ID   VRTR1_PENAE             Reviewed;         715 AA.
AC   D7PI00;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Transcription factor vrtR1 {ECO:0000303|PubMed:20534346};
DE   AltName: Full=Viridicatumtoxin synthesis protein R1 {ECO:0000303|PubMed:20534346};
GN   Name=vrtR1 {ECO:0000303|PubMed:20534346};
OS   Penicillium aethiopicum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=36650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=IBT 5753;
RX   PubMed=20534346; DOI=10.1016/j.chembiol.2010.03.015;
RA   Chooi Y.H., Cacho R., Tang Y.;
RT   "Identification of the viridicatumtoxin and griseofulvin gene clusters from
RT   Penicillium aethiopicum.";
RL   Chem. Biol. 17:483-494(2010).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=19168978; DOI=10.1038/ja.2008.84;
RA   Zheng C.J., Yu H.E., Kim E.H., Kim W.G.;
RT   "Viridicatumtoxin B, a new anti-MRSA agent from Penicillium sp. FR11.";
RL   J. Antibiot. 61:633-637(2008).
RN   [3]
RP   BIOTECHNOLOGY.
RX   PubMed=27049441; DOI=10.1038/ja.2016.35;
RA   Inokoshi J., Nakamura Y., Komada S., Komatsu K., Umeyama H., Tomoda H.;
RT   "Inhibition of bacterial undecaprenyl pyrophosphate synthase by small
RT   fungal molecules.";
RL   J. Antibiot. 69:798-805(2016).
CC   -!- FUNCTION: Probable transcription factor that regulates expression of
CC       the gene cluster that mediates the biosynthesis of viridicatumtoxin, a
CC       tetracycline-like fungal meroterpenoid with a unique, fused
CC       spirobicyclic ring system (PubMed:20534346).
CC       {ECO:0000269|PubMed:20534346}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- BIOTECHNOLOGY: Viridicatumtoxin and its derivative, viridicatumtoxin B,
CC       exhibit anti-methicillin-resistant Staphylococcus aureus (anti-MRSA)
CC       activity (PubMed:19168978). Moreover, viridicatumtoxin and a C2 acetyl
CC       analog, spirohexaline, have been demonstrated to inhibit bacterial
CC       undecaprenyl diphosphate synthase, a potential new target for
CC       antibiotic development (PubMed:27049441). {ECO:0000269|PubMed:19168978,
CC       ECO:0000269|PubMed:27049441}.
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DR   EMBL; GU574477; ADI24933.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7PI00; -.
DR   SMR; D7PI00; -.
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:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; -; 1.
DR   InterPro; IPR007219; Transcription_factor_dom_fun.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   Pfam; PF04082; Fungal_trans; 1.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00906; Fungal_trans; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..715
FT                   /note="Transcription factor vrtR1"
FT                   /id="PRO_0000436817"
FT   DNA_BIND        51..78
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          119..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   715 AA;  80128 MW;  3C145FA9F0E8941B CRC64;
     MEDTTETTET TDTTAVSRLV PLAPAPARAP SMDAVNGSFD SELTTARRFN CQSCVRKKIK
     CNRAVPTCAS CSKAKLHCVY QSRPPRKRKR SRGEEDVYER LAQYERILHD HNLLQAAAAS
     TPSGRDTETS AISTRAPTPV LPDAQTHTKA GKVLLSTDGR SRYIDNVLLL DAGEGDLCEL
     PESEQEDYNH DETSPDESTP TGLLGALAAH TISGAIIGNT QSLTNLHPTY EQAAKLWQAY
     VKNVEPLCKI LHVPTVAKMF DTVSKQPAAV SKNDECLMFV IYYFAVFSMS DDECLHEFNY
     PRAQLLSRYQ TTVIQALVNA SWLKTTAMPV LQAYTLFLIA LRTQIDSHTF WILTGIAVRL
     AQRMGLHRDG ESLGLPPFEV QMRRRLFWQL LPLDSYAGQT SGTGISISPS SWDTKQPLNI
     NDDQIFPGMT QPPCEQRGAS EMIFCLSRME LSNFYIRTGV KLKEHGDTIQ FRDAEDIERL
     IDEVEDLIET KFLRYCDILN PLHFLTTGIV RSAIDAVRLR ARMPLLKQQT ITDAQRRRLC
     ALAEKVLDTN STIFSNPSTQ NFRWQMQAFF LWDALLCILR NIAEVGFYSP SELAAAWSKV
     ANVYANHDEL VKARRTLYVT IAKVTLKAWL ANPPRDSSPQ PAFITALLTQ HEPKGINQQQ
     NSVLSDDKAA DGASLFDEFF DNMNGTDLDI NNAFNLDSSS DWLFWDQICR GTSLS