ID   A0A166HSN9_9TELE        Unreviewed;       217 AA.
AC   A0A166HSN9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   17-JUN-2020, entry version 14.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369};
DE            EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369};
DE   Flags: Fragment;
GN   Name=COI {ECO:0000313|EMBL:ANA09114.1};
OS   Capoeta damascina saadii.
OG   Mitochondrion {ECO:0000313|EMBL:ANA09114.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Capoeta.
OX   NCBI_TaxID=1051495 {ECO:0000313|EMBL:ANA09114.1};
RN   [1] {ECO:0000313|EMBL:ANA09114.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=15_Ex82B4 {ECO:0000313|EMBL:ANA09114.1}, M824_Ex90A3
RC   {ECO:0000313|EMBL:ANA09118.1}, M826_Ex90A5
RC   {ECO:0000313|EMBL:ANA09117.1}, M830_Ex90A11
RC   {ECO:0000313|EMBL:ANA09116.1}, and M832_Ex90A6
RC   {ECO:0000313|EMBL:ANA09115.1};
RX   PubMed=27394223; DOI=10.11646/zootaxa.4083.1.7;
RA   Zareian H., Esmaeili H.R., Freyhof J.;
RT   "Capoeta anamisensis, a new species from the Minab and Hasan Langhi River
RT   drainages in Iran (Teleostei: Cyprinidae).";
RL   Zootaxa 4083:126-142(2016).
CC   -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC       mitochondrial electron transport chain which drives oxidative
CC       phosphorylation. The respiratory chain contains 3 multisubunit
CC       complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC       cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC       CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC       transfer electrons derived from NADH and succinate to molecular oxygen,
CC       creating an electrochemical gradient over the inner membrane that
CC       drives transmembrane transport and the ATP synthase. Cytochrome c
CC       oxidase is the component of the respiratory chain that catalyzes the
CC       reduction of oxygen to water. Electrons originating from reduced
CC       cytochrome c in the intermembrane space (IMS) are transferred via the
CC       dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC       to the active site in subunit 1, a binuclear center (BNC) formed by
CC       heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC       water molecules using 4 electrons from cytochrome c in the IMS and 4
CC       protons from the mitochondrial matrix. {ECO:0000256|RuleBase:RU000369}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c]
CC         + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-
CC         COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9;
CC         Evidence={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; KU312353; ANA09114.1; -; Genomic_DNA.
DR   EMBL; KU312354; ANA09115.1; -; Genomic_DNA.
DR   EMBL; KU312355; ANA09116.1; -; Genomic_DNA.
DR   EMBL; KU312356; ANA09117.1; -; Genomic_DNA.
DR   EMBL; KU312357; ANA09118.1; -; 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:respirasome; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR023616; Cyt_c_oxase-like_su1_dom.
DR   InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR   InterPro; IPR000883; Cyt_C_Oxase_1.
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}; 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, ECO:0000313|EMBL:ANA09114.1};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369};
KW   Respiratory chain {ECO:0000256|RuleBase:RU000369};
KW   Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU000369}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        36..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        132..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        166..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..217
FT                   /note="COX1"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ANA09114.1"
FT   NON_TER         217
FT                   /evidence="ECO:0000313|EMBL:ANA09114.1"
SQ   SEQUENCE   217 AA;  23093 MW;  1390F64A377BC315 CRC64;
     LYLVFGAWAG MVGTALSLLI RAELSQPGSL LGDDQIYNVI VTAHAFVMIF FMVMPILIGG
     FGNWLVPLMI GAPDMAFPRM NNMSFWLLPP SFLLLLASSG VEAGAGTGWT VYPPLSGNLA
     HAGASVDLTI FSLHLAGVSS ILGAINFITT TINMKPPAIS QYQTPLFVWS VLVTAVLLLL
     SLPVLAAGIT MLLTDRNLNT TFFDPAGGGD PILYQHL
//