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RGT1_ASHGO
ID   RGT1_ASHGO              Reviewed;         856 AA.
AC   Q750N3;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Glucose transport transcription regulator RGT1;
DE   AltName: Full=Restores glucose transport protein 1;
GN   Name=RGT1; OrderedLocusNames=AGL083W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Glucose-responsive transcription factor that regulates
CC       expression of several glucose transporter (HXT) genes in response to
CC       glucose. In the absence of glucose, it functions as a transcriptional
CC       repressor, whereas high concentrations of glucose cause it to function
CC       as a transcriptional activator. In cells growing on low levels of
CC       glucose, has a neutral role, neither repressing nor activating
CC       transcription (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC       Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EDS1/RGT1 family. {ECO:0000305}.
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DR   EMBL; AE016820; AAS54407.1; -; Genomic_DNA.
DR   RefSeq; NP_986583.1; NM_211645.1.
DR   AlphaFoldDB; Q750N3; -.
DR   STRING; 33169.AAS54407; -.
DR   EnsemblFungi; AAS54407; AAS54407; AGOS_AGL083W.
DR   GeneID; 4622882; -.
DR   KEGG; ago:AGOS_AGL083W; -.
DR   eggNOG; ENOG502QRVJ; Eukaryota.
DR   HOGENOM; CLU_006525_0_0_1; -.
DR   InParanoid; Q750N3; -.
DR   OMA; HILENCC; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   3: Inferred from homology;
KW   Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Zinc.
FT   CHAIN           1..856
FT                   /note="Glucose transport transcription regulator RGT1"
FT                   /id="PRO_0000408012"
FT   DNA_BIND        46..75
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          168..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   856 AA;  92978 MW;  56A782F249045294 CRC64;
     MNGATATATA AVGAEEEGGA REGSRRRDSV ESAGDGRRRT KVSRACDQCR RKKIKCEYQE
     DAQSCSGCRK NSERCAFERV PLKRGPSKGY TRGEGAGDGA RETEGARGEL DTSRADGKAA
     PVSLPPLHYY LPISNGQPGG APAQAPAAPF PPMKQQFWKV PYYENQMQRR SSLESVNSDA
     SGPQSQQETY AASSASTSSH QRTSRSYFPS SDGASALFQE PCSSSYPPPL VRSSSTGGQL
     QQLPAPQYPY SQFAVALSGS TSASSQSVQL RTSATGSTSL PEDSSPSSSN AYSPQLRAHC
     MSESLTTPTA GSKTGGSVKR RKRLSEPADP IVPLSAREPR QAGHIGLPLQ AQQATGKTGV
     ICGKLSDAEL IDAYYEYVHV NYPIIPINKE TLTNEILLVN TQPISEVHEM NNYILYWFRV
     ALELLLHVAS DKTNQDTASG MDSNAVHDGG LYAHRGDFKQ NEEHHVPHQS QLLAALNDCF
     RKLLDIHPKI CAYQESTSPK VTTIYLSTYI IINYMLAMLG EDNTFVLGTS VTVFNEFKIY
     RLLVLHEVAD EPGDDSADVE RHGFELLYKR LYYSLLVFDA LQSCCFGAPR LASLPISHLV
     EPLFAPPPPL DSAKWAVESD AARREPLLAS IRLGALLTEL CETRVLAGAL PRAPTPALRA
     PRPFRVAPPA DDSVPGAFFH ALAAQRALLD RLLAIPAHPA FAADAPPDAT VDLCAQLGDA
     ICRFTSCVLD TLVRAGPRPA SPFAAALSRA LHHAINLSRN IPTSLIGCII GTAVHHSRDR
     DLIVALSRCM SDMIQIQGLT HCLRPCAPPR PRARVSCDLR RLYGHDGPPA SPHQVMLHQF
     IDIAWRLLRN DELGWF
 
 
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