The domain within your query sequence starts at position 666 and ends at position 896; the E-value for the NUC domain shown below is 1.32e-109.

WARNING!
Some of the required catalytic sites were not detected in this domain. It is probably inactive! Check the literature (PubMed 9257723 ) for details.

Catalytic residues
PositionAmino acidPresent?
DomainProtein
63728DNo
66731HNo
103768ENo
HTDFESGYSEIFLMPLWTSYTISKQAEVSSIPEHLTNCVRPDVRVSPGFSQNCLAYKNDK
QMSYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWTYFQRVLVKKYASERNGVNVI
SGPIFDYNYNGLRDIEDEIKQYVEGSSIPVPTHYYSIITSCLDFTQPADKCDGPLSVSSF
ILPHRPDNDESCNSSEDESKWVEELMKMHTARVRDIEHLTGLDFYRKTSRS

NUC

DNA/RNA non-specific endonuclease
NUC
SMART accession number:SM00477
Description: prokaryotic and eukaryotic double- and single-stranded DNA and RNA endonucleases also present in phosphodiesterases
Interpro abstract (IPR020821): 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-stranded nucleic acids and require a divalent ion such as magnesium for their activity. A histidine has been shown [(PUBMED:8078761)] 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.
GO function:metal ion binding (GO:0046872), nucleic acid binding (GO:0003676), hydrolase activity (GO:0016787)
Family alignment:
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There are 11868 NUC domains in 11849 proteins in SMART's nrdb database.

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