STUA_PHANO
ID STUA_PHANO Reviewed; 644 AA.
AC Q0U086;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 83.
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:20495056}; ORFNames=SNOG_14941;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20495056; DOI=10.1128/ec.00064-10;
RA IpCho S.V., Tan K.C., Koh G., Gummer J., Oliver R.P., Trengove R.D.,
RA Solomon P.S.;
RT "The transcription factor StuA regulates central carbon metabolism,
RT mycotoxin production, and effector gene expression in the wheat pathogen
RT Stagonospora nodorum.";
RL Eukaryot. Cell 9:1100-1108(2010).
CC -!- FUNCTION: Transcription factor that regulates asexual reproduction
CC (PubMed:20495056). 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 (By similarity). Required for pathogenicity and positively
CC regulates the synthesis of the mycotoxin alternariol (PubMed:20495056).
CC Acts as a positive regulator of Tox3 but is not required for the
CC expression of ToxA (PubMed:20495056). Acts also as a central regulator
CC of carbon metabolism including glycolysis, the TCA cycle, and amino
CC acid synthesis (PubMed:20495056). {ECO:0000250|UniProtKB:P36011,
CC ECO:0000269|PubMed:20495056}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P36011}.
CC -!- DISRUPTION PHENOTYPE: Produces thick white aerial hyphae but impairs
CC sporulation (PubMed:20495056). Affects the expression of genes involved
CC in central carbon metabolism including glycolysis, the TCA cycle, and
CC amino acid synthesis (PubMed:20495056). Decreases pathogenicity after
CC inoculation of detached wheat leaves (PubMed:20495056).
CC {ECO:0000269|PubMed:20495056}.
CC -!- SIMILARITY: Belongs to the EFG1/PHD1/stuA family. {ECO:0000305}.
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DR EMBL; CH445358; EAT77793.2; -; Genomic_DNA.
DR RefSeq; XP_001805109.1; XM_001805057.1.
DR AlphaFoldDB; Q0U086; -.
DR SMR; Q0U086; -.
DR STRING; 13684.SNOT_14941; -.
DR EnsemblFungi; SNOT_14941; SNOT_14941; SNOG_14941.
DR GeneID; 5982036; -.
DR KEGG; pno:SNOG_14941; -.
DR eggNOG; ENOG502QW2C; Eukaryota.
DR HOGENOM; CLU_016460_0_0_1; -.
DR InParanoid; Q0U086; -.
DR OrthoDB; 311987at2759; -.
DR PHI-base; PHI:2263; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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..644
FT /note="Cell pattern formation-associated protein StuA"
FT /id="PRO_0000435982"
FT DOMAIN 124..230
FT /note="HTH APSES-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT DNA_BIND 158..179
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT REGION 18..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..612
FT /note="Nuclear localization domain"
FT /evidence="ECO:0000250|UniProtKB:P36011"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 68488 MW; 5D99E57B5945ECCC CRC64;
MNQMQSYADV HPPHMSAATA HAPASAAPSG ISHYAYPPQS SMMQPGQHQY GPTPPGYPSY
GYSNGVPSGL PASSSMNNAM VPSTLQLPAM SSSGPSPSLS GAQSYAPHSF DHTGQVAPPG
MKPRVTATLW EDEGSLCFQV EAKGVCVARR EDNHMINGTK LLNVAGMTRG RRDGILKSEK
TRHVVKIGPM HLKGVWIPFE RALEFANKEK ITEQLYPLFV HDIGALLYHP SNQTRASVGS
AAMAAVDRRR PDSMQTQRYI SGPTTSQPPS LHHHHSMSNP IGAPMSQAPH ALQPHPSAGR
PGLDRAHTFP TPPTSASSIM GMSNSGSSYE WSGANVQTPQ GSQPLSIDTG LSNTRSVPTT
PATTPPGAVQ QAISYGSNQS YDNSRPMYSG PPSQPGQYNT QGQSMMGYRP DSGYTKTEMA
PPSRLADVSE EGDVKHSEGM MPQGNSQVVA PAPGPEGDHE HDNEYTHSTA SYNGSRGPYG
YASNGNAGGL HPEHPHMSPE MNGSPHQNGS GRATPRTTTT SQTQWNSGYP TPQRQGPPSS
NLYNVMSDPR GAPNGNAPHD AYPGPGAVPQ YASQGYPPAN GNAKRGRDDD DEDPYRPDSV
QSDDMGGLKR RKTMEGGAVG GAYAQDPTPG LQRAHTMTAQ RARR
