ID   TSF1_ELSFA              Reviewed;         959 AA.
AC   B0ZT45;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Transcription factor 1 {ECO:0000303|PubMed:18957608};
DE   AltName: Full=Elsinochromes biosynthesis cluster protein TSF1 {ECO:0000303|PubMed:18957608};
GN   Name=TSF1 {ECO:0000303|PubMed:18957608};
OS   Elsinoe fawcettii (Citrus scab fungus) (Sphaceloma fawcettii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX   NCBI_TaxID=40997;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, DISRUPTION
RP   PHENOTYPE, AND INDUCTION.
RX   PubMed=18957608; DOI=10.1099/mic.0.2008/019414-0;
RA   Chung K.R., Liao H.L.;
RT   "Determination of a transcriptional regulator-like gene involved in
RT   biosynthesis of elsinochrome phytotoxin by the citrus scab fungus, Elsinoe
RT   fawcettii.";
RL   Microbiology 154:3556-3566(2008).
RN   [2]
RP   REVIEW.
RX   PubMed=21199563; DOI=10.1111/j.1364-3703.2010.00663.x;
RA   Chung K.R.;
RT   "Elsinoe fawcettii and Elsinoe australis: the fungal pathogens causing
RT   citrus scab.";
RL   Mol. Plant Pathol. 12:123-135(2011).
CC   -!- FUNCTION: Elsinochromes biosynthesis cluster-specific transcription
CC       factor that positively regulates the expression of cluster genes
CC       including RDT1, PKS1, PRF1 and HP1, and subsequent elsinochromes
CC       production. {ECO:0000269|PubMed:18957608}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- INDUCTION: Expression is induced by the presence of the cluster-
CC       specific polyketide synthase PKS1 (PubMed:18957608). Expression is up-
CC       regulated during nitrogen starvation or at alkaline pH, but repressedin
CC       the presence of large amounts of glucose (PubMed:18957608).
CC       {ECO:0000269|PubMed:18957608}.
CC   -!- DISRUPTION PHENOTYPE: Blocks the expression of the elsinochrome cluster
CC       genes RDT1, PKS1, PRF1 and HP1, and impairs the production of
CC       elsinochrome. {ECO:0000269|PubMed:18957608}.
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DR   EMBL; EU401705; ABZ01831.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0ZT45; -.
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   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
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; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..959
FT                   /note="Transcription factor 1"
FT                   /id="PRO_0000445820"
FT   ZN_FING         2..24
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         30..52
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   DNA_BIND        79..105
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          154..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   959 AA;  106607 MW;  B1DFB0B4EE4A2D42 CRC64;
     MVFCTYCGHS FTRDEHLERH ILTHTNVKPF KCFTCHMSFA RRDLLQGHYT VHGRNQDQQE
     IPAANGMIPK SAGRTPIACS NCAKTKTKCD KKFPCSRCAS RNLRCTLRPT LVSTKNAARM
     GLITPETIAQ DIANGTLPPD QTVAAEKVPL PIAPTGHVEE SSKSSSPSGS PTSISHNSTG
     SDAPPAPMFD QFNGCPTPPQ GLSPTTPSGQ GFNGPASFPG FDDYNQQIGK TSAEDCNLHF
     MLDWQQLQLP IGLDPMLQPD MLGDQDLNFD MGAMGLGTQM EPILSINPEL TNNMPPPLIT
     PIETPKFDRS SSDLDAFSSG LHDRQYSVVS NQSVDSHYQA PPQPDPVVVA QDGWNVFRCV
     PSVHPSACPS TARWNLEALE STLQNHDGRS KWRPEVDENL FDGSDQLAVM QIHESTRDKL
     LAITQGFLHK ALEIHRGNEA AQTYAPSNFV LLPPTKVLEY FLRSYTNSFE RFYPLTSKGS
     LDANELMFCY QDRASSLLIL LMVAQGAMNV PSREARSLTG GLVETCRISL FDLIERNIVM
     ASDHNVLHAA LIFTELASWS GDKWQMDIAM GQRGMYAAML RHSGVLDRTT YPPQGSFSDG
     QTNADHMWNL WIQQESRSRP VYSWAMVDQE LALFHGASPL FSVTEFGIAL PHNEELWRAK
     SAGEWTSLMG QRVSTTDSDA TASPPSLRDL SRRFLDDEMD SAECFLNPMH LRLLLLPLQA
     MVGHYQQLMC CFSDSGSSRV KNKTVTASST RCRLEEVQCL LQRWYNIAMD YLKEHSVCSV
     MQASLVLYHL ISLNAVTDFV QIERLARRET FDGTYQSLVW THKRCITDVG EAIFHCGQVI
     SLIRSMPRSV RPPWWAASIY RVALVLWCDS LIDKDGSSSY GGKSGQTFAV DALPSDHPLI
     QRYLNKGEGT PRLSKRDGST IGLDHGLTVL NHCAEIIDEG ATSRFQEGIR GKLDRLMRT