ID   STUA_LEPMJ              Reviewed;         645 AA.
AC   E5AD52;
DT   13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2016, sequence version 2.
DT   25-MAY-2022, entry version 49.
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:25727237}; ORFNames=LEMA_P011910.1;
OS   Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS   (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Leptosphaeria; Leptosphaeria maculans species complex.
OX   NCBI_TaxID=985895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8;
RX   PubMed=21326234; DOI=10.1038/ncomms1189;
RA   Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA   Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA   Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA   Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA   Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA   Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA   Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA   Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT   "Effector diversification within compartments of the Leptosphaeria maculans
RT   genome affected by Repeat-Induced Point mutations.";
RL   Nat. Commun. 2:202-202(2011).
RN   [2]
RP   INDUCTION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=25727237; DOI=10.1111/mpp.12249;
RA   Soyer J.L., Hamiot A., Ollivier B., Balesdent M.H., Rouxel T., Fudal I.;
RT   "The APSES transcription factor LmStuA is required for sporulation,
RT   pathogenic development and effector gene expression in Leptosphaeria
RT   maculans.";
RL   Mol. Plant Pathol. 16:1000-1005(2015).
CC   -!- FUNCTION: Transcription factor that regulates asexual reproduction (By
CC       similarity). Binds the StuA-response elements (StRE) with the consensus
CC       sequence 5'-(A/T)CGCG(T/A)N(A/C)-3' at the promoters of target genes
CC       (By similarity). Regulates the expression of several effector genes
CC       (AvrLm1, AvrLm6 and AvrLm4-7) during infection stage (PubMed:25727237).
CC       {ECO:0000250|UniProtKB:P36011, ECO:0000269|PubMed:25727237}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P36011}.
CC   -!- INDUCTION: Expression is induced during mycelial growth and at 14 days
CC       after infection, corresponding to the development of pycnidia on
CC       oilseed rape leaves (PubMed:25727237). {ECO:0000269|PubMed:25727237}.
CC   -!- DISRUPTION PHENOTYPE: Alters growth in axenic culture and impairs
CC       conidia production and perithecia formation (PubMed:25727237).
CC       Abolishes the pathogenicity on oilseed rape leaves and results in a
CC       drastic decrease in expression of at least the three effector genes
CC       AvrLm1, AvrLm6 and AvrLm4-7, during infection (PubMed:25727237).
CC       {ECO:0000269|PubMed:25727237}.
CC   -!- SIMILARITY: Belongs to the EFG1/PHD1/stuA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CBY02404.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; FP929139; CBY02404.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_003845883.1; XM_003845835.1.
DR   AlphaFoldDB; E5AD52; -.
DR   SMR; E5AD52; -.
DR   STRING; 985895.E5AD52; -.
DR   EnsemblFungi; CBY02404; CBY02404; LEMA_P011910.1.
DR   GeneID; 13286538; -.
DR   eggNOG; ENOG502QW2C; Eukaryota.
DR   HOGENOM; CLU_016460_0_0_1; -.
DR   InParanoid; E5AD52; -.
DR   OrthoDB; 311987at2759; -.
DR   PHI-base; PHI:4519; -.
DR   Proteomes; UP000002668; Genome.
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   2: Evidence at transcript level;
KW   Conidiation; DNA-binding; Nucleus; Reference proteome; Sporulation;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..645
FT                   /note="Cell pattern formation-associated protein stuA"
FT                   /id="PRO_0000435977"
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          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          585..613
FT                   /note="Nuclear localization domain"
FT                   /evidence="ECO:0000250|UniProtKB:P36011"
FT   COMPBIAS        36..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..612
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   645 AA;  69005 MW;  BAB3B45A0C48E253 CRC64;
     MNQMQPYADV HQPHMSTAAH APASGPPAGL SHYSYPHQPS MMQPQQQQHQ YGGQPTGYPY
     AYNNGVPSQL PASSSMNNAL VPSTLQLPAM SAGAPNSSMP GSQSYQSHTF DHTGQVAPPG
     MKPRVTATLW EDEGSLCFQV EAKGVCVARR EDNHMINGTK LLNVAGMTRG RRDGILKSEK
     TRHVVKIGPM HLKGVWIPFE RALEFANKEK ITEQLYPLFV HDIGALLYHP SNQTRASVGG
     AAMAAVDRNR RPDSMQTQQR YMAGPTTSQA PSLHHHHSMT NSVGSAMSQP PHAIQPHPSS
     GRPSLDRAHT FPTPPTSASS MMGMGNQGSS YEWNGANVQQ HPQGNQPLSI DTGLSNARSV
     PTTPASTPPG AVQQGIPYGS SQSYDGSRPM YSAPPAQPSQ YAQGQPMMSY RPDNAYPKTE
     MAPPSRISDV PEEGEVKASD GMMPQGNEQV AAPPAGGEEE NEYTHSSAPY NGNRGPYGYN
     PNGPPGPMHA DHTHLSPEMT GSPHQNGSGR ATPRTATNGQ AQWGSSYPTP QRQAPPSSNL
     YNVMSDPRGA PNGNAAHDAY QGPGAVPQYA SQGYAPTNGV NSSGKRGRDE EDAETYRPDS
     VQGDDMGGLK RRKTMEGGAV GQTYAQDPSP GLQRAHTLAA QRARR