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Database: UniProt
Entry: W3WP99_PESFW
LinkDB: W3WP99_PESFW
Original site: W3WP99_PESFW 
ID   W3WP99_PESFW            Unreviewed;       599 AA.
AC   W3WP99;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Transcription factor {ECO:0000256|PIRNR:PIRNR002595};
GN   ORFNames=PFICI_12578 {ECO:0000313|EMBL:ETS75634.1};
OS   Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX   NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS75634.1, ECO:0000313|Proteomes:UP000030651};
RN   [1] {ECO:0000313|Proteomes:UP000030651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX   PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA   Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA   Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT   "Genomic and transcriptomic analysis of the endophytic fungus
RT   Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT   of natural products.";
RL   BMC Genomics 16:28-28(2015).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR002595}.
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DR   EMBL; KI912118; ETS75634.1; -; Genomic_DNA.
DR   RefSeq; XP_007839350.1; XM_007841159.1.
DR   AlphaFoldDB; W3WP99; -.
DR   STRING; 1229662.W3WP99; -.
DR   GeneID; 19277591; -.
DR   KEGG; pfy:PFICI_12578; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   eggNOG; KOG0627; Eukaryota.
DR   HOGENOM; CLU_008776_2_0_1; -.
DR   InParanoid; W3WP99; -.
DR   OMA; NWQSPGQ; -.
DR   OrthoDB; 1117127at2759; -.
DR   Proteomes; UP000030651; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:UniProtKB-UniRule.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR000232; HSF_DNA-bd.
DR   InterPro; IPR027725; HSF_fam.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR014402; Sig_transdc_resp-reg_Skn7.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10015; HEAT SHOCK TRANSCRIPTION FACTOR; 1.
DR   PANTHER; PTHR10015:SF361; TRANSCRIPTION FACTOR SKN7; 1.
DR   Pfam; PF00447; HSF_DNA-bind; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PIRSF; PIRSF002595; RR_SKN7; 1.
DR   PRINTS; PR00056; HSFDOMAIN.
DR   SMART; SM00415; HSF; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS00434; HSF_DOMAIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR002595};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR002595};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030651};
KW   Transcription {ECO:0000256|PIRNR:PIRNR002595};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR002595}.
FT   DOMAIN          340..456
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          173..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          568..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         391
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   599 AA;  65894 MW;  AE6D2B916C57C7A9 CRC64;
     MLEDPSYSEV VRWGDHGDSF VVLENEKFTK TILPKHFKHS NFASFVRQLN KYDFHKVRQN
     EETGQSVYGQ NAWEFKHPEF NRDAKHNLDN IRRKAPAPRK AQNNEEQFHH SNTQIVALTE
     NVAAMQQQVQ SLQESYFALT QANKVFVDEI LHLQRVVKAQ SQVNNELLSH LNKADQSRRH
     ARSASNHASG PAFSDNIMSD GTLEPAAELR RAREIMSSVS GDHIPERDLR QMSVQFQQVG
     ASPESAGSGT MMGPPGTGAM PQDFVHNPML DPRHMVYPVG QDIGIDPFAA EHLGNIPYNR
     PLSQNALAAA PETVPPTVPT ISPPSGAPGA SSPWGAKKPR ILLVEDDRIC SRIGSKFLAN
     FDCGVEVARD GLEAVHKINA NPNWFDLIFM DIVMPQLDGV SATAMIREVN PRIPIIAMTS
     NINQQDLDMY FHWGMKDVLA KPFTKEGMIG KLRKHLAGFM RNATAEAYID AYGNGQPPTP
     GPYSNAGMSL PISAASSSGM AKFETTPIQS PATSASWHSP GQMPHASPNL NHEQGYMAAG
     NGAQMGMNPG APSQPRFPNT MLPAMTAGHG RMPEGMPNDG PPEKRQRLHG PTFQGQYPQ
//
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