Homologous Superfamily

SNase-like, OB-fold/extended TUDOR domain superfamily (IPR035437)

Short name: SNase_OB-fold/TUDOR_sf


This superfamily is composed of the Staphylococcal nuclease (SNase-like), OB-fold domain and the extended TUDOR domain of the Tudor staphylococcal nuclease (Tudor-SN) protein.

The Tudor-SN protein (p100, SND1) is implicated in a variety of cellular processes, such as transcription, processing of edited double-stranded RNA, and splicing regulation. The aromatic cage of the extended TUDOR domain specifically binds a peptide containing symmetrically dimethylated arginines (sDMA) [PMID: 19232356].

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 [PMID: 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 [PMID: 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 [PMID: 8475069].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.