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annotation rule: PRU00236

General rule information [?]

Accession PRU00236
Dates 12-DEC-2003 (Created)
27-OCT-2018 (Last updated, Version 8)
Data class Domain
Predictors PROSITE; PS50305; SIRTUIN
Names Sirtuin catalytic domain; Sir2 domain
Function Sirtuins are responsible for a newly classified chemical reaction, NAD- dependent protein deacetylation.

Propagated annotation [?]


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;.

Gene Ontology [?]

GO:0016787; Molecular function: hydrolase activity.

Keywords [?]

case <FTGroup:1>
end case


Features [?]

From: PS50305
Key     From     To       Description   Tag   Condition   FTGroup
DOMAIN     from     to       Deacetylase sirtuin-type #        
ACT_SITE     115     115       Proton acceptor     H  
METAL     123     123       Zinc     C   1
METAL     126     126       Zinc     C   1
METAL     147     147       Zinc     C   1
METAL     150     150       Zinc     C   1

Additional information [?]

Size range 207-331 amino acids
Related rules None
Repeats 1
Topology Cytoplasmic
Example P06700 (SIR2_YEAST)
Scope
Eukaryota
Archaea
Bacteria

Copyright

PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to license@isb-sib.ch or see: prosite_license.html.



UniProtKB rule member sequences [?]