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NAD-dependent protein deacetylase hst2 (EC 3.5.1.-) (Homologous to sir2 protein 2) (Regulatory protein SIR2 homolog 2)

 HST2_SCHPO              Reviewed;         332 AA.
Q9USN7;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
28-FEB-2018, entry version 111.
RecName: Full=NAD-dependent protein deacetylase hst2;
EC=3.5.1.-;
AltName: Full=Homologous to sir2 protein 2;
AltName: Full=Regulatory protein SIR2 homolog 2;
Name=hst2; ORFNames=SPCC132.02;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=16823372; DOI=10.1038/nbt1222;
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the
fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
-!- FUNCTION: NAD-dependent histone deacetylase, which could function
in telomeric silencing, cell cycle progression and chromosome
stability. {ECO:0000250}.
-!- 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:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
Nucleus {ECO:0000305}.
-!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
{ECO:0000305}.
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EMBL; CU329672; CAB58129.1; -; Genomic_DNA.
PIR; T40929; T40929.
RefSeq; NP_588147.1; NM_001023136.2.
ProteinModelPortal; Q9USN7; -.
SMR; Q9USN7; -.
BioGrid; 275448; 32.
STRING; 4896.SPCC132.02.1; -.
iPTMnet; Q9USN7; -.
MaxQB; Q9USN7; -.
PaxDb; Q9USN7; -.
PRIDE; Q9USN7; -.
EnsemblFungi; SPCC132.02.1; SPCC132.02.1:pep; SPCC132.02.
GeneID; 2538868; -.
KEGG; spo:SPCC132.02; -.
EuPathDB; FungiDB:SPCC132.02; -.
PomBase; SPCC132.02; hst2.
HOGENOM; HOG000085952; -.
InParanoid; Q9USN7; -.
KO; K11121; -.
OMA; LYPGSFI; -.
OrthoDB; EOG092C1NXT; -.
PhylomeDB; Q9USN7; -.
Reactome; R-SPO-2151201; Transcriptional activation of mitochondrial biogenesis.
PRO; PR:Q9USN7; -.
Proteomes; UP000002485; Chromosome III.
GO; GO:0034507; C:chromosome, centromeric outer repeat region; IEA:GOC.
GO; GO:0005737; C:cytoplasm; IDA:PomBase.
GO; GO:0005829; C:cytosol; HDA:PomBase.
GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase.
GO; GO:0000790; C:nuclear chromatin; IDA:PomBase.
GO; GO:0031618; C:nuclear pericentric heterochromatin; IDA:PomBase.
GO; GO:1902377; C:nuclear rDNA heterochromatin; IDA:PomBase.
GO; GO:1990707; C:nuclear subtelomeric heterochromatin; IDA:PomBase.
GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
GO; GO:0017136; F:NAD-dependent histone deacetylase activity; ISO:PomBase.
GO; GO:0033558; F:protein deacetylase activity; IMP:PomBase.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006338; P:chromatin remodeling; ISO:PomBase.
GO; GO:0030702; P:chromatin silencing at centromere; IMP:PomBase.
GO; GO:1990141; P:chromatin silencing at centromere outer repeat region; IMP:PomBase.
GO; GO:0000183; P:chromatin silencing at rDNA; IMP:PomBase.
GO; GO:1990619; P:histone H3-K9 deacetylation; IMP:PomBase.
GO; GO:0060303; P:regulation of nucleosome density; IEP:PomBase.
GO; GO:1900392; P:regulation of transport by negative regulation of transcription from RNA polymerase II promoter; IC:PomBase.
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; IPR003000; Sirtuin.
InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
InterPro; IPR017328; Sirtuin_class_I.
InterPro; IPR026590; Ssirtuin_cat_dom.
Pfam; PF02146; SIR2; 1.
PIRSF; PIRSF037938; SIR2_euk; 1.
SUPFAM; SSF52467; SSF52467; 1.
PROSITE; PS50305; SIRTUIN; 1.
3: Inferred from homology;
Complete proteome; Cytoplasm; Hydrolase; Metal-binding; NAD; Nucleus;
Reference proteome; Repressor; Transcription;
Transcription regulation; Zinc.
CHAIN 1 332 NAD-dependent protein deacetylase hst2.
/FTId=PRO_0000316618.
DOMAIN 16 271 Deacetylase sirtuin-type.
{ECO:0000255|PROSITE-ProRule:PRU00236}.
NP_BIND 35 55 NAD. {ECO:0000250}.
NP_BIND 118 121 NAD. {ECO:0000250}.
NP_BIND 210 212 NAD. {ECO:0000250}.
NP_BIND 235 237 NAD. {ECO:0000250}.
ACT_SITE 138 138 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 146 146 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 149 149 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 170 170 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 173 173 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
BINDING 255 255 NAD; via amide nitrogen. {ECO:0000250}.
SEQUENCE 332 AA; 37916 MW; 936A08D240C8BCFF CRC64;
MVKNTVKHVD SSKHLEKVAS LIKEGKVKKI CVMVGAGIST AAGIPDFRSP ETGIYNNLQR
FNLPYAEAVF DLSYFRKNPR PFYELAHELM PEKYRPTYTH YFIRLLHDKR LLQKCYTQNI
DTLERLAGVP DKALIEAHGS FQYSRCIECY EMAETEYVRA CIMQKQVPKC NSCKGLIKPM
IVFYGEGLPM RFFEHMEKDT KVCDMALVIG TSLLVHPFAD LPEIVPNKCQ RVLINREPAG
DFGERKKDIM ILGDCDSQVR ALCKLLGWSD ELEKLIDTSV ETLTEEISLL SVDSTIEKNA
SEQKKDDNSV NPFTKIEEKK KDEVTLLVSD DE


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