GSM1_PICGU
ID GSM1_PICGU Reviewed; 520 AA.
AC A5DRJ2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Glucose starvation modulator protein 1;
GN Name=GSM1; ORFNames=PGUG_05893;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Transcription factor which regulates nonfermentable carbon
CC utilization. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC -!- SIMILARITY: Belongs to the ERT1/acuK family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH408162; EDK41795.2; -; Genomic_DNA.
DR RefSeq; XP_001482130.1; XM_001482080.1.
DR AlphaFoldDB; A5DRJ2; -.
DR STRING; 294746.A5DRJ2; -.
DR EnsemblFungi; EDK41795; EDK41795; PGUG_05893.
DR GeneID; 5123950; -.
DR KEGG; pgu:PGUG_05893; -.
DR VEuPathDB; FungiDB:PGUG_05893; -.
DR eggNOG; ENOG502R2ZP; Eukaryota.
DR HOGENOM; CLU_010748_2_2_1; -.
DR InParanoid; A5DRJ2; -.
DR OMA; CHEKHLQ; -.
DR OrthoDB; 681770at2759; -.
DR Proteomes; UP000001997; 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 CDD; cd00067; GAL4; 1.
DR InterPro; IPR000014; PAS.
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; PS50112; PAS; 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; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..520
FT /note="Glucose starvation modulator protein 1"
FT /id="PRO_0000406488"
FT DOMAIN 376..445
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DNA_BIND 20..48
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 63..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 520 AA; 59038 MW; D996B569CABA4CF0 CRC64;
MTKKLSPLEK QARRPASRAC SFCHSKHLQC SNNRPCKNCV KRNIADQCRD VERKRANYMT
LAAKNKQGSP NTVSLESSSS PFSPLHKGHI NSQSSQPLDP SSGRVNTDFF SQSETTVPSP
WPMDLESKER TNAILNTTDD VLNKILYDEQ ASKVPSAQAS EMTPSNSSID GVFNSNYLNQ
EYLMLGDIIL NSKPASPTPS STSEYQTIPP NEMMGTVDYN EVYRDTKSKK LKESRPFISL
GFSNPPDLDN RKLPGEINIA NEIMDPSKRA QVTTTNDYVS PLVTRHIYQS VQDIYANKII
NYEYPTSYHA LTFFLKKRFS GTSLPPEQKQ QKRNNLLIIL KLIASYRPTF ISAHKSLLKP
YDLMFLEMTF QRSLIDYEKL SHLNSSPTII WRRTGEIVSI SDEILSLLGY SLNSILSKRT
FIMELMYDDE SIINYFKLFK SVAVGNLHSS IITRCKLMKN PDRDRSTRAS TTGTEQQLTE
ADYIEFCAVW TVKRDLFDLP MLIMGQFLPV LPAGDGVRRY