SMART: Pfam domain zf-SAP30

The domain within your query sequence starts at position 23 and ends at position 94; the E-value for the zf-SAP30 domain shown below is 4.5e-40.

GYGQSCCLIADGERCVRPAGNASFSKRVQKSISQKKLKLDIDKSVRHLYICDFHKNFIQS
VRNKRKRKASDD

zf-SAP30

PFAM accession number:	PF13866
Interpro abstract (IPR025717):	SAP30 is a subunit of the histone deacetylase complex, and this domain is a zinc-finger. Solution of the structure shows a novel fold comprising two beta-strands and two alpha-helices with the zinc organising centre showing remote resemblance to the treble clef motif. In silico analysis of the structure reveals a highly conserved surface dominated by basic residues. NMR-based analysis of potential ligands for the SAP30 Zn-finger motif indicate a strong preference for nucleic acid substrates. The zinc-finger of SAP30 probably functions as a double-stranded DNA-binding motif, thereby expanding the known functions of both SAP30 and the mammalian Sin3 co-repressor complex [ (PUBMED:19223330) ].

PFAM accession number:

PF13866

Interpro abstract (IPR025717):

SAP30 is a subunit of the histone deacetylase complex, and this domain is a zinc-finger. Solution of the structure shows a novel fold comprising two beta-strands and two alpha-helices with the zinc organising centre showing remote resemblance to the treble clef motif. In silico analysis of the structure reveals a highly conserved surface dominated by basic residues. NMR-based analysis of potential ligands for the SAP30 Zn-finger motif indicate a strong preference for nucleic acid substrates. The zinc-finger of SAP30 probably functions as a double-stranded DNA-binding motif, thereby expanding the known functions of both SAP30 and the mammalian Sin3 co-repressor complex [ (PUBMED:19223330) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry zf-SAP30