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NAD-dependent histone deacetylase SIR2 (EC 3.5.1.-) (Regulatory protein SIR2) (Silent information regulator 2)

 SIR2_YEAST              Reviewed;         562 AA.
P06700; D6VRV4;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
23-MAY-2018, entry version 197.
RecName: Full=NAD-dependent histone deacetylase SIR2;
EC=3.5.1.-;
AltName: Full=Regulatory protein SIR2;
AltName: Full=Silent information regulator 2;
Name=SIR2; Synonyms=MAR1; OrderedLocusNames=YDL042C; ORFNames=D2714;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6098447;
Shore D., Squire M., Nasmyth K.A.;
"Characterization of two genes required for the position-effect
control of yeast mating-type genes.";
EMBO J. 3:2817-2823(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9046088;
DOI=10.1002/(SICI)1097-0061(199701)13:1<65::AID-YEA50>3.0.CO;2-T;
Saren A.-M., Laamanen P., Lejarcegui J.B., Paulin L.;
"The sequence of a 36.7 kb segment on the left arm of chromosome IV
from Saccharomyces cerevisiae reveals 20 non-overlapping open reading
frames (ORFs) including SIT4, FAD1, NAM1, RNA11, SIR2, NAT1, PRP9,
ACT2 and MPS1 and 11 new ORFs.";
Yeast 13:65-71(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
SUBCELLULAR LOCATION.
PubMed=9214640; DOI=10.1093/emboj/16.11.3243;
Gotta M., Strahl-Bolsinger S., Renauld H., Laroche T., Kennedy B.K.,
Grunstein M., Gasser S.M.;
"Localization of Sir2p: the nucleolus as a compartment for silent
information regulators.";
EMBO J. 16:3243-3255(1997).
[6]
PRELIMINARY FUNCTION.
PubMed=10619427; DOI=10.1016/S0092-8674(00)81671-2;
Tanny J.C., Dowd G.J., Huang J., Hilz H., Moazed D.;
"An enzymatic activity in the yeast Sir2 protein that is essential for
gene silencing.";
Cell 99:735-745(1999).
[7]
FUNCTION.
PubMed=10693811; DOI=10.1038/35001622;
Imai S., Armstrong C.M., Kaeberlein M., Guarente L.;
"Transcriptional silencing and longevity protein Sir2 is an NAD-
dependent histone deacetylase.";
Nature 403:795-800(2000).
[8]
FUNCTION.
PubMed=9278054; DOI=10.1038/42288;
Tsukamoto Y., Kato J., Ikeda H.;
"Silencing factors participate in DNA repair and recombination in
Saccharomyces cerevisiae.";
Nature 388:900-903(1997).
[9]
INTERACTION WITH SIR3 AND SIR4.
PubMed=9122169; DOI=10.1073/pnas.94.6.2186;
Moazed D., Kistler A., Axelrod A., Rine J., Johnson A.D.;
"Silent information regulator protein complexes in Saccharomyces
cerevisiae: a SIR2/SIR4 complex and evidence for a regulatory domain
in SIR4 that inhibits its interaction with SIR3.";
Proc. Natl. Acad. Sci. U.S.A. 94:2186-2191(1997).
[10]
IDENTIFICATION IN A RENT COMPLEX WITH CDC14.
PubMed=10219244; DOI=10.1016/S0092-8674(00)80733-3;
Shou W., Seol J.H., Shevchenko A., Baskerville C., Moazed D.,
Chen Z.W.S., Jang J., Shevchenko A., Charbonneau H., Deshaies R.J.;
"Exit from mitosis is triggered by Tem1-dependent release of the
protein phosphatase Cdc14 from nucleolar RENT complex.";
Cell 97:233-244(1999).
[11]
IDENTIFICATION IN A RENT COMPLEX WITH NET1.
PubMed=10219245; DOI=10.1016/S0092-8674(00)80734-5;
Straight A.F., Shou W., Dowd G.J., Turck C.W., Deshaies R.J.,
Johnson A.D., Moazed D.;
"Net1, a Sir2-associated nucleolar protein required for rDNA silencing
and nucleolar integrity.";
Cell 97:245-256(1999).
[12]
INTERACTION WITH ZDS2.
PubMed=10662670; DOI=10.1016/S0960-9822(00)00298-0;
Roy N., Runge K.W.;
"Two paralogs involved in transcriptional silencing that
antagonistically control yeast life span.";
Curr. Biol. 10:111-114(2000).
[13]
MECHANISM OF TRANSCRIPTION REPRESSION.
PubMed=11348596; DOI=10.1016/S0092-8674(01)00329-4;
Sekinger E.A., Gross D.S.;
"Silenced chromatin is permissive to activator binding and PIC
recruitment.";
Cell 105:403-414(2001).
[14]
REVIEW.
PubMed=11722841; DOI=10.1016/S0378-1119(01)00741-7;
Gasser S.M., Cockell M.M.;
"The molecular biology of the SIR proteins.";
Gene 279:1-16(2001).
[15]
INTERACTION WITH ESC8.
PubMed=12399377;
Cuperus G., Shore D.;
"Restoration of silencing in Saccharomyces cerevisiae by tethering of
a novel Sir2-interacting protein, Esc8.";
Genetics 162:633-645(2002).
[16]
MUTAGENESIS OF ARG-139; GLY-270 AND PHE-296.
PubMed=12399383;
Garcia S.N., Pillus L.;
"A unique class of conditional sir2 mutants displays distinct
silencing defects in Saccharomyces cerevisiae.";
Genetics 162:721-736(2002).
[17]
FUNCTION, AND INTERACTION WITH FOB1.
PubMed=12923057; DOI=10.1101/gad.1108403;
Huang J., Moazed D.;
"Association of the RENT complex with nontranscribed and coding
regions of rDNA and a regional requirement for the replication fork
block protein Fob1 in rDNA silencing.";
Genes Dev. 17:2162-2176(2003).
[18]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[19]
ENZYME REGULATION.
PubMed=12939617; DOI=10.1038/nature01960;
Howitz K.T., Bitterman K.J., Cohen H.Y., Lamming D.W., Lavu S.,
Wood J.G., Zipkin R.E., Chung P., Kisielewski A., Zhang L.-L.,
Scherer B., Sinclair D.A.;
"Small molecule activators of sirtuins extend Saccharomyces cerevisiae
lifespan.";
Nature 425:191-196(2003).
[20]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15274642; DOI=10.1021/bi049592e;
Borra M.T., Langer M.R., Slama J.T., Denu J.M.;
"Substrate specificity and kinetic mechanism of the Sir2 family of
NAD+-dependent histone/protein deacetylases.";
Biochemistry 43:9877-9887(2004).
[21]
INTERACTION WITH MCM10.
PubMed=16328881; DOI=10.1007/s11033-005-2312-x;
Douglas N.L., Dozier S.K., Donato J.J.;
"Dual roles for Mcm10 in DNA replication initiation and silencing at
the mating-type loci.";
Mol. Biol. Rep. 32:197-204(2005).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[23]
FUNCTION, AND INTERACTION WITH SLX5/HEX3.
PubMed=18086879; DOI=10.1128/MCB.01291-07;
Darst R.P., Garcia S.N., Koch M.R., Pillus L.;
"Slx5 promotes transcriptional silencing and is required for robust
growth in the absence of Sir2.";
Mol. Cell. Biol. 28:1361-1372(2008).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[25]
FUNCTION.
PubMed=19220062; DOI=10.1021/bi802093g;
Du J., Jiang H., Lin H.;
"Investigating the ADP-ribosyltransferase activity of sirtuins with
NAD analogues and 32P-NAD.";
Biochemistry 48:2878-2890(2009).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[27]
INTERACTION WITH NSI1.
PubMed=22362748; DOI=10.1093/nar/gks188;
Ha C.W., Sung M.K., Huh W.K.;
"Nsi1 plays a significant role in the silencing of ribosomal DNA in
Saccharomyces cerevisiae.";
Nucleic Acids Res. 40:4892-4903(2012).
[28]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 209-562 IN COMPLEX WITH ZINC
AND NICOTINAMIDE.
Hall B.E., Buchberger J.R., Gerber S.A., Ambrosio A.L.B., Gygi S.P.,
Filman D., Moazed D., Ellenberger T.;
"Autoregulation of the yeast Sir2 deacetylase by reaction and trapping
of a pseudosubstrate motif in the active site.";
Submitted (JUN-2006) to the PDB data bank.
[29]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 87-562 IN COMPLEX WITH SIR4;
ADP-RIBOSE AND ZINC.
PubMed=23307867; DOI=10.1101/gad.208140.112;
Hsu H.C., Wang C.L., Wang M., Yang N., Chen Z., Sternglanz R.,
Xu R.M.;
"Structural basis for allosteric stimulation of Sir2 activity by Sir4
binding.";
Genes Dev. 27:64-73(2013).
-!- FUNCTION: NAD-dependent deacetylase, which participates in a wide
range of cellular events including chromosome silencing,
chromosome segregation, DNA recombination and the determination of
life span. Involved in transcriptional repression of the silent
mating-type loci HML and HMR and telomeric silencing via its
association with SIR3 and SIR4. Plays a central role in ribosomal
DNA (rDNA) silencing via its association with the RENT complex,
preventing hyperrecombination, and repressing transcription from
foreign promoters, which contributes to extending life span.
Probably represses transcription via the formation of
heterochromatin structure, which involves the compaction of
chromatin fiber into a more condensed form, although this complex
in at least one case can still bind euchromatic levels of positive
transcription regulators. Although it displays some NAD-dependent
histone deacetylase activity on histone H3K9Ac and H3K14Ac and
histone H4K16Ac in vitro, such activity is unclear in vivo and may
not be essential. {ECO:0000269|PubMed:10693811,
ECO:0000269|PubMed:12923057, ECO:0000269|PubMed:15274642,
ECO:0000269|PubMed:18086879, ECO:0000269|PubMed:19220062,
ECO:0000269|PubMed:9278054}.
-!- CATALYTIC ACTIVITY: NAD(+) + an acetylprotein = nicotinamide + O-
acetyl-ADP-ribose + a protein. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:23307867};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:23307867};
-!- ENZYME REGULATION: Its activity is increased by calorie
restriction, which slows the pace of aging and increases maximum
lifespan. Activated by resveratrol (3,5,4'-trihydroxy-trans-
stilbene), which is found in red wine.
{ECO:0000269|PubMed:12939617}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=29.3 uM for NAD(+) {ECO:0000269|PubMed:15274642};
KM=239 uM for a synthetic histone H3K9 acetyllysine peptide
{ECO:0000269|PubMed:15274642};
KM=420 uM for a synthetic histone H3K14 acetyllysine peptide
{ECO:0000269|PubMed:15274642};
KM=140 uM for a synthetic histone H4K5 acetyllysine peptide
{ECO:0000269|PubMed:15274642};
KM=54 uM for a synthetic histone H4K8 acetyllysine peptide
{ECO:0000269|PubMed:15274642};
KM=105 uM for a synthetic histone H4K12 acetyllysine peptide
{ECO:0000269|PubMed:15274642};
KM=17 uM for a synthetic histone H4K16 acetyllysine peptide
{ECO:0000269|PubMed:15274642};
-!- SUBUNIT: Homomultimer. Forms a complex with SIR3 and SIR4
(PubMed:9122169). Component of the RENT complex, at least composed
of SIR2, CDC14 and NET1 (PubMed:10219244, PubMed:10219245). The
RENT complex interacts with FOB1 (PubMed:12923057). Interacts with
ESC8 (PubMed:12399377). Interacts with and ZDS2 (PubMed:10662670).
Interacts with MCM10 (PubMed:16328881). Interacts with SLX5
(PubMed:18086879). Interacts with NSI1 (PubMed:22362748).
{ECO:0000269|PubMed:10219244, ECO:0000269|PubMed:10219245,
ECO:0000269|PubMed:10662670, ECO:0000269|PubMed:12399377,
ECO:0000269|PubMed:12923057, ECO:0000269|PubMed:16328881,
ECO:0000269|PubMed:18086879, ECO:0000269|PubMed:22362748,
ECO:0000269|PubMed:9122169}.
-!- INTERACTION:
Q00684:CDC14; NbExp=5; IntAct=EBI-17219, EBI-4192;
P22146:GAS1; NbExp=2; IntAct=EBI-17219, EBI-7327;
P11978:SIR4; NbExp=7; IntAct=EBI-17219, EBI-17237;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:9214640}. Note=Associated with nucleolar
chromatin. Preferentially bound to the spacer regions of the rDNA
repeats through its interaction with NET1.
-!- MISCELLANEOUS: Its stability is directly linked to life span,
which is extended when it is present in high dosage. Conversely,
its absence shortens life span.
-!- MISCELLANEOUS: The reported ADP-ribosyltransferase activity of
sirtuins is likely some inefficient side reaction of the
deacetylase activity and may not be physiologically relevant.
{ECO:0000305|PubMed:19220062}.
-!- MISCELLANEOUS: Present with 3350 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
{ECO:0000305}.
-!- CAUTION: Was originally thought to be an ADP-ribosyltransferase.
{ECO:0000305|PubMed:10619427}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=In vino vita? - Issue
40 of November 2003;
URL="https://web.expasy.org/spotlight/back_issues/040";
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EMBL; X01419; CAA25667.1; -; Genomic_DNA.
EMBL; Z71781; CAA96447.1; -; Genomic_DNA.
EMBL; Z74090; CAA98600.1; -; Genomic_DNA.
EMBL; BK006938; DAA11814.1; -; Genomic_DNA.
PIR; S05891; RGBYS2.
RefSeq; NP_010242.1; NM_001180101.1.
PDB; 2HJH; X-ray; 1.85 A; A/B=209-562.
PDB; 4IAO; X-ray; 2.90 A; A/B=87-562.
PDBsum; 2HJH; -.
PDBsum; 4IAO; -.
ProteinModelPortal; P06700; -.
SMR; P06700; -.
BioGrid; 32017; 359.
DIP; DIP-596N; -.
IntAct; P06700; 49.
MINT; P06700; -.
STRING; 4932.YDL042C; -.
BindingDB; P06700; -.
ChEMBL; CHEMBL3275; -.
iPTMnet; P06700; -.
MaxQB; P06700; -.
PaxDb; P06700; -.
PRIDE; P06700; -.
EnsemblFungi; YDL042C; YDL042C; YDL042C.
GeneID; 851520; -.
KEGG; sce:YDL042C; -.
EuPathDB; FungiDB:YDL042C; -.
SGD; S000002200; SIR2.
GeneTree; ENSGT00870000136443; -.
HOGENOM; HOG000191845; -.
InParanoid; P06700; -.
KO; K11121; -.
OMA; PVKHAEF; -.
OrthoDB; EOG092C1NXT; -.
BioCyc; YEAST:MONOMER3O-4152; -.
Reactome; R-SCE-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-SCE-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-SCE-427359; SIRT1 negatively regulates rRNA expression.
SABIO-RK; P06700; -.
EvolutionaryTrace; P06700; -.
PRO; PR:P06700; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005677; C:chromatin silencing complex; IDA:SGD.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:SGD.
GO; GO:0005720; C:nuclear heterochromatin; IDA:SGD.
GO; GO:0005724; C:nuclear telomeric heterochromatin; IDA:SGD.
GO; GO:0005730; C:nucleolus; IDA:SGD.
GO; GO:0030869; C:RENT complex; IDA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
GO; GO:0017136; F:NAD-dependent histone deacetylase activity; IDA:SGD.
GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IDA:SGD.
GO; GO:0046969; F:NAD-dependent histone deacetylase activity (H3-K9 specific); IDA:SGD.
GO; GO:0046970; F:NAD-dependent histone deacetylase activity (H4-K16 specific); IDA:SGD.
GO; GO:0006333; P:chromatin assembly or disassembly; IDA:SGD.
GO; GO:0006325; P:chromatin organization; IGI:SGD.
GO; GO:0000183; P:chromatin silencing at rDNA; IMP:SGD.
GO; GO:0030466; P:chromatin silencing at silent mating-type cassette; IMP:SGD.
GO; GO:0006348; P:chromatin silencing at telomere; IMP:SGD.
GO; GO:0001300; P:chronological cell aging; IMP:SGD.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:SGD.
GO; GO:0097695; P:establishment of protein-containing complex localization to telomere; IMP:SGD.
GO; GO:1904524; P:negative regulation of DNA amplification; IMP:SGD.
GO; GO:0045910; P:negative regulation of DNA recombination; IMP:SGD.
GO; GO:0008156; P:negative regulation of DNA replication; IMP:SGD.
GO; GO:0001302; P:replicative cell aging; IMP:SGD.
GO; GO:0007062; P:sister chromatid cohesion; IMP:SGD.
GO; GO:0034398; P:telomere tethering at nuclear periphery; IMP:SGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.1600.10; -; 2.
InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
InterPro; IPR007654; NAD-dep_histone_deAcase_SIR2_N.
InterPro; IPR003000; Sirtuin.
InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
InterPro; IPR026590; Ssirtuin_cat_dom.
Pfam; PF04574; DUF592; 1.
Pfam; PF02146; SIR2; 1.
SUPFAM; SSF52467; SSF52467; 2.
PROSITE; PS50305; SIRTUIN; 1.
1: Evidence at protein level;
3D-structure; Chromatin regulator; Complete proteome; DNA damage;
DNA repair; Hydrolase; Metal-binding; NAD; Nucleus;
Reference proteome; Repressor; Transcription;
Transcription regulation; Zinc.
CHAIN 1 562 NAD-dependent histone deacetylase SIR2.
/FTId=PRO_0000110280.
DOMAIN 245 529 Deacetylase sirtuin-type.
{ECO:0000255|PROSITE-ProRule:PRU00236}.
NP_BIND 262 281 NAD. {ECO:0000269|PubMed:23307867,
ECO:0000269|Ref.28}.
NP_BIND 344 347 NAD. {ECO:0000250|UniProtKB:P53686}.
NP_BIND 471 473 NAD. {ECO:0000269|PubMed:23307867}.
NP_BIND 496 498 NAD. {ECO:0000269|PubMed:23307867}.
ACT_SITE 364 364 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 372 372 Zinc. {ECO:0000269|PubMed:23307867,
ECO:0000269|Ref.28}.
METAL 375 375 Zinc. {ECO:0000269|PubMed:23307867,
ECO:0000269|Ref.28}.
METAL 396 396 Zinc. {ECO:0000269|PubMed:23307867,
ECO:0000269|Ref.28}.
METAL 399 399 Zinc. {ECO:0000269|PubMed:23307867,
ECO:0000269|Ref.28}.
BINDING 513 513 NAD; via amide nitrogen.
{ECO:0000269|PubMed:23307867}.
MUTAGEN 139 139 R->K: Defects in telomeric silencing.
{ECO:0000269|PubMed:12399383}.
MUTAGEN 270 270 G->E: Defects in telomeric silencing.
{ECO:0000269|PubMed:12399383}.
MUTAGEN 296 296 F->L: Defects in telomeric silencing.
{ECO:0000269|PubMed:12399383}.
HELIX 102 105 {ECO:0000244|PDB:4IAO}.
STRAND 111 113 {ECO:0000244|PDB:4IAO}.
STRAND 124 126 {ECO:0000244|PDB:4IAO}.
HELIX 132 154 {ECO:0000244|PDB:4IAO}.
HELIX 163 170 {ECO:0000244|PDB:4IAO}.
STRAND 173 175 {ECO:0000244|PDB:4IAO}.
HELIX 178 187 {ECO:0000244|PDB:4IAO}.
STRAND 213 217 {ECO:0000244|PDB:2HJH}.
HELIX 244 253 {ECO:0000244|PDB:2HJH}.
STRAND 255 261 {ECO:0000244|PDB:2HJH}.
HELIX 263 269 {ECO:0000244|PDB:2HJH}.
STRAND 274 276 {ECO:0000244|PDB:2HJH}.
HELIX 280 283 {ECO:0000244|PDB:2HJH}.
HELIX 284 287 {ECO:0000244|PDB:2HJH}.
HELIX 292 296 {ECO:0000244|PDB:2HJH}.
HELIX 298 303 {ECO:0000244|PDB:2HJH}.
HELIX 306 311 {ECO:0000244|PDB:2HJH}.
HELIX 312 315 {ECO:0000244|PDB:2HJH}.
HELIX 324 334 {ECO:0000244|PDB:2HJH}.
STRAND 338 343 {ECO:0000244|PDB:2HJH}.
HELIX 349 352 {ECO:0000244|PDB:2HJH}.
TURN 357 359 {ECO:0000244|PDB:2HJH}.
STRAND 360 362 {ECO:0000244|PDB:2HJH}.
STRAND 365 372 {ECO:0000244|PDB:2HJH}.
TURN 373 375 {ECO:0000244|PDB:2HJH}.
STRAND 378 380 {ECO:0000244|PDB:2HJH}.
HELIX 381 384 {ECO:0000244|PDB:2HJH}.
HELIX 385 389 {ECO:0000244|PDB:2HJH}.
TURN 397 399 {ECO:0000244|PDB:2HJH}.
HELIX 400 406 {ECO:0000244|PDB:2HJH}.
TURN 417 420 {ECO:0000244|PDB:4IAO}.
TURN 433 436 {ECO:0000244|PDB:2HJH}.
STRAND 437 442 {ECO:0000244|PDB:2HJH}.
HELIX 451 460 {ECO:0000244|PDB:2HJH}.
TURN 461 463 {ECO:0000244|PDB:2HJH}.
STRAND 466 471 {ECO:0000244|PDB:2HJH}.
HELIX 479 481 {ECO:0000244|PDB:2HJH}.
HELIX 482 485 {ECO:0000244|PDB:2HJH}.
STRAND 492 498 {ECO:0000244|PDB:2HJH}.
STRAND 506 511 {ECO:0000244|PDB:2HJH}.
HELIX 513 524 {ECO:0000244|PDB:2HJH}.
HELIX 533 537 {ECO:0000244|PDB:2HJH}.
STRAND 541 547 {ECO:0000244|PDB:2HJH}.
STRAND 550 555 {ECO:0000244|PDB:2HJH}.
SEQUENCE 562 AA; 63262 MW; 52E6937533654586 CRC64;
MTIPHMKYAV SKTSENKVSN TVSPTQDKDA IRKQPDDIIN NDEPSHKKIK VAQPDSLRET
NTTDPLGHTK AALGEVASME LKPTNDMDPL AVSAASVVSM SNDVLKPETP KGPIIISKNP
SNGIFYGPSF TKRESLNARM FLKYYGAHKF LDTYLPEDLN SLYIYYLIKL LGFEVKDQAL
IGTINSIVHI NSQERVQDLG SAISVTNVED PLAKKQTVRL IKDLQRAINK VLCTRLRLSN
FFTIDHFIQK LHTARKILVL TGAGVSTSLG IPDFRSSEGF YSKIKHLGLD DPQDVFNYNI
FMHDPSVFYN IANMVLPPEK IYSPLHSFIK MLQMKGKLLR NYTQNIDNLE SYAGISTDKL
VQCHGSFATA TCVTCHWNLP GERIFNKIRN LELPLCPYCY KKRREYFPEG YNNKVGVAAS
QGSMSERPPY ILNSYGVLKP DITFFGEALP NKFHKSIRED ILECDLLICI GTSLKVAPVS
EIVNMVPSHV PQVLINRDPV KHAEFDLSLL GYCDDIAAMV AQKCGWTIPH KKWNDLKNKN
FKCQEKDKGV YVVTSDEHPK TL


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