ID A0A076JDS2_9MUSC Unreviewed; 511 AA. AC A0A076JDS2; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 09-DEC-2015, entry version 8. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369}; GN Name=COI {ECO:0000313|EMBL:AII71820.1}; OS Liriomyza langei. OG Mitochondrion {ECO:0000313|EMBL:AII71820.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Opomyzoidea; Agromyzidae; Phytomyzinae; Liriomyza. OX NCBI_TaxID=1484199 {ECO:0000313|EMBL:AII71820.1}; RN [1] {ECO:0000313|EMBL:AII71820.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Lang25 {ECO:0000313|EMBL:AII71878.1}, Lang36 RC {ECO:0000313|EMBL:AII71820.1}, Lang44 {ECO:0000313|EMBL:AII71884.1}, RC and Lang8 {ECO:0000313|EMBL:AII71802.1}; RA Scheffer S.J., Lewis M.L., Gaimari S.D., Reitz S.R.; RT "Molecular Survey for the Invasive Leafminer Pest Liriomyza RT huidobrensis (Diptera: Agromyzidae) in California Uncovers Only the RT Native Pest Liriomyza langei."; RL J. Econ. Entomol. 107:1959-1964(2014). 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: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. {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; KJ778705; AII71802.1; -; Genomic_DNA. DR EMBL; KJ778714; AII71820.1; -; Genomic_DNA. DR EMBL; KJ778743; AII71878.1; -; Genomic_DNA. DR EMBL; KJ778746; AII71884.1; -; 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:respiratory chain; 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:0005506; F:iron ion binding; IEA:InterPro. 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; IPR000883; COX1. DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR InterPro; IPR023616; Cyt_c_Oxase_su1_dom. 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:AII71820.1}; 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 12 35 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 55 81 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 124 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 144 169 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 181 208 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 228 249 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 270 289 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 301 325 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 337 357 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 377 398 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 410 428 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 448 471 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 510 COX1. {ECO:0000259|PROSITE:PS50855}. SQ SEQUENCE 511 AA; 56597 MW; A7B5B038BEBAE46F CRC64; MRQWLFSTNH KDIGTLYFMF GAWSGMVGTS LSILIRAELG HPGALIGDDQ IYNVIVTAHA FIMIFFMVMP IMIGGFGNWL VPLMLGAPDM AFPRMNNMSF WLLPPALTLL LMSSMVENGA GTGWTVYPPL SSIIAHGGAS VDLAIFSLHL AGISSILGAV NFITTIINMR STGITFDRMP LFVWSVLITA ILLLLSLPVL AGAITMLLTD RNFNTSFFDP AGGGDPILYQ HLFWFFGHPE VYILILPGFG MISHIISHES GKKETFGSLG MIYAMLAIGL LGFIVWAHHM FTVGLDVDTR AYFTSATMII AVPTGIKIFS WLATLHGTQL SYTPTTLWSL GFVFLFTVGG LTGVVLANSS IDVVLHDTYY VVAHFHYVLS MGAVFAIMAG FIHWYPLFTG LSLNVKLLKS QFFIMFIGVN LTFFPQHFLG LAGMPRRYSD YPDAYTAWNV ISTIGSSISL LGIILFLYII WESMMTQRQV IFPIQLNSSI EWYQNTPPAE HSYSELPMLT N //