ID A0A0F6P9B3_9HYME Unreviewed; 315 AA. AC A0A0F6P9B3; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 11-DEC-2019, entry version 16. 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; Pterygota; OC Neoptera; Holometabola; Hymenoptera; Apocrita; Parasitoida; Chalcidoidea; OC 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 Ooencyrtus RT pityocampae between the Pine Processionary Moth and the 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 1-3 CC form the functional core of the enzyme complex. CO I is the catalytic CC subunit of the enzyme. Electrons originating in cytochrome c are CC transferred via the copper A center of subunit 2 and heme A of subunit CC 1 to the bimetallic center formed by heme A3 and copper B. CC {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c] CC + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA- CC COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, 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}; 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, 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, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 32..56 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 68..96 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 116..140 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 152..176 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 188..212 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 224..244 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 256..281 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 293..311 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..315 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AJE26282.1" FT NON_TER 315 FT /evidence="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 //