ID   RADR_FLOCH              Reviewed;         453 AA.
AC   C5H883;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Transcription factor radR {ECO:0000303|PubMed:19101477};
DE   AltName: Full=Radicicol biosynthesis cluster regulator {ECO:0000303|PubMed:19101477};
GN   Name=radR {ECO:0000303|PubMed:19101477};
OS   Floropilus chiversii (Chaetomium chiversii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Floropilus.
OX   NCBI_TaxID=2587399;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=CS-36-62;
RX   PubMed=19101477; DOI=10.1016/j.chembiol.2008.10.006;
RA   Wang S., Xu Y., Maine E.A., Wijeratne E.M., Espinosa-Artiles P.,
RA   Gunatilaka A.A., Molnar I.;
RT   "Functional characterization of the biosynthesis of radicicol, an Hsp90
RT   inhibitor resorcylic acid lactone from Chaetomium chiversii.";
RL   Chem. Biol. 15:1328-1338(2008).
CC   -!- FUNCTION: Transcription factor that positively regulates the expression
CC       of the gene clusters that mediate the biosynthesis of pestheic acid, a
CC       diphenyl ether which is a biosynthetic precursor of the unique
CC       chloropupukeananes (PubMed:19101477). {ECO:0000269|PubMed:19101477}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Completely abolishes the production of radicicol
CC       (PubMed:19101477). {ECO:0000269|PubMed:19101477}.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR   EMBL; EU980390; ACM42404.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5H883; -.
DR   SMR; C5H883; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Nucleus; Transcription; Transcription regulation.
FT   CHAIN           1..453
FT                   /note="Transcription factor radR"
FT                   /id="PRO_0000443058"
FT   DOMAIN          30..62
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          33..50
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          51..58
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          160..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   453 AA;  49669 MW;  D4745AE02D1527AB CRC64;
     MPNNLQHQEG SYSLRSSNDV SPADDWTQTN DPKEKKRIQN RVAQRTYRNR IRARLEELEN
     KIRCHEKASK QDGNENEDRA SEKAMAQDFL ITDQALQSLT LPRRVSSAGL SQEPATPPDL
     LLPSFFHQQQ VKIPSAADEL NQPKPPSSPP AWAEGQLNVA PRAAQARSIA PTSTGMHQIS
     PSYGPPVFLP TEDLSIDIIS SRGLSSSWKT AADLTVQGTH PLPAFPSCSL ANIESPSPAS
     SQATDPMDMT FHTATEANTA ILPGHRSSLD ERLEYVLERA EQVGFDNFDS LVTAYYSETF
     HGSSRLASEQ RLSRNRRLPR VIAEIFRAAS HWSAWERGGM NQEVIKSAEC LLISEGTAAR
     NALEGSLSLL VDGGNGSGDA SSVERLVQNE IPNLWALMTS LASGTHSPRQ QDRSGTALAA
     IMLLYFSGSM PKEQLLRLLI ICLPDPVSPQ KNN