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| PROSITE documentation PDOC00821 |
DNA/RNA non-specific endonucleases active site
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 [1] 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.
Expert(s) to contact by email: Last update:July 1999 / Pattern and text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Friedhoof P. Gimadutdinow O. Pingoud A. |
| Title | Identification of catalytically relevant amino acids of the extracellular Serratia marcescens endonuclease by alignment-guided mutagenesis. | |
| Source | Nucleic Acids Res. 22:3280-3287(1994). | |
| PubMed ID | 8078761 |
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