ID   A0A343CWY9_ORYCU        Unreviewed;       518 AA.
AC   A0A343CWY9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   05-DEC-2018, 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=COI {ECO:0000313|EMBL:ARO89801.1};
OS   Oryzias curvinotus (Hynann ricefish) (Aplocheilus curvinotus).
OG   Mitochondrion {ECO:0000313|EMBL:ARO89801.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae;
OC   Oryziinae; Oryzias.
OX   NCBI_TaxID=104658 {ECO:0000313|EMBL:ARO89801.1};
RN   [1] {ECO:0000313|EMBL:ARO89801.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wang Z., Long S., Liao J., Huang C., Zhang H., Liu L., Guo Y.;
RT   "Complete mitogenome of Hainan medaka Oryzias curvinotus (Teleostei:
RT   Beloniformes) and transcriptional differences between male and female
RT   liver.";
RL   Mitochondrial DNA Part B Resour 2:157-158(2017).
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:
CC       Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4
CC         [Fe(III)cytochrome c] + 2 H2O; Xref=Rhea:RHEA:11436,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, Rhea:RHEA-COMP:10350,
CC         Rhea:RHEA-COMP:14399; EC=1.9.3.1;
CC         Evidence={ECO:0000256|RuleBase:RU000369,
CC         ECO:0000256|SAAS:SAAS00711152};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00887552}.
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; KY364884; ARO89801.1; -; Genomic_DNA.
DR   UniPathway; UPA00705; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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:SAAS00887236};
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:ARO89801.1};
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     15     37       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     57     83       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    104    128       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    148    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    326       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    338    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    511       COX1. {ECO:0000259|PROSITE:PS50855}.
SQ   SEQUENCE   518 AA;  57284 MW;  75819676AA76567A CRC64;
     MAITRWFFST NHKDIGTLYL IFGAWAGMVG TALSLLIRAE LSQPGSLLGD DQIYNVIVTA
     HAFVMIFFMV MPIMIGGFGN WLIPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSGVEA
     GAGTGWTVYP PLSGNLAHAG ASVDLTIFSL HLAGISSILG AINFITTIIN MKPPAISQYQ
     TPLFVWAVLI TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH
     PEVYILILPG FGMISHIVAY YSGKKEPFGY MGMVWAMMAI GLLGFIVWAH HMFTVGMDVD
     TRAYFTSATM IIAIPTGVKV FSWLATLHGG SIKWETPLLW ALGFIFLFTV GGLTGIVLAN
     SSLDIMLHDT YYVVAHFHYV LSMGAVFAIM GAFVHWFPLF SGYTLHNTWT KIHFGVMFVG
     VNLTFFPQHF LGLAGMPRRY SDYPDAYTLW NTISSLGSLI SLIAVIMFLF IIWEAFAAKR
     EVLSVELTAT NVEWLHGCPP PYHTFEEPAF VQIQQSKF
//