ID   AFLR_ASPPA              Reviewed;         444 AA.
AC   P43651; Q12409;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 3.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Aflatoxin biosynthesis regulatory protein;
GN   Name=aflR; Synonyms=apa-2;
OS   Aspergillus parasiticus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7887625; DOI=10.1128/aem.61.1.40-43.1995;
RA   Chang P.-K., Bhatnagar D., Cleveland T.E., Bennett J.W.;
RT   "Sequence variability in homologs of the aflatoxin pathway gene aflR
RT   distinguishes species in Aspergillus section Flavi.";
RL   Appl. Environ. Microbiol. 61:40-43(1995).
RN   [2]
RP   SEQUENCE REVISION.
RA   Chang P.-K.;
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 1-406.
RC   STRAIN=ATCC 62882 / CP461 / SRRC 2043;
RX   PubMed=8250554; DOI=10.1128/aem.59.10.3273-3279.1993;
RA   Chang P.-K., Cary J.W., Bhatnagar D., Cleveland T.E., Bennett J.W.,
RA   Linz J.E., Woloshuk C.P., Payne G.A.;
RT   "Cloning of the Aspergillus parasiticus apa-2 gene associated with the
RT   regulation of aflatoxin biosynthesis.";
RL   Appl. Environ. Microbiol. 59:3273-3279(1993).
CC   -!- FUNCTION: Involved in the regulation of aflatoxin biosynthesis. May
CC       have a role in nitrate assimilation and sclerotial morphogenesis.
CC   -!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
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DR   EMBL; L26222; AAC27357.1; -; mRNA.
DR   EMBL; L26220; AAA32685.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; L22177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P43651; -.
DR   SMR; P43651; -.
DR   UniPathway; UPA00287; -.
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:UniProtKB-UniPathway.
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   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..444
FT                   /note="Aflatoxin biosynthesis regulatory protein"
FT                   /id="PRO_0000114933"
FT   DNA_BIND        29..56
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        374
FT                   /note="A -> R (in Ref. 3; L22177)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        388
FT                   /note="V -> A (in Ref. 3; L22177)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   444 AA;  47286 MW;  B87FC91C0BC0A006 CRC64;
     MVDHISPRAS PGPIRSSQTR RARKLRDSCT SCASSKVRCT KEKPACARCI ERGLACQYMV
     SKRMGRNPRA PSPLDSTRRP SESLPSAGSE QGLPAHNTYS TPHAHTQAHT HAHSHPQPHP
     QSHPQSNQPP HALPTPNGSS SVSAIFSHQS PPPLVETQGL GGDLAGQAQS TLSSLTVDSE
     FGGSLQSMEH GNHADFLAES TGSLFDAFLE VGTPMIDPFL ESAPLPPFQA RYCCFSLALQ
     TLTCLFPHAP LGCQLRLTDG EDSSCNLMTT DMVISGNKKA TDAVRKILGC SCAQDGYLLS
     MVVLIVLKVL GWYAAAAGTQ CTSTAAGGET NSGSCSNSPA TVSSGCLTEE RVLHHPSMVG
     EDCVDEEDQP RVAAQLVLSE LHRVQSLVNL LAKRLQEGGD DAAGIPAHHP ASPFSLLGFS
     GLEANLRHRL RAVSSDIIDY LHRE