SMART: Pfam domain SNase

The domain within your query sequence starts at position 835 and ends at position 895; the E-value for the SNase domain shown below is 1.3e-7.

ASCPHVTLQFADSKGDVGLGLVKEGLVMVEVRKEKQFQKVITEYLNAQESAKSARLNLWR
Y

SNase

PFAM accession number:	PF00565
Interpro abstract (IPR016071):	Staphylococcus aureus nuclease (SNase) homologues, previously thought to be restricted to bacteria and archaea, are also in eukaryotes. Staphylococcal nuclease has a multi-domain organisation [ (PUBMED:9003410) ]. The human cellular coactivator p100 contains four repeats, each of which is a SNase homologue. These repeats are unlikely to possess SNase-like activities as each lacks equivalent SNase catalytic residues, yet they may mediate p100's single-stranded DNA-binding function [ (PUBMED:9041650) ]. A variety of proteins including many that are still uncharacterised belong to this group. SNase domains have an OB-fold consisting of a closed or partly open beta-barrel with Greek key topology [ (PUBMED:8475069) ].

PFAM accession number:

PF00565

Interpro abstract (IPR016071):

Staphylococcus aureus nuclease (SNase) homologues, previously thought to be restricted to bacteria and archaea, are also in eukaryotes. Staphylococcal nuclease has a multi-domain organisation [ (PUBMED:9003410) ]. The human cellular coactivator p100 contains four repeats, each of which is a SNase homologue. These repeats are unlikely to possess SNase-like activities as each lacks equivalent SNase catalytic residues, yet they may mediate p100's single-stranded DNA-binding function [ (PUBMED:9041650) ]. A variety of proteins including many that are still uncharacterised belong to this group.

SNase domains have an OB-fold consisting of a closed or partly open beta-barrel with Greek key topology [ (PUBMED:8475069) ].

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