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@@ -26,18 +26,23 @@ Originally found in a high throughput shotgun cloning of bacterial fragments in
## Molecular mechanisms
from :ref{doi=10.1016/j.molcel.2013.02.002} "The psyrT shares homology with domains of the RecQ helicase,
a family of proteins implicated in DNA repair (Bernstein et al.,
2010); and the antitoxin of the same system, psyrA, has a nucle-
otide binding domain (COG0758) that was previously described
in proteins involved in DNA uptake"
from :ref{10.1016/j.chom.2022.09.017} "Both systems encode an antitoxin
with homology to DprA, a single-stranded DNA (ssDNA)-binding
protein known to be involved in DNA transformation (Mortier-
Barrie
`
re et al., 2007). The toxin contains a phosphoribosyl trans-
ferase (PRTase) domain, which was previously found in effectors
of retron abortive infection systems "
from :ref{doi=10.1016/j.molcel.2013.02.002} :
> The psyrT shares homology with domains of the RecQ helicase,
> a family of proteins implicated in DNA repair (Bernstein et al.,
> 2010); and the antitoxin of the same system, psyrA, has a nucle-
> otide binding domain (COG0758) that was previously described
> in proteins involved in DNA uptake
from :ref{10.1016/j.chom.2022.09.017} :
> Both systems encode an antitoxin
> with homology to DprA, a single-stranded DNA (ssDNA)-binding
> protein known to be involved in DNA transformation (Mortier-
> Barrière et al., 2007). The toxin contains a phosphoribosyl trans-
> ferase (PRTase) domain, which was previously found in effectors
> of retron abortive infection systems "
## Example of genomic structure
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