ID   A0A3G2LLJ0_9BIVA        Unreviewed;       219 AA.
AC   A0A3G2LLJ0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   08-MAY-2019, entry version 3.
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:AYN73902.1};
OS   Lanceolaria eucylindrica.
OG   Mitochondrion {ECO:0000313|EMBL:AYN73902.1}.
OC   Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Bivalvia;
OC   Palaeoheterodonta; Unionida; Unionoidea; Unionidae; Unioninae;
OC   Lanceolaria.
OX   NCBI_TaxID=1974279 {ECO:0000313|EMBL:AYN73902.1};
RN   [1] {ECO:0000313|EMBL:AYN73902.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Huang Xc., Su Jh., Wu Xp.;
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AYN73902.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30308278; DOI=10.1016/j.ympev.2018.09.019;
RA   Huang X.C., Su J.H., Ouyang J.X., Ouyang S., Zhou C.H., Wu X.P.;
RT   "Towards a global phylogeny of freshwater mussels (Bivalvia:
RT   Unionida): Species delimitation of Chinese taxa, mitochondrial
RT   phylogenomics, and diversification patterns.";
RL   Mol. Phylogenet. Evol. 130:45-59(2018).
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, Rhea:RHEA-
CC         COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034; EC=1.9.3.1;
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}.
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DR   EMBL; MG463002; AYN73902.1; -; Genomic_DNA.
DR   EMBL; MG463003; AYN73903.1; -; Genomic_DNA.
DR   EMBL; MG463004; AYN73904.1; -; Genomic_DNA.
DR   EMBL; MG463005; AYN73905.1; -; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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};
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:AYN73902.1};
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   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU000369}.
FT   TRANSMEM     48     74       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     86    104       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    124    148       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    169    196       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    219       COX1. {ECO:0000259|PROSITE:PS50855}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:AYN73902.1}.
FT   NON_TER     219    219       {ECO:0000313|EMBL:AYN73902.1}.
SQ   SEQUENCE   219 AA;  23168 MW;  1ECFF783312C7CC4 CRC64;
     IGTLYLLLAL WSGLIGLALS LLIRAELGQP GSLLGDDQLY NVIVTAHAFM MIFFLVMPMM
     IGGFGNWLIP LMIGAPDMAF PRLNNLSFWL LVPALFLLLS SSLVESGVGT GWTVYPPLSG
     NVAHSGASVD LAIFSLHLAG ASSILGAINF ISTVGNMRSP GLVAERIPLF VWAVTVTAVL
     LVAALPVLAG AITMLLTDRN LNTSFFDPTG GGDPILYMH
//