ID M1EY13_AGRDO Unreviewed; 417 AA. AC M1EY13; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 16-JAN-2019, entry version 26. 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:AEZ68375.1}; OS Agriosphodrus dohrni (Japanese assassin-bug). OG Mitochondrion {ECO:0000313|EMBL:AEZ68375.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Paraneoptera; Hemiptera; Heteroptera; OC Panheteroptera; Cimicomorpha; Reduviidae; Harpactorinae; Harpactorini; OC Agriosphodrus. OX NCBI_TaxID=184613 {ECO:0000313|EMBL:AEZ68375.1}; RN [1] {ECO:0000313|EMBL:AEZ68375.1} RP NUCLEOTIDE SEQUENCE. RA Liu H., Li H., Ishikawa T., Su H.Z., Cai Z.W., Kamitani S.; RT "Invasion of the assassin bug Agriosphodrus dohrni (Hemiptera: RT Reduviidae) to Japan: Source estimation inferred from mitochondrial RT and nuclear gene sequences."; RL Submitted (JUN-2011) 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; JN089467; AEZ68375.1; -; 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:0045277; C:respiratory chain complex IV; IEA:InterPro. 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 CDD; cd01663; Cyt_c_Oxidase_I; 1. 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; IPR033944; 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. 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, KW ECO:0000256|SAAS:SAAS00711163, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:AEZ68375.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711093, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00711122, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}. FT SIGNAL 1 39 {ECO:0000256|SAM:SignalP}. FT CHAIN 40 417 Cytochrome c oxidase subunit 1. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004014510. FT TRANSMEM 62 87 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 99 126 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 146 171 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 183 207 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 219 242 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 254 275 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 295 316 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 328 346 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 366 389 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 417 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:AEZ68375.1}. FT NON_TER 417 417 {ECO:0000313|EMBL:AEZ68375.1}. SQ SEQUENCE 417 AA; 46006 MW; 40438448051B50EB CRC64; LMIGAPDMAF PRMNNMSFWL LPPSLTLLLI SSIAEGGAGT GWTVYPPLSS NIAHSGASVD LAIFSLHLAG VSSILGAVNF ISTIINMRPA GMTPERIPLF VWSVGITALL LLLSLPVLAG AITMLLTDRN FNTSFFDPSG GGDPILYQHL FWFFGHPXXX XXXXXXXXLI SHIISMETGK NEAFGSLGMI YAMMTIGLLG FIVWAHHMFT VGMDVDTRAY FTSATMIIAV PTGIKIFSWL ATLHGSKQLS TPSLLWALGF IFLFTIGGLT GVVLANSSID ITLHDTYYVV AHFHYVLSMG AVFAIMGSFI QWYPLFSGLT MNPKWLKIQF FTMFVGVNLT FFPQHFLGLS GMPRRYSDYP DSYTCWNIIS SLGSTISLIS IMLFIFIIWE SMVTKRQVLV AKQTSSNIEW MQKYPPA //