ID   E2DQN9_9CHON            Unreviewed;       218 AA.
AC   E2DQN9;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   01-OCT-2014, entry version 19.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369};
DE            EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369};
DE   Flags: Fragment {ECO:0000313|EMBL:ADK26838.1};
GN   Name=COI {ECO:0000313|EMBL:ADK26838.1};
OS   Odontaspis ferox (smalltooth sand tiger).
OG   Mitochondrion {ECO:0000313|EMBL:ADK26838.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Lamniformes; Odontaspididae;
OC   Odontaspis.
OX   NCBI_TaxID=57989 {ECO:0000313|EMBL:ADK26838.1};
RN   [1] {ECO:0000313|EMBL:ADK26838.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S53 {ECO:0000313|EMBL:ADK26838.1};
RX   PubMed=20457263; DOI=10.1016/j.ympev.2010.04.042;
RA   Straube N., Iglesias S.P., Sellos D.Y., Kriwet J., Schliewen U.K.;
RT   "Molecular phylogeny and node time estimation of bioluminescent
RT   Lantern Sharks (Elasmobranchii: Etmopteridae).";
RL   Mol. Phylogenet. Evol. 56:905-917(2010).
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; GU130673; ADK26838.1; -; Genomic_DNA.
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; 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.
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:ADK26838.1};
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}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:ADK26838.1}.
FT   NON_TER     218    218       {ECO:0000313|EMBL:ADK26838.1}.
SQ   SEQUENCE   218 AA;  23311 MW;  24F96DF5DEA04663 CRC64;
     LYLIFGAWAG MVGMALSLLI RAELGQPGSL LGDDQIYNVI VTAHAFVMIF FMVMPVMIGG
     FGNWLVPLMI GAPDMAFPRM NNMSFWLLPP SFLLLLASAG VEAGAGTGWT VYPPLAGNLA
     HAGASVDLAI FSLHLAGISS ILASINFITT IINMKPPAIS QYQTPLFVWS ILVTTILLLL
     SLPVLAAGIT MLLTDRNLNT TFFDPAGGGD PILYQHLF
//