RGT1_LACTC
ID RGT1_LACTC Reviewed; 979 AA.
AC C5DGQ7;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Glucose transport transcription regulator RGT1;
DE AltName: Full=Restores glucose transport protein 1;
GN Name=RGT1; OrderedLocusNames=KLTH0D07260g;
OS Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS (Yeast) (Kluyveromyces thermotolerans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=559295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284;
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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; CU928168; CAR22599.1; -; Genomic_DNA.
DR RefSeq; XP_002553037.1; XM_002552991.1.
DR AlphaFoldDB; C5DGQ7; -.
DR STRING; 559295.C5DGQ7; -.
DR EnsemblFungi; CAR22599; CAR22599; KLTH0D07260g.
DR GeneID; 8295268; -.
DR KEGG; lth:KLTH0D07260g; -.
DR eggNOG; ENOG502QRVJ; Eukaryota.
DR HOGENOM; CLU_006525_0_0_1; -.
DR InParanoid; C5DGQ7; -.
DR OMA; WFRNSLE; -.
DR OrthoDB; 754354at2759; -.
DR Proteomes; UP000002036; Chromosome D.
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..979
FT /note="Glucose transport transcription regulator RGT1"
FT /id="PRO_0000408015"
FT DNA_BIND 35..64
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 979 AA; 108536 MW; FE72E02C117B6511 CRC64;
MSASRRESEP KEAETSPEAG GAASDRRRSK TSRACDQCRE KKTRCDFSDE RPICSACQRM
GKTCTFERVP MKRGPTKGYT RNSEPPEGFD TSRRGSRKRS SSDVFKGDAG RPRADPVSLP
PLAQYLPQSG SQPRLQPLLA PGAQPQQQFW KVPYYEYQHQ RRGSIDSLGS DVSNRNGSEQ
LAYLPSNASS GSQFYPASQA QYASQLPSDV EGANPEDCRG SLSLPAIQKF QQPPSGYYLQ
YPYSQFSMLP QQQQQQQQQN AQQSYFTSQY VPPAAPPGAE HFKEFDEGFH SRKGSDVSVA
VSPSSPVQVT RTQQAGLNSE SRDTNTATAV SPKPLPKPSK PQMQTERSSS KSDGNHNGPR
KQKRKNSNRN KPGSQSSIES IASSSHASII YGKIPDKQLI DIYFEFIHPN FPVIPINKET
LTDDLLLVNT QPISPVHELN TYILHWFRNS LELLVRVALK KPSGSGQAYS DGAVDILDSQ
ATFINALNEC FQRIVDIHPG LRENEKLLSL KTKFIYLATF SILNYILAFV GYDNSFVLGM
SVTIYNECKL YRYLMYDELP SNDTEASENE DEAGAGDAHA SGTPERGKSA KHDLGHQVLF
KRLYVLLVVF DSLQSCAFGV PKLISVPLAE LTEETFKFST GKWCVERDPQ RFETIRQSLV
LGQVLSWLSI SRKSVRRNSL QAAPQDASWK DEKSDSVSSS LFAKFLVQKH EMMEDFLLLA
PLENSSHLLT FDLLSKSSTA ICGLISSMHR LLALLMKINP TNSVDPNNRP PLRQGDFVHT
DTEIQSESSN PPAATAAPDS CDADKFDVYR KLLGLNGGQE RHVAQGTISP FVISIVVEIR
NVLELVKHLP TSIIGVVVNL LPNGEGENYQ KRSHRLVMSL SNAMNELVQI TSLISLLKPF
KMFDHTLRSN RPSAKVSTKL LRQKFAPESV KTPSSQPPSS SPGPNSDGSN NTSLSQNTVM
HAILDAAWDL MDGEELGWL
