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A 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-standed nucleic acids and require a divalent ion such as
magnesium for their activity. The enzymes that belongs to this family are:
Extracellular nuclease from Serratia marcescens.
Extracellular nuclease nucA from the cyanobacteria Anabaena PCC 7120.
DNA-entry nuclease from Streptococcus pneumoniae.
Mammalian mitochondrial endonuclease G (endo G).
Yeast mitochondrial endonuclease NUC1.
Nuclease C1 from the fungi Cunninghamella echinulata.
An histidine has been shown  to be essential for the activity of the
Serratia marcescens nuclease. This residue is located in a conserved region
which can be used as a signature pattern and which also contains an aspartic
acid residue that could be implicated in the binding of the divalent ion.
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