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ProRule PRU00236


General rule information [?]

Accession PRU00236
Dates 12-DEC-2003 (Created)
19-NOV-2022 (Last updated, Version 14)
Data class Domain;
Predictors PROSITE; PS50305; SIRTUIN
Name Sirtuin catalytic domain
Function Sirtuins are responsible for a newly classified chemical reaction, NAD- dependent protein deacetylation.
Scope(s) Eukaryota
Archaea
Bacteria
Example(s) P06700 (SIR2_YEAST);

Propagated annotation [?]

Identifier, protein and gene names [?]

case <FTTag:act_site>
Protein name + RecName: EC=2.3.1.286;

Comments [?]

CATALYTIC ACTIVITY Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl- ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286;

Keywords [?]

NAD
Transferase
end case
case <FTGroup:1>
Metal-binding
Zinc
end case

Gene Ontology [?]

GO:0016407; Molecular function:acetyltransferase activity

Features [?]

From: PS50305
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="Deacetylase sirtuin-type #"
case <FTGroup:1>
ACT_SITE 129 129 /note="Proton acceptor" act_site H
end case
BINDING 137 137 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"		 C 1
BINDING 140 140 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"		 C 1
BINDING 161 161 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"		 [CH] 1
BINDING 164 164 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"		 C 1

Additional information [?]

Size range 207-331 amino acids
Related rules None
Fusion None
Repeats 1
Topology Cytoplasmic

Copyright

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.



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UniProtKB rule member sequences [?]