GSFR2_PENAE
ID GSFR2_PENAE Reviewed; 415 AA.
AC D7PI10;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Transcription factor gsfR2 {ECO:0000303|PubMed:20534346};
DE AltName: Full=Griseofulvin synthesis protein R2A {ECO:0000303|PubMed:20534346};
GN Name=gsfR2 {ECO:0000303|PubMed:20534346};
OS Penicillium aethiopicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36650;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=IBT 5753;
RX PubMed=20534346; DOI=10.1016/j.chembiol.2010.03.015;
RA Chooi Y.H., Cacho R., Tang Y.;
RT "Identification of the viridicatumtoxin and griseofulvin gene clusters from
RT Penicillium aethiopicum.";
RL Chem. Biol. 17:483-494(2010).
RN [2]
RP BIOTECHNOLOGY.
RX PubMed=13577889; DOI=10.1038/182476a0;
RA Gentles J.C.;
RT "Experimental ringworm in guinea pigs: oral treatment with griseofulvin.";
RL Nature 182:476-477(1958).
RN [3]
RP BIOTECHNOLOGY.
RX PubMed=4583105; DOI=10.1038/244292a0;
RA Gull K., Trinci A.P.;
RT "Griseofulvin inhibits fungal mitosis.";
RL Nature 244:292-294(1973).
RN [4]
RP FUNCTION.
RX PubMed=23978092; DOI=10.1021/cb400541z;
RA Cacho R.A., Chooi Y.H., Zhou H., Tang Y.;
RT "Complexity generation in fungal polyketide biosynthesis: a spirocycle-
RT forming P450 in the concise pathway to the antifungal drug griseofulvin.";
RL ACS Chem. Biol. 8:2322-2330(2013).
CC -!- FUNCTION: Transcription factor that regulates expression of the gene
CC cluster that mediates the biosynthesis of Griseofulvin, an important
CC antifungal drug that has been in use for a long time for treating
CC dermatophyte infections (PubMed:20534346).
CC {ECO:0000269|PubMed:20534346}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC -!- BIOTECHNOLOGY: Griseofulvin is a spirocyclic fungal natural product
CC used in treatment of fungal dermatophytes (PubMed:13577889,
CC PubMed:4583105). {ECO:0000269|PubMed:13577889,
CC ECO:0000269|PubMed:4583105}.
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DR EMBL; GU574478; ADI24952.1; -; Genomic_DNA.
DR AlphaFoldDB; D7PI10; -.
DR SMR; D7PI10; -.
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..415
FT /note="Transcription factor gsfR2"
FT /id="PRO_0000436728"
FT DNA_BIND 9..36
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 65..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 47126 MW; 4C7001D245F31CF2 CRC64;
MPPLYRRSCI TCVQSKRKCD QGLPKCQRCL AKNIHCEYNP RYPNRRRQTT ERNVDENVSL
VEPIAEEPSR GCQLQRSPAR PTSPTHSPHA NDIFFNFAND PFNLESIPQD NFLNSTIFED
VVTQQAPNDT ERITSDTTAQ ARVEFAAKKL SVIPKIFSQQ GQTMFIHRQL FQDRAPPALQ
DALSACALYC LKSTENQTLV FRNLEHKRKQ LISSIDPLLA SKLDLLEALQ ALVLYQIISL
FDGDIRLRAQ AEADEPVLLM WAAQLTLRTP QFQPPLGLSN PQSLAGSASM DWGRWLIEES
SRRTLITASM LKGVYSFVKL GYDTVPDMRM SFTAQAVLWN SQSEISWRRA YKEKERLEIQ
VTHWDETIAK AKANDLEELG VLIMVMLKGT GATGEWLGHS QNIRYGLEEA YYGSV