SIR2_KLULA
ID SIR2_KLULA Reviewed; 670 AA.
AC P33294; Q6CK00;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=NAD-dependent histone deacetylase SIR2;
DE EC=2.3.1.286;
DE AltName: Full=Regulatory protein SIR2;
DE AltName: Full=Silent information regulator 2;
GN Name=SIR2; OrderedLocusNames=KLLA0F14663g;
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].
RC STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RX PubMed=8007956; DOI=10.1128/mcb.14.7.4501-4508.1994;
RA Chen X.-J., Clark-Walker D.G.;
RT "SIR2 mutants of Kluyveromyces lactis are hypersensitive to DNA-targeting
RT drugs.";
RL Mol. Cell. Biol. 14:4501-4508(1994).
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: NAD-dependent deacetylase, which asts as a key regulator of
CC gene expression believed to help form modified chromatin structures on
CC the genes it regulates. It is involved in telomeric silencing and in hm
CC mating type loci silencing (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-
CC ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767;
CC EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000305}.
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DR EMBL; X74569; CAA52661.1; -; Genomic_DNA.
DR EMBL; CR382126; CAG98447.1; -; Genomic_DNA.
DR PIR; A56048; S36616.
DR RefSeq; XP_455739.1; XM_455739.1.
DR AlphaFoldDB; P33294; -.
DR SMR; P33294; -.
DR STRING; 28985.XP_455739.1; -.
DR PRIDE; P33294; -.
DR EnsemblFungi; CAG98447; CAG98447; KLLA0_F14663g.
DR GeneID; 2895003; -.
DR KEGG; kla:KLLA0_F14663g; -.
DR eggNOG; KOG2684; Eukaryota.
DR HOGENOM; CLU_023643_5_0_1; -.
DR InParanoid; P33294; -.
DR OMA; KRKQYFP; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1600.10; -; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR007654; NAD-dep_histone_deAcase_SIR2_N.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR Pfam; PF04574; DUF592; 1.
DR Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 3: Inferred from homology;
KW Metal-binding; NAD; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Transferase; Zinc.
FT CHAIN 1..670
FT /note="NAD-dependent histone deacetylase SIR2"
FT /id="PRO_0000110277"
FT DOMAIN 301..585
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT REGION 1..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..71
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 420
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 318..337
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 400..403
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 455
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 527..529
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 552..554
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 569
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 121
FT /note="A -> S (in Ref. 1; CAA52661)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 670 AA; 74212 MW; 1BF4D9C74334B050 CRC64;
MTEYYGTLQK RPLEQESVAE GNGGLESGKK ARGDSDVFAA RSPENEDVDV DADADVDADA
DADADAEEDA QKDILEETKA DELDEVVDEY EEKEVSSNFN GTASDHVGIT SSNTGSTALA
ASSADTNSGS GNGTGTMATN GTLSDRQYAP QKPEHPIKLE RRSVSRKYVF PVISKEDSLN
ARSYLKQFGS ARFLDDYLPE DLNSLYVYHM IKLLGFQIKD KELMLAIQEV VHNADNDDSL
PQKNSSETKN VSDTYTATYP SPSFEDPLEK KHAVRLIKDL QKAMNKVLST RIRLTNFHTI
DDFVAKLKTA KKIIVLTGAG ISTSLGIPDF RSSEGFYSKL GDLGLNDPQD VFSLEVFTED
PSVFYNIAHM VLPPENMYSP LHSFIKMIQD KDKLLRNYTQ NIDNLESYAG VEPEKMVQCH
GSFATASCVT CHWKIQGERI FPNIRNLQLP ICPYCYSKRL EFFKTKTDEE LADGEDDDMD
DHHGRSVPKS FGVLKPDITF FGEALPSKFH RLIREDVLQC DLLICIGTSL KVAPVSEIVN
MIPAHVPQVL INKDPVKHAE FDLSLLGLCD DVAALVAQKC GWDIPHDNWN KLKNKVFDSE
EVERGVYKVH PLNESPAELE AEEEKHLPLQ QSTAALTPPV SLSADSPGRS SSSSPQPPTQ
TDIANNQTST
