ID A0A0F6P9B3_9HYME Unreviewed; 315 AA. AC A0A0F6P9B3; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 16-JAN-2019, entry version 15. 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; OS Ooencyrtus pityocampae. OG Mitochondrion {ECO:0000313|EMBL:AJE26282.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Parasitoida; OC Chalcidoidea; Encyrtidae; Encyrtinae; Ooencyrtus. OX NCBI_TaxID=1545928 {ECO:0000313|EMBL:AJE26282.1}; RN [1] {ECO:0000313|EMBL:AJE26282.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25856082; RA Samra S., Ghanim M., Protasov A., Branco M., Mendel Z.; RT "Genetic Diversity and Host Alternation of the Egg Parasitoid RT Ooencyrtus pityocampae between the Pine Processionary Moth and the RT Caper Bug."; RL PLoS ONE 10:E0122788-E0122788(2015). 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; KM485921; AJE26282.1; -; 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 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:AJE26282.1}; 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 32 56 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 68 96 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 116 140 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 152 176 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 188 212 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 224 244 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 256 281 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 293 311 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 315 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:AJE26282.1}. FT NON_TER 315 315 {ECO:0000313|EMBL:AJE26282.1}. SQ SEQUENCE 315 AA; 35360 MW; 610DC7F642CEE960 CRC64; SSMFVGSGTG TGWTVYPPLS SNLGHMGPSV DLSIFSLHIA GVSSIMGSIN FITTIINMKL YKMEMIPLFS WAMLLTAILL LLSLPVLAGA ITMLLFDRNL NTSFFDPIGG GDPILYQHLF WFFGHPEVYI LILPGFGLIS HMISNESMKK EVFGVMGMIY AMISIGLLGF IVWAHHMFTV GMDVDTRAYF TSATMIIAVP TGIKIFSWLA SLNGMKLYMN VSNLWIMGFI FLFTLGGLTG IMLSNSSIDI VLHDTYYVVA HFHYVLSMGA VFAIFGSFIY WYPMMFGYSM NKLWLKIQFF FMFLGVNMTF FPQHF //