ID   VERZ_CLORO              Reviewed;         458 AA.
AC   A0A1U9YI06;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Transcription factor verZ {ECO:0000303|PubMed:28376389};
DE   AltName: Full=Verticillin biosynthesis cluster protein Z {ECO:0000303|PubMed:28376389};
GN   Name=verZ {ECO:0000303|PubMed:28376389};
OS   Clonostachys rogersoniana.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Bionectriaceae; Clonostachys.
OX   NCBI_TaxID=122658;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=XZC04-CC-302;
RX   PubMed=28376389; DOI=10.1016/j.fgb.2017.03.007;
RA   Wang Y., Hu P., Pan Y., Zhu Y., Liu X., Che Y., Liu G.;
RT   "Identification and characterization of the verticillin biosynthetic gene
RT   cluster in Clonostachys rogersoniana.";
RL   Fungal Genet. Biol. 103:25-33(2017).
RN   [2]
RP   FUNCTION, DNA-BINDING, AND DISRUPTION PHENOTYPE.
RX   PubMed=29058652; DOI=10.1099/mic.0.000557;
RA   Guo Z., Hao T., Wang Y., Pan Y., Ren F., Liu X., Che Y., Liu G.;
RT   "VerZ, a Zn(II)2Cys6 DNA-binding protein, regulates the biosynthesis of
RT   verticillin in Clonostachys rogersoniana.";
RL   Microbiology 163:1654-1663(2017).
CC   -!- FUNCTION: Transcription factor; part of the gene cluster that mediates
CC       the biosynthesis of 11'-deoxyverticillin A, one of the dimeric
CC       epipolythiodioxopiperazines (ETPs) from the verticillin family that act
CC       as mycotoxins (PubMed:28376389, PubMed:29058652). 11'-deoxyverticillin
CC       A is required for normal conidiation (PubMed:28376389). Directly binds
CC       the consensus motif 5'-(T/C)(C/A)(G/T)GN3CC(G/T)(A/G)(G/C)-3' localized
CC       in the upstream regions of the verticillin biosynthetic genes
CC       (PubMed:29058652). {ECO:0000269|PubMed:28376389,
CC       ECO:0000269|PubMed:29058652}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- DISRUPTION PHENOTYPE: Significantly decreases 11'-deoxyverticillin A
CC       production.
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DR   EMBL; KY359203; AQZ42167.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U9YI06; -.
DR   SMR; A0A1U9YI06; -.
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; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..458
FT                   /note="Transcription factor verZ"
FT                   /id="PRO_0000450171"
FT   DNA_BIND        117..144
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          153..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   458 AA;  49886 MW;  F3B96D6C10F4325E CRC64;
     MVPRTGRRKT NYAVPPPVLQ LASGWSALVV CLLHLLFSFL YGGGQQPIHP RPSSRLPRIF
     SFADRDIMRI GLPTQDFHAE HLGAIDPSSH HHMSQMAGQN GISHAQGRRG PKYRTSCDRC
     QAAKVKCGHE KPSCRRCTYH KVECVYGISR RMGRPRAKKN SGKDASPSPQ GSINGASDEN
     SRSKSATPAP VSFTGTEPIT EARQSPVANA EGGRISRAES TQRAEPWTPS LTTNFEHPET
     SEGADDSAHG PMMQSMNTPL TFLPTENRME LDDFNDYPPM SSFMEDLADP MMSQQPISAP
     PSLDILDPHA LIPDRTPTGN TRDTFNQVDT GLSVSLPQTT QLWNTSQAHQ LHALFESNST
     SKSKRRASTG QEISGIVSFN SVGHSNSGFG NKRMGELQIA TGPLVSIGAG EQSAMMNIGP
     NPDTSSVAAS RKFAMEEEDD PCSEIKLNPN RLRLEDGK