ID   R4J0R3_9EMBE            Unreviewed;       516 AA.
AC   R4J0R3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   01-OCT-2014, entry version 10.
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   Testudines + Archosauria group; Archosauria; Dinosauria; Saurischia;
OC   Theropoda; Coelurosauria; Aves; Neognathae; Passeriformes;
OC   Passeroidea; 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   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000256|RuleBase:RU000369}.
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}.
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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:0070469; C:respiratory chain; IEA:UniProtKB-KW.
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   Gene3D; 1.20.210.10; -; 1.
DR   InterPro; IPR000883; COX1.
DR   InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR   InterPro; IPR023616; 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};
KW   Electron transport {ECO:0000256|RuleBase:RU000369};
KW   Heme {ECO:0000256|RuleBase:RU000369};
KW   Iron {ECO:0000256|RuleBase:RU000369};
KW   Membrane {ECO:0000256|RuleBase:RU000369};
KW   Metal-binding {ECO:0000256|RuleBase:RU000369};
KW   Mitochondrion {ECO:0000256|RuleBase:RU000369,
KW   ECO:0000313|EMBL:AGG10781.1};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000369};
KW   Respiratory chain {ECO:0000256|RuleBase:RU000369};
KW   Transmembrane {ECO:0000256|RuleBase:RU000369};
KW   Transport {ECO:0000256|RuleBase:RU000369}.
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
//