ID R4J0R3_9EMBE Unreviewed; 516 AA. AC R4J0R3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. 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; OC Fringillidae; 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: RT 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- CC 3 form the functional core of the enzyme complex. CO I is the CC catalytic subunit of the enzyme. Electrons originating in CC cytochrome c are transferred via the copper A center of subunit 2 CC and heme A of subunit 1 to the bimetallic center formed by heme A3 CC and copper B. {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. {ECO:0000256|RuleBase:RU000369, CC ECO:0000256|SAAS:SAAS00711152}. CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00748058}. 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:0005506; F:iron ion binding; IEA:InterPro. 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; 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:SAAS00747927}; 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, KW ECO:0000256|SAAS:SAAS00711163, 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, KW ECO:0000256|SAAS:SAAS00711099}. FT TRANSMEM 20 38 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 58 84 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 105 127 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 147 172 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 184 211 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 244 264 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 271 292 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 304 328 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 340 360 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 380 401 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 413 431 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 451 474 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 7 513 COX1. {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 //