ID CYB_CHEMY STANDARD; PRT; 381 AA. AC Q9TEC1; DT 25-JAN-2005 (Rel. 46, Created) DT 25-JAN-2005 (Rel. 46, Last sequence update) DT 25-JAN-2005 (Rel. 46, Last annotation update) DE Cytochrome b. GN Name=MTCYB; Synonyms=COB, CYTB; OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Testudines; Cryptodira; Chelonioidea; Cheloniidae; Chelonia. OX NCBI_TaxID=8469; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=99297345; PubMed=10368956; RA Kumazawa Y., Nishida M.; RT "Complete mitochondrial DNA sequences of the green turtle and blue- RT tailed mole skink: statistical evidence for archosaurian affinity of RT turtles."; RL Mol. Biol. Evol. 16:784-792(1999). CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase CC complex (complex III or cytochrome b-c1 complex), which is a CC respiratory chain that generates an electrochemical potential CC coupled to ATP synthesis (By similarity). CC -!- COFACTOR: Binds two heme groups non-covalently. Heme 1 (or BL or CC b562) is low-potential and absorbs at about 562 nm, and heme 2 (or CC BH or b566) is high-potential and absorbs at about 566 nm (By CC similarity). CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b, CC cytochrome c1 and the Rieske protein (By similarity). CC -!- SIMILARITY: Belongs to the cytochrome b family. 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; AB012104; BAA79209.1; -. DR HSSP; P18946; 2BCC. DR InterPro; IPR005798; Cytb_b6_C. DR InterPro; IPR005797; Cytb_b6_N. DR Pfam; PF00032; Cytochrom_B_C; 1. DR Pfam; PF00033; Cytochrom_B_N; 1. DR PROSITE; PS51003; CYTB_CTER; 1. DR PROSITE; PS51002; CYTB_NTER; 1. KW Electron transport; Heme; Mitochondrion; Respiratory chain; KW Transmembrane. FT METAL 84 84 Iron 1 (heme b562 axial ligand). FT METAL 98 98 Iron 2 (heme b566 axial ligand). FT METAL 183 183 Iron 1 (heme b562 axial ligand). FT METAL 197 197 Iron 2 (heme b566 axial ligand). SQ SEQUENCE 381 AA; 42859 MW; DE980F3AFE9E17D7 CRC64; MATNLRKTHP MMKIINNLVI DLPSPSNISA WWNFGSLLAT CLALQIITGI FLAMHYSPDI SMAFSSIAHI TRDVQYGWLI RNMHANGASL FFMCIYLHIG RGIYYGSYLY KETWNTGIIL LLLVMATAFV GYVLPWGQMS FWGATVITNL LSAIPYIGNT LVQWIWGGFS VDNATLTRFF TFHFLLPFAI TGLTAVHLLF LHETGSNNPT GLNSNTDKIP FHPYFSYKDL LGLILMLTFL LTLTLFSPYL LGDPDNFTPA NPLSTPPHIK PEWYFLFAYA ILRSIPNKLG GVLALLFSIL ILFLMPTLHT SKQRTASFRP LTQILFWSLV ADLLVLTWIG GQPVEDPFII IGQVASTFYF LILLLLMPAA GMIENKMLNL K //