{PDOC00821}
{PS01070; NUCLEASE_NON_SPEC}
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* DNA/RNA non-specific endonucleases active site *
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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  [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.

-Consensus pattern: D-R-G-H-[QLIM]-x(3)-[AG]
                    [H is the active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: 1.

-Expert(s) to contact by email:
           Friedhoff P.; friedhoff@mpasmb.desy.de

-Last update: July 1999 / Pattern and text revised.

[ 1] Friedhoof P., Gimadutdinow O., Pingoud A.
     "Identification of catalytically relevant amino acids of the
     extracellular Serratia marcescens endonuclease by alignment-guided
     mutagenesis."
     Nucleic Acids Res. 22:3280-3287(1994).
     PubMed=8078761;

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