ID A0A514E8C8_TETUR Unreviewed; 381 AA. AC A0A514E8C8; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 13-NOV-2019, entry version 2. 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:QDI02282.1}; OS Tetranychus urticae (Two-spotted spider mite). OG Mitochondrion {ECO:0000313|EMBL:QDI02282.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; OC Acari; Acariformes; Trombidiformes; Prostigmata; Eleutherengona; OC Raphignathae; Tetranychoidea; Tetranychidae; Tetranychus. OX NCBI_TaxID=32264 {ECO:0000313|EMBL:QDI02282.1}; RN [1] {ECO:0000313|EMBL:QDI02282.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GSS {ECO:0000313|EMBL:QDI02282.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:QDI02282.1}; RX PubMed=31250237; DOI=.1007/s10493-019-00398-w; RA Inak E., Alpkent Y.N., Cobanoglu S., Dermauw W., Van Leeuwen T.; RT "Resistance incidence and presence of resistance mutations in RT populations of Tetranychus urticae from vegetable crops in Turkey."; RL Exp. Appl. Acarol. 78:343-360(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}. 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; MK508722; QDI02282.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. 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 InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 1. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 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:QDI02282.1}; 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 33 54 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 75 97 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 117 142 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 154 182 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 214 233 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 245 262 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 274 295 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 307 328 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 348 370 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 369 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:QDI02282.1}. FT NON_TER 381 381 {ECO:0000313|EMBL:QDI02282.1}. SQ SEQUENCE 381 AA; 42867 MW; DB418F644283EFF0 CRC64; GTSMSIIIRL ELMTPGSLIQ NDFIYNSMVT THAMIMIFFM VMPAMIGGFG NWLIPLMINT VDLCFPRINN MSFWLLIPSL MLMISSSMKS VLNGVGWTMY PPLTSIQYFM SSSIEMMIFS LHIAGISSIA SSINFISTIL LMKNKNYFLS NLTLFSLSIL ITTFLLLLAL PVLAGAITMI LMDRNFNTSF FDPSGGGDPI LYQHLFWFFG HPEVYILILP GFGMISHVIS YNLGKKEVFG KIGMMFAMMS IGLLGFIVWA HHMFTVGMDV DTRAYFTAAT MIIAIPTGIK IFSWFTTILN SHINFNISMY WSMGFLIMFS IGGFTGIVAS NSCLDINLHD SYYIVAHFHY VLSMGAVFAI FSGLFLWIPL NNMMYILMMM C //