ID A0A317SSL5_9PEZI Unreviewed; 394 AA.
AC A0A317SSL5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=SIR2 family histone deacetylase {ECO:0000313|EMBL:PWW77383.1};
GN ORFNames=C7212DRAFT_356674 {ECO:0000313|EMBL:PWW77383.1};
OS Tuber magnatum (white Piedmont truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=42249 {ECO:0000313|EMBL:PWW77383.1, ECO:0000313|Proteomes:UP000246991};
RN [1] {ECO:0000313|EMBL:PWW77383.1, ECO:0000313|Proteomes:UP000246991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=091103-1 {ECO:0000313|EMBL:PWW77383.1};
RA Murat C., Payen T., Noel B., Kuo A., Martin F.M.;
RT "Genomes of Pezizomycetes fungi and the evolution of truffles.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000256|ARBA:ARBA00006924}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWW77383.1}.
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DR EMBL; PYWC01000023; PWW77383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317SSL5; -.
DR STRING; 42249.A0A317SSL5; -.
DR Proteomes; UP000246991; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 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 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 SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR PROSITE; PS50305; SIRTUIN; 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:UP000246991};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 15..276
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 394 AA; 42344 MW; 68017E9B8E93869F CRC64;
MGGELSTQID ADIPPQTLSR RDLPAVAEFI LSGKCEKIVF LCGAGISTSA GIPDFRTPGT
GLYSNLQTLN LPHPEAVFDM SFFRTNPQPF YTLAKSLHPG QFTPTVAHAF ISLTAKKNLL
HKCFTQNIDT LERAAGVPPE KLVEAHGSFA GQSCIDCHVA YPADKMKEHL LAGSVPQCEA
CPGLVKPDIV FFGESLPGEF RMGIGMVEEA DLVVVMGSSL SVYPFAALPL RAREGAVRLL
INNERAGEIG GRADDVLFLG GCDEGVRKLA EELGWAEELE EVWMSVGGGT DKKAEAESSE
DAEPVESMDA KVGRLTEEVE RGLSVVDGWK ENCYARAPAR SKNPASYRGT VHPEPAEMGF
GSGVHHHSKR PGHLRNGGWS TFVGTGTVVH DTEV
//
