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CYB_LECMU
ID   CYB_LECMU               Reviewed;         385 AA.
AC   Q8HG55;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Cytochrome b;
DE   AltName: Full=Complex III subunit 3;
DE   AltName: Full=Complex III subunit III;
DE   AltName: Full=Cytochrome b-c1 complex subunit 3;
DE   AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome b subunit;
GN   Name=cob; Synonyms=cytB;
OS   Lecanicillium muscarium (Verticillium lecanii).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces.
OX   NCBI_TaxID=2231603;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15341915; DOI=10.1016/j.fgb.2004.07.003;
RA   Kouvelis V.N., Ghikas D.V., Typas M.A.;
RT   "The analysis of the complete mitochondrial genome of Lecanicillium
RT   muscarium (synonym Verticillium lecanii) suggests a minimum common gene
RT   organization in mtDNAs of Sordariomycetes: phylogenetic implications.";
RL   Fungal Genet. Biol. 41:930-940(2004).
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:0000250|UniProtKB:P00163}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P00163};
CC       Note=Binds 2 heme b groups non-covalently.
CC       {ECO:0000250|UniProtKB:P00163};
CC   -!- SUBUNIT: Fungal cytochrome b-c1 complex contains 10 subunits; 3
CC       respiratory subunits, 2 core proteins and 5 low-molecular weight
CC       proteins. Cytochrome b-c1 complex is a homodimer.
CC       {ECO:0000250|UniProtKB:P00163}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00163}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00163}.
CC   -!- MISCELLANEOUS: Heme 1 (or BL or b562) is low-potential and absorbs at
CC       about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs
CC       at about 566 nm. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00967, ECO:0000255|PROSITE-ProRule:PRU00968}.
CC   -!- CAUTION: The protein contains only eight transmembrane helices, not
CC       nine as predicted by bioinformatics tools.
CC       {ECO:0000250|UniProtKB:P00163}.
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DR   EMBL; AF487277; AAO14664.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8HG55; -.
DR   SMR; Q8HG55; -.
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-KW.
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; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Respiratory chain; Transmembrane;
KW   Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN           1..385
FT                   /note="Cytochrome b"
FT                   /id="PRO_0000061746"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        76..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        322..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00163"
FT   BINDING         82
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:0000255|PROSITE-ProRule:PRU00968"
FT   BINDING         96
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:0000255|PROSITE-ProRule:PRU00968"
FT   BINDING         183
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:0000255|PROSITE-ProRule:PRU00968"
FT   BINDING         197
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:0000255|PROSITE-ProRule:PRU00968"
FT   BINDING         202
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
SQ   SEQUENCE   385 AA;  43339 MW;  505CD68116E40545 CRC64;
     MRILKSHPLL KLLNAYIIDH SQPTNINYLW NFGSLLGLCL GIQIITGVTL AMHYNPSVAE
     AFNSVEHIMR DVNNGWLIRY LHSNTASAFF FLVYLHIGRG FYYGSYRSPR TLAWILGVII
     LILMMGIGFL GYVLPYGQMS LWGATVITNL ISAIPWIGQD IVEFIWGGFS VNNATLNRFF
     ALHFVLPFVL AALVIMHLIA VHETAGASNP LGTPAYYDRI PFAPYYLFKD LITIFLFMFG
     LSIFVFFMPN VLGDSENYIM ANPMQTPAAI VPEWYLLPFY AILRSIPNKL LGVIAMFASL
     VILMVLPKTD LGITKGLQFR PLSKIAFYLF VTNFLLLLQL GAKHVESPFI EFGQISTALY
     FAYYLIIMPG VSILENTLID LSQKG
 
 
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