SIR2A_DICDI
ID SIR2A_DICDI Reviewed; 512 AA.
AC Q54QE6;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=NAD-dependent deacetylase sir2A;
DE EC=2.3.1.286;
DE AltName: Full=Silent information regulator sir2A;
GN Name=sir2A; ORFNames=DDB_G0283917;
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; AAFI02000058; EAL65446.1; -; Genomic_DNA.
DR RefSeq; XP_638798.1; XM_633706.1.
DR AlphaFoldDB; Q54QE6; -.
DR SMR; Q54QE6; -.
DR STRING; 44689.DDB0216430; -.
DR PaxDb; Q54QE6; -.
DR EnsemblProtists; EAL65446; EAL65446; DDB_G0283917.
DR GeneID; 8624322; -.
DR KEGG; ddi:DDB_G0283917; -.
DR dictyBase; DDB_G0283917; sir2A.
DR eggNOG; KOG1343; Eukaryota.
DR eggNOG; KOG2682; Eukaryota.
DR HOGENOM; CLU_600549_0_0_1; -.
DR InParanoid; Q54QE6; -.
DR OMA; CHFISAT; -.
DR PhylomeDB; Q54QE6; -.
DR PRO; PR:Q54QE6; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0061909; P:autophagosome-lysosome fusion; 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:0044671; P:sorocarp spore cell differentiation; IMP:dictyBase.
DR GO; GO:0031149; P:sorocarp stalk cell differentiation; IMP:dictyBase.
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 InterPro; IPR001607; Znf_UBP.
DR Pfam; PF02146; SIR2; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; NAD; Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..512
FT /note="NAD-dependent deacetylase sir2A"
FT /id="PRO_0000393125"
FT DOMAIN 239..505
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT ZN_FING 7..110
FT /note="UBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 113..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 361
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 512 AA; 57413 MW; E117B76700157565 CRC64;
MYAVNPIECI HLKDEYDTCI NKSIFDKDLK ITKCHACNDE SENWICMTCG VVSCSRHVNG
HAGEHFENTK HPISASFSDH SFWCYTCDTY VHNTPLFDIC EILENIKSSN KKDKIVPKKD
QKEEEEEDQV VPSASITTSS TTTSISKQTT VNNTTTTSSS STTTTTTTTS TTINNNEEEE
ESESETDESS SEGEESLSLI QRMREMIFGV GRGPKIVAPS EQEESEEDES CVLKKPTIEE
IAKYINSAKC KNIIVMTGAG ISVAAGIPDF RSPKTGLYEK LDKYDLPYRE AIFDIEYFKK
NPKPFYVLSK ELFPGSFNPT TVHYFIKLLS DKGLLLRNFT QNIDTLERIA GIPANKLVEA
HGSFATSHCV SCKKEYSTEY VKERIFKDEL PECTETSGCK GIVKPDIVFF GESLPSRFND
CAREDFTKCD LLLVIGTSLK VHPFASLINF AKGCPRVLIN FEEVGTNPYG GFKFNQPSNK
LDVKCIGDCQ TLVLDLIKLL GWENEFNQIV KN
