SIR2_CANGA
ID SIR2_CANGA Reviewed; 509 AA.
AC Q6FWI7;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=CAGL0C05357g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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. Heterochromatin component that
CC silences transcription at silent mating loci, telomeres and the
CC ribosomal DNA, and that also suppresses recombination in the rDNA and
CC extends replicative life span. It acts as a NAD-dependent histone
CC deacetylase, which deacetylates 'Lys-9' and 'Lys-14' of Histone H3 and
CC 'Lys-16' of Histone H4 (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:0000250}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000305}.
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DR EMBL; CR380949; CAG58313.1; -; Genomic_DNA.
DR RefSeq; XP_445407.1; XM_445407.1.
DR AlphaFoldDB; Q6FWI7; -.
DR SMR; Q6FWI7; -.
DR STRING; 5478.XP_445407.1; -.
DR EnsemblFungi; CAG58313; CAG58313; CAGL0C05357g.
DR GeneID; 2886842; -.
DR KEGG; cgr:CAGL0C05357g; -.
DR CGD; CAL0127390; HST1.
DR VEuPathDB; FungiDB:CAGL0C05357g; -.
DR eggNOG; KOG2684; Eukaryota.
DR HOGENOM; CLU_023643_5_0_1; -.
DR InParanoid; Q6FWI7; -.
DR OMA; KRKQYFP; -.
DR Proteomes; UP000002428; Chromosome C.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004407; F:histone deacetylase activity; IDA:CGD.
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..509
FT /note="NAD-dependent histone deacetylase SIR2"
FT /id="PRO_0000110276"
FT DOMAIN 193..478
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 312
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 210..229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 292..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 420..422
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 445..447
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 462
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 509 AA; 58274 MW; 6822A1CBED3D7964 CRC64;
MIISRGSHVD EEPVAKKPRI SVGEMTDDTT DDGLNTEEIR APYTTEEMDE PEKAALLPKI
PKKSPVSIGM NPENGKYVLP NYSKDESLNA RKFLKYYGLR KFLDTYLPEE LNSLYIYSLI
KLLGFEIRDK ELLSSLYRFF HPVKSSDQFK LEYEDFTDPL EKKEAVKLIK DLQKAINRVL
ATRIRLSNFY TIDHFVSKIK KAERILVLTG AGVSTSLGIP DFRSSEGFYS KIQHLGLDDP
QDVFNYDIFM QDPSVFYNIA HMILPPENMY SPLHSFIKML QDKGKLLRNY TQNIDNLESY
AGIDPEKLVQ CHGSFATASC VTCHWQIPGE KIFSNIRSME LPLCPYCYQK RREYFPNTGD
EEYDTLKGNL ESGIQNNNFA LKSYGVLKPD ITFFGEALPS KFHKTIREDI MKCDLLICIG
TSLKVAPVSE IVNMIPAYVP QVLINKDPVK HAEFDIELLG FCDDVATVVA QKCEWDIPHK
DWEGKLKKKR FDVNEIERGV FNIEAGSPE
