Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2012) Nucleic Acids Res , doi:10.1093/nar/gkr931

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VRR_NUC

SMART accession number:	SM00990
Description:	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.
Interpro abstract (IPR014883):	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:	View or CHROMA formatCLUSTALW formatMSF formatFASTA formatPIR format

There are 547 VRR_NUC domains in 547 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a VRR_NUC domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with VRR_NUC domain is also avaliable.

  Useful shortcuts: Expand all nodes or Collapse tree
  Go to specific node: Arabidopsis thaliana, Caenorhabditis elegans, Homo sapiens, Mus musculus, Rattus norvegicus, Takifugu rubripes

• Cellular role (predicted cellular role)

• Cellular role: chromatin
  

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Kinch LN, Ginalski K, Rychlewski L, Grishin NV
  • 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.

• Links (links to other resources describing this domain)

• PFAM	VRR_NUC
  INTERPRO	IPR014883

Send comments to Ivica Letunic