ID   STUA_MAGOR              Reviewed;         618 AA.
AC   Q4R1B9; C8KGA5;
DT   13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Cell pattern formation-associated protein MSTU1 {ECO:0000305};
DE   AltName: Full=Stunted protein A {ECO:0000250|UniProtKB:P36011};
GN   Name=MSTU1 {ECO:0000303|PubMed:19661696};
OS   Magnaporthe oryzae (Rice blast fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=318829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=Guyane 11;
RX   PubMed=19661696; DOI=10.1271/bbb.90146;
RA   Nishimura M., Fukada J., Moriwaki A., Fujikawa T., Ohashi M., Hibi T.,
RA   Hayashi N.;
RT   "Mstu1, an APSES transcription factor, is required for appressorium-
RT   mediated infection in Magnaporthe grisea.";
RL   Biosci. Biotechnol. Biochem. 73:1779-1786(2009).
CC   -!- FUNCTION: Transcription factor that regulates asexual reproduction
CC       (PubMed:19661696). 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 appressorium-mediated
CC       infection of rice leaves due to its involvement in the mobilization of
CC       lipids and glycogen (PubMed:19661696). {ECO:0000250|UniProtKB:P36011,
CC       ECO:0000269|PubMed:19661696}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P36011}.
CC   -!- DISRUPTION PHENOTYPE: Leads to reduced conidiation and mycelial growth
CC       (PubMed:19661696). Delays the transfer of conidial glycogen and lipid
CC       droplets and decreases efficiency of appressorium-mediated invasion of
CC       rice leaves (PubMed:19661696). {ECO:0000269|PubMed:19661696}.
CC   -!- SIMILARITY: Belongs to the EFG1/PHD1/stuA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAI39646.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB218802; BAE00061.1; -; Genomic_DNA.
DR   EMBL; AB218803; BAI39646.1; ALT_FRAME; mRNA.
DR   AlphaFoldDB; Q4R1B9; -.
DR   SMR; Q4R1B9; -.
DR   OMA; MDVHSSH; -.
DR   PHI-base; PHI:2065; -.
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; Sporulation; Transcription;
KW   Transcription regulation; Virulence.
FT   CHAIN           1..618
FT                   /note="Cell pattern formation-associated protein MSTU1"
FT                   /id="PRO_0000435979"
FT   DOMAIN          110..216
FT                   /note="HTH APSES-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT   DNA_BIND        144..165
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT   REGION          13..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          566..588
FT                   /note="Nuclear localization domain"
FT                   /evidence="ECO:0000250|UniProtKB:P36011"
FT   COMPBIAS        24..70
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..449
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..590
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   618 AA;  66835 MW;  59773D2D2605DC0A CRC64;
     MNQGHDMYYQ QHMSAGPTQQ PPTVTSYNPQ PPIMQPSHGS YPAPPQPYGG YPYTNGMPSP
     QGPPVPGQMG PGSVLPSIAG HHGQAPGPVA NQYSGFDTSG QIAPPGMKPR VTATLWEDEG
     SLCFQVEARG VCVARREDNH MINGTKLLNV AGMTRGRRDG ILKSEKMRHV VKIGPMHLKG
     VWIPFERALD FANKEKITEL LYPLFVHNIS ALLYHPANQN RNNQLMAAAE RRKAETGGMR
     NPQGPPGLPA LHHHSMSQNG SQSLSGNIGR PSLDRAHTFP TPPTSASSAV NMGSSDSFTW
     PPHQAMSNGQ QNPMSIDTSL SNTRSMPTTP ATTPPGSTLQ SMQAYPPASQ SYDGSRQLYN
     APQLQQSPYQ PTSTSPQDRS LYNQATYVKS EMGPPSARPM GSVLPGDHQN DQKPVNGLMH
     PPQGADQGHN NGVEDEADHE HDPEYTHDSR TYDNSQSQYN YTAPPVSSIS SEQAHVSTDM
     PPGGQHGNSG RSTPRSAAAP QAYYQQAYST SPRSATHQST SNLYNVMSND RGSTTNGSAN
     GDVYSQSTDL SNGYATPVTN GNANLKRGRD DDDDRSSSSG QMDLKRRKTL MDNPISSPVY
     ETMNRPAAAI AHPVSRRR