(data stored in SCRATCH zone)

SWISSPROT: Q750H1_ASHGO

ID   Q750H1_ASHGO            Unreviewed;       340 AA.
AC   Q750H1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 106.
DE   RecName: Full=NAD-dependent protein deacetylase {ECO:0000256|PIRNR:PIRNR037938};
DE            EC=2.3.1.286 {ECO:0000256|PIRNR:PIRNR037938};
GN   ORFNames=AGOS_AGL018C {ECO:0000313|EMBL:AAS54472.1};
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 {ECO:0000313|EMBL:AAS54472.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54472.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
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., Pohlmann 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] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
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   -!- 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:0000256|PIRNR:PIRNR037938};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR037938};
CC   -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC       {ECO:0000256|PIRNR:PIRNR037938}.
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DR   EMBL; AE016820; AAS54472.1; -; Genomic_DNA.
DR   RefSeq; NP_986648.1; NM_211710.1.
DR   STRING; 33169.AAS54472; -.
DR   EnsemblFungi; AAS54472; AAS54472; AGOS_AGL018C.
DR   GeneID; 4622947; -.
DR   KEGG; ago:AGOS_AGL018C; -.
DR   HOGENOM; HOG000085952; -.
DR   InParanoid; Q750H1; -.
DR   KO; K11121; -.
DR   OMA; DFRGDVM; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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); IEA:EnsemblFungi.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000183; P:chromatin silencing at rDNA; IEA:EnsemblFungi.
DR   GO; GO:0001300; P:chronological cell aging; IEA:EnsemblFungi.
DR   GO; GO:0031939; P:negative regulation of chromatin silencing at telomere; IEA:EnsemblFungi.
DR   GO; GO:0045950; P:negative regulation of mitotic recombination; IEA:EnsemblFungi.
DR   Gene3D; 3.30.1600.10; -; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR003000; Sirtuin.
DR   InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR   InterPro; IPR017328; Sirtuin_class_I.
DR   InterPro; IPR026590; Ssirtuin_cat_dom.
DR   Pfam; PF02146; SIR2; 1.
DR   PIRSF; PIRSF037938; SIR2_euk; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   PROSITE; PS50305; SIRTUIN; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750H1.
DR   SWISS-2DPAGE; Q750H1.
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR037938,
KW   ECO:0000256|PIRSR:PIRSR037938-3};
KW   NAD {ECO:0000256|PIRNR:PIRNR037938, ECO:0000256|PIRSR:PIRSR037938-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transferase {ECO:0000256|PIRNR:PIRNR037938};
KW   Zinc {ECO:0000256|PIRNR:PIRNR037938, ECO:0000256|PIRSR:PIRSR037938-3}.
FT   DOMAIN          10..272
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   NP_BIND         30..34
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT   NP_BIND         40..42
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT   NP_BIND         112..115
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT   NP_BIND         211..212
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT   NP_BIND         235..237
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT   ACT_SITE        132
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-1"
FT   METAL           140
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-3"
FT   METAL           143
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-3"
FT   METAL           164
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-3"
FT   METAL           167
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-3"
FT   BINDING         256
FT                   /note="NAD; via amide nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
SQ   SEQUENCE   340 AA;  38289 MW;  BBC9AD5DA1BB79E7 CRC64;
     MDPQELASIN KVAKYIKNHP KAKVVFLVGA GISTSCGIPD FRSPNTGLYH NLSKFKLPYA
     EAVFAIDYFQ RDPKPFYTLA REMYPGKYIP SRFHYLMKLF ESKGYLKAVY TQNIDTLERE
     AGIAADYIIE AHGSFATNHC IDCDKTFPTE TFKAMLESGE YARCEDCEGL IKPRIVFFGE
     DLPSVFYTSW DKLLSEMQAG KEDYLVIVAG TSLVVYPFAS LPSETPRKVH RVLMNMEVVG
     DFKTPRKTDI IIHGETDHIA EELARALGWY DELVDISSGR SSSETTVVEK DTENQTDIKS
     ASASVIKYKE VSSVSKEESS IDKIAEKILK LDLSRENSDD
//

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