{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"H2BGB9","uniProtkbId":"H2BGB9_9BASI","entryAudit":{"firstPublicDate":"2012-03-21","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2012-03-21","entryVersion":34,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Dasyspora winteri","taxonId":1006463,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AED98889.1"}],"lineage":["Eukaryota","Fungi","Dikarya","Basidiomycota","Pucciniomycotina","Pucciniomycetes","Pucciniales","Sphaerophragmiaceae","Dasyspora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015944"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003375"}],"value":"Cytochrome c oxidase subunit 3"}},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AED98889.1"}],"value":"CO3"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003375"}],"value":"Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix"}],"commentType":"FUNCTION"},{"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:0000256","source":"ARBA","id":"ARBA00010581"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003375"}],"value":"Belongs to the cytochrome c oxidase subunit 3 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":89,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"Heme-copper oxidase subunit III family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50253"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AED98889.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AED98889.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AED98889.1"}],"geneEncodingType":"Mitochondrion"}],"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:0000256","source":"RuleBase","id":"RU003375"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AED98889.1"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003375"}],"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":"22223173","citationType":"journal article","authors":["Beenken L.","Zoller S.","Berndt R."],"citationCrossReferences":[{"database":"PubMed","id":"22223173"},{"database":"DOI","id":"10.3852/11-068"}],"title":"Rust fungi on Annonaceae II: the genus Dasyspora Berk. & M.A. Curtis.","publicationDate":"2012","journal":"Mycologia","firstPage":"659","lastPage":"681","volume":"104"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AED98889.1"}],"value":"37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AED98889.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JF263524","properties":[{"key":"ProteinId","value":"AED98889.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"H2BGB9","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0016020","properties":[{"key":"GoTerm","value":"C:membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005739","properties":[{"key":"GoTerm","value":"C:mitochondrion"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004129","properties":[{"key":"GoTerm","value":"F:cytochrome-c oxidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006123","properties":[{"key":"GoTerm","value":"P:mitochondrial electron transport, cytochrome c to oxygen"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01665","properties":[{"key":"EntryName","value":"Cyt_c_Oxidase_III"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.120.80","properties":[{"key":"EntryName","value":"Cytochrome c oxidase, subunit III, four-helix bundle"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR024791","properties":[{"key":"EntryName","value":"Cyt_c/ubiquinol_Oxase_su3"}]},{"database":"InterPro","id":"IPR033945","properties":[{"key":"EntryName","value":"Cyt_c_oxase_su3_dom"}]},{"database":"InterPro","id":"IPR000298","properties":[{"key":"EntryName","value":"Cyt_c_oxidase-like_su3"}]},{"database":"InterPro","id":"IPR035973","properties":[{"key":"EntryName","value":"Cyt_c_oxidase_su3-like_sf"}]},{"database":"InterPro","id":"IPR013833","properties":[{"key":"EntryName","value":"Cyt_c_oxidase_su3_a-hlx"}]},{"database":"PANTHER","id":"PTHR11403:SF7","properties":[{"key":"EntryName","value":"CYTOCHROME C OXIDASE SUBUNIT 3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11403","properties":[{"key":"EntryName","value":"CYTOCHROME C OXIDASE SUBUNIT III"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00510","properties":[{"key":"EntryName","value":"COX3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81452","properties":[{"key":"EntryName","value":"Cytochrome c oxidase subunit III-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50253","properties":[{"key":"EntryName","value":"COX3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"YGVALGFISVVGVISLWFRDVSAEGALGGYHTFDVQRSLNIGVVLFIVSEIFFFVSIFWAYFHSALSPTVELGSQWPAPGVEPLNAFDIPLLNTILLLTSASSLTYAHHAIINGNRKSCLIGFLVTLALAVTFTGFQALEYIEAPFTISDGAFGSTFFFSTGFHGIHVIIGTLFLIVALARIISYQLTDHHHLGFEAAALYWHFVD","length":206,"molWeight":22538,"crc64":"39BF1519410F2140","md5":"50F9BD0618B71B2F6E542B55EBE2E469"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":5,"Domain":1,"Non-terminal residue":2},"uniParcId":"UPI000249574A"}}]}