ID A0A0F6UV47_ERYTA Unreviewed; 236 AA. AC A0A0F6UV47; A0A0F6S1Z1; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 2. DT 29-MAY-2024, entry version 21. DE RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531}; DE AltName: Full=Complex III subunit 3 {ECO:0000256|ARBA:ARBA00031681}; DE AltName: Full=Complex III subunit III {ECO:0000256|ARBA:ARBA00032600}; DE AltName: Full=Cytochrome b-c1 complex subunit 3 {ECO:0000256|ARBA:ARBA00029812}; DE AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome b subunit {ECO:0000256|ARBA:ARBA00032818}; DE Flags: Fragment; OS Eryx tataricus (Tartar sand boa). OG Mitochondrion {ECO:0000313|EMBL:AKE78823.2}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Henophidia; Boidae; Erycinae; Eryx. OX NCBI_TaxID=51873 {ECO:0000313|EMBL:AKE78823.2}; RN [1] {ECO:0000313|EMBL:AKE78823.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_Fariman {ECO:0000313|EMBL:AKE78825.2}, 22_Birjand RC {ECO:0000313|EMBL:AKE78823.2}, 30_Shaskoh RC {ECO:0000313|EMBL:AKE78822.2}, 4_Fariman RC {ECO:0000313|EMBL:AKE78819.2}, 6_Fariman RC {ECO:0000313|EMBL:AKE78821.2}, and ERP_1051_Torbat_Jam RC {ECO:0000313|EMBL:AKE78809.2}; 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 sequences of RT the mitochondrial genome."; RL Zool Middle East 60:320-326(2014). RN [2] {ECO:0000313|EMBL:AKE78823.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1_Fariman {ECO:0000313|EMBL:AKE78825.2}, 22_Birjand RC {ECO:0000313|EMBL:AKE78823.2}, 30_Shaskoh RC {ECO:0000313|EMBL:AKE78822.2}, 4_Fariman RC {ECO:0000313|EMBL:AKE78819.2}, 6_Fariman RC {ECO:0000313|EMBL:AKE78821.2}, and ERP_1051_Torbat_Jam RC {ECO:0000313|EMBL:AKE78809.2}; RA Ploux O.; RL Submitted (MAR-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|ARBA:ARBA00002566}. CC -!- SUBUNIT: The cytochrome bc1 complex contains 3 respiratory subunits CC (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and UQCRC2) and CC probably 6 low-molecular weight proteins. CC {ECO:0000256|ARBA:ARBA00011660}. 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}; Multi-pass membrane CC protein {ECO:0000256|ARBA:ARBA00004448}. 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; KJ841054; AKE78809.2; -; Genomic_DNA. DR EMBL; KJ841064; AKE78819.2; -; Genomic_DNA. DR EMBL; KJ841066; AKE78821.2; -; Genomic_DNA. DR EMBL; KJ841067; AKE78822.2; -; Genomic_DNA. DR EMBL; KJ841068; AKE78823.2; -; Genomic_DNA. DR EMBL; KJ841070; AKE78825.2; -; Genomic_DNA. DR AlphaFoldDB; A0A0F6UV47; -. DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:TreeGrafter. DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:TreeGrafter. DR CDD; cd00284; Cytochrome_b_N; 1. DR InterPro; IPR005798; Cyt_b/b6_C. DR InterPro; IPR005797; Cyt_b/b6_N. DR InterPro; IPR027387; Cytb/b6-like_sf. DR InterPro; IPR048259; Cytochrome_b_N_euk/bac. DR InterPro; IPR016174; Di-haem_cyt_TM. DR PANTHER; PTHR19271; CYTOCHROME B; 1. DR PANTHER; PTHR19271:SF16; CYTOCHROME B; 1. DR Pfam; PF00033; Cytochrome_B; 1. DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1. DR PROSITE; PS51003; CYTB_CTER; 1. DR PROSITE; PS51002; CYTB_NTER; 1. PE 4: Predicted; KW Electron transport {ECO:0000256|ARBA:ARBA00022982}; KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000313|EMBL:AKE78823.2}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}; KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075}. FT TRANSMEM 49..69 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 81..102 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 108..135 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 147..168 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 198..219 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..178 FT /note="Cytochrome b/b6 N-terminal region profile" FT /evidence="ECO:0000259|PROSITE:PS51002" FT DOMAIN 179..236 FT /note="Cytochrome b/b6 C-terminal region profile" FT /evidence="ECO:0000259|PROSITE:PS51003" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AKE78823.2" FT NON_TER 236 FT /evidence="ECO:0000313|EMBL:AKE78823.2" SQ SEQUENCE 236 AA; 26567 MW; 4FB435A8E1044D2B CRC64; NFGSMLLACS SMQVLTGFFL AVHYTANINL AFSSIVHITR DVPYGWMMQN LHAIGASMFF ICIYIHIARG LYYGSYLNKK TWLSGTTLLI MLMATAFFGY VLPWGQMSFW AATVITNLLT AIPYLGTTMT TWLWGGFAIN DPTLTRFFAL HFILPFGIIS LSSLHIMLLH EDGSSNPLGT NSDIDKIPFH PYHTYKDLLM LSLMVLMLLM TVSFLPDIFN DPENFSKANP LVTPQH //