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FGSR_GIBZE
ID   FGSR_GIBZE              Reviewed;         492 AA.
AC   I1RC73; A0A098D5P4;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Zn(2)-C6 fungal-type transcription factor {ECO:0000303|PubMed:30874562};
GN   Name=SR {ECO:0000303|PubMed:30874562}; ORFNames=FG01176, FGRAMPH1_01T02919;
OS   Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS   / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=229533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA   Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA   Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA   Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA   Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA   Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA   Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA   King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA   Hammond-Kosack K.E.;
RT   "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT   graminearum.";
RL   BMC Genomics 16:544-544(2015).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP   THR-82; SER-92; SER-102; THR-217 AND SER-305, MUTAGENESIS OF THR-82;
RP   SER-92; SER-102; THR-217 AND SER-305, AND INTERACTION WITH HOG1.
RX   PubMed=30874562; DOI=10.1038/s41467-019-09145-6;
RA   Liu Z., Jian Y., Chen Y., Kistler H.C., He P., Ma Z., Yin Y.;
RT   "A phosphorylated transcription factor regulates sterol biosynthesis in
RT   Fusarium graminearum.";
RL   Nat. Commun. 10:1228-1228(2019).
CC   -!- FUNCTION: Transcription factor that targets gene promoters containing 2
CC       conserved CGAA repeat sequences (PubMed:30874562). Positively regulates
CC       the expression of ergosterol biosynthesis genes including CYP51A and
CC       CYP51B encoding the sterol 14-alpha demethylase, and ERG6A and ERG6B
CC       encoding the sterol 24-C-methyltransferase (PubMed:30874562).
CC       {ECO:0000269|PubMed:30874562}.
CC   -!- SUBUNIT: Interacts with HOG1. {ECO:0000269|PubMed:30874562}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30874562}.
CC   -!- PTM: Phosphorylation at Thr-82, Ser-92, Ser-102, thr-117 and ser-305 by
CC       HOG1 is required for regulating expression of ergosterol biosynthesis
CC       genes. {ECO:0000269|PubMed:30874562}.
CC   -!- DISRUPTION PHENOTYPE: Reduces the production of ergosterol
CC       (PubMed:30874562). Leads to increased sensitivity to azole compounds,
CC       but not to iprodione and fludioxonil that target the high osmolarity
CC       glycerol (HOG) pathway (PubMed:30874562).
CC       {ECO:0000269|PubMed:30874562}.
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DR   EMBL; HG970332; CEF73261.1; -; Genomic_DNA.
DR   RefSeq; XP_011316947.1; XM_011318645.1.
DR   SMR; I1RC73; -.
DR   GeneID; 23548625; -.
DR   KEGG; fgr:FGSG_01176; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G02919; -.
DR   eggNOG; ENOG502SP5N; Eukaryota.
DR   HOGENOM; CLU_024934_6_2_1; -.
DR   InParanoid; I1RC73; -.
DR   PHI-base; PHI:1933; -.
DR   PHI-base; PHI:6134; -.
DR   Proteomes; UP000070720; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; -; 1.
DR   InterPro; IPR021858; Fun_TF.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   Pfam; PF11951; Fungal_trans_2; 1.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..492
FT                   /note="Zn(2)-C6 fungal-type transcription factor"
FT                   /id="PRO_0000454349"
FT   DNA_BIND        14..41
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          58..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..106
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         82
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:30874562"
FT   MOD_RES         92
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:30874562"
FT   MOD_RES         102
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:30874562"
FT   MOD_RES         217
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:30874562"
FT   MOD_RES         305
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:30874562"
FT   MUTAGEN         82
FT                   /note="T->A: Impairs phosphorylation by HOG1, blocks
FT                   induction of CYP51A expression and exhibits
FT                   hypersensitivity to tebuconazole; when associated with A-
FT                   92, A-102, A-217 and A-305."
FT                   /evidence="ECO:0000269|PubMed:30874562"
FT   MUTAGEN         82
FT                   /note="T->D: Mimics phosphorylation by HOG1; when
FT                   associated with D-92, D-102, D-217 and D-305."
FT                   /evidence="ECO:0000269|PubMed:30874562"
FT   MUTAGEN         92
FT                   /note="S->A: Impairs phosphorylation by HOG1, blocks
FT                   induction of CYP51A expression and exhibits
FT                   hypersensitivity to tebuconazole; when associated with A-
FT                   82, A-102, A-217 and A-305."
FT                   /evidence="ECO:0000269|PubMed:30874562"
FT   MUTAGEN         92
FT                   /note="S->D: Mimics phosphorylation by HOG1; when
FT                   associated with D-82, D-102, D-217 and D-305."
FT                   /evidence="ECO:0000269|PubMed:30874562"
FT   MUTAGEN         102
FT                   /note="S->A: Impairs phosphorylation by HOG1, blocks
FT                   induction of CYP51A expression and exhibits
FT                   hypersensitivity to tebuconazole; when associated with A-
FT                   82, A-92, A-217 and A-305."
FT                   /evidence="ECO:0000269|PubMed:30874562"
FT   MUTAGEN         102
FT                   /note="S->D: Mimics phosphorylation by HOG1; when
FT                   associated with D-82, D-92, D-217 and D-305."
FT                   /evidence="ECO:0000269|PubMed:30874562"
FT   MUTAGEN         217
FT                   /note="T->A: Impairs phosphorylation by HOG1, blocks
FT                   induction of CYP51A expression and exhibits
FT                   hypersensitivity to tebuconazole; when associated with A-
FT                   82, A-92, A-102 and A-305."
FT                   /evidence="ECO:0000269|PubMed:30874562"
FT   MUTAGEN         217
FT                   /note="T->D: Mimics phosphorylation by HOG1; when
FT                   associated with D-82, D-92, D-102 and D-305."
FT                   /evidence="ECO:0000269|PubMed:30874562"
FT   MUTAGEN         305
FT                   /note="S->A: Impairs phosphorylation by HOG1, blocks
FT                   induction of CYP51A expression and exhibits
FT                   hypersensitivity to tebuconazole; when associated with A-
FT                   82, A-92, A-102 and A-217."
FT                   /evidence="ECO:0000269|PubMed:30874562"
FT   MUTAGEN         305
FT                   /note="S->D: Mimics phosphorylation by HOG1; when
FT                   associated with D-82, D-92, D-102 and D-217."
FT                   /evidence="ECO:0000269|PubMed:30874562"
SQ   SEQUENCE   492 AA;  54123 MW;  FC67D7AEA3DCC187 CRC64;
     MPPRRSHKKS RAGCRRCKNR KIKCDEVHPR CGNCAKHGVP CDFSNPDVLE ELAISTNTST
     ESVGAPTPSP APTVNFNSAP RTPLTRPRAP SSPARAPRPN PSPPTSVYSQ PSISSSTNTI
     DHGERMLELR LMHHYTNVTS KTLLTNSPAA EDIWQRAVPQ MAFSGNGKTY LADAILSVAA
     LHLRSMSPND KALVRASHAY SASSLSAFGA SLGAGITPEN AEALFLTATL IAFQASASRI
     FVKDDGDAAP GDPTVRYVPP LSWFHAFQGV KTVVANSWQW IHHSDIVKVI IDSQPSFQLN
     LNPRSPDSFF GHMLEGLADE LSNEDPRLVA STTQAYSHAV SVLNWAHKNY HAAAALTFTA
     TVSKRYVDLV DARRPRALAI LACFFALLKR MDNVWWLQDV ARREVMGLVS LFEPGSKWWR
     HLEWPIRIAV LDGSSIPQDI WGTELEEQAP EQQNVLGSMT QHIEMFAEML NQHTQPPIPI
     ADEDLIVPDS PD
 
 
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