位置:首页 > 蛋白库 > CYB_FARAB
CYB_FARAB
ID   CYB_FARAB               Reviewed;         371 AA.
AC   O48087;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, 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=MT-CYB; Synonyms=COB, CYTB, MTCYB;
OS   Farancia abacura (Mud snake).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Dipsadidae; Farancia.
OX   NCBI_TaxID=39306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Campbell B.N.;
RT   "Hic Sunt Serpentes -- molecular phylogenetics and the Boidae (Serpentes:
RT   Booidea).";
RL   Thesis (1997), Queen's University / Kingston, Canada.
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:P00157}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P00157};
CC       Note=Binds 2 heme b groups non-covalently.
CC       {ECO:0000250|UniProtKB:P00157};
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:0000250|UniProtKB:P00157}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00157}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00157}.
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 full-length protein contains only eight transmembrane
CC       helices, not nine as predicted by bioinformatics tools.
CC       {ECO:0000250|UniProtKB:P00157}.
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; U69832; AAC01866.1; -; 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-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..371
FT                   /note="Cytochrome b"
FT                   /id="PRO_0000060971"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        69..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        339..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   BINDING         75
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:0000250|UniProtKB:P00157"
FT   BINDING         89
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:0000250|UniProtKB:P00157"
FT   BINDING         174
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:0000250|UniProtKB:P00157"
FT   BINDING         188
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:0000250|UniProtKB:P00157"
FT   BINDING         193
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
SQ   SEQUENCE   371 AA;  41852 MW;  7468B8C42F6B7887 CRC64;
     MPNQHMLLLS NLLPVGLNIS TWWNFGSMLL TCLALQITTG FFLAIHYTAN INLAFSSIIH
     ITRDVPHGWI MQNLHATGAS MFFICIYIHI ARGLYYGSYL NKGVWLSGTI LLITLMATAF
     FGYVLPWGQM SFWAATVITN LLTAVPYLGT PLTTWLWGGF SINDPTLTRF FALHLILPFA
     IISLSSIHII LLHNEGSSNP LGXNSDIDKI PFHPYHSHKD ALMLTILITL LFIILSFTPN
     IFNDPENFSK ANPLVTPQHI KPEWYFLFAY GILRSIPNKL GGTLALILSV TILLTVPFTH
     TSYVRSMTFR PLAQLMFWTL IATFMTITWA ATKPVEPPFT IIGQTTSILY FSFFIINPLL
     GWLENKIMIT H
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024