This entry contains proteins with the VRR-NUC domain. It is associated with members of the PD-(D/E)XK nuclease superfamily, which include the type III restriction modification enzymes, for example StyLTI.
This entry contains proteins with the VRR-NUC domain. It is associated with members of the PD-(D/E)XK nuclease superfamily, which include the type III restriction modification enzymes [ (PUBMED:15972856) ].
GO function:
hydrolase activity, acting on ester bonds (GO:0016788)
Family alignment:
There are 7433 VRR_NUC domains in 7432 proteins in SMART's nrdb database.
Click on the following links for more information.
Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing VRR_NUC domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with VRR_NUC domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing VRR_NUC domain in the selected taxonomic class.
Identification of novel restriction endonuclease-like fold families amonghypothetical proteins.
Nucleic Acids Res. 2005; 33: 3598-605
Display abstract
Restriction endonucleases and other nucleic acid cleaving enzymes form alarge and extremely diverse superfamily that display little sequencesimilarity despite retaining a common core fold responsible for cleavage.The lack of significant sequence similarity between protein families makeshomology inference a challenging task and hinders new familyidentification with traditional sequence-based approaches. Using theconsensus fold recognition method Meta-BASIC that combines sequenceprofiles with predicted protein secondary structure, we identify nine newrestriction endonuclease-like fold families among previouslyuncharacterized proteins and predict these proteins to cleave nucleic acidsubstrates. Application of transitive searches combined with geneneighborhood analysis allow us to confidently link these unknown familiesto a number of known restriction endonuclease-like structures and thusassign folds to the uncharacterized proteins. Finally, our methodidentifies a novel restriction endonuclease-like domain in the C-terminusof RecC that is not detected with structure-based searches of the existingPDB database.
