SMART: Pfam domain NYN

The domain within your query sequence starts at position 351 and ends at position 492; the E-value for the NYN domain shown below is 1.5e-21.

PIGVFWDIENCSVPSGRSATTVVQRIREKFFRGHREAEFICVCDISKENKEVIQELNNCQ
VTVAHINATAKNAADDKLRQSLRRFANTHTAPATVVLVSTDVNFALELSDLRHRHGFHII
LVHKNQASEALLHHANQLIRFE

NYN

PFAM accession number:	PF01936
Interpro abstract (IPR021139):	This NYN domain is found in limkain-b1 [ (PUBMED:15932519) ] and in uncharacterised proteins. The NYN domains are found in the eukaryotic proteins typified by the Nedd4-binding protein 1 and the bacterial YacP-like proteins. The NYN (for Nedd4-BP1, YacP-like Nuclease) domain shares a common protein fold with two other previously characterised groups of nucleases, namely the PIN (PilT N-terminal) and FLAP/5' --> 3' exonuclease superfamilies. These proteins share a common set of 4 acidic conserved residues that are predicted to constitute their active site. Based on the conservation of the acidic residues and structural elements it has been suggested that PIN and NYN domains are likely to bind only a single metal ion, unlike the FLAP/5' --> 3' exonuclease superfamily, which binds two metal ions [ (PUBMED:17114934) ]. Based on conserved gene neighbourhoods the bacterial members are likely to be components of the processome/degradosome that process tRNAs or ribosomal RNAs.

PFAM accession number:

PF01936

Interpro abstract (IPR021139):

This NYN domain is found in limkain-b1 [ (PUBMED:15932519) ] and in uncharacterised proteins. The NYN domains are found in the eukaryotic proteins typified by the Nedd4-binding protein 1 and the bacterial YacP-like proteins. The NYN (for Nedd4-BP1, YacP-like Nuclease) domain shares a common protein fold with two other previously characterised groups of nucleases, namely the PIN (PilT N-terminal) and FLAP/5' --> 3' exonuclease superfamilies. These proteins share a common set of 4 acidic conserved residues that are predicted to constitute their active site. Based on the conservation of the acidic residues and structural elements it has been suggested that PIN and NYN domains are likely to bind only a single metal ion, unlike the FLAP/5' --> 3' exonuclease superfamily, which binds two metal ions [ (PUBMED:17114934) ]. Based on conserved gene neighbourhoods the bacterial members are likely to be components of the processome/degradosome that process tRNAs or ribosomal RNAs.

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