Literature summary for 3.1.13.1 extracted from

Amblar, M.; Barbas, A.; Gomez-Puertas, P.; Arraiano, C.M.
The role of the S1 domain in exoribonucleolytic activity: substrate specificity and multimerization (2007), RNA, 13, 317-327.

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Protein Variants

Protein Variants	Comment	Organism
additional information	hybrid proteins are constructed by replacing the S1 domain of RNase II for the S1 from RNase R and PNPase, and their exonucleolytic activity and RNA-binding ability are examined. Both the S1 domains of RNase R and PNPase are able to partially reverse the drop of RNA-binding ability and exonucleolytic activity resulting from removal of the S1 domain of RNase II. The S1 domains investigated are not equivalent	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P30850	-	-

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Release 2023.1 (January 2023)