ID   GSM1_CANGA              Reviewed;         629 AA.
AC   Q6FLG1;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Glucose starvation modulator protein 1;
GN   Name=GSM1; OrderedLocusNames=CAGL0L03674g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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}.
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DR   EMBL; CR380958; CAG61903.1; -; Genomic_DNA.
DR   RefSeq; XP_448933.1; XM_448933.1.
DR   AlphaFoldDB; Q6FLG1; -.
DR   STRING; 284593.Q6FLG1; -.
DR   PRIDE; Q6FLG1; -.
DR   EnsemblFungi; CAG61903; CAG61903; CAGL0L03674g.
DR   GeneID; 2890536; -.
DR   KEGG; cgr:CAGL0L03674g; -.
DR   CGD; CAL0135434; CAGL0L03674g.
DR   VEuPathDB; FungiDB:CAGL0L03674g; -.
DR   eggNOG; ENOG502R2ZP; Eukaryota.
DR   HOGENOM; CLU_010748_2_2_1; -.
DR   InParanoid; Q6FLG1; -.
DR   Proteomes; UP000002428; Chromosome L.
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   CDD; cd00130; PAS; 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   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..629
FT                   /note="Glucose starvation modulator protein 1"
FT                   /id="PRO_0000406482"
FT   DOMAIN          472..542
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DNA_BIND        5..33
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          34..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..350
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   629 AA;  70600 MW;  4C435E867DA9F9C8 CRC64;
     MVKACEFCHE KHLHCDPGRP CINCVKRNRG QLCRDKERKK SKKSGVEKSV GGSDAQSSGS
     SQSNNTAEVN VSADYTAGTM FNNMGFDPLQ QSNYGFDTMT RQNNNNDNTL LNSSNNNAID
     MGNRWSSQPD VVDNMVSPNI TDGSNTVEFD SAWANNEYMK LDELTKNGPP MMFSSYPNSV
     TENLDQDNAV EDLPISVLPG SKTKNGTAEN LSQFLNIGRP LHKTQSRPYI SLDMMTAGMK
     DDILPPETYN TTSLGDNYLS PINSVGSSTN QLNDYQDSIP HQKTMTSPVL PTQSPSSAFN
     PAKLPTQVSI SAISPDDNNE DDQKSSSGIP SKSDKEKNNK TKKAKEKIFK TSPNDILISK
     KNPKGHKSTK RKNEKADISP YKFRQLVKVP EDLYEKQYLI KPHNYRHTYK KLLEQLEKIF
     LSDNSPKRRG QLQSIVKCIL EDYVPTFIAL TSNMIESDLY LQELTLQRTL LELESMAKLV
     NCSPICIWRR SGEISYVSDE FLQLTGFKRK EILASRRFIF EFLDPTSIVN YFTNFHEYLA
     FGSKNQMTSN ISLIKQGLLV NGAVVRKSNP IVSSSPMCGT NTDGIFDECH LLLSNGYYLK
     CATCWTVKRD SFNIPLLIMG QFLPVFEGQ