ID D0E983_9HEMI Unreviewed; 177 AA. AC D0E983; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 11-DEC-2019, entry version 38. DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU000457}; DE Flags: Fragment; GN Name=COII {ECO:0000313|EMBL:ACX48336.1}; OS Diaspididae sp. D0752A. OG Mitochondrion {ECO:0000313|EMBL:ACX48336.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Coccoidea; Diaspididae; OC unclassified Diaspididae. OX NCBI_TaxID=670958 {ECO:0000313|EMBL:ACX48336.1}; RN [1] {ECO:0000313|EMBL:ACX48336.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=D0752A {ECO:0000313|EMBL:ACX48336.1}; RX PubMed=20460159; DOI=10.1016/j.ympev.2010.05.002; RA Andersen J.C., Wu J., Gruwell M.E., Gwiazdowski R., Santana S.E., RA Feliciano N.M., Morse G.E., Normark B.B.; RT "A phylogenetic analysis of armored scale insects (Hemiptera: Diaspididae), RT based upon nuclear, mitochondrial, and endosymbiont gene sequences."; RL Mol. Phylogenet. Evol. 57:992-1003(2010). 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. Subunit 2 transfers the CC electrons from cytochrome c via its binuclear copper A center to the CC bimetallic center of the catalytic subunit 1. CC {ECO:0000256|RuleBase:RU000457}. CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|RuleBase:RU000457}; CC Note=Binds a copper A center. {ECO:0000256|RuleBase:RU000457}; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU000457}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000457}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family. CC {ECO:0000256|RuleBase:RU000457}. 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; GQ425057; ACX48336.1; -; Genomic_DNA. 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:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro. DR Gene3D; 1.10.287.90; -; 1. DR Gene3D; 2.60.40.420; -; 1. DR InterPro; IPR002429; CcO_II-like_C. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom. DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf. DR Pfam; PF00116; COX2; 1. DR Pfam; PF02790; COX2_TM; 1. DR SUPFAM; SSF49503; SSF49503; 1. DR SUPFAM; SSF81464; SSF81464; 1. DR PROSITE; PS50857; COX2_CUA; 1. DR PROSITE; PS50999; COX2_TM; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|RuleBase:RU000457}; KW Electron transport {ECO:0000256|RuleBase:RU000457}; KW Membrane {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00883094, KW ECO:0000256|SAM:Phobius}; Metal-binding {ECO:0000256|RuleBase:RU000457}; KW Mitochondrion {ECO:0000256|RuleBase:RU000457, ECO:0000313|EMBL:ACX48336.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000457}; KW Respiratory chain {ECO:0000256|RuleBase:RU000457}; KW Transmembrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00882981, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00883111, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000457}. FT TRANSMEM 20..41 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 62..84 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..90 FT /note="COX2_TM" FT /evidence="ECO:0000259|PROSITE:PS50999" FT DOMAIN 91..177 FT /note="COX2_CUA" FT /evidence="ECO:0000259|PROSITE:PS50857" FT NON_TER 177 FT /evidence="ECO:0000313|EMBL:ACX48336.1" SQ SEQUENCE 177 AA; 21657 MW; CD2E59E71E97CBD2 CRC64; MTWMNLNFQN PNSMNLFKLI MFNNLLMIII MNIFIIMLMM MKFNMKNKFN NKNMFNNQLM EFMWTMLPMM LIMMIMIVSM NILFMNNEAK KNFINIKMMG NQWFWNYEYP NFNKSFNSYL MMNKNFNFFM METDNNLIIP FNYQMMMSLS SMDVIHSWTI PSMNIKMDAI PNQLNNF //