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 03-AUG-2022, entry version 107.
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}.
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DR EMBL; AE016818; AAS52672.1; -; Genomic_DNA.
DR RefSeq; NP_984848.1; NM_210202.1.
DR AlphaFoldDB; Q757M7; -.
DR SMR; Q757M7; -.
DR STRING; 33169.AAS52672; -.
DR EnsemblFungi; AAS52672; AAS52672; AGOS_AEL013C.
DR GeneID; 4621047; -.
DR KEGG; ago:AGOS_AEL013C; -.
DR eggNOG; KOG2684; Eukaryota.
DR HOGENOM; CLU_023643_5_0_1; -.
DR InParanoid; Q757M7; -.
DR OMA; PYCYKKR; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0005634; C:nucleus; 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;
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 REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 248..267
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 330..333
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 458..460
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 483..485
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 500
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
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
