ID A0A0F6UV47_ERYTA Unreviewed; 304 AA. AC A0A0F6UV47; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 16-SEP-2015, entry version 2. DE RecName: Full=Cytochrome b {ECO:0000256|RuleBase:RU000300}; DE Flags: Fragment; OS Eryx tataricus (Tartar sand boa). OG Mitochondrion {ECO:0000313|EMBL:AKE78823.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Henophidia; Boidae; Erycinae; Eryx. OX NCBI_TaxID=51873 {ECO:0000313|EMBL:AKE78823.1}; RN [1] {ECO:0000313|EMBL:AKE78823.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=22_Birjand {ECO:0000313|EMBL:AKE78823.1}, and 30_Shaskoh RC {ECO:0000313|EMBL:AKE78822.1}; RA Rastegar-Pouyani E., Eskandarzadeh N., Darvish J.; RT "Re-evaluation of the taxonomic status of sand boas of the genus Eryx RT (Daudin, 1803) (Serpentes: Boidae) in northeastern Iran using RT sequences of the mitochondrial genome."; RL Zool Middle East 60:320-326(2014). 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. {ECO:0000256|RuleBase:RU000300}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|RuleBase:RU000300}; CC Note=Binds 2 heme groups non-covalently. CC {ECO:0000256|RuleBase:RU000300}; CC -!- SIMILARITY: Belongs to the cytochrome b family. CC {ECO:0000256|RuleBase:RU000300}. 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; KJ841067; AKE78822.1; -; Genomic_DNA. DR EMBL; KJ841068; AKE78823.1; -; Genomic_DNA. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR Gene3D; 1.20.810.10; -; 1. DR InterPro; IPR005798; Cyt_b/b6_C. DR InterPro; IPR005797; Cyt_b/b6_N. DR InterPro; IPR027387; Cytb/b6-like. DR InterPro; IPR016174; Di-haem_cyt_TM. DR Pfam; PF13631; Cytochrom_B_N_2; 1. DR SUPFAM; SSF81342; SSF81342; 1. DR PROSITE; PS51003; CYTB_CTER; 1. DR PROSITE; PS51002; CYTB_NTER; 1. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|RuleBase:RU000300}; KW Heme {ECO:0000256|RuleBase:RU000300}; KW Iron {ECO:0000256|RuleBase:RU000300}; KW Membrane {ECO:0000256|RuleBase:RU000300}; KW Metal-binding {ECO:0000256|RuleBase:RU000300}; KW Mitochondrion {ECO:0000256|RuleBase:RU000300, KW ECO:0000313|EMBL:AKE78823.1}; KW Respiratory chain {ECO:0000256|RuleBase:RU000300}; KW Transmembrane {ECO:0000256|RuleBase:RU000300}; KW Transport {ECO:0000256|RuleBase:RU000300}. FT NON_TER 1 1 {ECO:0000313|EMBL:AKE78823.1}. FT NON_TER 304 304 {ECO:0000313|EMBL:AKE78823.1}. SQ SEQUENCE 304 AA; 34809 MW; 82A8B158A78B83EF CRC64; NFGSMLLACS SMQVLTGFFL AVHYTANINL AFSSIVHITR DVPYGWMMQN LHAIGASMFF ICIYIHIARG LYYGSYLNKK TWLSGTTLLI MLMATAFFGY VLPWGQMSFW AATVITNLLT AIPYLGTTMT TWLWGGFAIN DPTLTRFFAL HFILPFGIIS LSSLHIMLLH EDGSSNPLGT NSDIDKIPFH PYHTYKDLLM LSLMVLMLLM TVSFLPDIFN DPENFSKANP LVTPQHINQN DTSYSHMASY DQSQTNLEAH WPWRYQLFYL QSHLHTHQPS DPYSDLSYNS YSEHQHLQLH EQPQ //