RGLT_ASPFC
ID RGLT_ASPFC Reviewed; 410 AA.
AC B0XQ41;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Transcription factor rglT {ECO:0000303|PubMed:32667960};
DE AltName: Full=Regulator of gliotoxin {ECO:0000303|PubMed:32667960};
GN Name=rglT {ECO:0000303|PubMed:32667960}; ORFNames=AFUB_008610;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=32667960; DOI=10.1371/journal.ppat.1008645;
RA Ries L.N.A., Pardeshi L., Dong Z., Tan K., Steenwyk J.L., Colabardini A.C.,
RA Ferreira Filho J.A., de Castro P.A., Silva L.P., Preite N.W., Almeida F.,
RA de Assis L.J., Dos Santos R.A.C., Bowyer P., Bromley M., Owens R.A.,
RA Doyle S., Demasi M., Hernandez D.C.R., Netto L.E.S., Pupo M.T., Rokas A.,
RA Loures F.V., Wong K.H., Goldman G.H.;
RT "The Aspergillus fumigatus transcription factor RglT is important for
RT gliotoxin biosynthesis and self-protection, and virulence.";
RL PLoS Pathog. 16:e1008645-e1008645(2020).
CC -!- FUNCTION: Transcription factor that is involved in protection against
CC oxidative stress (PubMed:32667960). Binds to promoter regions of the
CC gliotoxin (GT) biosynthetic genes gliZ, gliF, gliT, gliM, gliA and gtmA
CC (PubMed:32667960). Two related but different DNA motifs (5'-TCGG-3' and
CC 5'-CGGNCGG-3') are specifically enriched among rglT binding sites in
CC GT-inducing conditions (PubMed:32667960). Also indirectly regulates the
CC expression of gliP, gliG, gliH and gliN (PubMed:32667960). Plays a key
CC role in resistance against exogenously-added GT and GT biosynthesis,
CC mainly through the direct regulation of gliT (PubMed:32667960).
CC Furthermore, rglT is important for virulence in chemotherapeutic mice
CC with invasive pulmonary aspergillosis (IPA) (PubMed:32667960).
CC {ECO:0000269|PubMed:32667960}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227,
CC ECO:0000269|PubMed:32667960}.
CC -!- DISRUPTION PHENOTYPE: Leads to high sensitivity to allyl alcohol, a
CC compound indicative for potential defects in carbon catabolite
CC repression (CCR), but does not affect growth in non-stress conditions,
CC nor in the presence of 2-deoxyglucose (2DG), an additional indicator
CC for defects in CCR (PubMed:32667960). Leads also to sensitivity to
CC acrolein, menadione and t-butyl hydroperoxide (PubMed:32667960).
CC Abolishes the production of gliotoxin (GT) and accumulates
CC bisdethiobis(methylthio)-gliotoxin (BmGT) (PubMed:32667960). Leads to
CC reduced expression of gliZ, gliT, gliF and gtmA in GT-inducing
CC conditions (PubMed:32667960). Loses all ability to protect itself
CC against exogenously added GT as well and reduces virulence
CC (PubMed:32667960). {ECO:0000269|PubMed:32667960}.
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DR EMBL; DS499594; EDP56155.1; -; Genomic_DNA.
DR EnsemblFungi; EDP56155; EDP56155; AFUB_008610.
DR VEuPathDB; FungiDB:AFUB_008610; -.
DR HOGENOM; CLU_026660_1_0_1; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
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:0008152; P:metabolic process; IEA:UniProt.
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; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 3: Inferred from homology;
KW DNA-binding; Nucleus; Transcription; Transcription regulation; Virulence;
KW Zinc.
FT CHAIN 1..410
FT /note="Transcription factor rglT"
FT /id="PRO_0000454487"
FT DNA_BIND 28..55
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 410 AA; 44548 MW; 89E28C422A33C872 CRC64;
MQFDSLPLPP SSSHDTTSVP PLKRHAACDE CRKRKLKCSG EATGCSRCLK QSLPCHYSLQ
KPMGRPPKKR PREDNDASVY EITDNGMWAD IDDGGILTEE AGAEATAASD ALRLCPPVYT
APMRMPQAFP NLLSTDDSHN HLWQLESGRS LDPIPATTGP WPDFSSVTAA TSSPFTLPSS
LTLIDSPSVS SPSSDGGNSS QCTCLSYLYL CLSHLSSLAP FPISQHTLCS LFIAAKTARA
VIRCEVCPTS FALGMQNVMF TGTLLNVIAD AWLRVSQADA EELGKLAAPP AYVASVTQNS
PNPAEAWKDW LRQTVRSAIT GGPADPAGQV KCSDSPTLLS LIEEMEARQH RWHRTRTVES
PNEPGSCSPV SHEDHREEDM LCFRVIRSAR DVIAKFEFAP HEYPEGVVPV
