ID   A0A1U9G5H2_CHLPG        Unreviewed;       522 AA.
AC   A0A1U9G5H2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   05-JUL-2017, entry version 2.
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:AOR40688.1};
OS   Chlorocebus pygerythrus (Vervet monkey) (Cercopithecus pygerythrus).
OG   Mitochondrion {ECO:0000313|EMBL:AOR40688.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60710 {ECO:0000313|EMBL:AOR40688.1};
RN   [1] {ECO:0000313|EMBL:AOR40688.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C8 {ECO:0000313|EMBL:AOR40688.1};
RA   Dolotovskaya S., Torroba Bordallo J., Haus T., Zinner D., Roos C.;
RT   "Mitogenomic Phylogeny of African Savanna Monkeys (Chlorocebus).";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KU682698; AOR40688.1; -; Genomic_DNA.
DR   UniPathway; UPA00705; -.
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:AOR40688.1};
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     18     37       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     57     83       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    104    126       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    146    171       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    183    210       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    243    261       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    268    291       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    303    325       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    337    359       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    379    400       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    412    430       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    450    473       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    512       COX1. {ECO:0000259|PROSITE:PS50855}.
SQ   SEQUENCE   522 AA;  57901 MW;  A9AA26DC9863593C CRC64;
     MFINRWLFST NHKDIGTLYL LFGAWAGITG TALSLLIRAE LGQPGSLLGS DHIYNVIVTA
     HAFVMIFFMV MPIMIGGFGN WLVPLMIGAP DMAFPRLNNM SFWLLPPSFL LLMASTMIEA
     GAGTGWTVYP PLAGNLSHPG ASVDLVIFSL HLAGISSILG AINFITTIIN MKPPAMSQYQ
     TPLFVWSVLI TAILLLLSLP VLAAGITMLL TDRNLNTTFF DPTGGGDPIL YQHLFWFFGH
     PEVYILILPG FGMISHIVTY YSGKKEPFGY MGMTWAMMSI GFLGFIVWAH HMFTVGMDVD
     TRAYFTSATM IIAIPTGVKV FSWLATLHGG NIKWSAAMLW ALGFIFLFTM GGLTGIILAN
     SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM GGFIHWFPLF SGYTLDQTYA KAHFIIMFVG
     VNLTFFPQHF LGLSGMPRRY SDYPDAYTTW NILSSIGSFI SLVAVILMIY MIWEAFASKR
     KVSMTEQSPT NLEWLNGCPP PYHTFEEPAY IKLNEKGGSR TP
//