ID A0A4P1TNJ2_9NEOP Unreviewed; 217 AA. AC A0A4P1TNJ2; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 18-SEP-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:ADH23254.1}; OS Melanargia ines. OG Mitochondrion {ECO:0000313|EMBL:ADH23254.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia; OC Papilionoidea; Nymphalidae; Satyrinae; Satyrini; Melanargiina; OC Melanargia. OX NCBI_TaxID=679095 {ECO:0000313|EMBL:ADH23254.1}; RN [1] {ECO:0000313|EMBL:ADH23254.1} RP NUCLEOTIDE SEQUENCE. RG International Barcode of Life (iBOL); RT "iBOL Data Release."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. 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; GU673595; ADH23254.1; -; 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 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:ADH23254.1}; 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 24 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 36 58 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 112 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 132 154 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 166 193 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 217 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:ADH23254.1}. FT NON_TER 217 217 {ECO:0000313|EMBL:ADH23254.1}. SQ SEQUENCE 217 AA; 23158 MW; B671FC98FB7277B7 CRC64; LYLVFGAWAG MVGTALSLLI RAELSQPGAL LGDDQIYNVI VTAHAFVMIF FMVMPIMIGG FGNWLIPLMV GAPDMAFPRM NNMSFWLLPP SFLLLLASSG VEAGAGTGWT VYPPLAGNLA HAGASVDLTI FSLHLAGISS ILGAINFITT IINMKPPTVT MYHIPLFVWA VLITAVLLLL SLPVLAAGIT MLLTDRNLNT TFFDPAGGGD PILYQHL //