ID   Q101K9_9CHON            Unreviewed;       185 AA.
AC   Q101K9;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 2.
DT   09-DEC-2015, entry version 53.
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;
GN   Name=COI {ECO:0000313|EMBL:AAZ91995.2};
OS   Bathyraja lindbergi (cmmander skate).
OG   Mitochondrion {ECO:0000313|EMBL:AAZ91995.2}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Rajiformes; Bathyraja.
OX   NCBI_TaxID=341245 {ECO:0000313|EMBL:AAZ91995.2};
RN   [1] {ECO:0000313|EMBL:AAZ91995.2}
RP   NUCLEOTIDE SEQUENCE.
RA   Spies I.B., Gaichas S., Stevenson D.E., Orr J.W., Canino M.F.;
RT   "DNA-based identification of Alaska skates (Amblyraja, Bathyraja and
RT   Raja: Rajidae) using cytochrome c oxidase subunit I (coI) variation.";
RL   J. Fish Biol. 69:283-292(2006).
RN   [2] {ECO:0000313|EMBL:AAZ91995.2}
RP   NUCLEOTIDE SEQUENCE.
RA   Canino M.F., Spies I.B., Gaichas S., Orr J.W., Stevenson D.E.;
RL   Submitted (AUG-2009) 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   -!- 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ104909; AAZ91995.2; -; Genomic_DNA.
DR   HOVERGEN; HBG102108; -.
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, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU000369};
KW   Mitochondrion {ECO:0000256|RuleBase:RU000369,
KW   ECO:0000313|EMBL:AAZ91995.2};
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   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU000369}.
FT   TRANSMEM     18     48       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     69     93       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    113    136       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    148    175       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    185       COX1. {ECO:0000259|PROSITE:PS50855}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:AAZ91995.2}.
FT   NON_TER     185    185       {ECO:0000313|EMBL:AAZ91995.2}.
SQ   SEQUENCE   185 AA;  19922 MW;  22B08E17F0626B3A CRC64;
     LIRAELSQPG TLLGDDQIYN VIVTAHAFVM IFFMVMPIMI GGFGNWLVPL MIGSPDMAFP
     RMNNMSFWLL PPSFLLLLAS AGVEAGAGTG WTVYPPLAGN LAHAGASVDL TIFSLHLAGI
     SSILASINFI TTIINMKPPA ISQYQTPLFV WSVLVTTVLL LLALPILAAA ITMLLTDRNL
     NTTFF
//