ID A8V364_9DIPT Unreviewed; 238 AA. AC A8V364; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 24-JUL-2024, entry version 63. DE RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, ECO:0000256|RuleBase:RU362117}; DE Flags: Fragment; OS Sergentomyia sintoni. OG Mitochondrion {ECO:0000313|EMBL:ABW96291.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Nematocera; Psychodoidea; Psychodidae; OC Sergentomyia; Sergentomyia. OX NCBI_TaxID=447276 {ECO:0000313|EMBL:ABW96291.1}; RN [1] {ECO:0000313|EMBL:ABW96291.1} RP NUCLEOTIDE SEQUENCE. RA Parvizi P., Amirkhani A.; RT "Mitochondrial DNA characterization of populations of Sergentomyia sintoni RT and finding mammalian Leishmania infections in this sandfly by using ITS- RT rDNA gene."; RL Iran. J. Vet. Res. 9:9-18(2008). 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 b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|RuleBase:RU362117}; CC Note=Binds 2 heme groups non-covalently. CC {ECO:0000256|RuleBase:RU362117}; CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b, CC cytochrome c1 and the Rieske protein. {ECO:0000256|ARBA:ARBA00011649}. 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 -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000256|PROSITE- CC ProRule:PRU00967, 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; EU159492; ABW96291.1; -; Genomic_DNA. DR AlphaFoldDB; A8V364; -. DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. 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; cd00290; cytochrome_b_C; 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; IPR048260; Cytochrome_b_C_euk/bac. DR InterPro; IPR016174; Di-haem_cyt_TM. DR PANTHER; PTHR19271; CYTOCHROME B; 1. DR PANTHER; PTHR19271:SF16; CYTOCHROME B; 1. DR Pfam; PF00032; Cytochrom_B_C; 1. DR Pfam; PF13631; Cytochrom_B_N_2; 1. DR SUPFAM; SSF81648; a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1. DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 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, ECO:0000256|PROSITE- KW ProRule:PRU00967}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362117}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362117}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE- KW ProRule:PRU00967}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU362117}; 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, ECO:0000256|PROSITE- KW ProRule:PRU00967}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE- KW ProRule:PRU00967}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PROSITE- KW ProRule:PRU00967}; Ubiquinone {ECO:0000256|ARBA:ARBA00023075}. FT TRANSMEM 7..27 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 39..61 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 90..111 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 149..168 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 180..201 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 207..225 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT DOMAIN 1..70 FT /note="Cytochrome b/b6 N-terminal region profile" FT /evidence="ECO:0000259|PROSITE:PS51002" FT DOMAIN 71..238 FT /note="Cytochrome b/b6 C-terminal region profile" FT /evidence="ECO:0000259|PROSITE:PS51003" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ABW96291.1" SQ SEQUENCE 238 AA; 27254 MW; 9C19F7D9B860E5F0 CRC64; FWGATVITNL LSAIPYLGTM LVQWIWGGFA VDNATLTRFF TFHFLFPFIV AAMTMIHLLF LHQTGSNNPL GLNSNSDKIP FHPYFSFKDL IGFIVMLMLL TFLTIISPYF LGDPDNFIPA NPLVTPPHIQ PEWYFLFAYA ILRSIPNKLG GVIALVMSIA ILFVLPILHV SKSQGLQFYP INQILFWYMV ITIVLLTWIG ARPVEDPYIL TGQILTVLYF LYYLLNPLII KMWDNLLN //