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AURR1_GIBZE
ID   AURR1_GIBZE             Reviewed;         398 AA.
AC   I1RF54;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Aurofusarin biosynthesis regulatory protein aurR1 {ECO:0000303|PubMed:16879655};
DE   AltName: Full=Aurofusarin biosynthesis cluster protein R1 {ECO:0000303|PubMed:16879655};
DE   AltName: Full=Gibberella pigment protein 2 {ECO:0000303|PubMed:16461721};
GN   Name=aurR1 {ECO:0000303|PubMed:16879655};
GN   Synonyms=GIP2 {ECO:0000303|PubMed:16461721};
GN   ORFNames=FG02320, FGRAMPH1_01T05585;
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.
RX   PubMed=15809006; DOI=10.1016/j.fgb.2005.01.010;
RA   Malz S., Grell M.N., Thrane C., Maier F.J., Rosager P., Felk A.,
RA   Albertsen K.S., Salomon S., Bohn L., Schaefer W., Giese H.;
RT   "Identification of a gene cluster responsible for the biosynthesis of
RT   aurofusarin in the Fusarium graminearum species complex.";
RL   Fungal Genet. Biol. 42:420-433(2005).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16879655; DOI=10.1111/j.1365-2958.2006.05295.x;
RA   Frandsen R.J., Nielsen N.J., Maolanon N., Soerensen J.C., Olsson S.,
RA   Nielsen J., Giese H.;
RT   "The biosynthetic pathway for aurofusarin in Fusarium graminearum reveals a
RT   close link between the naphthoquinones and naphthopyrones.";
RL   Mol. Microbiol. 61:1069-1080(2006).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX   PubMed=16461721; DOI=10.1128/aem.72.2.1645-1652.2006;
RA   Kim J.E., Jin J., Kim H., Kim J.C., Yun S.H., Lee Y.W.;
RT   "GIP2, a putative transcription factor that regulates the aurofusarin
RT   biosynthetic gene cluster in Gibberella zeae.";
RL   Appl. Environ. Microbiol. 72:1645-1652(2006).
RN   [7]
RP   INDUCTION.
RX   PubMed=17897620; DOI=10.1016/j.bbrc.2007.09.027;
RA   Ochiai N., Tokai T., Nishiuchi T., Takahashi-Ando N., Fujimura M.,
RA   Kimura M.;
RT   "Involvement of the osmosensor histidine kinase and osmotic stress-
RT   activated protein kinases in the regulation of secondary metabolism in
RT   Fusarium graminearum.";
RL   Biochem. Biophys. Res. Commun. 363:639-644(2007).
CC   -!- FUNCTION: Transcription factor that specifically regulates the
CC       expression of the gene cluster that mediates the biosynthesis of
CC       aurofusarin, a red mycelium pigment which is acting as a mycotoxin
CC       (PubMed:15809006, PubMed:16879655, PubMed:16461721).
CC       {ECO:0000269|PubMed:15809006, ECO:0000269|PubMed:16461721,
CC       ECO:0000269|PubMed:16879655}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- INDUCTION: Expression correlates with aurofusarin production and is
CC       restricted to vegetative mycelia (PubMed:16461721). Expression is
CC       negatively regulated by the MAPK-mediated osmotic stress-signaling
CC       pathway (PubMed:17897620). {ECO:0000269|PubMed:16461721,
CC       ECO:0000269|PubMed:17897620}.
CC   -!- DISRUPTION PHENOTYPE: Leads to an albinos phenotype (PubMed:16879655).
CC       Inactivates the expression of the aurofusarin biosynthetic gene cluster
CC       (PubMed:16879655, PubMed:16461721). {ECO:0000269|PubMed:16461721,
CC       ECO:0000269|PubMed:16879655}.
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DR   EMBL; HG970332; CEF74597.1; -; Genomic_DNA.
DR   RefSeq; XP_011318229.1; XM_011319927.1.
DR   AlphaFoldDB; I1RF54; -.
DR   SMR; I1RF54; -.
DR   GeneID; 23549702; -.
DR   KEGG; fgr:FGSG_02320; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G05585; -.
DR   eggNOG; ENOG502SUCM; Eukaryota.
DR   HOGENOM; CLU_051725_1_0_1; -.
DR   InParanoid; I1RF54; -.
DR   PHI-base; PHI:1973; -.
DR   Proteomes; UP000070720; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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   GO; GO:0045122; P:aflatoxin biosynthetic process; IEA:InterPro.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; -; 1.
DR   InterPro; IPR013700; AflR.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   Pfam; PF08493; AflR; 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   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..398
FT                   /note="Aurofusarin biosynthesis regulatory protein aurR1"
FT                   /id="PRO_0000441084"
FT   DNA_BIND        18..45
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          52..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..299
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   398 AA;  43142 MW;  29A0508B096E2EE6 CRC64;
     MSSTDPLLRR VENYRESCDN CAKSKVRCGK EQPWCQRCER RGQVCSYSPS QRSRKRTLDA
     AHPESDQRNG TPPFTAISSA SSVAAVSTGF SSMLSQADSW GTCPDLVELL TSGSSSESLT
     PDNNHLVWLS DMESIAGDSN ISKSMERMDV FPYPKSIASS AAGVVNGSGA GADSMGRRST
     CPLQNKQHCE ADLISALAKP ELPSLSCWGN PKASQNLGTI LTASRATLKC VTTAMSCTCT
     PNDNVALLAT AVLLRILSWY HIVLKNCNGP NDTSAATIDD HTSPTPSNDG KDTERSVSRD
     TNVSQDGSEP SSLIMPPMTI GAYELDSENR ERMIGHIMLS ELGKMGNLLS DFSKKFCDPQ
     STMLGNDNRS QLFLALEMLI RNKHMATVLD VRKKLEVK
 
 
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