ID   STUA_FUSOX              Reviewed;         550 AA.
AC   Q6L612;
DT   13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
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:15590816};
OS   Fusarium oxysporum (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=5507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=Mel02010;
RX   PubMed=15590816; DOI=10.1128/ec.3.6.1412-1422.2004;
RA   Ohara T., Tsuge T.;
RT   "FoSTUA, encoding a basic helix-loop-helix protein, differentially
RT   regulates development of three kinds of asexual spores, macroconidia,
RT   microconidia, and chlamydospores, in the fungal plant pathogen Fusarium
RT   oxysporum.";
RL   Eukaryot. Cell 3:1412-1422(2004).
CC   -!- FUNCTION: Transcription factor that regulates asexual reproduction
CC       (PubMed:15590816). 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). Differentially regulates the development
CC       of macroconidia, microconidia, and chlamydospores (PubMed:15590816).
CC       Acts as a positive regulator for the development of macroconidia and as
CC       a negative regulator for the development of chlamydospores
CC       (PubMed:15590816). Involved in microconidium formation specifically in
CC       infected plants (PubMed:15590816). {ECO:0000250|UniProtKB:P36011,
CC       ECO:0000269|PubMed:15590816}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15590816}.
CC   -!- DISRUPTION PHENOTYPE: Lacks conidiophores and produces macroconidia at
CC       low frequencies only from intercalary phialides (PubMed:15590816).
CC       Produces markedly fewer macroconidia and microconidia in infected
CC       plants but does not affect the disease-causing ability
CC       (PubMed:15590816). {ECO:0000269|PubMed:15590816}.
CC   -!- SIMILARITY: Belongs to the EFG1/PHD1/stuA family. {ECO:0000305}.
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DR   EMBL; AB180746; BAD21357.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6L612; -.
DR   SMR; Q6L612; -.
DR   VEuPathDB; FungiDB:FOC1_g10012715; -.
DR   VEuPathDB; FungiDB:FOC4_g10013712; -.
DR   VEuPathDB; FungiDB:FOIG_07247; -.
DR   VEuPathDB; FungiDB:FOMG_06664; -.
DR   VEuPathDB; FungiDB:FOXG_05278; -.
DR   VEuPathDB; FungiDB:FOZG_11054; -.
DR   VEuPathDB; FungiDB:HZS61_003862; -.
DR   PhylomeDB; Q6L612; -.
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; Sporulation; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..550
FT                   /note="Cell pattern formation-associated protein STUA"
FT                   /id="PRO_0000435974"
FT   DOMAIN          86..192
FT                   /note="HTH APSES-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT   DNA_BIND        120..141
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT   REGION          246..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..546
FT                   /note="Nuclear localization domain"
FT                   /evidence="ECO:0000250|UniProtKB:P36011"
FT   REGION          527..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   550 AA;  59651 MW;  05BFE79AC65E9C1B CRC64;
     MNQGHPQPDM YYSPHYSTPQ YGYGYSTNGA PTTAVSTPMP APQNVLPVPS ALSNQGAMQQ
     PGYSNSSNNG AFDTTGQHNP PGMKPRVTAT LWEDEGSLCF QVEARGICVA RREDNHMING
     TKLLNVAGMT RGRRDGILKS EKVRHVVKIG PMHLKGVWIP YDRALDFANK EKITELLFPL
     FVHNIGALLY HPSNSNRTSQ VMAAAERRKH EGLGGQRPAA PNALPSIGQH HPMMPGLPTG
     GYVPQSLANG PQSLASTPQP LTNGSQPPMP NGGGMLKRGR EEEEDLHRPV SNGHDPMSNM
     HAMSNGYPQQ PPLANVHQPP MQNGGDMLKR GRDEDDEVHR SAHTAHDTMN NMPGSMPGLS
     NAYAQPLPNV HHQPLANGDG GMLKRGRDED DDVHRSSPNG HDSAGNFEVK RRKTITSNDS
     MVSPGGFYTL HNGYGQPGVM NGMSPYKRRD DEAETPRPGP NVHDHLNNFD LKRHKTMETS
     VPAPQYDAMN RPHSSIGTSP TYAPAPVYDN LARPASTVAA SPSYPSAPVY DTGARPPSAI
     SAPRRQQSFG