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CLAE_PASFU
ID   CLAE_PASFU              Reviewed;         446 AA.
AC   P0CU72;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2018, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Cladofulvin biosynthesis regulatory protein claE {ECO:0000303|PubMed:27274078};
DE   AltName: Full=Cladofulvin biosynthesis cluster protein E {ECO:0000303|PubMed:27274078};
GN   Name=claE {ECO:0000303|PubMed:27274078}; ORFNames=Clafu184394;
OS   Passalora fulva (Tomato leaf mold) (Cladosporium fulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Fulvia.
OX   NCBI_TaxID=5499;
RN   [1]
RP   IDENTIFICATION, AND FUNCTION.
RX   PubMed=24465762; DOI=10.1371/journal.pone.0085877;
RA   Collemare J., Griffiths S., Iida Y., Karimi Jashni M., Battaglia E.,
RA   Cox R.J., de Wit P.J.;
RT   "Secondary metabolism and biotrophic lifestyle in the tomato pathogen
RT   Cladosporium fulvum.";
RL   PLoS ONE 9:E85877-E85877(2014).
RN   [2]
RP   INDUCTION, AND FUNCTION.
RX   PubMed=27274078; DOI=10.1073/pnas.1603528113;
RA   Griffiths S., Mesarich C.H., Saccomanno B., Vaisberg A., De Wit P.J.,
RA   Cox R., Collemare J.;
RT   "Elucidation of cladofulvin biosynthesis reveals a cytochrome P450
RT   monooxygenase required for anthraquinone dimerization.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:6851-6856(2016).
RN   [3]
RP   INDUCTION.
RX   PubMed=27997759; DOI=10.1111/mpp.12527;
RA   Griffiths S., Mesarich C.H., Overdijk E.J.R., Saccomanno B.,
RA   de Wit P.J.G.M., Collemare J.;
RT   "Down-regulation of cladofulvin biosynthesis is required for biotrophic
RT   growth of Cladosporium fulvum on tomato.";
RL   Mol. Plant Pathol. 19:369-380(2018).
CC   -!- FUNCTION: Transcription factor involved in regulation of the gene
CC       cluster that mediates the biosynthesis of cladofulvin, a conidial
CC       pigment not required for virulence but that plays a role in fitness and
CC       resistance to environmental stresses including UV light and low-
CC       temperature stress. {ECO:0000269|PubMed:24465762,
CC       ECO:0000269|PubMed:27274078}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- INDUCTION: Expression is positively regulated by the transcriptional
CC       regulator wor1 (PubMed:27274078). Expression is down-regulated during
CC       biotrophic growth within tomato leaves (PubMed:27997759).
CC       {ECO:0000269|PubMed:27274078, ECO:0000269|PubMed:27997759}.
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DR   AlphaFoldDB; P0CU72; -.
DR   SMR; P0CU72; -.
DR   OMA; ACARCIE; -.
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..446
FT                   /note="Cladofulvin biosynthesis regulatory protein claE"
FT                   /id="PRO_0000445892"
FT   DNA_BIND        59..86
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          13..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          94..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..134
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   446 AA;  48397 MW;  F3F6FC2D732220AA CRC64;
     MSLSRSVAAM HFPVTAPPPV PVPHAPHTGG LHEATATASS SAGPTSTSIA AGPRVRSSCE
     TCAASKLKCS KERPRCARCV KRGLDCTYVL LKRAGRKPGQ PQTSSRSRRR EPSSGGPSPP
     SGVTGTSTSS DMLQDLFGTP LDMTVDGFDA AMSDSSTFHS SDLLDDHSLS AFTADPFFIH
     GLDDQQLHSI CDDDPHSMLG VPPLMNHALM EPRTPRALSI SDNGSQHLRT GRLDGVSCSC
     LARVLSLFQR YSASSESLCM HQRKPELDER LENVSTQSIL SQNGTAVELL SGILESPCCQ
     DGYLVVMVAL VTFKILGWYS AVAQRTKTLL PGERHNPSPS FDEQHSNTTT TIRGFCLDGE
     DSERRTVQLI LGELHPVRQL IERFALRLKL LVEEMQDADK AGVAAKDLCA NAMLSTSTLV
     YKQLETDLRS EWRALSARVI DRLKNL
 
 
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