ID A0A3G1CWY9_ARCFO Unreviewed; 379 AA. AC A0A3G1CWY9; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 08-MAY-2019, entry version 3. DE RecName: Full=Cytochrome b {ECO:0000256|RuleBase:RU362117}; GN Name=CYTB {ECO:0000313|EMBL:AMM04980.1}; OS Arctocephalus forsteri (New Zealand fur seal) (Arctocephalus australis OS forsteri). OG Mitochondrion {ECO:0000313|EMBL:AMM04980.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Otariidae; OC Arctocephalus. OX NCBI_TaxID=29084 {ECO:0000313|EMBL:AMM04980.1}; RN [1] {ECO:0000313|EMBL:AMM04980.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NZFS22 {ECO:0000313|EMBL:AMM04980.1}, NZFS23 RC {ECO:0000313|EMBL:AMM04993.1}, and NZFS24 RC {ECO:0000313|EMBL:AMM05006.1}; RX PubMed=27246241; RA Emami-Khoyi A., Hartley D.A., Ross J.G., Murphy E.C., Paterson A.M., RA Cruickshank R.H., Else T.A.; RT "Complete mitochondrial genome of the stoat (Mustela erminea) and New RT Zealand fur seal (Arctocephalus forsteri) and their significance for RT mammalian phylogeny."; RL Mitochondrial DNA A DNA MappSeq Anal 27:4597-4599(2016). 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|RuleBase:RU362117}; CC Note=Binds 2 heme groups non-covalently. CC {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; KT693354; AMM04980.1; -; Genomic_DNA. DR EMBL; KT693355; AMM04993.1; -; Genomic_DNA. DR EMBL; KT693356; AMM05006.1; -; 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:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. 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|RuleBase:RU362117}; KW Iron {ECO:0000256|RuleBase:RU362117}; KW Membrane {ECO:0000256|RuleBase:RU362117}; KW Metal-binding {ECO:0000256|RuleBase:RU362117}; KW Mitochondrion {ECO:0000256|RuleBase:RU362117, KW ECO:0000313|EMBL:AMM04980.1}; 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 30 56 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 77 98 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 113 133 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 140 158 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 178 200 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 229 246 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 288 308 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 320 340 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 346 372 Helical. {ECO:0000256|RuleBase:RU362117}. FT DOMAIN 1 209 CYTB_NTER. {ECO:0000259|PROSITE:PS51002}. FT DOMAIN 210 379 CYTB_CTER. {ECO:0000259|PROSITE:PS51003}. SQ SEQUENCE 379 AA; 42575 MW; 417510B308CB36C6 CRC64; MTNIRKMHPL AKIINNSLID LPAPSNISAW WNFGSLLAVC LALQILTGLF LAMHYTSDTT TAFSSVTHIC RDVNYGWIIR YMHANGASMF FICLYMHVGR GLYYGSYTLM ETWNIGIILL FTIMATAFMG YVLPWGQMSF WGATVITNLL SAVPYVGTNL VEWIWGGFSV DKATLTRFFA FHFILPFVVS ALVMVHLLFL HETGSNNPSG VSSDSDKIPF HPYYTIKDIL GALLLILILM LLVMFSPDLL GDPDNYIPAN PLSTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALLLSILI LAIIPLLHTS KQRGMMFRPI SQFLFWLLVA DLLTLTWIGG QPVEHPFIAI GQLASILYFT ILLILMPIAG IIENHILKW //