ID   CTB8_CERNC              Reviewed;         397 AA.
AC   A0ST46;
DT   12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Cercosporin biosynthesis regulatory protein CTB8 {ECO:0000303|PubMed:17462021};
DE   AltName: Full=Cercosporin toxin biosynthesis cluster protein 8 {ECO:0000303|PubMed:17462021};
GN   Name=CTB8 {ECO:0000303|PubMed:17462021};
OS   Cercospora nicotianae (Barn spot disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=29003;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17462021; DOI=10.1111/j.1365-2958.2007.05689.x;
RA   Chen H., Lee M.H., Daub M.E., Chung K.R.;
RT   "Molecular analysis of the cercosporin biosynthetic gene cluster in
RT   Cercospora nicotianae.";
RL   Mol. Microbiol. 64:755-770(2007).
RN   [2]
RP   REVIEW ON CERCOSPORIN.
RX   PubMed=11701851; DOI=10.1146/annurev.phyto.38.1.461;
RA   Daub M.E., Ehrenshaft M.;
RT   "The photoactivated cercospora toxin cercosporin: contributions to plant
RT   disease and fundamental biology.";
RL   Annu. Rev. Phytopathol. 38:461-490(2000).
RN   [3]
RP   FUNCTION.
RX   PubMed=26938470; DOI=10.1021/jacs.6b00633;
RA   Newman A.G., Townsend C.A.;
RT   "Molecular characterization of the cercosporin biosynthetic pathway in the
RT   fungal plant pathogen Cercospora nicotianae.";
RL   J. Am. Chem. Soc. 138:4219-4228(2016).
CC   -!- FUNCTION: Transcription regulator of the gene cluster that mediates the
CC       biosynthesis of cercosporin, a light-activated, non-host-selective
CC       toxin (PubMed:17462021, PubMed:26938470). The perylenequinone
CC       chromophore of cercosporin absorbs light energy to attain an
CC       electronically-activated triplet state and produces active oxygen
CC       species such as the hydroxyl radical, superoxide, hydrogen peroxide or
CC       singlet oxygen upon reaction with oxygen molecules. These reactive
CC       oxygen species cause damage to various cellular components including
CC       lipids, proteins and nucleic acids (PubMed:11701851).
CC       {ECO:0000269|PubMed:17462021, ECO:0000269|PubMed:26938470,
CC       ECO:0000303|PubMed:11701851}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- DISRUPTION PHENOTYPE: Blocks the expression of the cercosporin cluster
CC       and abolishes the production of cercosporin.
CC       {ECO:0000269|PubMed:17462021}.
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DR   EMBL; DQ991510; ABK64185.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0ST46; -.
DR   SMR; A0ST46; -.
DR   PHI-base; PHI:1050; -.
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   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..397
FT                   /note="Cercosporin biosynthesis regulatory protein CTB8"
FT                   /id="PRO_0000444972"
FT   DNA_BIND        26..53
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          62..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   397 AA;  42300 MW;  85E400E1EBEF8603 CRC64;
     MAKGSAGDAP NTRDTSFKRP KIRESCTHCS SQKIRCTKER PACARCVNKG LLCQYNISRR
     TGTRRHSVRA TPEPETTISN APTSSVPPDS VKIDGKQSPA MSDFALLDGL ETFNNSLWHQ
     PITTDIQDID MQYFDFFDPG GYQAEPEPIN SFDIDSTLLC GTSTAGYLPE LDAEASTRPS
     SSSSPPSQRS DGGRATTHGG GGCISTALQI FSELHVSSSA CPIAAGAPSH NIREFDHVLD
     SNRAALEKLS SILDCPPCCH DQEVLTALFL AVQKALSWYS AALDVAGDGE PTSPSSRVKS
     PPAFLGSYAL GAQAQTLARA YVVMAQLQQH FQPLLAKLQR KSSLSALGAR SSSTTSLSSV
     SSLQSSTSGS AVIECQKRAL QEALEDVVAK IEGIKRG