ID   BOA13_BOTFB             Reviewed;         568 AA.
AC   G0LEU0;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=C6 finger domain transcription factor BOA13 {ECO:0000303|PubMed:21722295};
DE   AltName: Full=Botcinic acid biosynthesis cluster B protein 13 {ECO:0000303|PubMed:21722295};
GN   Name=BOA13 {ECO:0000303|PubMed:21722295};
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=B05.10;
RX   PubMed=21722295; DOI=10.1111/j.1364-3703.2010.00692.x;
RA   Dalmais B., Schumacher J., Moraga J., Le Pecheur P., Tudzynski B.,
RA   Collado I.G., Viaud M.;
RT   "The Botrytis cinerea phytotoxin botcinic acid requires two polyketide
RT   synthases for production and has a redundant role in virulence with
RT   botrydial.";
RL   Mol. Plant Pathol. 12:564-579(2011).
RN   [2]
RP   FUNCTION.
RX   PubMed=23203902; DOI=10.1002/cbic.201200487;
RA   Massaroli M., Moraga J., Bastos Borges K., Ramirez-Fernandez J., Viaud M.,
RA   Gonzalez Collado I., Duran-Patron R., Hernandez-Galan R.;
RT   "A shared biosynthetic pathway for botcinins and botrylactones revealed
RT   through gene deletions.";
RL   ChemBioChem 14:132-136(2013).
CC   -!- FUNCTION: Transcription factor that probably regulates the gene
CC       clusters that mediates the biosynthesis of botcinin acid and its
CC       botcinin derivatives, acetate-derived polyketides that contribute to
CC       virulence when combined with the sesquiterpene botrydial (Probable).
CC       Botcinin acid and its derivatives have been shown to induce chlorosis
CC       and necrosis during host plant infection, but also have antifungal
CC       activities (Probable). {ECO:0000305|PubMed:21722295}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- INDUCTION: Expression of the botcinic acid clusters genes BOA1-13 and
CC       BOA17 is coregulated by BCG1 during both in vitro and in planta growth.
CC       {ECO:0000269|PubMed:21722295}.
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DR   EMBL; FR718881; CBX87035.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0LEU0; -.
DR   SMR; G0LEU0; -.
DR   VEuPathDB; FungiDB:Bcin01g00130; -.
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; 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; Virulence; Zinc.
FT   CHAIN           1..568
FT                   /note="C6 finger domain transcription factor BOA13"
FT                   /id="PRO_0000444653"
FT   DNA_BIND        14..41
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          92..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          467..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..278
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   568 AA;  63089 MW;  127AECCB1BD12678 CRC64;
     MSPPQKPPKL RHACNECHAS KVRCSGERTG CRRCVYNQQK CTYSVSMVGK VQGHRRRAAV
     TGTAPRSGAQ SLNINTSTEI ISVANADVIH DEANGNDLNS KPNDVPVESS EGITSSPAHC
     SILPGGNNGK VTTSSAPENF STSLESIDTS SLETPIIEHE FSWDFSSDER ADALNSLALE
     NPSNVDSMKN PEYGDFEYDF SIHEVPATSS SQDDSRSPKR QIADPIPISP VPKFYPSRKR
     THSDLSEKQA QHAQNDLRWR SQSQSYKRPT ISTQHHNHSF SREMYEYPES SASFDADCSF
     DRGSTSHSTT SQTNMNHQSM NRIPQTTQSN RISFTAQSHY MVSSMSSSVT HYEASWRFTS
     KCFIIISKLQ KLLRDSSSLS LDVILATNKS AISELAQMFD STLASNTARS TSPEDFFSIH
     SEIQPSNTCD TSLSTDFIPL MVYMIALKCI HDLYSQACFI FTQDDHRSRS LSTPSPRNTP
     STSNSPFSNP FGLPQLDFGT FKIDIADQRR LFSEIIAREL GNCLSACTRL RSYFLMQPGD
     ISTSTGLIEE MFLGIEEGLQ SMIKRVKI