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GSM1_KLULA
ID   GSM1_KLULA              Reviewed;         579 AA.
AC   Q6CK33;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Glucose starvation modulator protein 1;
GN   Name=GSM1; OrderedLocusNames=KLLA0F13904g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382126; CAG98414.1; -; Genomic_DNA.
DR   RefSeq; XP_455706.1; XM_455706.1.
DR   AlphaFoldDB; Q6CK33; -.
DR   STRING; 28985.XP_455706.1; -.
DR   EnsemblFungi; CAG98414; CAG98414; KLLA0_F13904g.
DR   GeneID; 2894879; -.
DR   KEGG; kla:KLLA0_F13904g; -.
DR   eggNOG; ENOG502R2ZP; Eukaryota.
DR   HOGENOM; CLU_010748_2_2_1; -.
DR   InParanoid; Q6CK33; -.
DR   OMA; CHEKHLQ; -.
DR   Proteomes; UP000000598; Chromosome F.
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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
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; SSF55785; SSF55785; 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..579
FT                   /note="Glucose starvation modulator protein 1"
FT                   /id="PRO_0000406486"
FT   DOMAIN          444..516
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          43..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   579 AA;  65394 MW;  E45C645F2E1B9922 CRC64;
     MTKKLTAQEK LNRKPIPTAC VFCHEKHLQC DLGRPCQNCS KRGIGDTCRD KERKPRKRGP
     RKVKKEREVS ASTKSEISNT INQQLIPVIN TATAVSNRQN SSKIIKAKQT GVSTKKTRIS
     KLAMDSLPLQ MPVINSPSDM FGKQKKVMSP ELPKIPSLTQ LFNPTAEPII SDALLPSNQN
     SAANLPSLAD KTPLEEFKNK PLSERAPQQG PQQPAQQLLP IPEKLNSDHT SSNSSTGEFG
     SVWTTEEYTK LNDMLSTPNL SRNNSKTYLN SNIAWSPSNM MKMDPITESQ RPINTQELLN
     LTSNGLKRTH SRPHISLDQM ASESKRHSAN DTSPESQGGE TVENLSPYRF RLLVKTPEDL
     YKHQALIQPH NYKSAYLELL RFLRWRFINS DKPSSGKSQR DGPEQLQNIA HSIKTHYAPI
     FVTLTNSLIA QDLKLQEIIL QRALLEYESM AKLVNCTPMC IWRRSGEICF ASNEFISLTG
     FNKKEILNKR KFIMEFMDNE SIVDYYDIFH EYLAFGSTQS GPFNSSTGTS DGQAIFSECN
     LLLKNGCYLR CACIWTVKRD AFNIPMLIMG QFLPIFDIE
 
 
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