ID   CLAA_PENCR              Reviewed;         476 AA.
AC   A0A481WNM7;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-JUN-2019, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Transcriptional regulator claA {ECO:0000303|PubMed:30811183};
DE   AltName: Full=Clavatol biosynthesis cluster protein A {ECO:0000303|PubMed:30811183};
GN   Name=claA {ECO:0000303|PubMed:30811183};
OS   Penicillium crustosum (Blue mold fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=36656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=PRB-2;
RX   PubMed=30811183; DOI=10.1021/jacs.9b00110;
RA   Fan J., Liao G., Kindinger F., Ludwig-Radtke L., Yin W.B., Li S.M.;
RT   "Peniphenone and penilactone formation in Penicillium crustosum via 1,4-
RT   Michael additions of ortho-quinone methide from hydroxyclavatol to gamma-
RT   butyrolactones from Crustosic Acid.";
RL   J. Am. Chem. Soc. 141:4225-4229(2019).
CC   -!- FUNCTION: Transcriptional regulator; part of the cla gene cluster that
CC       produces clavatol and ortho-quinone methide (PubMed:30811183). The
CC       clavatol biosynthesis cluster cla and the terrestric acid cluster tra
CC       are both involved in the production of peniphenones and penilactones
CC       (PubMed:30811183). {ECO:0000269|PubMed:30811183}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
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DR   EMBL; MK360918; QBK15039.1; -; Genomic_DNA.
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   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; -; 1.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; SSF57701; 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..476
FT                   /note="Transcriptional regulator claA"
FT                   /id="PRO_0000455056"
FT   DNA_BIND        25..52
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          63..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   476 AA;  51649 MW;  18AE2ADB18BD07AC CRC64;
     MLLQPESSSK PRNDSPPGFK FHSSCDTCLK AKIKCSQAKP TCARCLQQGR QCVYSPYRKI
     GRPSTKNLPL DQLQQPKGRT AGGTARRSLS RRVSLASPGI ENGSRVGNVR HATNRVLHAQ
     ESVLVPSQTW SDQELTGNIN RLDYGLEGTN WSALEGLLDA SMSTLPQADH ELASAVPRLD
     QVHDLDPNPG QEDLTGYLSP SSLSSRESLA TTFPPEAEAG SFGLSSEFPF SAGYSLGTGP
     VLSESLNAFP VLSSFPSSAS SPVTEARGFN LLSAPTDRCT FQCYPVLINI LNDMNEFQRK
     SSGLPLDVLL NLDKRVRKVH ETILGCPCCL VSCAAALTLM LITMVNINLL SLFERSCGST
     DGGSGSSMSR GELNVAPRIA FGGGNYAGQD RSRNPLPYTT GHLTLGNIHL DETVKLVFSR
     RLVRLYLERQ LGVVQQLSQL LGRVEGDGAS IKVTQDLLRD QLRRLEHFVG FITLTD