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
//