ID A0A4Y5N1J1_9ARAC Unreviewed; 219 AA.
AC A0A4Y5N1J1;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 11-DEC-2019, entry version 4.
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; Araneae;
OC Araneomorphae; Entelegynae; Dionycha; Salticidae; Salticoida; Salticinae;
OC 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 (Arachnida:
RT 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 1-3
CC form the functional core of the enzyme complex. CO I is the catalytic
CC subunit of the enzyme. Electrons originating in cytochrome c are
CC transferred via the copper A center of subunit 2 and heme A of subunit
CC 1 to the bimetallic center formed by heme A3 and copper B.
CC {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=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: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: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, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|RuleBase:RU000369}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..219
FT /note="COX1"
FT /evidence="ECO:0000259|PROSITE:PS50855"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:QCW08832.1"
FT NON_TER 219
FT /evidence="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
//