STUA_GIBZE
ID STUA_GIBZE Reviewed; 560 AA.
AC I1S0A8; A0A098DAM9;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Cell pattern formation-associated protein StuA {ECO:0000305};
DE AltName: Full=Stunted protein A {ECO:0000250|UniProtKB:P36011};
GN Name=StuA {ECO:0000303|PubMed:20879840}; ORFNames=FGRRES_10129, FGSG_10129;
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, AND DISRUPTION PHENOTYPE.
RX PubMed=20879840; DOI=10.1094/mpmi-03-10-0075;
RA Lysoee E., Pasquali M., Breakspear A., Kistler H.C.;
RT "The transcription factor FgStuAp influences spore development,
RT pathogenicity, and secondary metabolism in Fusarium graminearum.";
RL Mol. Plant Microbe Interact. 24:54-67(2011).
CC -!- FUNCTION: Transcription factor that regulates asexual reproduction
CC (PubMed:20879840). Binds the StuA-response elements (StRE) with the
CC consensus sequence 5'-(A/T)CGCG(T/A)N(A/C)-3' at the promoters of
CC target genes (PubMed:20879840). Controls the expression of the gene
CC clusters involved in the production of deoxynivalenol (DON) and 15-
CC acetyldeoxynivalenol (15ADON) (PubMed:20879840). Regulates the
CC expression of genes involved in chitin and glucan metabolism
CC (PubMed:20879840). Controls also catalase activity and cell surface
CC hydrophobicity (PubMed:20879840). Plays an important role in
CC pathogenicity (PubMed:20879840). {ECO:0000269|PubMed:20879840}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P36011}.
CC -!- DISRUPTION PHENOTYPE: Does not develop perithecia and sexual
CC ascospores, and lacks conidiophores and phialides (PubMed:20879840).
CC Greatly reduces pathogenicity on wheat heads and production of
CC secondary metabolites such as deoxynivalenol (DON) and 15-
CC acetyldeoxynivalenol (15ADON) (PubMed:20879840). Leads to up-regulation
CC of cell-cycle genes which promoters are highly enriched in StuA-
CC response elements (StRE) (PubMed:20879840).
CC {ECO:0000269|PubMed:20879840}.
CC -!- SIMILARITY: Belongs to the EFG1/PHD1/stuA family. {ECO:0000305}.
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DR EMBL; DS231669; ESU16805.1; -; Genomic_DNA.
DR EMBL; HG970332; CEF75482.1; -; Genomic_DNA.
DR RefSeq; XP_011319067.1; XM_011320765.1.
DR AlphaFoldDB; I1S0A8; -.
DR SMR; I1S0A8; -.
DR STRING; 5518.FGSG_10129P0; -.
DR EnsemblFungi; ESU16805; ESU16805; FGSG_10129.
DR GeneID; 23557049; -.
DR KEGG; fgr:FGSG_10129; -.
DR eggNOG; ENOG502QW2C; Eukaryota.
DR HOGENOM; CLU_016460_0_0_1; -.
DR InParanoid; I1S0A8; -.
DR PHI-base; PHI:1290; -.
DR PHI-base; PHI:1295; -.
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:0048315; P:conidium formation; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.10.260.10; -; 1.
DR InterPro; IPR029790; EFG1/Phd1/StuA.
DR InterPro; IPR036887; HTH_APSES_sf.
DR InterPro; IPR018004; KilA_N/APSES_HTH.
DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR PANTHER; PTHR47792; PTHR47792; 1.
DR SMART; SM01252; KilA-N; 1.
DR SUPFAM; SSF54616; SSF54616; 1.
DR PROSITE; PS51299; HTH_APSES; 1.
PE 3: Inferred from homology;
KW Conidiation; DNA-binding; Nucleus; Reference proteome; Sporulation;
KW Transcription; Transcription regulation; Virulence.
FT CHAIN 1..560
FT /note="Cell pattern formation-associated protein StuA"
FT /id="PRO_0000435975"
FT DOMAIN 87..193
FT /note="HTH APSES-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT DNA_BIND 121..142
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT REGION 233..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..556
FT /note="Nuclear localization domain"
FT /evidence="ECO:0000250|UniProtKB:P36011"
FT REGION 532..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 61557 MW; BC7E837308B2BA00 CRC64;
MNQSHHQQSE MYYPQYPTQQ YNPYPYPTNG AHAPAVSTPM PGPQNVLPVP SALSNQGAMP
QAAYSNNAPA GNFDTTGQHN PPGMKPRVTA TLWEDEGSLC FQVEARGICV ARREDNHMIN
GTKLLNVAGM TRGRRDGILK SEKVRHVVKI GPMHLKGVWI PYDRALDFAN KEKITELLYP
LFVHNIGALL YHPSNSNRTS QVMAAAERKK NEAIVGNRSL PSLVQSHHQM MPAMPTGYTS
QQPLTNGHQS MANTPQPLTN GSQPPMNGSQ TPMNGPQPPM QNGGSMLKRV REDDDDLHRS
GPNGHDPMNN IHGMPNGYPH QSPLGSVHQP PMQNGNDGGL KRGREEHDDM HRAGPNGHDP
MNNMPGGMPS LPNYAPPPLQ NLHQPLSNGD SGMLKRGRDD DDDVHRSSPN GHDANGNFEL
KRRKTETSTS NDMLPQSPYY TLSNGAYQGP MMNSMNHYKR RDDEAETPRP GPNMNDLNNF
DLKQRHKTME SSVPAPQYDA MNRPHSSIGN SPAYASAPTG YDHLTRPAST VAVSPSYPAG
PGYELARPVT NVPRRQQSFG
