TAS2_MAGO7
ID TAS2_MAGO7 Reviewed; 771 AA.
AC G4N134;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Transcription factor TAS2 {ECO:0000303|PubMed:28820236};
DE AltName: Full=Tenuazonic acid biosynthesis cluster protein 2 {ECO:0000303|PubMed:28820236};
GN Name=TAS2 {ECO:0000303|PubMed:28820236}; ORFNames=MGG_07800;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28820236; DOI=10.1021/acschembio.7b00353;
RA Yun C.S., Motoyama T., Osada H.;
RT "Regulatory mechanism of mycotoxin tenuazonic acid production in
RT Pyricularia oryzae.";
RL ACS Chem. Biol. 12:2270-2274(2017).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=32765467; DOI=10.3389/fmicb.2020.01641;
RA Ninomiya A., Urayama S.I., Suo R., Itoi S., Fuji S.I., Moriyama H.,
RA Hagiwara D.;
RT "Mycovirus-induced tenuazonic acid production in a rice blast fungus
RT Magnaporthe oryzae.";
RL Front. Microbiol. 11:1641-1641(2020).
CC -!- FUNCTION: Transcription factor; part of the gene cluster that mediates
CC the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of
CC protein biosynthesis on ribosomes by suppressing the release of new
CC protein (PubMed:28820236, PubMed:32765467). Directly regulates the
CC expression of the hybrid PKS-NRPS synthetase TAS1 and the susequent
CC production of TeA (PubMed:32765467). {ECO:0000269|PubMed:28820236,
CC ECO:0000269|PubMed:32765467}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC -!- INDUCTION: Expression is induced by the presence of dimethylsulphoxide
CC (DMSO) or by the deletion of OSM1, a HOG1-related mitogen-activated
CC protein kinase (PubMed:28820236). Expression is positively regulated by
CC the secondary metabolism regulator LAE1 (PubMed:28820236). Infection by
CC the totivirus induces the transcription of TAS2 (PubMed:32765467).
CC {ECO:0000269|PubMed:28820236, ECO:0000269|PubMed:32765467}.
CC -!- DISRUPTION PHENOTYPE: Impairs the ability to produce TeA under the
CC DMSO-added, TeA-inducing culture conditions.
CC {ECO:0000269|PubMed:28820236}.
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DR EMBL; CM001233; EHA53210.1; -; Genomic_DNA.
DR RefSeq; XP_003713017.1; XM_003712969.1.
DR AlphaFoldDB; G4N134; -.
DR EnsemblFungi; MGG_07800T0; MGG_07800T0; MGG_07800.
DR GeneID; 2683727; -.
DR KEGG; mgr:MGG_07800; -.
DR VEuPathDB; FungiDB:MGG_07800; -.
DR eggNOG; ENOG502SJ9D; Eukaryota.
DR HOGENOM; CLU_013260_2_0_1; -.
DR InParanoid; G4N134; -.
DR OMA; RCSRQFP; -.
DR OrthoDB; 1056082at2759; -.
DR PHI-base; PHI:5606; -.
DR Proteomes; UP000009058; Chromosome 3.
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:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF04082; Fungal_trans; 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; Reference proteome; Transcription;
KW Transcription regulation; Virulence; Zinc.
FT CHAIN 1..771
FT /note="Transcription factor TAS2"
FT /id="PRO_0000452834"
FT DNA_BIND 54..80
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 33..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 83821 MW; DF82D245EB6AAC53 CRC64;
MRQNSDYPSL GPFFFAGKIK LSIATESFSA MKRSRAESAS GPQQPSRRQP QTSCDLCRSR
KIKCDRGTPC GNCRTRGLAC SIMSPSSAPS PGASSAESAG HGRLDTAILA RLAALEQAVF
RSTSAVGGSG NAENGAHGDA TPRVPLSGLE REGRQTANFL DKAYDRCSSA STRSGYRPLD
IRVAESCRDS FATGAPDPVW LMPQKDAVAM VHDFVENIYH LMPIVHIGST VSVIDNVYPA
LQAGNINHVD PAQVALILGI CAACAFFWDG GVPCQHRFET EGEATSASLI WKTSALYAFE
EAQRRGSRSL EGAQACAILA YLTYNMDGPS TRFYRLHTCS VTACRELGIH LVDSRGCEST
DSTARRELKR RLWWHVAATD WMLGLNGGPL DGTYTVHPRQ ARVALPRNLN DSDLAIDSEI
LTMPPHVPTQ ASCFLQVIRL AEICRMVVDS QSPDDSIADT AYNERVLASD ELFKKAIESM
PPPLVLTSPI PEGAPRFLCL QRASLHLGFH SRRARLLRPF LLYKDSDGRQ GTTYRRSREL
CVRSAQTVLE ISTSLLEHSL RIRSPEPFRR QILHHPGHHS CPASPIHRLG VVVNHLFCAC
AILAFECSLR KNSSVHPRQQ HRGAGGEDDL DGMLVHAYRL LAAAGEECTV AADLVCAMRG
VFAKYRVDGD LATVDGRGGQ NQIVGSSRSA MASVQTSAGG ACNEQQQIGP AAWPGMRGAI
PDENQPMGEG SLETGKAWDG FDKDLDDLFV ANDTYCSWDQ IFARLGSYCG P