ID   CPAR_ASPOZ              Reviewed;         598 AA.
AC   F5HN75;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Transcription factor cpaR {ECO:0000303|PubMed:21608094};
DE   AltName: Full=Cyclopiazonic acid biosynthesis cluster protein R {ECO:0000303|PubMed:21608094};
GN   Name=cpaR {ECO:0000303|PubMed:21608094};
OS   Aspergillus oryzae (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, AND FUNCTION.
RC   STRAIN=NBRC 4177;
RX   PubMed=21608094; DOI=10.1002/cbic.201000672;
RA   Kato N., Tokuoka M., Shinohara Y., Kawatani M., Uramoto M., Seshime Y.,
RA   Fujii I., Kitamoto K., Takahashi T., Takahashi S., Koyama Y., Osada H.;
RT   "Genetic safeguard against mycotoxin cyclopiazonic acid production in
RT   Aspergillus oryzae.";
RL   ChemBioChem 12:1376-1382(2011).
CC   -!- FUNCTION: Transcription factor; part of the gene cluster that mediates
CC       the biosynthesis of the fungal neurotoxin cyclopiazonic acid (CPA), a
CC       nanomolar inhibitor of Ca(2+)-ATPase with a unique pentacyclic indole
CC       tetramic acid scaffold. {ECO:0000269|PubMed:21608094}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- DISRUPTION PHENOTYPE: Has no significant effect on the synthesis of 2-
CC       oxocyclopiazonic acid, cyclopiazonic acid (CPA) and their biosynthetic
CC       intermediates. {ECO:0000269|PubMed:21608094}.
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DR   EMBL; AB506492; BAK26563.1; -; Genomic_DNA.
DR   AlphaFoldDB; F5HN75; -.
DR   SMR; F5HN75; -.
DR   VEuPathDB; FungiDB:AO090103000027; -.
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   InterPro; IPR007219; Transcription_factor_dom_fun.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   Pfam; PF04082; Fungal_trans; 1.
DR   SMART; SM00906; Fungal_trans; 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..598
FT                   /note="Transcription factor cpaR"
FT                   /id="PRO_0000445389"
FT   DNA_BIND        22..51
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
SQ   SEQUENCE   598 AA;  67672 MW;  995B871B57140B4C CRC64;
     MPETHQNTLT WKGTRLPAGE ACNGCRERKR RCVRRKRELP CLSCQAENRP CDVSRYRRRR
     RRRRGPNKRN CKSLRVLGGQ SAEPFNMHQQ PDTDSCSEIQ HGIETDECGS QCRIPSQSPG
     PYPEPQPAAS TYSLCLPSYV TGVPKHLALV TLNALREKGA FTLPPAEIQT YLISSYIMHV
     HPDMPFLDLE RLLEAVILRC RGRQTSMLLL QAVMFAGSIF LDPVYLHLMG YTSRRAAMRD
     LFGRAKLLYE CGFEVQPTYK LQSLLLFTLF HEDDLAGSSF WMGEAWNLAK TIGLQYDLQE
     VPVDESSSEL AFRRRLWWCV YTRDRLLALS TRSAMHISDG DYNVPMLALA DFKSCFGTAE
     AYRALQLDSD LRTDGTKTAL ALTFIYKTKL SQLIGRVLMS QYTIGSASPT TMLYYPRPTP
     ISLSDFLGME NDLDVWETSL PSLLEFPLPL LSPVSQAEKI IYAQRAMLHM IYLTCINALH
     RPWSSSAQPT SSDPWEGAFR DLSAWKIEYA SQAILMIATH LHSIGLTNFL ADTAVPSLLS
     AMITHIVRLN SDILVAPEAN AVCFVQGWEC LQGLREKYEW ARHAAAFIRF TTRSLRTG