GAL80_KLULA
ID GAL80_KLULA Reviewed; 457 AA.
AC Q06433;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Galactose/lactose metabolism regulatory protein GAL80;
GN Name=GAL80; OrderedLocusNames=KLLA0A08162g;
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 [GENOMIC DNA].
RX PubMed=8246973; DOI=10.1128/mcb.13.12.7566-7576.1993;
RA Zenke F.T., Zachariae W., Lunkes A., Breunig K.D.;
RT "Gal80 proteins of Kluyveromyces lactis and Saccharomyces cerevisiae are
RT highly conserved but contribute differently to glucose repression of the
RT galactose regulon.";
RL Mol. Cell. Biol. 13:7566-7576(1993).
RN [2]
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: This protein is a negative regulator for the gene expression
CC of the lactose/galactose metabolic genes. It seems to block activation
CC by the transcriptional activator LAC9 in the absence of an inducing
CC sugar.
CC -!- SIMILARITY: To yeast GAL80. {ECO:0000305}.
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DR EMBL; Z21512; CAA79724.1; -; Genomic_DNA.
DR EMBL; CR382121; CAH02951.1; -; Genomic_DNA.
DR PIR; A54604; A54604.
DR RefSeq; XP_451363.1; XM_451363.1.
DR PDB; 2NVW; X-ray; 2.10 A; A/B=2-457.
DR PDB; 3E1K; X-ray; 3.00 A; A/C/E/G/I/K/M/O=1-457.
DR PDBsum; 2NVW; -.
DR PDBsum; 3E1K; -.
DR AlphaFoldDB; Q06433; -.
DR SMR; Q06433; -.
DR STRING; 28985.XP_451363.1; -.
DR EnsemblFungi; CAH02951; CAH02951; KLLA0_A08162g.
DR GeneID; 2896324; -.
DR KEGG; kla:KLLA0_A08162g; -.
DR eggNOG; KOG2741; Eukaryota.
DR HOGENOM; CLU_023194_25_0_1; -.
DR InParanoid; Q06433; -.
DR OMA; ADPSHCT; -.
DR EvolutionaryTrace; Q06433; -.
DR Proteomes; UP000000598; Chromosome A.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0005667; C:transcription regulator complex; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0019210; F:kinase inhibitor activity; IEA:EnsemblFungi.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:EnsemblFungi.
DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IEA:EnsemblFungi.
DR GO; GO:0033673; P:negative regulation of kinase activity; IEA:EnsemblFungi.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0000435; P:positive regulation of transcription from RNA polymerase II promoter by galactose; IEA:EnsemblFungi.
DR DisProt; DP01624; -.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; DNA-binding; Galactose metabolism;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..457
FT /note="Galactose/lactose metabolism regulatory protein
FT GAL80"
FT /id="PRO_0000087426"
FT REGION 333..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:2NVW"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:2NVW"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:2NVW"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:2NVW"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:2NVW"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2NVW"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2NVW"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 118..128
FT /evidence="ECO:0007829|PDB:2NVW"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:2NVW"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:2NVW"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:2NVW"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 173..182
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:2NVW"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:2NVW"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:2NVW"
FT TURN 207..210
FT /evidence="ECO:0007829|PDB:2NVW"
FT HELIX 211..223
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:2NVW"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:3E1K"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 262..270
FT /evidence="ECO:0007829|PDB:2NVW"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 292..301
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:2NVW"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:3E1K"
FT STRAND 318..326
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:2NVW"
FT HELIX 376..393
FT /evidence="ECO:0007829|PDB:2NVW"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:2NVW"
FT HELIX 427..446
FT /evidence="ECO:0007829|PDB:2NVW"
FT TURN 453..456
FT /evidence="ECO:0007829|PDB:2NVW"
SQ SEQUENCE 457 AA; 51043 MW; E8E68821837FC4DE CRC64;
MNNNKRSKLS TVPSSRPIRV GFVGLTSGKS WVAKTHFLAI QQLSSQFQIV ALYNPTLKSS
LQTIEQLQLK HATGFDSLES FAQYKDIDMI VVSVKVPEHY EVVKNILEHS SQNLNLRYLY
VEWALAASVQ QAEELYSISQ QRANLQTIIC LQGRKSPYIV RAKELISEGC IGDINSIEIS
GNGGWYGYER PMRSPEYLYD IESGVNLISN SFGHTIDVLQ YITGSYFQKI NAMISNNIPT
QFLLDENGKR TKETISKTCP DHLLFQGILE NGKVPVSCSF KGGTPVKKLT KNLVIDIHGT
KGDLKIEGDA GFVEISNLVL YFYGIKNGNG SSNGTDNNGA AAIKDKEKVT KSPSPSTGTS
EEEQTMEVFH LRNYNSVVGN ILRIYESIAD YHFLGKPESK SSRGPDDLFA STKFDKQGFR
FEGFPTFKDA IILHRLIDAV FRSDKEEKTL DVSKIMI
