ID   A0A8K1EMT2_9RODE        Unreviewed;       374 AA.
AC   A0A8K1EMT2;
DT   03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT   03-AUG-2022, sequence version 1.
DT   05-FEB-2025, entry version 10.
DE   RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, ECO:0000256|RuleBase:RU362117};
DE   Flags: Fragment;
GN   Name=cytb {ECO:0000313|EMBL:QTF48693.1};
OS   Gerbilliscus guineae (Guinean gerbil).
OG   Mitochondrion {ECO:0000313|EMBL:QTF48693.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Gerbillinae; Gerbilliscus.
OX   NCBI_TaxID=410300 {ECO:0000313|EMBL:QTF48693.1};
RN   [1] {ECO:0000313|EMBL:QTF48693.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VN1167 {ECO:0000313|EMBL:QTF48693.1};
RA   Krasova J., Mikula O., Bryja J., Baptista N.L., Antonio T., Aghova T.,
RA   Sumbera R.;
RT   "Biogeography of Angolan rodents: The first glimpse based on phylogenetic
RT   evidence.";
RL   Divers. Distrib. 0:0-0(2021).
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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR038885-2};
CC       Note=Binds 2 heme groups non-covalently.
CC       {ECO:0000256|PIRSR:PIRSR038885-2};
CC   -!- SUBUNIT: The cytochrome bc1 complex contains 11 subunits: 3 respiratory
CC       subunits (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and
CC       UQCRC2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7,
CC       UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of
CC       UQCRFS1). This cytochrome bc1 complex then forms a dimer.
CC       {ECO:0000256|ARBA:ARBA00011088}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004448}.
CC   -!- SIMILARITY: Belongs to the cytochrome b family.
CC       {ECO:0000256|RuleBase:RU362117}.
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DR   EMBL; MW537478; QTF48693.1; -; Genomic_DNA.
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:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:TreeGrafter.
DR   CDD; cd00290; cytochrome_b_C; 1.
DR   CDD; cd00284; Cytochrome_b_N; 1.
DR   FunFam; 1.20.810.10:FF:000002; Cytochrome b; 1.
DR   Gene3D; 1.20.810.10; Cytochrome Bc1 Complex, Chain 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; IPR030689; Cytochrome_b.
DR   InterPro; IPR048260; Cytochrome_b_C_euk/bac.
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; PF00032; Cytochrom_B_C; 1.
DR   Pfam; PF00033; Cytochrome_B; 1.
DR   PIRSF; PIRSF038885; COB; 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,
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        26..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        141..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        174..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        225..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        342..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   DOMAIN          1..205
FT                   /note="Cytochrome b/b6 N-terminal region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51002"
FT   DOMAIN          206..374
FT                   /note="Cytochrome b/b6 C-terminal region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51003"
FT   BINDING         79
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b562"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038885-2"
FT   BINDING         93
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b566"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038885-2"
FT   BINDING         178
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b562"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038885-2"
FT   BINDING         192
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b566"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038885-2"
FT   BINDING         197
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038885-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:QTF48693.1"
FT   NON_TER         374
FT                   /evidence="ECO:0000313|EMBL:QTF48693.1"
SQ   SEQUENCE   374 AA;  42176 MW;  61BBD262C2A882AF CRC64;
     RKSHPLLKII NHSFIDLPTP PNISSWWNFG SLLGLCLIIQ ITTGLFLAMH YTADTTTAFS
     SVSHICRDVN YGWLIRYMHA NGASMFFICL FIHIGRGIYY GSYLYTETWN IGVILLFAVM
     ATAFMGYVLP WGQMSFWGAT VITNLLSAIP YVGTTIVEWI WGGFSVDKAT LTRFFAFHFI
     LPFIIAALAV VHLLFLHETG SNNPMGINSN ADKIPFHPYY TIKDFLGAIL LLLLLMLMVL
     FSPDLLGDPD NYMPANPLNT PPHIKPEWYF LFAYAILRSI PNKLGGVLAL ILSILVLMIL
     PLIHTSKQRS LMFRPISQFM FWILVANLLV LTWIGGQPVE HPFVIIGQLA SISYFSIILV
     FLPIAGIIED HMLK
//