ID A0A1X9YLU5_OVIAM Unreviewed; 352 AA. AC A0A1X9YLU5; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 11-DEC-2019, entry version 7. DE RecName: Full=Cytochrome b {ECO:0000256|RuleBase:RU362117}; DE Flags: Fragment; OS Ovis ammon (Argali). OG Mitochondrion {ECO:0000313|EMBL:ARS33775.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Caprinae; Ovis. OX NCBI_TaxID=30527 {ECO:0000313|EMBL:ARS33775.1}; RN [1] {ECO:0000313|EMBL:ARS33775.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=77Oa {ECO:0000313|EMBL:ARS33775.1}; RA Kholodova M.V., Kashinina N.V.; RT "Mountain Hunters Club trophies genetic analyses."; RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex CC (complex III or cytochrome b-c1 complex) that is part of the CC mitochondrial respiratory chain. The b-c1 complex mediates electron CC transfer from ubiquinol to cytochrome c. Contributes to the generation CC of a proton gradient across the mitochondrial membrane that is then CC used for ATP synthesis. {ECO:0000256|RuleBase:RU362117}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|PIRSR:PIRSR038885-2, CC ECO:0000256|RuleBase:RU362117}; CC Note=Binds 2 heme groups non-covalently. CC {ECO:0000256|PIRSR:PIRSR038885-2, ECO:0000256|RuleBase:RU362117}; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU362117}. CC -!- SIMILARITY: Belongs to the cytochrome b family. CC {ECO:0000256|RuleBase:RU362117}. 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; KY366502; ARS33775.1; -; 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:0045275; C:respiratory chain complex III; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro. DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:InterPro. DR CDD; cd00290; cytochrome_b_C; 1. DR CDD; cd00284; Cytochrome_b_N; 1. DR Gene3D; 1.20.810.10; -; 1. DR InterPro; IPR005798; Cyt_b/b6_C. DR InterPro; IPR036150; Cyt_b/b6_C_sf. DR InterPro; IPR005797; Cyt_b/b6_N. DR InterPro; IPR027387; Cytb/b6-like_sf. DR InterPro; IPR030689; Cytochrome_b. DR InterPro; IPR016174; Di-haem_cyt_TM. DR Pfam; PF00032; Cytochrom_B_C; 1. DR Pfam; PF00033; Cytochrome_B; 1. DR PIRSF; PIRSF038885; COB; 1. DR SUPFAM; SSF81342; SSF81342; 1. DR SUPFAM; SSF81648; SSF81648; 1. DR PROSITE; PS51003; CYTB_CTER; 1. DR PROSITE; PS51002; CYTB_NTER; 1. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|RuleBase:RU362117}; KW Heme {ECO:0000256|PIRSR:PIRSR038885-2, ECO:0000256|RuleBase:RU362117}; KW Iron {ECO:0000256|PIRSR:PIRSR038885-2, ECO:0000256|RuleBase:RU362117}; KW Membrane {ECO:0000256|RuleBase:RU362117}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR038885-2, KW ECO:0000256|RuleBase:RU362117}; KW Mitochondrion {ECO:0000256|RuleBase:RU362117, ECO:0000313|EMBL:ARS33775.1}; KW Respiratory chain {ECO:0000256|RuleBase:RU362117}; KW Transmembrane {ECO:0000256|RuleBase:RU362117}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362117}; KW Transport {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 6..28 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 63..83 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 89..109 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 116..134 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 154..176 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 205..222 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 264..283 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 295..316 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 322..348 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT DOMAIN 1..185 FT /note="CYTB_NTER" FT /evidence="ECO:0000259|PROSITE:PS51002" FT DOMAIN 186..352 FT /note="CYTB_CTER" FT /evidence="ECO:0000259|PROSITE:PS51003" FT METAL 59 FT /note="Iron 1 (heme b562 axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT METAL 73 FT /note="Iron 2 (heme b566 axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT METAL 158 FT /note="Iron 1 (heme b562 axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT METAL 172 FT /note="Iron 2 (heme b566 axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT BINDING 177 FT /note="Ubiquinone" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-1" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ARS33775.1" FT NON_TER 352 FT /evidence="ECO:0000313|EMBL:ARS33775.1" SQ SEQUENCE 352 AA; 39680 MW; 380ECC198CED15CC CRC64; SNISSWWNFG SLLGICLILQ ILTGLFLAMH YTPDTTTAFS SVTHICRDVN YGWIIRYMHA NGASMFFICL FMHVGRGLYY GSYTFLETWN IGVILLFATM ATAFMGYVLP WGQMSFWGAT VITNLLSAIP YIGTNLVEWI WGGFSVDKAT LTRFFAFHFI FPFIIAALAM VHLLFLHETG SNNPTGIPSD TDKIPFHPYY TIKDILGAIL LILTLMLLVL FTPDLLGDPD NYTPANPLNT PPHIKPEWYF LFAYAILRSI PNKLGGVLAL VLSILVLVIM PLLHTSKQRS MMFRPISQCM FWILVADLLT LTWIGGQPVE HPYIIIGQLA SIMYFLIILV MMPVASIIEN NL //