Old_exonuclease

Contributors: Marian Dominguez-Mirazo

Description

The OLD proteins are a family of nucleases present in bacteria, archaea, and viruses (N/A) . The OLD protein found in the P2 E.coli prophage is the best characterized one. The protein is an exonuclease that digests dsDNA in the 5' to 3' direction (N/A) . It also has nuclease activity against single-stranded DNA and RNA (N/A) . It's been shown to protect against phage lambda (N/A) , and when cloned with the P2 Tin accessory gene, it was shown to protect against other E. coli phages (N/A) . The protein also contains an ATPase domain that affects nuclease activity (N/A) . Inhibition of the RecBCD complex activates the OLD nuclease (N/A) . OLD proteins are divided into two classes based on amino acid sequence conservation and gene neighborhood (N/A) . The P2-associated protein belongs to class 2 (N/A) .

Molecular Mechanisms

The old_exonuclease is dsDNA exonuclease that digests in the 5' to 3' direction (N/A) . To our knowledge, other aspects of the molecular mechanisms remain unknown.

Example of genomic structure

The Old_exonuclease is composed of 1 protein: Old_exonuclease.

Here is an example found in the RefSeq database:

old_exonuclease

The Old_exonuclease system in Shewanella xiamenensis (GCF_022453805.1, NZ_CP092630) is composed of 1 protein: Old_exonuclease (WP_240293412.1)

Distribution of the system among prokaryotes

Structure

Experimental validation