ID A0A0K0YD85_9ANNE Unreviewed; 263 AA. AC A0A0K0YD85; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 09-DEC-2015, entry version 2. DE RecName: Full=Cytochrome c oxidase subunit 3 {ECO:0000256|RuleBase:RU003375}; GN Name=COX3 {ECO:0000313|EMBL:AKS48934.1}; OS Trypanosyllis (Trypanobia) sp. CB-2015. OG Mitochondrion {ECO:0000313|EMBL:AKS48934.1}. OC Eukaryota; Metazoa; Lophotrochozoa; Annelida; Polychaeta; Palpata; OC Aciculata; Phyllodocida; Syllidae; Trypanosyllis. OX NCBI_TaxID=1648961 {ECO:0000313|EMBL:AKS48934.1}; RN [1] {ECO:0000313|EMBL:AKS48934.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26183383; DOI=10.1038/srep12072; RA Aguado M.T., Glasby C.J., Schroeder P.C., Weigert A., Bleidorn C.; RT "The making of a branching annelid: an analysis of complete RT mitochondrial genome and ribosomal data of Ramisyllis multicaudata."; RL Sci. Rep. 5:12072-12072(2015). CC -!- FUNCTION: Subunits I, II and III form the functional core of the CC enzyme complex. {ECO:0000256|RuleBase:RU003375}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family. CC {ECO:0000256|RuleBase:RU003375}. 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; KR534503; AKS48934.1; -; Genomic_DNA. DR Gene3D; 1.20.120.80; -; 1. DR InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3. DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx. DR InterPro; IPR000298; Cyt_c_oxidase_su3_dom. DR PANTHER; PTHR11403; PTHR11403; 1. DR Pfam; PF00510; COX3; 1. DR SUPFAM; SSF81452; SSF81452; 1. DR PROSITE; PS50253; COX3; 1. PE 3: Inferred from homology; KW Membrane {ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU003375, KW ECO:0000313|EMBL:AKS48934.1}; KW Transmembrane {ECO:0000256|RuleBase:RU003375, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 36 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 59 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 79 103 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 128 148 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 160 180 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 192 219 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 240 260 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 263 AA; 30427 MW; 79C3D434C551417E CRC64; MMKKVFHPYH LVEFSPWPLT GSLGALTLMT GLVNWFHQDL TPTILVGILI ILMTMIQWWR DVTRESTYLG HHTTGVQQLL KWGMILFITS EVFFFLAFFW AFFHSSLAPT MELGCDWPPM GINPLDSFAI PLLNTAVLLS SGVTVTWAHH SIMSHKIKEF KLGLTYTILL GLYFTLLQVW EYLESSFTIA DSVYGSTFFV ATGFHGLHVI IGTSFLIVCR MRSNFNHYSP THHFGFEAAA WYWHFVDVVW IFLYLCIYWW GSM //