Literature summary for 3.1.21.5 extracted from

Wagenfuehr, K.; Pieper, S.; Mackeldanz, P.; Linscheid, M.; Krueger, D.H.; Reuter, M.
Structural domains in the type III restriction endonuclease EcoP15I: characterization by limited proteolysis, mass spectrometry and insertional mutagenesis (2007), J. Mol. Biol., 366, 93-102.

Search for more literature for 3.1.21.5

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
additional information	study on the predicted linker region between the two domains of the restriction subunit by insertional mutagenesis. Introduction of up to 18 amino acids in the N- and C-terminal region of the linker. The region tolerated the introduced genetic alterations without loss of catalytic function or changes in cleavage position	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	isoform EcoP15I	-

Subunits

Subunits	Comment	Organism
More	in the presence of specific DNA, the entire modification subunit of the enzyme is protected from trypsin digestion, whereas in the absence of DNA stable protein domains of the modification subunit are not detected. In contrast, the restriction subunit is comprised of two trypsin-resistant domains of about 77000-79000 Da and 27000-29000 Da, respectively. Both structural restriction domains are connected by a flexible linker region that spans 23 amino acid residues	Escherichia coli

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Release 2023.1 (January 2023)