ID K4K2Q2_9TELE Unreviewed; 380 AA. AC K4K2Q2; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 02-JUN-2021, entry version 35. DE RecName: Full=Cytochrome b {ECO:0000256|RuleBase:RU362117}; GN Name=cytb {ECO:0000313|EMBL:AFU93285.1}; GN Synonyms=CYTB {ECO:0000313|EMBL:QIE12074.1}; OS Salvethymus svetovidovi (long-finned charr). OG Mitochondrion {ECO:0000313|EMBL:AFU93285.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes; OC Salmonidae; Salmoninae; Salvethymus. OX NCBI_TaxID=152109 {ECO:0000313|EMBL:AFU93285.1}; RN [1] {ECO:0000313|EMBL:AFU93285.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=#97 {ECO:0000313|EMBL:AFU93285.1}; RX PubMed=23071608; DOI=10.1371/journal.pone.0046662; RA Crete-Lafreniere A., Weir L.K., Bernatchez L.; RT "Framing the salmonidae family phylogenetic portrait: a more complete RT picture from increased taxon sampling."; RL PLoS ONE 7:E46662-E46662(2012). RN [2] {ECO:0000313|EMBL:QBF58665.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SVET17_001 {ECO:0000313|EMBL:QBF58665.1}, SVET17_002 RC {ECO:0000313|EMBL:QBF58666.1}, SVET17_003 RC {ECO:0000313|EMBL:QBF58667.1}, and SVET17_004 RC {ECO:0000313|EMBL:QBF58668.1}; RA Oleinik A.G., Semenchenko A.A., Kukhlevskiy A.D., Skurikhina L.A.; RT "The relationships of arctic phylogenetic group of charrs of genus RT Salvelinus revised."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:QIE12074.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SVET17_001 {ECO:0000313|EMBL:QIE12074.1}, SVET17_002 RC {ECO:0000313|EMBL:QIE12087.1}, and SVET17_004 RC {ECO:0000313|EMBL:QIE12100.1}; RA Oleinik A.G., Skurikhina L.A., Kukhlevsky A.D., Semenchenko A.A.; RT "First report of three complete mitochondrial genomes#of the long-finned RT charr Salvethymus svetovidovi Chereshnev et Skopetz, 1990 (Salmoniformes: RT Salmonidae) with phylogenetic consideration."; RL Mitochondrial DNA Part B Resour 4:2464-2466(2019). 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|ARBA:ARBA00002566, CC ECO:0000256|RuleBase:RU362117}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|ARBA:ARBA00001971}; 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|ARBA:ARBA00004448, CC ECO:0000256|RuleBase:RU362117}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004448}. 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; JX960859; AFU93285.1; -; Genomic_DNA. DR EMBL; MH430807; QBF58665.1; -; Genomic_DNA. DR EMBL; MH430808; QBF58666.1; -; Genomic_DNA. DR EMBL; MH430809; QBF58667.1; -; Genomic_DNA. DR EMBL; MH430810; QBF58668.1; -; Genomic_DNA. DR EMBL; MK695627; QIE12074.1; -; Genomic_DNA. DR EMBL; MK695628; QIE12087.1; -; Genomic_DNA. DR EMBL; MK695629; QIE12100.1; -; 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:0022904; P:respiratory electron transport chain; 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|ARBA:ARBA00022982, KW ECO:0000256|RuleBase:RU362117}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038885-2}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038885-2}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362117}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR038885-2}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, KW ECO:0000256|RuleBase:RU362117}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660, KW ECO:0000256|RuleBase:RU362117}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU362117}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU362117}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362117}; KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075}. FT TRANSMEM 29..52 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 87..107 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 113..133 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 145..166 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 178..200 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 229..250 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 288..308 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 320..341 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 347..372 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT DOMAIN 1..209 FT /note="CYTB_NTER" FT /evidence="ECO:0000259|PROSITE:PS51002" FT DOMAIN 210..380 FT /note="CYTB_CTER" FT /evidence="ECO:0000259|PROSITE:PS51003" FT METAL 83 FT /note="Iron 1 (heme b562 axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT METAL 97 FT /note="Iron 2 (heme b566 axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT METAL 182 FT /note="Iron 1 (heme b562 axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT METAL 196 FT /note="Iron 2 (heme b566 axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT BINDING 201 FT /note="Ubiquinone" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-1" SQ SEQUENCE 380 AA; 42344 MW; 19B0284D48D93EFF CRC64; MANLRKTHPL LKIANDALVD LPAPSNISVW WNFGSLLGLC LATQILTGLF LAMHYTSDIS TAFSSVCHIC RDVSYGWLIR NIHANGASFF FICIYMHIAR GLYYGSYLYK ETWNIGVVLL LLTMMTAFVG YVLPWGQMSF WGATVITNLF SAVPYVGGAL VQWIWGGFSV DSATLTRFFA FHFLFPFVIA AATVLHLLFL HETGSNNPAG INSDADKISF HPYFSYKDLL GFVAMLLGLT ALALFTPNLL GDPDNFTPAN PLVTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALLFSILV LMVVPILHTS KQRGLTFRPL TQFLFWTLVA DMLILTWIGG MPVEHPFIII GQVASVIYFT IFLILAPLAG WAENKALEWT //