ID R4J0R3_9EMBE Unreviewed; 516 AA. AC R4J0R3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 11-DEC-2019, entry version 29. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369}; GN Name=COX1 {ECO:0000313|EMBL:AGG10781.1}; OS Emberiza pusilla. OG Mitochondrion {ECO:0000313|EMBL:AGG10781.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Fringillidae; OC Emberizinae; Emberizini; Emberiza. OX NCBI_TaxID=74588 {ECO:0000313|EMBL:AGG10781.1}; RN [1] {ECO:0000313|EMBL:AGG10781.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=23391161; DOI=10.3109/19401736.2013.763238; RA Pan T., Ren L., Zhu X., Yan L., Hu C., Chang Q., Zhang B.; RT "Mitochondrial genome of the Emberiza pusilla (Emberizidae: Emberiza)."; RL Mitochondrial DNA 24:382-384(2013). CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1-3 CC form the functional core of the enzyme complex. CO I is the catalytic CC subunit of the enzyme. Electrons originating in cytochrome c are CC transferred via the copper A center of subunit 2 and heme A of subunit CC 1 to the bimetallic center formed by heme A3 and copper B. CC {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c] CC + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA- CC COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.9.3.1; CC Evidence={ECO:0000256|RuleBase:RU000369, CC ECO:0000256|SAAS:SAAS01116628}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00939438}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000369}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000256|RuleBase:RU000369}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KC407232; AGG10781.1; -; Genomic_DNA. DR RefSeq; YP_008081050.1; NC_021408.1. DR GeneID; 15822590; -. DR CTD; 4512; -. DR UniPathway; UPA00705; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045277; C:respiratory chain complex IV; IEA:InterPro. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. DR CDD; cd01663; Cyt_c_Oxidase_I; 1. DR Gene3D; 1.20.210.10; -; 1. DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom. DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf. DR InterPro; IPR000883; Cyt_C_Oxase_1. DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR InterPro; IPR033944; Cyt_c_oxase_su1_dom. DR PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 1. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00939258}; KW Electron transport {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711094}; KW Heme {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711161}; KW Iron {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711183}; KW Membrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711163, KW ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711155}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711157, ECO:0000313|EMBL:AGG10781.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711097}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711106}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711093, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00711122, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711099}. FT TRANSMEM 20..38 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 58..84 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 105..127 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 147..172 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 184..211 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 244..264 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 271..292 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 304..328 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 340..360 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 380..401 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 413..431 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 451..474 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 7..513 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" SQ SEQUENCE 516 AA; 56879 MW; CCD9298BB959DC36 CRC64; MTFINRWLFS TNHKDIGTLY LIFGAWAGMV GTALSLLIRA ELGQPGALLG DDQVYNVVVT AHAFVMIFFM VMPIMIGGFG NWLVPLMIGA PDMAFPRMNN MSFWLLPPSF LLLLASSTVE AGVGTGWTVY PPLAGNLAHA GASVDLAIFS LHLAGISSIL GAINFITTAI NMKPPALSQY QTPLFVWSVL ITAVLLLLSL PVLAAGITML LTDRNLNTTF FDPAGGGDPV LYQHLFWFFG HPEVYILILP GFGIISHVVT YYAGKKEPFG YMGMVWAMLS IGFLGFIVWA HHMFTVGMDV DTRAYFTSAT MIIAIPTGIK VFSWLATLHG GTIKWDPPML WALGFIFLFT IGGLTGIILA NSSLDIALHD TYYVVAHFHY VLSMGAVFAI LAGFTHWFPL FTGYTLHSTW AKTHFGVMFV GVNLTFFPQH FLGLAGMPRR YSDYPDAYTL WNTISSVGSL ISLTAVIMLV FIIWEAFASK RKVLQPTLTS TNVEWIHGCP PPFHTFEEPP FVQVQE //