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SWI6_MAGOR
ID   SWI6_MAGOR              Reviewed;         895 AA.
AC   Q3S405;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Transcription factor SWI6 {ECO:0000303|PubMed:22321443};
GN   Name=SWI6 {ECO:0000303|Ref.1};
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].
RC   STRAIN=Guyane 11;
RA   Cartwright Z.J., Talbot N.J.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH PPS1.
RX   PubMed=22321443; DOI=10.1111/j.1364-3703.2011.00779.x;
RA   Qi Z., Wang Q., Dou X., Wang W., Zhao Q., Lv R., Zhang H., Zheng X.,
RA   Wang P., Zhang Z.;
RT   "MoSwi6, an APSES family transcription factor, interacts with MoMps1 and is
RT   required for hyphal and conidial morphogenesis, appressorial function and
RT   pathogenicity of Magnaporthe oryzae.";
RL   Mol. Plant Pathol. 13:677-689(2012).
CC   -!- FUNCTION: Transcription factor that plays a role downstream of the
CC       MCK1-MKK2-MPS1 cascade (PubMed:22321443). Required for hyphal
CC       morphogenesis and pathogenicity (PubMed:22321443). Is an important
CC       oxidative stress response regulator and plays a positive role in the
CC       regulation of extracellular peroxidases (PubMed:22321443).
CC       {ECO:0000269|PubMed:22321443}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:22321443}.
CC   -!- DISRUPTION PHENOTYPE: Leads to deformed and non-melanized appressoria
CC       that are unable to penetrate plant surface due to the impaired cell
CC       wall integrity (PubMed:22321443). Shows abnormal hyphae as a result of
CC       altered chitin synthesis (PubMed:22321443). Leads to sensitivity to
CC       H(2)O(2) (PubMed:22321443). {ECO:0000269|PubMed:22321443}.
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DR   EMBL; DQ168586; ABA02072.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3S405; -.
DR   SMR; Q3S405; -.
DR   OMA; HHIAMMA; -.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:UniProt.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:UniProt.
DR   GO; GO:0048315; P:conidium formation; IEA:UniProtKB-KW.
DR   GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IEA:UniProt.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.20; -; 1.
DR   Gene3D; 3.10.260.10; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR036887; HTH_APSES_sf.
DR   InterPro; IPR018004; KilA_N/APSES_HTH.
DR   InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR   Pfam; PF13637; Ank_4; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM01252; KilA-N; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF54616; SSF54616; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS51299; HTH_APSES; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Coiled coil; Conidiation; Nucleus; Repeat; Sporulation;
KW   Transcription; Transcription regulation; Virulence.
FT   CHAIN           1..895
FT                   /note="Transcription factor SWI6"
FT                   /id="PRO_0000453105"
FT   DOMAIN          112..219
FT                   /note="HTH APSES-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT   REPEAT          458..488
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          607..636
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000255"
FT   DNA_BIND        143..164
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT   REGION          1..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          653..684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          698..759
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        670..684
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   895 AA;  97714 MW;  AABE05BC8DD8412D CRC64;
     MASTVAGNSF VSQQHPGNLH SANLQSQSQG FRRQNSTSSV PSTASFDPPN GSIANTGSQK
     HHPMSSQQSQ PPASQQSFSM SQTGSQPQPS QSSFRSYSDQ NVPQQPQEAS PIYTAVYSNV
     EVYEFEVNGV AVMKRIGDSK LNATQILKVA GVEKGKRTKI LEKEIQTGEH EKVQGGYGKY
     QGTWIKYERA LEVCRQYGVE ELLRPLLEYN RNPDGSVSQA NLNTPTKEQA MAAQRKKMYN
     SGADSRNNNG GGTFFKNISQ TAHSAMTAIS KARFDSPGPR GRNGPTRAPS FQRQLSTQSI
     DDFHGGNSQA SNFAENFPPQ DVNMAFSAGS EPQPGGLNGT EPPRKRQRMD MTPANSFGAY
     ANNSQMQAYA DAFPGSPTEP NDSFIYTQHA AANDTLLQQQ HDQQTPLQPL PYEQSVEAEN
     KRSMLMSIFM NDGMSEQARV DTLRQIHPRD LDMPIDSQCH TALHWAATLS RMTILRRLIE
     AGASPFRVNT SGETPLMRAC IVTNSHDNDS MPAILDILGN TMEVRDSKER TVLHHIALTS
     AVSGRSAASR YYLQCLLGWV VRQGAANGGQ LNSQTFNGGA TVSQSQNATR LDLGRFMSEM
     LNAQDSAGDT ALNIAARIGN RSIISQLLEV CASPHIANRS GLRPTDFGIG VDSDGAMKTK
     GDSGGDVENG DVGGSSQKSN ESSNEIVTSI THLLTETSAN FQEEIKNKQK NIDSLHATLR
     LTTTDVNDLR RKLDEAQARV KAQQLARQKV TNLQRAEERE RYRLTQLEQT TGRRDIASAN
     GWEAESNTLL ATINATTNGE PDADAKLPSS ALLRARIEAV KKQTESTRQS VVALKGRSRE
     VEGRYRHLVA LATKCRDEDV DSTMEGLLKA VESEKGELEI GRVRRFLGGV EGVIG
 
 
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