASRFAITFISVFLQTFILPGTSLKTFGAKKDAWAVVTGASDGIGKEFALQLAGSGFNVLLVARTTSLLDAASEEIKAKYPGIRTAVHTIDFATADERAYEALTAEVDALDIGVLVNNVGKSHAYPAYLIDTPVAEMEDIVKINVGATLRVTYAILPGMIRRNRGLVLNIGSFAGAIPSPMLATYSGTKAFLATFTSALAEEVRAHNIVVEHINTYFVVSKLSKIRRASALVPQPKAYVRAVLGKIGLACGAANGGRPGTSTPFWSHSLMEYVLNALGLPGLYIWYTHQLHKDIRRRALKKAAKTQ","length":322,"molWeight":34525,"crc64":"2543B9F2951F54D0","md5":"BC10CA4D19CA5805033B2C20597A5586"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Active site":1,"Binding site":1},"uniParcId":"UPI002972DD37"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6S2R9","uniProtkbId":"A0AAD6S2R9_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-05-29","entryVersion":9,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7020008.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"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"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7020008.1"}],"value":"C8F04DRAFT_313835"}]}],"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":"KAJ7020008.1"}],"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":57,"modifier":"EXACT"},"end":{"value":524,"modifier":"EXACT"}},"description":"Protein kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50011"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":311,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":582,"modifier":"EXACT"},"end":{"value":626,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":321,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":587,"modifier":"EXACT"},"end":{"value":597,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":604,"modifier":"EXACT"},"end":{"value":613,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":614,"modifier":"EXACT"},"end":{"value":626,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10027"}]},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":86,"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"}}],"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: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":"Proteomes","id":"UP001218188"}],"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-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7020008.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7020008.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000277","properties":[{"key":"ProteinId","value":"KAJ7020008.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6S2R9","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","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:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004674","properties":[{"key":"GoTerm","value":"F:protein serine/threonine kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050684","properties":[{"key":"GoTerm","value":"P:regulation of mRNA processing"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000245","properties":[{"key":"GoTerm","value":"P:spliceosomal complex assembly"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd14136","properties":[{"key":"EntryName","value":"STKc_SRPK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.510.10:FF:000409","properties":[{"key":"EntryName","value":"CMGC/SRPK protein kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.200.20:FF:000076","properties":[{"key":"EntryName","value":"CMGC/SRPK protein kinase"},{"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":"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":"PTHR47634","properties":[{"key":"EntryName","value":"PROTEIN KINASE DOMAIN-CONTAINING PROTEIN-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR47634:SF9","properties":[{"key":"EntryName","value":"PROTEIN KINASE DOMAIN-CONTAINING PROTEIN-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":"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":"MSHLPAIYPGSPPDNEGDPDSPNSEISDAEDEEDWEDYKPGGYHPVKIGDAFSDNRYVVVRKLGWGHFSTVWLTWDSKMKRHVALKVVKSAARYTETALDEIKLLQRLITSSTPNGAPNHPGRSHVISFLDHFRHTGPNGTHVCMVFEVLGENLLGLVKRHQNKGVPMPVVKQIAKQVLLGLDYMHRCCGVIHTDIKPENVLIHIDDVESIIQSELALASASPSSSAPKPKIIGVPPSQGRGGNQTPRTQSSIFVSQPLPSPKSSGSLSSSYAAASGSVDRWGLGMTRIENKSPGTSSPSSELDLVSLSISPKSAHPPQNGPSLLSQQAPSGTKPVSMPPSHGAMDVDSDERYANGLADRITVKIADLGNATWTHHHFTDDIQTRQYRSPEVIVGAKWGTSADIWSVACVIFELITGGDYLFDPAKGSRYTKDDDHMAQIMELMGEVPKNISLGGKYSSEFFNRRGELRHISKLRFWPLDLVLHDKYLFPKPEADALASFLTPMLRLHPDKRAKASELVHHNWLEGVAVQGELDVIRRAERNDEMNAAAGMGLVAPPAGGVGADAAMAMAVAGFAAAAGAGAAAQPEAHETTEEKLQRTQSEADALKPVEDIRASAASGSASGAPQ","length":626,"molWeight":67504,"crc64":"53A8C9FE1FEBDF2E","md5":"4B8633BD64BDE3FC78C66EE9760C5427"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":4,"Compositional bias":7,"Active site":1,"Binding site":1},"uniParcId":"UPI002973A9B5"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6S336","uniProtkbId":"A0AAD6S336_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2024-05-29","entryVersion":6,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7020188.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"value":"alpha-1,2-Mannosidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"value":"3.2.1.-"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7020188.1"}],"value":"C8F04DRAFT_1145192"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) + 4 H2O = N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2) + 4 beta-D-mannose","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:56008"},{"database":"Rhea","id":"RHEA-COMP:14356"},{"database":"Rhea","id":"RHEA-COMP:14367"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28563"},{"database":"ChEBI","id":"CHEBI:59087"},{"database":"ChEBI","id":"CHEBI:139493"}],"ecNumber":"3.2.1.113","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048605"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) + 3 H2O = N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2) + 3 beta-D-mannose","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:56028"},{"database":"Rhea","id":"RHEA-COMP:14358"},{"database":"Rhea","id":"RHEA-COMP:14367"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28563"},{"database":"ChEBI","id":"CHEBI:59087"},{"database":"ChEBI","id":"CHEBI:60628"}],"ecNumber":"3.2.1.113","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047669"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Ca(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001913"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-2"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004922"}],"value":"Protein modification; protein glycosylation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007658"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"value":"Belongs to the glycosyl hydrolase 47 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7020188.1"}],"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":38,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-1"}]},{"type":"Active site","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-1"}]},{"type":"Active site","location":{"start":{"value":448,"modifier":"EXACT"},"end":{"value":448,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-1"}]},{"type":"Active site","location":{"start":{"value":485,"modifier":"EXACT"},"end":{"value":485,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-1"}]},{"type":"Binding site","location":{"start":{"value":572,"modifier":"EXACT"},"end":{"value":572,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-2"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108"}},{"type":"Disulfide bond","location":{"start":{"value":388,"modifier":"EXACT"},"end":{"value":435,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-3"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-2"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-3"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-2"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"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-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7020188.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7020188.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000271","properties":[{"key":"ProteinId","value":"KAJ7020188.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6S336","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005783","properties":[{"key":"GoTerm","value":"C:endoplasmic reticulum"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016020","properties":[{"key":"GoTerm","value":"C:membrane"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005509","properties":[{"key":"GoTerm","value":"F:calcium ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004571","properties":[{"key":"GoTerm","value":"F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0036503","properties":[{"key":"GoTerm","value":"P:ERAD pathway"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"Gene3D","id":"1.50.10.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR012341","properties":[{"key":"EntryName","value":"6hp_glycosidase-like_sf"}]},{"database":"InterPro","id":"IPR001382","properties":[{"key":"EntryName","value":"Glyco_hydro_47"}]},{"database":"InterPro","id":"IPR050749","properties":[{"key":"EntryName","value":"Glycosyl_Hydrolase_47"}]},{"database":"InterPro","id":"IPR036026","properties":[{"key":"EntryName","value":"Seven-hairpin_glycosidases"}]},{"database":"PANTHER","id":"PTHR11742:SF55","properties":[{"key":"EntryName","value":"ENDOPLASMIC RETICULUM MANNOSYL-OLIGOSACCHARIDE 1,2-ALPHA-MANNOSIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11742","properties":[{"key":"EntryName","value":"MANNOSYL-OLIGOSACCHARIDE ALPHA-1,2-MANNOSIDASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01532","properties":[{"key":"EntryName","value":"Glyco_hydro_47"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00747","properties":[{"key":"EntryName","value":"GLYHDRLASE47"}]},{"database":"SUPFAM","id":"SSF48225","properties":[{"key":"EntryName","value":"Seven-hairpin glycosidases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MADSTSTLRNRRHPTSNAAVPAQARDTKKPVRGTTSGILALFFLFLGVVALLALAGAAAAYIYYQNPGGYFWPKPQAPWVAVPGETEWTVDFSADLTKRDTIVAAFKHAWSAYERDAMGDDEYHPITKKGSNLTDAGGIGYTVIDSIDTMLLMGLEDEYARARKWVETSMSFDRDANFNTFETTIRVLGGLLSAYELTDGDELYLERAVDLADRLLPVFDTPSGLPYSQVNLAQRVGVADPDNRGLVSTAEASTLQLEFRYLGFLTDNLDYWDKAENVMKVIRRARLPNALTPIFMSSAEGKFMTSEIRLGSRGDSYYEYLKQYLQTGSIETVYRDMYDDSMQAIHENLIATSNKRKLIHTVEIHPRRLAHNNQMSWVRTLKQDHLVCFLGGSLMLGATTAGARTRPVSVPPRIEELSPVGRRDWTTGVGLIETCVDTYRTASGLSPEIVHFRESIETGSDWFIKDAKPPGELPVYDARYILRPETVESLFLAWRLTGNPKYRTYGWDIFQAIETHCRVPSGGYASVLNVEQVPVTWEDKMETFLMSETLKYLYLLFSDNTVLPLDQYVFNTEAHPLPIFSPTTVRSGFNF","length":591,"molWeight":66443,"crc64":"EA15F2A1E088FF63","md5":"F7FB66DC562976BCF50C1ADCE4B03AFF"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":1,"Region":1,"Active site":4,"Binding site":1,"Disulfide bond":1},"uniParcId":"UPI00297B4620"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6S389","uniProtkbId":"A0AAD6S389_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2024-05-29","entryVersion":6,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7020419.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"value":"alpha-1,2-Mannosidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"value":"3.2.1.-"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7020419.1"}],"value":"C8F04DRAFT_1144297"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) + 4 H2O = N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2) + 4 beta-D-mannose","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:56008"},{"database":"Rhea","id":"RHEA-COMP:14356"},{"database":"Rhea","id":"RHEA-COMP:14367"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28563"},{"database":"ChEBI","id":"CHEBI:59087"},{"database":"ChEBI","id":"CHEBI:139493"}],"ecNumber":"3.2.1.113","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048605"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) + 3 H2O = N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2) + 3 beta-D-mannose","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:56028"},{"database":"Rhea","id":"RHEA-COMP:14358"},{"database":"Rhea","id":"RHEA-COMP:14367"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28563"},{"database":"ChEBI","id":"CHEBI:59087"},{"database":"ChEBI","id":"CHEBI:60628"}],"ecNumber":"3.2.1.113","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047669"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Ca(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001913"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-2"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004922"}],"value":"Protein modification; protein glycosylation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007658"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"value":"Belongs to the glycosyl hydrolase 47 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7020419.1"}],"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":38,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-1"}]},{"type":"Active site","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-1"}]},{"type":"Active site","location":{"start":{"value":448,"modifier":"EXACT"},"end":{"value":448,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-1"}]},{"type":"Active site","location":{"start":{"value":485,"modifier":"EXACT"},"end":{"value":485,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-1"}]},{"type":"Binding site","location":{"start":{"value":572,"modifier":"EXACT"},"end":{"value":572,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-2"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108"}},{"type":"Disulfide bond","location":{"start":{"value":388,"modifier":"EXACT"},"end":{"value":435,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-3"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-2"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-3"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361193"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601382-2"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"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-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7020419.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7020419.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000264","properties":[{"key":"ProteinId","value":"KAJ7020419.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6S389","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005783","properties":[{"key":"GoTerm","value":"C:endoplasmic reticulum"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016020","properties":[{"key":"GoTerm","value":"C:membrane"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005509","properties":[{"key":"GoTerm","value":"F:calcium ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004571","properties":[{"key":"GoTerm","value":"F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0036503","properties":[{"key":"GoTerm","value":"P:ERAD pathway"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"Gene3D","id":"1.50.10.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR012341","properties":[{"key":"EntryName","value":"6hp_glycosidase-like_sf"}]},{"database":"InterPro","id":"IPR001382","properties":[{"key":"EntryName","value":"Glyco_hydro_47"}]},{"database":"InterPro","id":"IPR050749","properties":[{"key":"EntryName","value":"Glycosyl_Hydrolase_47"}]},{"database":"InterPro","id":"IPR036026","properties":[{"key":"EntryName","value":"Seven-hairpin_glycosidases"}]},{"database":"PANTHER","id":"PTHR11742:SF55","properties":[{"key":"EntryName","value":"ENDOPLASMIC RETICULUM MANNOSYL-OLIGOSACCHARIDE 1,2-ALPHA-MANNOSIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11742","properties":[{"key":"EntryName","value":"MANNOSYL-OLIGOSACCHARIDE ALPHA-1,2-MANNOSIDASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01532","properties":[{"key":"EntryName","value":"Glyco_hydro_47"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00747","properties":[{"key":"EntryName","value":"GLYHDRLASE47"}]},{"database":"SUPFAM","id":"SSF48225","properties":[{"key":"EntryName","value":"Seven-hairpin glycosidases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MADSTSTLRNRRHPTSDEAAPAQARDTKKPVKGTTSGILALFFLFLGVVALLALAGAAAAYIYYQNLGGYFWPEPQAPWVAVPGETEWTVDFSADLTKRDTVVAAFKHAWSAYERDAMGDDEYHPITKKGSNLTDAGGIGYTVIDSIDTMLIMGLDDEYARARKWVETSMSFDRDANFNTFETTIRVLGGLLSAYELTDGDELYLERAVDLADRLLPVFDTPSGLPYSQVNLAQRVGVADPDNRGLVSTAEASTLQLEFRYLGFLTDNLDYWDKAENVMKVIRRARLPNALTPIFMSSAEGKFMTSEIRLGSRGDSYYEYLKQYLQTGSVETVYRDMYDDSMQAIHENLIATSNKRKLIHTVEIHPRRLAHNNQMSWVRTLKQDHLVCFLGGSLMLGATTAGAHTRPVSVPPRIEELSPVGRRDWTTGVGLIETCVDTYRTASGLSPEIVHFRESIETGSDWFIKDAKPPGELPVYDARYILRPETIESLFLAWRLTGNPKYRTYGWDIFQAIETHCRVPSGGYASVLNVEQVPVTWEDKMETFLMSETLKYLYLLFSDNTVLPLDQYVFNTEAHPLPIFSPTAVRSGFNF","length":591,"molWeight":66386,"crc64":"5E4E8F8ED1A80648","md5":"D47F8565E53A4221838D47723347F0C3"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":1,"Region":1,"Active site":4,"Binding site":1,"Disulfide bond":1},"uniParcId":"UPI00297A30DD"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AAD6S3G8","uniProtkbId":"A0AAD6S3G8_9AGAR","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2024-05-29","entryVersion":9,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Mycena alexandri","taxonId":1745969,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7019847.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Agaricomycotina","Agaricomycetes","Agaricomycetidae","Agaricales","Marasmiineae","Mycenaceae","Mycena"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012780"}],"value":"glucan endo-1,3-beta-D-glucosidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012780"}],"value":"3.2.1.39"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043078"}],"value":"Endo-1,3-beta-glucanase btgC"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00042373"}],"value":"Laminarinase btgC"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7019847.1"}],"value":"C8F04DRAFT_1275834"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00037649"}],"value":"Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation. Active on laminarin and lichenan"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.","ecNumber":"3.2.1.39","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000382"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004401"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004401"}],"value":"Single-pass type II membrane protein","id":"SL-9906"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008773"}],"value":"Belongs to the glycosyl hydrolase 17 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7019847.1"}],"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":101,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":461,"modifier":"EXACT"}},"description":"Glycoside hydrolase family 17","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF29664"}]},{"type":"Region","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023180"}],"id":"KW-0325","category":"PTM","name":"Glycoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7019847.1"}],"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:0000256","source":"ARBA","id":"ARBA00023326"}],"id":"KW-0624","category":"Biological process","name":"Polysaccharide degradation"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001218188"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022968"}],"id":"KW-0735","category":"Domain","name":"Signal-anchor"},{"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-72QEQ62960K9F","citationType":"submission","authoringGroup":["Lawrence Berkeley National Laboratory"],"authors":["Harder C.B.","Miyauchi S.","Viragh M.","Kuo A.","Thoen E.","Andreopoulos B.","Lu D.","Skrede I.","Drula E.","Henrissat B.","Morin E.","Kohler A.","Barry K.","LaButti K.","Morin E.","Salamov A.","Lipzen A.","Mereny Z.","Hegedus B.","Baldrian P.","Stursova M.","Weitz H.","Taylor A.","Grigoriev I.V.","Nagy L.G.","Martin F.","Kauserud H."],"title":"Massive genome expansion in bonnet fungi (Mycena s.s.) driven by repeated elements and novel gene families across ecological guilds.","publicationDate":"MAR-2023","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7019847.1"}],"value":"CBHHK200","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ7019847.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JARJCM010000282","properties":[{"key":"ProteinId","value":"KAJ7019847.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0AAD6S3G8","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001218188","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0009986","properties":[{"key":"GoTerm","value":"C:cell surface"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009277","properties":[{"key":"GoTerm","value":"C:fungal-type cell wall"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0042973","properties":[{"key":"GoTerm","value":"F:glucan endo-1,3-beta-D-glucosidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0071555","properties":[{"key":"GoTerm","value":"P:cell wall organization"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"3.20.20.80","properties":[{"key":"EntryName","value":"Glycosidases"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR050732","properties":[{"key":"EntryName","value":"Beta-glucan_modifiers"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR000490","properties":[{"key":"EntryName","value":"Glyco_hydro_17"}]},{"database":"PANTHER","id":"PTHR16631","properties":[{"key":"EntryName","value":"GLUCAN 1,3-BETA-GLUCOSIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR16631:SF17","properties":[{"key":"EntryName","value":"GLUCAN ENDO-1,3-BETA-GLUCOSIDASE BTGC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF29664","properties":[{"key":"EntryName","value":"BtgE-BtgC_glyc-hydro"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MALWRVIPPSRLFPLSLPLIMASYRTGRPPSRSQTDLQQYYDAPYDSDRDGGAQAIPMQQKYAYGYRAPAAADSQTNFGVGRGGRDPKIPRRNSAWLEKNILSLLALTVLIAAGVVVGVFVAQHKFSSSSSASTASTSASSKNSDSPPDPSVFTKNPALVQSFYGIAYTPEGSQLPVCGNSLDDIITDIQLLSQLTTRIRLYGADCNQTELVLEAIKQTQVNLTIWVGNYAIATDGGTAYARQRDAIGAAIKKYGVGSVGGVTVGNEFVLDYLDAHDAIDPNGAVGDAGAAILIEDIRDTRAMMSGLGLGNVSIGTSDAGSYFNTEVLEAVDYGMANVHPWFANTRIEDAARWTADFFASTDLAAAAALSNAPQMYIAETGWPTNSSTAAASSNGAATASEANLQVRFALSSFPFADRVGQIFLDTFVCQANANGTKYFFFEYFDEEWKNIQYGGVEGYWGLFYQNRTLKGVTIPTCD","length":478,"molWeight":51328,"crc64":"1E3343190340A8C6","md5":"80BBBBB860EEBEF9374D5AB3C3B0210E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":1,"Domain":1,"Region":1,"Compositional bias":1},"uniParcId":"UPI002975E1B7"}}]}