SIR2D_DICDI
ID SIR2D_DICDI Reviewed; 542 AA.
AC Q54GV7;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=NAD-dependent deacetylase sir2D;
DE EC=2.3.1.286;
DE AltName: Full=Silent information regulator sir2D;
GN Name=sir2D; ORFNames=DDB_G0289967;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP DEVELOPMENTAL STAGE.
RX DOI=10.1264/jsme2.23.40;
RA Katayama T., Yasukawa H.;
RT "Developmental and spatial expression of sir2 genes in the cellular slime
RT mold Dictyostelium discoideum.";
RL Microbes Environ. 23:40-43(2008).
CC -!- FUNCTION: NAD-dependent deacetylase, which plays an important role in
CC the regulation of transcriptional repression. {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 -!- DEVELOPMENTAL STAGE: Expressed at high levels in growing cells, but at
CC decreased levels in developing cells. Expressed in both prestalk and
CC prespore cells. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the sirtuin family. {ECO:0000305}.
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DR EMBL; AAFI02000149; EAL62496.1; -; Genomic_DNA.
DR RefSeq; XP_635962.1; XM_630870.1.
DR AlphaFoldDB; Q54GV7; -.
DR SMR; Q54GV7; -.
DR STRING; 44689.DDB0219946; -.
DR PaxDb; Q54GV7; -.
DR PRIDE; Q54GV7; -.
DR EnsemblProtists; EAL62496; EAL62496; DDB_G0289967.
DR GeneID; 8627377; -.
DR KEGG; ddi:DDB_G0289967; -.
DR dictyBase; DDB_G0289967; sir2D.
DR eggNOG; KOG2684; Eukaryota.
DR HOGENOM; CLU_502928_0_0_1; -.
DR InParanoid; Q54GV7; -.
DR OMA; KLVNCHG; -.
DR PhylomeDB; Q54GV7; -.
DR Reactome; R-DDI-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DDI-427359; SIRT1 negatively regulates rRNA expression.
DR PRO; PR:Q54GV7; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IMP:dictyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:dictyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR GO; GO:0044671; P:sorocarp spore cell differentiation; IMP:dictyBase.
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; IPR026590; Ssirtuin_cat_dom.
DR Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Metal-binding; NAD; Reference proteome; Transferase; Zinc.
FT CHAIN 1..542
FT /note="NAD-dependent deacetylase sir2D"
FT /id="PRO_0000393128"
FT DOMAIN 291..542
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 165..193
FT /evidence="ECO:0000255"
FT COMPBIAS 7..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 411
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 542 AA; 62142 MW; FF53AAF9CDB31377 CRC64;
MNKRSLENNE LNEIQNNQNK NNNNKINKEI PSDNTPLKKL KSINSLEQLQ EVDEDEDLDV
EIDTKLINKL DKKGRKYEFV GEGYSDEEQI SDDYEDDESS EYEYGYENED ELLDDEDHLD
NINEIKKIQK KLVNTETSTS ITNTSSTTTT STSTTTTTTT KTQINETILL DILNNNKDEV
DDEIQRIGNN VGNSKEEEGE EEEENIELVA RSFIYKHIQE KKSLGIDPIE FTKDIGFKLE
LEKDDDAWEI ITAFLTRKKV AVNLFLNYLK YNTLARPYRK KIATLDLSTF EKVCQLFESS
KNIVIITGAG VSVSCGIPDF RSKGGVYETI EKKYNLPRPE SLFDIHYLRA NPLPFFEFAK
EIFPGNHKPS PTHSFIKLLD EKGKLLRNYT QNIDTLEHVA GIDREKLVNC HGSFSTATCI
TCKLTVDGTT IRDTIMKMEI PLCQQCNDGQ SFMKPDIVFF GENLPDRFDQ CVLKDVKDID
LLIVMGSSLQ VQPVSLLPDI VDKQIPQILI NRELVAQPHE FDYVYLGDCD QFVQDLLNKV
KW
