SMART: Pfam domain SIR2

The domain within your query sequence starts at position 253 and ends at position 439; the E-value for the SIR2 domain shown below is 1.3e-62.

GAGVSVSCGIPDFRSRDGIYARLAVDFPDLPDPQAMFDIEYFRKDPRPFFKFAKEIYPGQ
FQPSLCHKFIALSDKEGKLLRNYTQNIDTLEQVAGIQRILQCHGSFATASCLICKYKVDC
EAVRGDIFNQVVPRCPRCPADEPLAIMKPEIVFFGENLPEQFHRAMKYDKDEVDLLIVIG
SSLKVRP

SIR2

PFAM accession number:	PF02146
Interpro abstract (IPR003000):	The sirtuin (also known as Sir2) family is broadly conserved from bacteria to human. Yeast Sir2 (silent mating-type information regulation 2), the founding member, was first isolated as part of the SIR complex required for maintaining a modified chromatin structure at telomeres. Sir2 functions in transcriptional silencing, cell cycle progression, and chromosome stability [ (PUBMED:7498786) ]. Although most sirtuins in eukaryotic cells are located in the nucleus, others are cytoplasmic or mitochondrial. This family is divided into five classes (I-IV and U) on the basis of a phylogenetic analysis of 60 sirtuins from a wide array of organisms [ (PUBMED:10873683) ]. Class I and class IV are further divided into three and two subgroups, respectively. The U-class sirtuins are found only in Gram-positive bacteria [ (PUBMED:10873683) ]. The S. cerevisiae genome encodes five sirtuins, Sir2 and four additional proteins termed 'homologues of sir two' (Hst1p-Hst4p) [ (PUBMED:7498786) ]. The human genome encodes seven sirtuins, with representatives from classes I-IV [ (PUBMED:10873683) (PUBMED:15128440) ]. Sirtuins are responsible for a newly classified chemical reaction, NAD-dependent protein deacetylation. The final products of the reaction are the deacetylated peptide and an acetyl ADP-ribose [ (PUBMED:11747420) ]. In nuclear sirtuins this deacetylation reaction is mainly directed against histones acetylated lysines [ (PUBMED:11722841) ]. Sirtuins typically consist of two optional and highly variable N- and C- terminal domain (50-300 aa) and a conserved catalytic core domain (~250 aa). Mutagenesis experiments suggest that the N- and C-terminal regions help direct catalytic core domain to different targets [ (PUBMED:11722841) (PUBMED:10381378) ]. The 3D-structure of an archaeal sirtuin in complex with NAD reveals that the protein consists of a large domain having a Rossmann fold and a small domain containing a three-stranded zinc ribbon motif. NAD is bound in a pocket between the two domains [ (PUBMED:11336676) ].
GO function:	NAD+ binding (GO:0070403)

PFAM accession number:

PF02146

Interpro abstract (IPR003000):

The sirtuin (also known as Sir2) family is broadly conserved from bacteria to human. Yeast Sir2 (silent mating-type information regulation 2), the founding member, was first isolated as part of the SIR complex required for maintaining a modified chromatin structure at telomeres. Sir2 functions in transcriptional silencing, cell cycle progression, and chromosome stability [ (PUBMED:7498786) ]. Although most sirtuins in eukaryotic cells are located in the nucleus, others are cytoplasmic or mitochondrial.

This family is divided into five classes (I-IV and U) on the basis of a phylogenetic analysis of 60 sirtuins from a wide array of organisms [ (PUBMED:10873683) ]. Class I and class IV are further divided into three and two subgroups, respectively. The U-class sirtuins are found only in Gram-positive bacteria [ (PUBMED:10873683) ]. The S. cerevisiae genome encodes five sirtuins, Sir2 and four additional proteins termed 'homologues of sir two' (Hst1p-Hst4p) [ (PUBMED:7498786) ]. The human genome encodes seven sirtuins, with representatives from classes I-IV [ (PUBMED:10873683) (PUBMED:15128440) ].

Sirtuins are responsible for a newly classified chemical reaction, NAD-dependent protein deacetylation. The final products of the reaction are the deacetylated peptide and an acetyl ADP-ribose [ (PUBMED:11747420) ]. In nuclear sirtuins this deacetylation reaction is mainly directed against histones acetylated lysines [ (PUBMED:11722841) ].

Sirtuins typically consist of two optional and highly variable N- and C- terminal domain (50-300 aa) and a conserved catalytic core domain (~250 aa). Mutagenesis experiments suggest that the N- and C-terminal regions help direct catalytic core domain to different targets [ (PUBMED:11722841) (PUBMED:10381378) ].

The 3D-structure of an archaeal sirtuin in complex with NAD reveals that the protein consists of a large domain having a Rossmann fold and a small domain containing a three-stranded zinc ribbon motif. NAD is bound in a pocket between the two domains [ (PUBMED:11336676) ].

GO function:

NAD+ binding (GO:0070403)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry SIR2