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CYF_WHEAT
ID   CYF_WHEAT               Reviewed;         320 AA.
AC   P05151;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 3.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Cytochrome f;
DE   Flags: Precursor;
GN   Name=petA;
OS   Triticum aestivum (Wheat).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Willey D.L., Howe C.J., Auffret A.D., Bowman C.M., Dyer T.A., Gray J.C.;
RT   "Location and nucleotide sequence of the gene for cytochrome f in wheat
RT   chloroplast DNA.";
RL   Mol. Gen. Genet. 194:416-422(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring;
RA   Ogihara Y., Isono K., Kojima T., Endo A., Hanaoka M., Shiina T.,
RA   Terachi T., Utsugi S., Murata M., Mori N., Takumi S., Ikeo K., Gojobori T.,
RA   Murai R., Murai K., Matsuoka Y., Ohnishi Y., Tajiri H., Tsunewaki K.;
RT   "Chinese spring wheat (Triticum aestivum L.) chloroplast genome: complete
RT   sequence and contig clones.";
RL   Plant Mol. Biol. Rep. 18:243-253(2000).
CC   -!- FUNCTION: Component of the cytochrome b6-f complex, which mediates
CC       electron transfer between photosystem II (PSII) and photosystem I
CC       (PSI), cyclic electron flow around PSI, and state transitions.
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC       Note=Binds 1 heme group covalently. {ECO:0000250};
CC   -!- SUBUNIT: The 4 large subunits of the cytochrome b6-f complex are
CC       cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and
CC       the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and
CC       PetN. The complex functions as a dimer (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome f family. {ECO:0000305}.
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DR   EMBL; X00538; CAA25213.1; -; Genomic_DNA.
DR   EMBL; AB042240; BAB47046.1; -; Genomic_DNA.
DR   PIR; S07296; S07296.
DR   RefSeq; NP_114271.1; NC_002762.1.
DR   AlphaFoldDB; P05151; -.
DR   SMR; P05151; -.
DR   STRING; 4565.EPlTAEP00000010051; -.
DR   PRIDE; P05151; -.
DR   GeneID; 803113; -.
DR   KEGG; taes:803113; -.
DR   eggNOG; ENOG502QPT8; Eukaryota.
DR   HOGENOM; CLU_033498_0_0_1; -.
DR   Proteomes; UP000019116; Chloroplast.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031361; C:integral component of thylakoid membrane; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.40.830; -; 1.
DR   HAMAP; MF_00610; Cytb6_f_cytF; 1.
DR   InterPro; IPR024058; Cyt-f_TM.
DR   InterPro; IPR002325; Cyt_f.
DR   InterPro; IPR024094; Cyt_f_lg_dom.
DR   InterPro; IPR036826; Cyt_f_lg_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF01333; Apocytochr_F_C; 1.
DR   Pfam; PF16639; Apocytochr_F_N; 1.
DR   PRINTS; PR00610; CYTOCHROMEF.
DR   SUPFAM; SSF103431; SSF103431; 1.
DR   SUPFAM; SSF49441; SSF49441; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   PROSITE; PS51010; CYTF; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Photosynthesis; Plastid; Reference proteome; Signal; Thylakoid;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000250"
FT   CHAIN           36..320
FT                   /note="Cytochrome f"
FT                   /id="PRO_0000023840"
FT   TRANSMEM        286..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         36
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        291..294
FT                   /note="FFFA -> NVLE (in Ref. 2; BAB47046)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        303..307
FT                   /note="LVLKK -> WFSST (in Ref. 2; BAB47046)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   320 AA;  35363 MW;  721D2B3188552289 CRC64;
     MENRNTFSWV KEQITRSISV SIMIYVITRT SISNAYPIFA QQGYENPREA TGRIVCANCH
     LASKPVDIEV PQAVLPDTVF EAVLRIPYDM QLKQVLANGK KGGLNVGAVL ILPEGFELAP
     PDRISPELKE KIGNLAFQSY RPDKKNILVI GPVPGKKYSE IVFPILSPDP ATKKDAHFLK
     YPIYVGGNRG RGQIYPDGSK SNNTVYNATS TGIVRKILRK EKGGYEISIV DASDGRQVID
     IIPPGPELLV SEGESIKLDQ PLTSNPNVGG FGQGDAEIVL QDPLRVQGLL FFFASVILAQ
     VFLVLKKKQF EKVQLYEMNF
 
 
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