ID   A0A4Y5N1J1_9ARAC        Unreviewed;       219 AA.
AC   A0A4Y5N1J1;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   13-NOV-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:QCW08832.1};
OS   Trite sp. 1GAB_PAK.
OG   Mitochondrion {ECO:0000313|EMBL:QCW08832.1}.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Araneae; Araneomorphae; Entelegynae; Dionycha; Salticidae; Salticoida;
OC   Salticinae; Trite; unclassified Trite.
OX   NCBI_TaxID=2579438 {ECO:0000313|EMBL:QCW08832.1};
RN   [1] {ECO:0000313|EMBL:QCW08832.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=31116764; DOI=.1371/journal.pone.0217086;
RA   Ashfaq M., Blagoev G., Tahir H.M., Khan A.M., Mukhtar M.K., Akhtar S.,
RA   Butt A., Mansoor S., Hebert P.D.N.;
RT   "Assembling a DNA barcode reference library for the spiders
RT   (Arachnida: Araneae) of Pakistan.";
RL   PLoS ONE 14:e0217086-e0217086(2019).
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; MK153929; QCW08428.1; -; Genomic_DNA.
DR   EMBL; MK153989; QCW08488.1; -; Genomic_DNA.
DR   EMBL; MK154333; QCW08832.1; -; Genomic_DNA.
DR   EMBL; MK154858; QCW09357.1; -; 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   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:QCW08832.1};
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      6     25       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     37     67       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     87    113       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    134    155       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    167    194       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    219       COX1. {ECO:0000259|PROSITE:PS50855}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:QCW08832.1}.
FT   NON_TER     219    219       {ECO:0000313|EMBL:QCW08832.1}.
SQ   SEQUENCE   219 AA;  23608 MW;  059F0F1A9AED482B CRC64;
     TLYLIFGAWS AMVGTAMSML IRMELGQTGS FLGNDHMYNV IVTAHAFVMI FFMVMPILIG
     GFGNWLVPLM LGAPDMAFPR MNNLSFWLLP PSLFLLFVSS MAEMGVGAGW TVYPPLASIV
     GHNGSSVDFA IFSLHLAGAS SIMGAINFIS TVINMRSVGM SLDSVPLFVW SVVITAVLLL
     LSLPVLAGAI TMLLTDRNFN TSFFDPAGGG DPILFQHLF
//