LAC9_KLULA
ID LAC9_KLULA Reviewed; 865 AA.
AC P08657;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Lactose regulatory protein LAC9;
GN Name=LAC9; OrderedLocusNames=KLLA0D12672g;
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=3550430; DOI=10.1128/mcb.7.3.1111-1121.1987;
RA Wray L.V. Jr., Witte M.M., Dickson R.C., Riley M.I.;
RT "Characterization of a positive regulatory gene, LAC9, that controls
RT induction of the lactose-galactose regulon of Kluyveromyces lactis:
RT structural and functional relationships to GAL4 of Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 7:1111-1121(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=3022234; DOI=10.1093/nar/14.19.7767;
RA Salmeron J.M., Johnston S.A.;
RT "Analysis of the Kluyveromyces lactis positive regulatory gene LAC9 reveals
RT functional homology to, but sequence divergence from, the Saccharomyces
RT cerevisiae GAL4 gene.";
RL Nucleic Acids Res. 14:7767-7781(1986).
RN [3]
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).
RN [4]
RP MUTAGENESIS.
RX PubMed=2107531; DOI=10.1093/nar/18.4.745;
RA Kuger P., Goedecke A., Breunig K.D.;
RT "A mutation in the Zn-finger of the GAL4 homolog LAC9 results in glucose
RT repression of its target genes.";
RL Nucleic Acids Res. 18:745-751(1990).
RN [5]
RP STRUCTURE BY NMR OF 85-144.
RX PubMed=7552715; DOI=10.1038/nsb1095-898;
RA Gardner K.H., Anderson S.F., Coleman J.E.;
RT "Solution structure of the Kluyveromyces lactis LAC9 Cd2 Cys6 DNA-binding
RT domain.";
RL Nat. Struct. Biol. 2:898-905(1995).
CC -!- FUNCTION: Positive regulatory protein, that controls induction of the
CC lactose-galactose regulation of Kluyveromyces lactis.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; M15210; AAA35266.1; -; Genomic_DNA.
DR EMBL; X06215; CAA29565.1; -; Genomic_DNA.
DR EMBL; CR382124; CAH00723.1; -; Genomic_DNA.
DR PIR; A93641; A25762.
DR PIR; S08482; S08482.
DR RefSeq; XP_453627.1; XM_453627.1.
DR PDB; 1CLD; NMR; -; A=85-144.
DR PDB; 3E1K; X-ray; 3.00 A; B/D/F/H/J/L/N/P=844-865.
DR PDBsum; 1CLD; -.
DR PDBsum; 3E1K; -.
DR AlphaFoldDB; P08657; -.
DR SMR; P08657; -.
DR STRING; 28985.XP_453627.1; -.
DR EnsemblFungi; CAH00723; CAH00723; KLLA0_D12672g.
DR GeneID; 2893282; -.
DR KEGG; kla:KLLA0_D12672g; -.
DR eggNOG; ENOG502QSMN; Eukaryota.
DR HOGENOM; CLU_008599_2_0_1; -.
DR InParanoid; P08657; -.
DR OMA; SYPFIHE; -.
DR EvolutionaryTrace; P08657; -.
DR Proteomes; UP000000598; Chromosome D.
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 GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR CDD; cd14654; ZIP_Gal4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR005600; Gal4_dimer_dom.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF03902; Gal4_dimer; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00906; Fungal_trans; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Carbohydrate metabolism; DNA-binding;
KW Galactose metabolism; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..865
FT /note="Lactose regulatory protein LAC9"
FT /id="PRO_0000114953"
FT DNA_BIND 95..122
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:1CLD"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1CLD"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:1CLD"
FT HELIX 853..859
FT /evidence="ECO:0007829|PDB:3E1K"
SQ SEQUENCE 865 AA; 97038 MW; D6CC912F238DBEBE CRC64;
MGSRASNSPS FSSKAETLLP SEYKKNAVKK ETIRNGKKRK LPDTESSDPE FASRRLIANE
TGTDAVSNGN KNDSNANNNN NNNNKKSSEV MHQACDACRK KKWKCSKTVP TCTNCLKYNL
DCVYSPQVVR TPLTRAHLTE MENRVAELEQ FLKELFPVWD IDRLLQQKDT YRIRELLTMG
STNTVPGLAS NNIDSSLEQP VAFGTAQPAQ SLSTDPAVQS QAYPMQPVPM TELQSITNLR
HTPSLLDEQQ MNTISTATLR NMYSSGNNNN NLGNISGLSP VTEAFFRWQE GETSIDNSYF
GKGSILFWLN QLLSSEKIAG VTSKVGNDIN TNNNNINHQK LPLILNNNIT HNVSDITTTS
TSSNKRAMSP LSANDSVYLA KRETISAYID AYFKHYHALY PLVSKEMFFA QYNDQIKPEN
VEIWHILLNA VLALGSWCSN SCSSHHTLYY QNALSYLSTA VLETGSTDLT IALILLTHYV
QKMHKPNTAW SLIGLCSHMA TSLGLHRDLP NSTIHDQQLR RVLWWTIYCT GCDLSLETGR
PSLLPNLQAI DIPLPASSAT IKEPSIYSSI IQESQWSQIL QQKLSNNSYQ QSAGECLSWF
DSVQAFLDHW PTPSTEAELK ALNETQLDWL PLVKFRPYWM FHCSLISLFS VFFEEDAPTD
NNVIRCKELC LQLSSRNIFS VATFVRSYAF NSLSCWYATH YLVRSALVPL HFASRISPQH
ALWETVKAQL LSAHEAMGIL SQESSLAAKF DGILTKNYSE ILQREGINKS QLMPPPTPLL
QSTSFSDLLS LWSANAEDAP RVSNSQMPQS ITITDSLLQS STTQMRPPTT SGWPDTNNFL
NPSTQQLFNT TTMDDVYNYI FDNDE