CYB_THEPA
ID CYB_THEPA Reviewed; 363 AA.
AC Q36099;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 92.
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=MT-CYB; Synonyms=COB, CYTB, MTCYB;
OS Theileria parva (East coast fever infection agent).
OG Mitochondrion.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5875;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Muguga;
RX PubMed=8112303; DOI=10.1002/j.1460-2075.1994.tb06333.x;
RA Kairo A., Fairlamb A., Gobright E., Nene V.;
RT "A 7.1 kb linear DNA molecule of Theileria parva has scrambled rDNA
RT sequences and open reading frames for mitochondrially-encoded proteins.";
RL EMBO J. 13:898-905(1994).
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: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein. {ECO:0000250}.
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 an even number of transmembrane helices,
CC fewer than predicted by bioinformatics tools.
CC {ECO:0000250|UniProtKB:P00163}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA80800.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z23263; CAA80800.1; ALT_INIT; Genomic_DNA.
DR PIR; S41691; S41691.
DR RefSeq; YP_001994287.1; NC_011005.1.
DR AlphaFoldDB; Q36099; -.
DR SMR; Q36099; -.
DR GeneID; 6741533; -.
DR InParanoid; Q36099; -.
DR Proteomes; UP000001949; Mitochondrion.
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:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
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; IPR016174; Di-haem_cyt_TM.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR Pfam; PF00033; Cytochrome_B; 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; Reference proteome; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..363
FT /note="Cytochrome b"
FT /id="PRO_0000232682"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 67..89
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00163"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 73
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 87
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 168
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 182
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 187
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00157"
SQ SEQUENCE 363 AA; 40985 MW; 9475AFE43DDE891E CRC64;
MNMFNAHIPS YLVPKNLNSN WNVGFILGIL LILQILSGLL LTFFYVPCKE GAFESLSRLV
TETQFGWFVR LYHSVGVSFY FFFMFIHIIK GMWYSSKYMP WSWYSGIVIL ILSIVIAFTG
YVLPDGQMSF WGATVISNLL EWFGKAKVIT FGGFTVGPET LKRFFILHFV LPAVVLVIVL
LHLYFLHREG SSNPLTLAEA VALLKFYQLI LFSDVKFLVI ISMFIGPQVG YGIWTLFQAD
NDNSILSSSE NTPAHIIPEW YLLLFYATLK VFPTKVSGLV AMVVVLKLLI ILVESRSKSQ
AVSTAHHHRV WTTTSVPLVP ALFLLGCIGR MVINLDLIII GIYGVLLSTT FVQKLLDSSR
VRA
