(data stored in ACNUC7421 zone)

SWISSPROT: SIR2_ASHGO

ID   SIR2_ASHGO              Reviewed;         559 AA.
AC   Q757M7;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 98.
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=AEL013C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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}.
DR   EMBL; AE016818; AAS52672.1; -; Genomic_DNA.
DR   RefSeq; NP_984848.1; NM_210202.1.
DR   SMR; Q757M7; -.
DR   STRING; 33169.AAS52672; -.
DR   EnsemblFungi; AAS52672; AAS52672; AGOS_AEL013C.
DR   GeneID; 4621047; -.
DR   KEGG; ago:AGOS_AEL013C; -.
DR   HOGENOM; HOG000191845; -.
DR   InParanoid; Q757M7; -.
DR   KO; K11121; -.
DR   OMA; SQGFYSM; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005677; C:chromatin silencing complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
DR   GO; GO:0005720; C:nuclear heterochromatin; IBA:GO_Central.
DR   GO; GO:0031618; C:nuclear pericentric heterochromatin; IBA:GO_Central.
DR   GO; GO:0005724; C:nuclear telomeric heterochromatin; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0034967; C:Set3 complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR   GO; GO:0017136; F:NAD-dependent histone deacetylase activity; IBA:GO_Central.
DR   GO; GO:0046970; F:NAD-dependent histone deacetylase activity (H4-K16 specific); IBA:GO_Central.
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;
DR   PRODOM; Q757M7.
DR   SWISS-2DPAGE; Q757M7.
KW   Metal-binding; NAD; Nucleus; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Transferase; Zinc.
FT   CHAIN           1..559
FT                   /note="NAD-dependent histone deacetylase SIR2"
FT                   /id="PRO_0000110274"
FT   DOMAIN          231..516
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT   NP_BIND         248..267
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         330..333
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         458..460
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         483..485
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        350
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT   METAL           358
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT   METAL           361
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT   METAL           382
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT   METAL           385
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT   BINDING         500
FT                   /note="NAD; via amide nitrogen"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   559 AA;  62561 MW;  C8817AE0DC14D24C CRC64;
     MSESASMLQG SKRGTDSSVD VGGAKRTKVD MDDGSSSNND EKELLEATKA DELDEVVDDY
     AEQNDHSAQE VAGEYVPKKP EQPIMLTKDS NSGKYVFPPI SKEDSLNARY FLKYHGSAQF
     LDSYLPEDLN SLYVFHLIKL LGFQLKDREL LTAVQKAVQN DVTSGVSSVV GTNPMVERVS
     PPQLSASTPS GDGYDDPLEK KHAVRLIKDL QKAMNKVLST RIRLANFFTL DHFISKLKSA
     KKVLVLTGAG ISTSLGIPDF RSSKGFYSQV TNLGLDDPQD VFNLDIFMEN PSVFYTIAEK
     ILPPEHKFSP LHSFIKMIQD KGKLLRNYTQ NIDNLESYAG IFKENIVQCH GSFATASCVT
     CHLKMPGERI FQQIKDREIP LCAYCYPKRQ EEYPTVSDDP GTKNGQQSSH NSSSIFHMSR
     SFGVIKPDIT FFGEALPLEF HTNIRQDVLQ CDLLICIGTS LKVAPVSEIV NMVPAHVPQV
     LINRDPVKHA EFDLTLLGLC DDVAAFIAQK CGWDIPHENW PQLKQRNIQY DELERGMYYV
     YDPVKEQAKD TGQRQVQAP
//

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