ID F0ZBN8_DICPU Unreviewed; 511 AA.
AC F0ZBN8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Deacetylase sirtuin-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DICPUDRAFT_28319 {ECO:0000313|EMBL:EGC38627.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC38627.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the sirtuin family.
CC {ECO:0000256|ARBA:ARBA00006988}.
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DR EMBL; GL870972; EGC38627.1; -; Genomic_DNA.
DR RefSeq; XP_003284820.1; XM_003284772.1.
DR AlphaFoldDB; F0ZBN8; -.
DR STRING; 5786.F0ZBN8; -.
DR EnsemblProtists; EGC38627; EGC38627; DICPUDRAFT_28319.
DR GeneID; 10506850; -.
DR KEGG; dpp:DICPUDRAFT_28319; -.
DR eggNOG; KOG1343; Eukaryota.
DR eggNOG; KOG2682; Eukaryota.
DR InParanoid; F0ZBN8; -.
DR OMA; DHSFWCY; -.
DR OrthoDB; 10545at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblProtists.
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; IEA:EnsemblProtists.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:EnsemblProtists.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:EnsemblProtists.
DR GO; GO:0044671; P:sorocarp spore cell differentiation; IEA:EnsemblProtists.
DR GO; GO:0031149; P:sorocarp stalk cell differentiation; IEA:EnsemblProtists.
DR CDD; cd01408; SIRT1; 1.
DR Gene3D; 3.30.1600.10; SIR2/SIRT2 'Small Domain; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 PANTHER; PTHR11085:SF10; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-2; 1.
DR PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02146; SIR2; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00236};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00502}.
FT DOMAIN 8..115
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 225..497
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 117..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 355
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 511 AA; 57222 MW; D3851B91D4BA4311 CRC64;
MVFAVNPIAC KHLVEEFDSC INISVFDNSN LSSPQCNVCN DKSENWICLR CGTVSCSRHV
NGHAGEHYES TGHPISASFI DHSFWCYTCD TYVYDRCLHE VEDILGTIKF FSKKENVDNT
GSNEKDIEED KVNDDKTTTT TTTTTTTTTT TTSESTTTTT TTQTIPQKPT PPLPTLDDYV
DKIINSDEDD SSSSSDEEVT PTLVQRMKEM FFGRSSGKTE TTPSSGLKQP TIEEVANYIN
SGKCKNIIVM TGAGISVAAG IPDFRSPKTG LYQKLGQYNL PYPEAIFEID FFKNNPKPFY
VLSKELYPGS FNPTPVHYFI KLLNDKGLLL RNFTQNIDTL ERVAGIPSEK LVEAHGSFAS
SKCVTCRQSH TTEYVREKVF SDSIPYCKET IECKGVVKPD IVFFGESLPS RFNECVREDF
PKCDLLIVIG TSLKVQPFAS LINFAKDIPR VLINFEEVGA NPYGGFKFND PSNKNDVKYI
GDCQVLIEQF IKLLGWENDF EQILNQSKNK K
//
