TOXE_COCCA
ID TOXE_COCCA Reviewed; 441 AA.
AC O74205;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Transcription factor TOXE;
GN Name=TOXE;
OS Cochliobolus carbonum (Maize leaf spot fungus) (Bipolaris zeicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=5017 {ECO:0000312|EMBL:AAD13811.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 90305 / SB111 / 2R15;
RX PubMed=9894916; DOI=10.1007/pl00008632;
RA Ahn J.-H., Walton J.D.;
RT "Regulation of cyclic peptide biosynthesis and pathogenicity in
RT Cochliobolus carbonum by TOXEp, a novel protein with a bZIP basic DNA-
RT binding motif and four ankyrin repeats.";
RL Mol. Gen. Genet. 260:462-469(1998).
RN [2] {ECO:0000305}
RP FUNCTION.
RC STRAIN=ATCC 90305 / SB111 / 2R15;
RX PubMed=11698648; DOI=10.1073/pnas.231491298;
RA Pedley K.F., Walton J.D.;
RT "Regulation of cyclic peptide biosynthesis in a plant pathogenic fungus by
RT a novel transcription factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14174-14179(2001).
CC -!- FUNCTION: A pathway-specific transcription factor which co-ordinates
CC the expression of genes involved in HC-toxin biosynthesis. Binds to the
CC tox-box, a 10-bp motif with the consensus 5'-ATCTCNCGNA-3', which is
CC found in the promoter of all genes involved in HC-toxin biosynthesis.
CC Required for pathogenicity of the fungus on maize.
CC {ECO:0000269|PubMed:11698648, ECO:0000269|PubMed:9894916}.
CC -!- PATHWAY: Mycotoxin biosynthesis; HC-toxin biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11698648, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; AF038874; AAD13811.1; -; Genomic_DNA.
DR AlphaFoldDB; O74205; -.
DR SMR; O74205; -.
DR PRIDE; O74205; -.
DR UniPathway; UPA00874; -.
DR PHI-base; PHI:233; -.
DR PHI-base; PHI:6810; -.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0009403; P:toxin biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF13637; Ank_4; 1.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 3: Inferred from homology;
KW Activator; ANK repeat; DNA-binding; Nucleus; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..441
FT /note="Transcription factor TOXE"
FT /id="PRO_0000076640"
FT REPEAT 289..318
FT /note="ANK 1"
FT /evidence="ECO:0000305"
FT REPEAT 322..351
FT /note="ANK 2"
FT /evidence="ECO:0000305"
FT REPEAT 355..384
FT /note="ANK 3"
FT /evidence="ECO:0000305"
FT REPEAT 413..440
FT /note="ANK 4"
FT /evidence="ECO:0000305"
FT REGION 209..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 48983 MW; AD0473DFD9E65A19 CRC64;
MGTTSPNSEK RQITDINERR KLQNRVAQRK YRTRQKTRMK LAEAVLNDYT YIHPTLGTIQ
SKKKSPLTME CDRSSASYPD LSSYAEICSE TRSETQATRA RQLTSQRTCF RESVDNNQAD
SHAQLSRCLN RQEMFYGISG ETEFSEGDTR DRVECIDPNL TRGWLDMDLR SGTPNSSTVV
DCGLCTVGAN SQPPTRTNVQ EAIETLELFE PNDQRKTENL PREPCGSCPS SSHGYSPTSG
NPSTLLLTPS ESLMNSVIVT SDSPLLAADD KSPGDLVISE ANTHGPKEDQ FSPLMTAISL
GRLDIARILL QSGAPLDIPD DSGKTALHRA VGRRELHMVE ALLNLGAEML ATDHEGNSLL
HIAVKTNSLS ITRLLLERYK SCRELKDAQL GHGCRQHGNQ VHSESWIDLR NREGMTAVHL
SVIFNRPEIL QLLVKYSANV N