ID B3SG81_9BIVA Unreviewed; 93 AA. AC B3SG81; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 25-MAY-2022, entry version 42. DE SubName: Full=Cytochrome oxidase subunit II {ECO:0000313|EMBL:ABN04255.1}; DE Flags: Fragment; GN Name=COII {ECO:0000313|EMBL:ABN04255.1}; OS Glebula rotundata. OG Mitochondrion {ECO:0000313|EMBL:ABN04255.1}. OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia; OC Autobranchia; Heteroconchia; Palaeoheterodonta; Unionida; Unionoidea; OC Unionidae; Ambleminae; Lampsilini; Glebula. OX NCBI_TaxID=152244 {ECO:0000313|EMBL:ABN04255.1}; RN [1] {ECO:0000313|EMBL:ABN04255.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=H1035 {ECO:0000313|EMBL:ABN04255.1}; RX PubMed=18513440; DOI=10.1186/1471-2148-8-165; RA Chapman E.G., Piontkivska H., Walker J.M., Stewart D.T., Curole J.P., RA Hoeh W.R.; RT "Extreme primary and secondary protein structure variability in the RT chimeric male-transmitted cytochrome c oxidase subunit II protein in RT freshwater mussels: evidence for an elevated amino acid substitution rate RT in the face of domain-specific purifying selection."; RL BMC Evol. Biol. 8:165-165(2008). CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)- CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=7.1.1.9; CC Evidence={ECO:0000256|ARBA:ARBA00029331}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000256|ARBA:ARBA00029331}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|ARBA:ARBA00001935}; CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family. CC {ECO:0000256|ARBA:ARBA00007866}. 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; EF033284; ABN04255.1; -; Genomic_DNA. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR Gene3D; 2.60.40.420; -; 1. DR InterPro; IPR045187; CcO_II. DR InterPro; IPR002429; CcO_II-like_C. DR InterPro; IPR001505; Copper_CuA. DR InterPro; IPR008972; Cupredoxin. DR PANTHER; PTHR22888; PTHR22888; 1. DR Pfam; PF00116; COX2; 1. DR SUPFAM; SSF49503; SSF49503; 1. DR PROSITE; PS00078; COX2; 1. DR PROSITE; PS50857; COX2_CUA; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|ARBA:ARBA00023008}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Mitochondrion {ECO:0000313|EMBL:ABN04255.1}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}. FT DOMAIN 1..93 FT /note="COX2_CUA" FT /evidence="ECO:0000259|PROSITE:PS50857" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ABN04255.1" FT NON_TER 93 FT /evidence="ECO:0000313|EMBL:ABN04255.1" SQ SEQUENCE 93 AA; 10289 MW; 31787465C7BED645 CRC64; YRLLEVDNRC VLPYGVDSRV LVSSADVIHA WALPSIGVKV DAIPGRINQL GVHLMSSGVM YGQCSEICGV NHSFMPIGLE SVSPEVFYYW LVY //