{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A140GZI0","uniProtkbId":"A0A140GZI0_9MUSC","entryAudit":{"firstPublicDate":"2016-05-11","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-05-11","entryVersion":35,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Anastrepha grandis","commonName":"South American cucurbit fruit fly","taxonId":87114,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN87403.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Allotriocarida","Hexapoda","Insecta","Pterygota","Neoptera","Eumetabola","Endopterygota","Aparaglossata","Panorpida","Diptera","Brachycera","Muscomorpha","Tephritoidea","Tephritidae","Anastrepha"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015947"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Cytochrome c oxidase subunit 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"7.1.1.9"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN87403.1"}],"value":"COI"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"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":"CATALYTIC ACTIVITY","reaction":{"name":"4 Fe(II)-[cytochrome c] + O2 + 8 H(+)(in) = 4 Fe(III)-[cytochrome c] + 2 H2O + 4 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11436"},{"database":"Rhea","id":"RHEA-COMP:10350"},{"database":"Rhea","id":"RHEA-COMP:14399"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:29033"},{"database":"ChEBI","id":"CHEBI:29034"}],"ecNumber":"7.1.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049512"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:11437"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049512"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001971"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004673"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Energy metabolism; oxidative phosphorylation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011164"}],"value":"Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of a catalytic core of 3 subunits and several supernumerary subunits. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009578"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Belongs to the heme-copper respiratory oxidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"Cytochrome oxidase subunit I profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50855"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN87403.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN87403.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN87403.1"}],"geneEncodingType":"Mitochondrion"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0186","category":"Ligand","name":"Copper"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"},{"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":"RuleBase","id":"RU000369"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022792"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0999","category":"Cellular component","name":"Mitochondrion inner membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022660"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"},{"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"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"27126185","citationType":"journal article","authors":["Scally M.","Into F.","Thomas D.B.","Ruiz-Arce R.","Barr N.B.","Schuenzel E.L."],"citationCrossReferences":[{"database":"PubMed","id":"27126185"}],"title":"Resolution of inter and intra-species relationships of the West Indian fruit fly Anastrepha obliqua.","publicationDate":"2016","journal":"Mol. Phylogenet. Evol.","firstPage":"286","lastPage":"293","volume":"101"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN87402.1"}],"value":"X101026-002","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN87403.1"}],"value":"X101026-004","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AMN87403.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KT594077","properties":[{"key":"ProteinId","value":"AMN87402.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"KT594078","properties":[{"key":"ProteinId","value":"AMN87403.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A140GZI0","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00705","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0005743","properties":[{"key":"GoTerm","value":"C:mitochondrial inner membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004129","properties":[{"key":"GoTerm","value":"F:cytochrome-c oxidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0015990","properties":[{"key":"GoTerm","value":"P:electron transport coupled proton transport"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006123","properties":[{"key":"GoTerm","value":"P:mitochondrial electron transport, cytochrome c to oxygen"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"1.20.210.10","properties":[{"key":"EntryName","value":"Cytochrome c oxidase-like, subunit I domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023616","properties":[{"key":"EntryName","value":"Cyt_c_oxase-like_su1_dom"}]},{"database":"InterPro","id":"IPR036927","properties":[{"key":"EntryName","value":"Cyt_c_oxase-like_su1_sf"}]},{"database":"InterPro","id":"IPR000883","properties":[{"key":"EntryName","value":"Cyt_C_Oxase_1"}]},{"database":"PANTHER","id":"PTHR10422","properties":[{"key":"EntryName","value":"CYTOCHROME C OXIDASE SUBUNIT 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10422:SF18","properties":[{"key":"EntryName","value":"CYTOCHROME C OXIDASE SUBUNIT 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00115","properties":[{"key":"EntryName","value":"COX1"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01165","properties":[{"key":"EntryName","value":"CYCOXIDASEI"}]},{"database":"SUPFAM","id":"SSF81442","properties":[{"key":"EntryName","value":"Cytochrome c oxidase subunit I-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50855","properties":[{"key":"EntryName","value":"COX1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"SQQWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRTELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSLIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSAGMTFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGM","length":271,"molWeight":29402,"crc64":"7F8BB210602825B5","md5":"02CC87890576DF3E896B091EDDAC060D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":6,"Domain":1,"Non-terminal residue":2},"uniParcId":"UPI00078E9D6D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6C0NAA9","uniProtkbId":"A0A6C0NAA9_9MUSC","entryAudit":{"firstPublicDate":"2020-06-17","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2020-06-17","entryVersion":21,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Anastrepha grandis","commonName":"South American cucurbit fruit fly","taxonId":87114,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QHW07644.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Allotriocarida","Hexapoda","Insecta","Pterygota","Neoptera","Eumetabola","Endopterygota","Aparaglossata","Panorpida","Diptera","Brachycera","Muscomorpha","Tephritoidea","Tephritidae","Anastrepha"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015947"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Cytochrome c oxidase subunit 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"7.1.1.9"}]},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QHW07644.1"}],"value":"COI"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"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":"CATALYTIC ACTIVITY","reaction":{"name":"4 Fe(II)-[cytochrome c] + O2 + 8 H(+)(in) = 4 Fe(III)-[cytochrome c] + 2 H2O + 4 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11436"},{"database":"Rhea","id":"RHEA-COMP:10350"},{"database":"Rhea","id":"RHEA-COMP:14399"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:29033"},{"database":"ChEBI","id":"CHEBI:29034"}],"ecNumber":"7.1.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049512"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:11437"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049512"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001971"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004673"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Energy metabolism; oxidative phosphorylation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011164"}],"value":"Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of a catalytic core of 3 subunits and several supernumerary subunits. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009578"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"value":"Belongs to the heme-copper respiratory oxidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"Cytochrome oxidase subunit I profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50855"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QHW07644.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QHW07644.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QHW07644.1"}],"geneEncodingType":"Mitochondrion"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0186","category":"Ligand","name":"Copper"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"},{"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":"RuleBase","id":"RU000369"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022792"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0999","category":"Cellular component","name":"Mitochondrion inner membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022660"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"},{"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"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000369"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-912258NBH0BCA","citationType":"submission","authors":["Bartolini I.M.","Rivera J.","Nolazco N.","Olortegui A."],"publicationDate":"SEP-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QHW07644.1"}]},{"referenceNumber":2,"citation":{"id":"32004351","citationType":"journal article","authors":["Bartolini I.","Rivera J.","Nolazco N.","Olortegui A."],"citationCrossReferences":[{"database":"PubMed","id":"32004351"}],"title":"Towards the implementation of a DNA barcode library for the identification of Peruvian species of Anastrepha (Diptera: Tephritidae).","publicationDate":"2020","journal":"PLoS ONE","firstPage":"0","lastPage":"e0228136","volume":"15"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QHW07644.1"}]},{"referenceNumber":3,"citation":{"id":"CI-T2G9IANLKB8S","citationType":"submission","authors":["Moore M.R.","Steck G.J.","Rodriguez E.J.","Norrbom A.L.","Ruiz acre R.","Sutton B.D.","Srivastava P.","Todd T.N.","Roberts C.G.","Troya H.","Vilatuna J.E.","Donoso D.A.","Wiegmann B.M.","Cassel B.","Soghigian J.","Xuan J.L.I.","Muller A.","Gangadin A.","Nolazco N.","Rodriguez clavijo P.A.","Arevalo penaranda E.","Drovetsky S.","Quisberth ramos E.","Lagrava sanchez J.O.S.E.","Colque F.","Savaris M.","Lampert S.","Martinez J.","Canal N.A.","Keil C.","Padilla A.","Tigrero J.O.","Branham M.A."],"title":"COI Barcode Library for the genus Anastrepha Schiner (Diptera: Tephritidae).","publicationDate":"AUG-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UED14414.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"MN454418","properties":[{"key":"ProteinId","value":"QHW07644.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"MN454484","properties":[{"key":"ProteinId","value":"QHW07710.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"MN454486","properties":[{"key":"ProteinId","value":"QHW07712.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"MT884176","properties":[{"key":"ProteinId","value":"UED14414.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"MT884231","properties":[{"key":"ProteinId","value":"UED14469.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A6C0NAA9","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00705","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0005743","properties":[{"key":"GoTerm","value":"C:mitochondrial inner membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004129","properties":[{"key":"GoTerm","value":"F:cytochrome-c oxidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0015990","properties":[{"key":"GoTerm","value":"P:electron transport coupled proton transport"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006123","properties":[{"key":"GoTerm","value":"P:mitochondrial electron transport, cytochrome c to oxygen"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"1.20.210.10","properties":[{"key":"EntryName","value":"Cytochrome c oxidase-like, subunit I domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023616","properties":[{"key":"EntryName","value":"Cyt_c_oxase-like_su1_dom"}]},{"database":"InterPro","id":"IPR036927","properties":[{"key":"EntryName","value":"Cyt_c_oxase-like_su1_sf"}]},{"database":"InterPro","id":"IPR000883","properties":[{"key":"EntryName","value":"Cyt_C_Oxase_1"}]},{"database":"PANTHER","id":"PTHR10422","properties":[{"key":"EntryName","value":"CYTOCHROME C OXIDASE SUBUNIT 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10422:SF18","properties":[{"key":"EntryName","value":"CYTOCHROME C OXIDASE SUBUNIT 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00115","properties":[{"key":"EntryName","value":"COX1"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01165","properties":[{"key":"EntryName","value":"CYCOXIDASEI"}]},{"database":"SUPFAM","id":"SSF81442","properties":[{"key":"EntryName","value":"Cytochrome c oxidase subunit I-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50855","properties":[{"key":"EntryName","value":"COX1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"TLYFIFGAWAGMVGTSLSILIRTELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSLIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSAGMTFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF","length":219,"molWeight":23522,"crc64":"CBDAC5AAFB880E26","md5":"1C1BA71CA847002C157A1A1463D30D87"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":4,"Domain":1,"Non-terminal residue":2},"uniParcId":"UPI001397CB16"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2L0VXY7","uniProtkbId":"A0A2L0VXY7_9MUSC","entryAudit":{"firstPublicDate":"2018-04-25","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-04-25","entryVersion":28,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Anastrepha grandis","commonName":"South American cucurbit fruit fly","taxonId":87114,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AVA16834.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Allotriocarida","Hexapoda","Insecta","Pterygota","Neoptera","Eumetabola","Endopterygota","Aparaglossata","Panorpida","Diptera","Brachycera","Muscomorpha","Tephritoidea","Tephritidae","Anastrepha"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015946"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000457"}],"value":"Cytochrome c oxidase subunit 2"}},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AVA16834.1"}],"value":"COII"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000457"}],"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":"CATALYTIC ACTIVITY","reaction":{"name":"4 Fe(II)-[cytochrome c] + O2 + 8 H(+)(in) = 4 Fe(III)-[cytochrome c] + 2 H2O + 4 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11436"},{"database":"Rhea","id":"RHEA-COMP:10350"},{"database":"Rhea","id":"RHEA-COMP:14399"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:29033"},{"database":"ChEBI","id":"CHEBI:29034"}],"ecNumber":"7.1.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049512"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:11437"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049512"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Cu cation","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000457"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:23378"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000457"}],"value":"Binds a copper A center."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000457"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000457"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007866"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000457"}],"value":"Belongs to the cytochrome c oxidase subunit 2 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"Cytochrome oxidase subunit II transmembrane region profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50999"}]},{"type":"Domain","location":{"start":{"value":83,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"Cytochrome oxidase subunit II copper A binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50857"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AVA16834.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AVA16834.1"}]}],"geneLocations":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AVA16834.1"}],"geneEncodingType":"Mitochondrion"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023008"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000457"}],"id":"KW-0186","category":"Ligand","name":"Copper"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000457"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000457"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000457"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000457"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022792"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000457"}],"id":"KW-0999","category":"Cellular component","name":"Mitochondrion inner membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022660"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000457"}],"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"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":"RU000457"}],"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"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000457"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"29391551","citationType":"journal article","authors":["Jiang F.","Liang L.","Li Z.","Yu Y.","Wang J.","Wu Y.","Zhu S."],"citationCrossReferences":[{"database":"PubMed","id":"29391551"},{"database":"DOI","id":"10.1038/s41598-018-20555-2"}],"title":"A conserved motif within cox 2 allows broad detection of economically important fruit flies (Diptera: Tephritidae).","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"2077","lastPage":"2077","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AVA16834.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"MG020786","properties":[{"key":"ProteinId","value":"AVA16834.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A2L0VXY7","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005743","properties":[{"key":"GoTerm","value":"C:mitochondrial inner membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005507","properties":[{"key":"GoTerm","value":"F:copper ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004129","properties":[{"key":"GoTerm","value":"F:cytochrome-c oxidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0042773","properties":[{"key":"GoTerm","value":"P:ATP synthesis coupled electron transport"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd13912","properties":[{"key":"EntryName","value":"CcO_II_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.287.90","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.420","properties":[{"key":"EntryName","value":"Cupredoxins - blue copper proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR045187","properties":[{"key":"EntryName","value":"CcO_II"}]},{"database":"InterPro","id":"IPR002429","properties":[{"key":"EntryName","value":"CcO_II-like_C"}]},{"database":"InterPro","id":"IPR034210","properties":[{"key":"EntryName","value":"CcO_II_C"}]},{"database":"InterPro","id":"IPR008972","properties":[{"key":"EntryName","value":"Cupredoxin"}]},{"database":"InterPro","id":"IPR011759","properties":[{"key":"EntryName","value":"Cyt_c_oxidase_su2_TM_dom"}]},{"database":"InterPro","id":"IPR036257","properties":[{"key":"EntryName","value":"Cyt_c_oxidase_su2_TM_sf"}]},{"database":"PANTHER","id":"PTHR22888:SF9","properties":[{"key":"EntryName","value":"CYTOCHROME C OXIDASE SUBUNIT 2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR22888","properties":[{"key":"EntryName","value":"CYTOCHROME C OXIDASE, SUBUNIT II"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00116","properties":[{"key":"EntryName","value":"COX2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02790","properties":[{"key":"EntryName","value":"COX2_TM"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01166","properties":[{"key":"EntryName","value":"CYCOXIDASEII"}]},{"database":"SUPFAM","id":"SSF49503","properties":[{"key":"EntryName","value":"Cupredoxins"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81464","properties":[{"key":"EntryName","value":"Cytochrome c oxidase subunit II-like, transmembrane region"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50857","properties":[{"key":"EntryName","value":"COX2_CUA"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50999","properties":[{"key":"EntryName","value":"COX2_TM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"QDSASPLMEQLAFFHDHTLMILVMITTLVGYLMFMLFFNSYTNRNLLHGQTIEVIWTILPAIILLFIAFPSLRLLYLIDEINEPSVTLKAIGHQWYWSYEYSDFMNVEFDSYMIPTNELTNSSFRLLDVDNRVILPMNSQIRILVTAADVIHSWTVPALGVKVDGTPGRLNQINFLMNRPGLFYG","length":185,"molWeight":21341,"crc64":"5BA95C4D3C7C106D","md5":"ECFAE1DCB13FD5395A759F785CE3C9B5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":2,"Domain":2,"Non-terminal residue":2},"uniParcId":"UPI000CE2B4AA"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q06W10","uniProtkbId":"Q06W10_9MUSC","entryAudit":{"firstPublicDate":"2006-10-31","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2006-10-31","entryVersion":62,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Anastrepha grandis","commonName":"South American cucurbit fruit fly","taxonId":87114,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ABF50946.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Allotriocarida","Hexapoda","Insecta","Pterygota","Neoptera","Eumetabola","Endopterygota","Aparaglossata","Panorpida","Diptera","Brachycera","Muscomorpha","Tephritoidea","Tephritidae","Anastrepha"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ABF50946.1"}],"value":"Male doublesex"}}]},"comments":[{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00070"}],"value":"Nucleus","id":"SL-0191"}}]}],"features":[{"type":"Domain","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"DM","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50809"}]},{"type":"DNA binding","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"DM","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00070"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":350,"modifier":"EXACT"},"end":{"value":396,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Coiled coil","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Compositional bias","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"Gly residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":396,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00070"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00070"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00070"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00070"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-ED0RQJ936UF97","citationType":"submission","authors":["Ruiz M.F.","Eirin-Lopez J.M.","Stefani R.N.","Perondini A.L.P.","Selivon D.","Sanchez L."],"title":"The molecular evolution of gene doublesex in Anastrepha fruit flies.","publicationDate":"APR-2006","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ABF50946.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"DQ494337","properties":[{"key":"ProteinId","value":"ABF50946.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"Q06W10","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000981","properties":[{"key":"GoTerm","value":"F:DNA-binding transcription factor activity, RNA polymerase II-specific"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000978","properties":[{"key":"GoTerm","value":"F:RNA polymerase II cis-regulatory region sequence-specific DNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0007548","properties":[{"key":"GoTerm","value":"P:sex differentiation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"FunFam","id":"4.10.1040.10:FF:000001","properties":[{"key":"EntryName","value":"doublesex- and mab-3-related transcription factor 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"4.10.1040.10","properties":[{"key":"EntryName","value":"DM DNA-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.10","properties":[{"key":"EntryName","value":"DNA helicase RuvA subunit, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001275","properties":[{"key":"EntryName","value":"DM_DNA-bd"}]},{"database":"InterPro","id":"IPR036407","properties":[{"key":"EntryName","value":"DM_DNA-bd_sf"}]},{"database":"InterPro","id":"IPR026607","properties":[{"key":"EntryName","value":"DMRT"}]},{"database":"InterPro","id":"IPR014932","properties":[{"key":"EntryName","value":"DSX_dimer"}]},{"database":"PANTHER","id":"PTHR12322","properties":[{"key":"EntryName","value":"DOUBLESEX AND MAB-3 RELATED TRANSCRIPTION FACTOR DMRT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12322:SF100","properties":[{"key":"EntryName","value":"PROTEIN DOUBLESEX"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00751","properties":[{"key":"EntryName","value":"DM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08828","properties":[{"key":"EntryName","value":"DSX_dimer"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00301","properties":[{"key":"EntryName","value":"DM"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01143","properties":[{"key":"EntryName","value":"DSX_dimer"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF82927","properties":[{"key":"EntryName","value":"Cysteine-rich DNA binding domain, (DM domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS40000","properties":[{"key":"EntryName","value":"DM_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50809","properties":[{"key":"EntryName","value":"DM_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVSEDNWNSDTMSDSDMLDSKADVCGGASSSSGSSISPRTPPNCARCRNHGLKITLKGHKRYCKFRYCTCEKCRLTADRQRVMALQTALRRAQAQDEQRVLQMHEVPPVVHAPTALLNHHHLHHHHHLNQNHHATAAAAAAAAAAHHHISTAIRSPPQTEHGSGGGGGGMVGGTVPTITSVPVSAPPPEHHMTTVPTPAQSLEGSSDTSSPSPSSTSGAVLPISVVGRKPPLHPNGVNIPLAQDVFLEHCQKLLEKFRYPWEMMPLMYVILKDAGADIEEASRRIEEAKRIVNQTISLQLMDRQLYYNYYSSAALVNGPPTYLPYPLAFGTNGLLTSQFSHFTASIRPPSPELPALSRTPPSPSKLSRPASTLSETMSPVAATTSLKSSATAAAAT","length":396,"molWeight":42516,"crc64":"319393EB4475E465","md5":"01A41D087B5CC0B77FED785C5A553091"},"extraAttributes":{"countByCommentType":{"SUBCELLULAR LOCATION":1},"countByFeatureType":{"Domain":1,"DNA binding":1,"Region":3,"Coiled coil":1,"Compositional bias":7},"uniParcId":"UPI0000E2D009"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A9QDQ7","uniProtkbId":"A9QDQ7_9MUSC","entryAudit":{"firstPublicDate":"2008-02-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2008-02-05","entryVersion":23,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Anastrepha grandis","commonName":"South American cucurbit fruit fly","taxonId":87114,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ABW04170.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Allotriocarida","Hexapoda","Insecta","Pterygota","Neoptera","Eumetabola","Endopterygota","Aparaglossata","Panorpida","Diptera","Brachycera","Muscomorpha","Tephritoidea","Tephritidae","Anastrepha"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ABW04170.1"}],"value":"Transformer"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ABW04170.1"}],"value":"Tra"}}],"features":[{"type":"Region","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":263,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":307,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"references":[{"referenceNumber":1,"citation":{"id":"18043746","citationType":"journal article","authors":["Ruiz M.F.","Milano A.","Salvemini M.","Eirin-Lopez J.M.","Perondini A.L.","Selivon D.","Polito C.","Saccone G.","Sanchez L."],"citationCrossReferences":[{"database":"PubMed","id":"18043746"},{"database":"DOI","id":"10.1371/journal.pone.0001239"}],"title":"The gene transformer of anastrepha fruit flies (Diptera, tephritidae) and its evolution in insects.","publicationDate":"2007","journal":"PLoS ONE","firstPage":"e1239","lastPage":"e1239","volume":"2"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ABW04170.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"EU024503","properties":[{"key":"ProteinId","value":"ABW04170.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A9QDQ7","properties":[{"key":"Description","value":"-"}]}],"sequence":{"value":"MNIPKASTATRKIQIEQSIPTGSIRKGPYAIERSVDANEVVIKRRFGEGSKPLFQRDDIVVNPNSVINVADSHTEKHLISESKKRAKGVSNEYLKRSRSSTDSSSPEGYRKYSSRYNDCITSTNNSAAPRTKPLKSTNERKRTIRCDSPPPFNHRRRTPEKLPYFIDETRERDRLRRKYETKPKIPSTSPPLTSRSRHRRSRSKPRSRSHSREFEHRLKPANFRRSVSTDRYIGETSRRERGSRSEKTSSRYRHRSEDRSKNDRRQRHWRSPSRSPSRSRDRLTRSHKQSRHDERHKNCHSEHKGSSNDELAQRNLPPPQIITIPVPVPADFMNYTYPTWPTQWNPPMAHPVRYGPPAAYHIPTILPAAVMPPMRPPLPPYGPHPPPLRYGVRGFRLPPQYNASRPWRPNFRTKNT","length":416,"molWeight":48486,"crc64":"D7C6DEDB6175AD07","md5":"57A330E7C664A58A762689F8755D46BB"},"extraAttributes":{"countByFeatureType":{"Region":1,"Compositional bias":6},"uniParcId":"UPI0001608415"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"D6CHG5","uniProtkbId":"D6CHG5_9MUSC","entryAudit":{"firstPublicDate":"2010-07-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2010-07-13","entryVersion":35,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Anastrepha grandis","commonName":"South American cucurbit fruit fly","taxonId":87114,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"CBJ17285.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Allotriocarida","Hexapoda","Insecta","Pterygota","Neoptera","Eumetabola","Endopterygota","Aparaglossata","Panorpida","Diptera","Brachycera","Muscomorpha","Tephritoidea","Tephritidae","Anastrepha"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"CBJ17285.1"}],"value":"Transformer-2"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"CBJ17285.1"}],"value":"tra-2"}}],"features":[{"type":"Domain","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"RRM","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50102"}]},{"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":180,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00176"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-D8RB4M9TATGH0","citationType":"journal article","authors":["Sarno F.","Ruiz M.F.","Eirin-Lopez J.M.","Perondini A.L.","Selivon D.","Sanchez L."],"title":"The gene transformer-2 of Anastrepha fruit flies (Diptera, Tephritidae) and its evolution in insects.","publicationDate":"2010","journal":"BMC Evol. Biol.","firstPage":"140","lastPage":"140","volume":"10"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"CBJ17285.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"FN658612","properties":[{"key":"ProteinId","value":"CBJ17285.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"D6CHG5","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0003723","properties":[{"key":"GoTerm","value":"F:RNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd12363","properties":[{"key":"EntryName","value":"RRM_TRA2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.330","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR012677","properties":[{"key":"EntryName","value":"Nucleotide-bd_a/b_plait_sf"}]},{"database":"InterPro","id":"IPR035979","properties":[{"key":"EntryName","value":"RBD_domain_sf"}]},{"database":"InterPro","id":"IPR050441","properties":[{"key":"EntryName","value":"RBM"}]},{"database":"InterPro","id":"IPR000504","properties":[{"key":"EntryName","value":"RRM_dom"}]},{"database":"PANTHER","id":"PTHR48034","properties":[{"key":"EntryName","value":"TRANSFORMER-2 SEX-DETERMINING PROTEIN-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00076","properties":[{"key":"EntryName","value":"RRM_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00360","properties":[{"key":"EntryName","value":"RRM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54928","properties":[{"key":"EntryName","value":"RNA-binding domain, RBD"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50102","properties":[{"key":"EntryName","value":"RRM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSPRTRSRSISPRRSYSKSPARRSNGRRRHSREKVYNSRSRSASRHPPSPPPLPAGRAARYSDASKSSSTSLSPRHGRRVSRSRTRSPYDKRRANREKPVQNRCIGVFGLSVYTTQQKIRDIFSRFGPIERIQVVIDAQTGRSRGFCFIYYQDIADAKAAKDACSGMEIDDRRIRVDYSTTQRPHTPTPGVYMGRYTRRERDHDRYRDDYRSRRRSVTPYNNRNSYRGDRRRRYDRSRSRSYSPRRTRY","length":249,"molWeight":29409,"crc64":"69CD372E2D1B0D82","md5":"EA5D04A1DCBCF70A83011BF4A6B460DF"},"extraAttributes":{"countByFeatureType":{"Domain":1,"Region":2,"Compositional bias":6},"uniParcId":"UPI0001D280C3"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q06W19","uniProtkbId":"Q06W19_9MUSC","entryAudit":{"firstPublicDate":"2006-10-31","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2006-10-31","entryVersion":65,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Anastrepha grandis","commonName":"South American cucurbit fruit fly","taxonId":87114,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ABF50956.1"}],"lineage":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Altocrustacea","Allotriocarida","Hexapoda","Insecta","Pterygota","Neoptera","Eumetabola","Endopterygota","Aparaglossata","Panorpida","Diptera","Brachycera","Muscomorpha","Tephritoidea","Tephritidae","Anastrepha"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ABF50956.1"}],"value":"Female doublesex"}}]},"comments":[{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00070"}],"value":"Nucleus","id":"SL-0191"}}]}],"features":[{"type":"Domain","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"DM","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50809"}]},{"type":"DNA binding","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"DM","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00070"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"Gly residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00070"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00070"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00070"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00070"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-ED0RQJ936UF97","citationType":"submission","authors":["Ruiz M.F.","Eirin-Lopez J.M.","Stefani R.N.","Perondini A.L.P.","Selivon D.","Sanchez L."],"title":"The molecular evolution of gene doublesex in Anastrepha fruit flies.","publicationDate":"APR-2006","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ABF50956.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"DQ494328","properties":[{"key":"ProteinId","value":"ABF50956.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"Q06W19","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000981","properties":[{"key":"GoTerm","value":"F:DNA-binding transcription factor activity, RNA polymerase II-specific"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000978","properties":[{"key":"GoTerm","value":"F:RNA polymerase II cis-regulatory region sequence-specific DNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0007548","properties":[{"key":"GoTerm","value":"P:sex differentiation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"FunFam","id":"4.10.1040.10:FF:000001","properties":[{"key":"EntryName","value":"doublesex- and mab-3-related transcription factor 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"4.10.1040.10","properties":[{"key":"EntryName","value":"DM DNA-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.10","properties":[{"key":"EntryName","value":"DNA helicase RuvA subunit, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001275","properties":[{"key":"EntryName","value":"DM_DNA-bd"}]},{"database":"InterPro","id":"IPR036407","properties":[{"key":"EntryName","value":"DM_DNA-bd_sf"}]},{"database":"InterPro","id":"IPR026607","properties":[{"key":"EntryName","value":"DMRT"}]},{"database":"InterPro","id":"IPR014932","properties":[{"key":"EntryName","value":"DSX_dimer"}]},{"database":"PANTHER","id":"PTHR12322","properties":[{"key":"EntryName","value":"DOUBLESEX AND MAB-3 RELATED TRANSCRIPTION FACTOR DMRT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12322:SF100","properties":[{"key":"EntryName","value":"PROTEIN DOUBLESEX"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00751","properties":[{"key":"EntryName","value":"DM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08828","properties":[{"key":"EntryName","value":"DSX_dimer"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00301","properties":[{"key":"EntryName","value":"DM"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01143","properties":[{"key":"EntryName","value":"DSX_dimer"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF82927","properties":[{"key":"EntryName","value":"Cysteine-rich DNA binding domain, (DM domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS40000","properties":[{"key":"EntryName","value":"DM_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50809","properties":[{"key":"EntryName","value":"DM_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVSEDNWNSDTMSDSDMLDSKADVCGGASSSSGSSISPRTPPNCARCRNHGLKVTLKGHKRYCKFRYCTCEKCRLTADRQRVMALQTALRRAQAQDEQRVLQTHEVPPVVHAPTALLNHHHLHHHHHLNQNHHATAAAAAAAAAAHHHISTAIRSPPQTEHGSGGGGGGMVGGTVPTITSVPVSAPPPEHHMTTVPTPAQSLEGSSDTSSPSPSSTSGAVLPISVVGRKPPLHPNGVNIPLAQDVFLEHCQKLLEKFRYPWEMMPLMYVILKDAGADIEEASRRIEEGQHVVNEYSRQHNLNIYDGGELRSTTRQCG","length":317,"molWeight":34328,"crc64":"0B308C261DF827E7","md5":"86CF22E8D84D0DC3EB8DC98449B194B5"},"extraAttributes":{"countByCommentType":{"SUBCELLULAR LOCATION":1},"countByFeatureType":{"Domain":1,"DNA binding":1,"Region":2,"Compositional bias":6},"uniParcId":"UPI0000E2D001"}}]}