ID A0A1X9YLU5_OVIAM Unreviewed; 352 AA. AC A0A1X9YLU5; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 03-JUL-2019, entry version 6. 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; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; 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 CC complex (complex III or cytochrome b-c1 complex) that is part of CC the mitochondrial respiratory chain. The b-c1 complex mediates CC electron transfer from ubiquinol to cytochrome c. Contributes to CC the generation of a proton gradient across the mitochondrial CC membrane that is then used for ATP synthesis. CC {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, KW 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 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 63 83 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 89 109 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 116 134 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 154 176 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 205 222 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 264 283 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 295 316 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 322 348 Helical. {ECO:0000256|RuleBase:RU362117}. FT DOMAIN 1 185 CYTB_NTER. {ECO:0000259|PROSITE:PS51002}. FT DOMAIN 186 352 CYTB_CTER. {ECO:0000259|PROSITE:PS51003}. FT METAL 59 59 Iron 1 (heme b562 axial ligand). FT {ECO:0000256|PIRSR:PIRSR038885-2}. FT METAL 73 73 Iron 2 (heme b566 axial ligand). FT {ECO:0000256|PIRSR:PIRSR038885-2}. FT METAL 158 158 Iron 1 (heme b562 axial ligand). FT {ECO:0000256|PIRSR:PIRSR038885-2}. FT METAL 172 172 Iron 2 (heme b566 axial ligand). FT {ECO:0000256|PIRSR:PIRSR038885-2}. FT BINDING 177 177 Ubiquinone. {ECO:0000256|PIRSR: FT PIRSR038885-1}. FT NON_TER 1 1 {ECO:0000313|EMBL:ARS33775.1}. FT NON_TER 352 352 {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 //