ID   VDTR1_BYSSP             Reviewed;         436 AA.
AC   A0A443HK05;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Transcriptionnal regulator VdtR {ECO:0000303|PubMed:31304040};
DE   AltName: Full=Viriditoxin biosynthesis cluster protein R {ECO:0000303|PubMed:31304040};
GN   Name=VdtR {ECO:0000303|PubMed:31304040}; ORFNames=C8Q69DRAFT_105452;
OS   Byssochlamys spectabilis (Paecilomyces variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=264951;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101075;
RX   PubMed=30619145; DOI=10.3389/fmicb.2018.03058;
RA   Urquhart A.S., Mondo S.J., Maekelae M.R., Hane J.K., Wiebenga A., He G.,
RA   Mihaltcheva S., Pangilinan J., Lipzen A., Barry K., de Vries R.P.,
RA   Grigoriev I.V., Idnurm A.;
RT   "Genomic and genetic insights into a cosmopolitan fungus, Paecilomyces
RT   variotii (Eurotiales).";
RL   Front. Microbiol. 9:3058-3058(2018).
RN   [2]
RP   IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=31304040; DOI=10.1186/s40694-019-0072-y;
RA   Urquhart A.S., Hu J., Chooi Y.H., Idnurm A.;
RT   "The fungal gene cluster for biosynthesis of the antibacterial agent
RT   viriditoxin.";
RL   Fungal Biol. Biotechnol. 6:2-2(2019).
CC   -!- FUNCTION: Transcription factor that regulates expression of the
CC       viriditoxin biosynthesis cluster and viriditoxin synthesis.
CC       {ECO:0000269|PubMed:31304040}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- DISRUPTION PHENOTYPE: Leads to reduced transcript levels of genes in
CC       the viriditoxin biosynthesis cluster and the loss of the ability to
CC       synthesize viriditoxin. {ECO:0000269|PubMed:31304040}.
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DR   EMBL; RCNU01000014; RWQ92173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A443HK05; -.
DR   SMR; A0A443HK05; -.
DR   Proteomes; UP000283841; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045122; P:aflatoxin biosynthetic process; IEA:InterPro.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; -; 1.
DR   InterPro; IPR013700; AflR.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   Pfam; PF08493; AflR; 1.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..436
FT                   /note="Transcriptionnal regulator VdtR"
FT                   /id="PRO_0000448348"
FT   DNA_BIND        17..44
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          51..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   436 AA;  48546 MW;  C5126C135F23CF21 CRC64;
     MSWQGHEGPK VKLRSACDRC SANKVKCTQE KPECERCRLL SLPCNYSRSM RIGKPPKSRQ
     RGLSNIDPKT LMGGTVTKKL RPCPSAPESA CRGSFEDGDG GPWTETMTFE EMLSRPSPPP
     FAGPSHNSNR PTNMASTNQD QYYHDKGKHG ETMDEMLQTL VPDSVQFIEF PNTAREDQKQ
     HPELRSEEEY SDYRSKSLFE EGLARIAPDC AGGIMDVLYG EEALVQMPNL PSSTHEGSSN
     THVTSSHNCT RAVMENLAKL YQVCAPAGVE NGSHPTTDQV LKANSDAMKD AADLLACPCA
     KDFCFPIILG ITACRVLAWY QVVIDMYDPE IPMATMPTAR EDIKHCPIAF GAYQLDEEVS
     QAMTSQFVLR NLRAMTRFVK TYVENFCSDI NKNRPGSCSL IYRSLGTFMQ TRLGNTIEQL
     EDRLAAFDGE YTKNIG