ID   CTB8_CERBT              Reviewed;         397 AA.
AC   A0A2G5ICB4;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Cercosporin biosynthesis regulatory protein CTB8 {ECO:0000303|PubMed:29844193};
DE   AltName: Full=Cercosporin toxin biosynthesis cluster protein 8 {ECO:0000303|PubMed:29844193};
GN   Name=CTB8 {ECO:0000303|PubMed:29844193}; ORFNames=CB0940_00837;
OS   Cercospora beticola (Sugarbeet leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=122368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=09-40;
RX   PubMed=29844193; DOI=10.1073/pnas.1712798115;
RA   de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA   Spanner R.E., Neubauer J.D., Jurick W.M. II, Stott K.A., Secor G.A.,
RA   Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT   "Gene cluster conservation provides insight into cercosporin biosynthesis
RT   and extends production to the genus Colletotrichum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:E5459-E5466(2018).
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).
CC   -!- FUNCTION: Transcription regulator of the gene cluster that mediates the
CC       biosynthesis of cercosporin, a light-activated, non-host-selective
CC       toxin (By similarity). The perylenequinone chromophore of cercosporin
CC       absorbs light energy to attain an electronically-activated triplet
CC       state and produces active oxygen species such as the hydroxyl radical,
CC       superoxide, hydrogen peroxide or singlet oxygen upon reaction with
CC       oxygen molecules (PubMed:11701851). These reactive oxygen species cause
CC       damage to various cellular components including lipids, proteins and
CC       nucleic acids (PubMed:11701851). {ECO:0000250|UniProtKB:A0ST46,
CC       ECO:0000303|PubMed:11701851}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
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DR   EMBL; LKMD01000100; PIB02401.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5ICB4; -.
DR   SMR; A0A2G5ICB4; -.
DR   OrthoDB; 1396569at2759; -.
DR   Proteomes; UP000230605; Chromosome 1.
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   3: Inferred from homology;
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_0000449872"
FT   DNA_BIND        26..53
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          63..90
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..87
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;  42288 MW;  C73815F8421C778A CRC64;
     MAKGSAGDAP NTRDTSFKRP KIRESCTHCS SQKIRCTKER PACARCVNKG LLCQYNISRR
     TGTRRHSVRA TPEPETTISN APTSSVAPDS VKIDGKRSPA MSDFALLDGL ETFDNSLWHQ
     PITTDIQDID MQYFDFFDPG GYQAEPEPIN SFDIDSTLLC GTSTAGYLPE LDAEASTRPS
     SSSSPPSQRS DGGRATTHGG GGCISTALQI FSELHVSSSA CPIAAGAPSH NIREFDHVLD
     SNRAALEKLS SILDCPPCCH DQEVLTALFL AVQKALSWYS AALDVAGDGE PTSPSSRVKS
     PPAFLGSYAL GAQAQTLARA YVVMAQLQQH FQPLLAKLQR ISSLSALGAR SSSTTSLSSV
     SSLQSSTSGS AVIECQKRAL QEALEDVVAK IEGIKRG