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DNA/RNA non-specific endonuclease

From Wikipedia, the free encyclopedia
Endonuclease_NS
identification of the serratia endonuclease dimer: structural basis and implications for catalysis
Identifiers
SymbolEndonuclease_NS
PfamPF01223
Pfam clanCL0263
InterProIPR001604
PROSITEPDOC00821
SCOP21smn / SCOPe / SUPFAM
CDDcd00091
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In molecular biology, enzymes in the DNA/RNA non-specific endonuclease family of bacterial and eukaryotic endonucleases EC 3.1.30.- share the following characteristics: they act on both DNA and RNA, cleave double-stranded and single-stranded nucleic acids and require a divalent ion such as magnesium for their activity. A histidine has been shown to be essential for the activity of the Serratia marcescens nuclease. This residue is located in a conserved region which also contains an aspartic acid residue that could be implicated in the binding of the divalent ion.[1]

Notable members of the family include Serratia marcescens NucA and human Exonuclease G.

References

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  1. ^ Friedhoff P, Gimadutdinow O, Pingoud A (August 1994). "Identification of catalytically relevant amino acids of the extracellular Serratia marcescens endonuclease by alignment-guided mutagenesis". Nucleic Acids Res. 22 (16): 3280–7. doi:10.1093/nar/22.16.3280. PMC 523719. PMID 8078761.
This article incorporates text from the public domain Pfam and InterPro: IPR001604