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SIR2C_DICDI
ID   SIR2C_DICDI             Reviewed;         456 AA.
AC   Q54P49;
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 sir2C;
DE            EC=2.3.1.286;
DE   AltName: Full=Silent information regulator sir2C;
GN   Name=sir2C; ORFNames=DDB_G0284795;
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; AAFI02000071; EAL65050.1; -; Genomic_DNA.
DR   RefSeq; XP_638409.1; XM_633317.1.
DR   AlphaFoldDB; Q54P49; -.
DR   SMR; Q54P49; -.
DR   STRING; 44689.DDB0216433; -.
DR   PaxDb; Q54P49; -.
DR   EnsemblProtists; EAL65050; EAL65050; DDB_G0284795.
DR   GeneID; 8624779; -.
DR   KEGG; ddi:DDB_G0284795; -.
DR   dictyBase; DDB_G0284795; sir2C.
DR   eggNOG; KOG2682; Eukaryota.
DR   HOGENOM; CLU_600549_0_0_1; -.
DR   InParanoid; Q54P49; -.
DR   OMA; HIENCNI; -.
DR   PhylomeDB; Q54P49; -.
DR   PRO; PR:Q54P49; -.
DR   Proteomes; UP000002195; Chromosome 4.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1600.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 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   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF02146; SIR2; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   PROSITE; PS50305; SIRTUIN; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; NAD; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..456
FT                   /note="NAD-dependent deacetylase sir2C"
FT                   /id="PRO_0000393127"
FT   DOMAIN          169..445
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT   ACT_SITE        294
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT   BINDING         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT   BINDING         305
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT   BINDING         331
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT   BINDING         336
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
SQ   SEQUENCE   456 AA;  52428 MW;  BD793FF9BED69AAB CRC64;
     MSKQTQCVHI ENCNINYESI DIQLYDNENI TIPNCYKCSS QDNILICLEC GIVVCMEDCK
     LHSNHSIFKI FHGDDKTLWC NDCNELIKES TMIEKCTKNS DLINKKLKDI ENLFKVMKLF
     IYYDQRNLKY NKNFDSIDNS IKDIIKNSNI IKNEIKIENE IEIENNKIKE FIKLIKNDKC
     KNIIVLTGAG ISVASGIPDF RSVETGLYNN ENVSKFKLPF KEAVFDIDYF KFNPEPFYQL
     SKDLYPSGKF KCTPVHYFIK LLSDKGLLLR NYAQNADTLE RIAGIPLDKL IEAHGSFAVS
     RCTNCGLEYS QEYIKDSIFN NDPLKSVVPR CKVVQCNNAV IKPDIVFFGE SLPPIFNQNI
     LDDINRCDCL IVIGTSLKVQ PIASMVHFFP HFKNIPRLLI NNQIVGENSF GGFNFNNNKN
     FDFKMIGDCQ ESVLNLSKLL NWDTELLNLI NSKNHN
 
 
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