ID   DMR14_CRYX8             Reviewed;         436 AA.
AC   A0A4P8DK24;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   31-JUL-2019, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Transcriptional regulator dmxR14 {ECO:0000303|PubMed:30996871};
DE   AltName: Full=Dimeric xanthone biosynthesis cluster protein R14 {ECO:0000303|PubMed:30996871};
GN   Name=dmxR14 {ECO:0000303|PubMed:30996871};
OS   Cryptosporiopsis sp. (strain 8999).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Dermateaceae; Cryptosporiopsis; unclassified Cryptosporiopsis.
OX   NCBI_TaxID=2572248;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=8999;
RX   PubMed=30996871; DOI=10.1039/c8sc05126g;
RA   Greco C., de Mattos-Shipley K., Bailey A.M., Mulholland N.P., Vincent J.L.,
RA   Willis C.L., Cox R.J., Simpson T.J.;
RT   "Structure revision of cryptosporioptides and determination of the genetic
RT   basis for dimeric xanthone biosynthesis in fungi.";
RL   Chem. Sci. 10:2930-2939(2019).
CC   -!- FUNCTION: Transcriptional regulator; part of the gene cluster that
CC       mediates the biosynthesis of the dimeric xanthones cryptosporioptides.
CC       {ECO:0000269|PubMed:30996871}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
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DR   EMBL; MK182094; QCL09105.1; -; Genomic_DNA.
DR   SMR; A0A4P8DK24; -.
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; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..436
FT                   /note="Transcriptional regulator dmxR14"
FT                   /id="PRO_0000453507"
FT   DNA_BIND        34..61
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   436 AA;  47332 MW;  B94001D3437BEDB6 CRC64;
     MEEAETNTQV DSVPSNSVRS GAELSSKSKL RDSCHACARS KVRCPKQKPS CSRCEARGTT
     CQYFFSRRPG RRRETSKSPN PEKQIAIGSS HANNRNSPSF SSTRSTLPSP IASDSNSNFT
     QPQNSSITTV HNGPENSIES PCWEDFSCEF SDTDFVMPTI DTPFDLSPAY SGSVVQEMND
     TAPFPLSSSR ISMGTTPSGK SSISSYSQIL PSITPTTTPV AHISSCRCLA TALDLLKTLS
     LAGLADADSL VSAPIILAEN KQSIESVNNL MACPLCSGDS FPLTIFSMIA LKILERYAVA
     ARTQHQGTRP QEAEGTVEIK LADIVISNNE DQTRLPSHSN IVCCDDKTQA RAAAQLVLGE
     LHHMQRLVNQ LSSMIKRSAE RDGRKLEILN GYNDSIDSGN SMLASFSAST LELVESDVRK
     SLRSLSTDII KELRQH