InterPro : IPR004473

Name  Restriction endonuclease, type I, HsdR Short Name  Restrct_endonuc_typeI_HsdR
Type  Family Description  There are four classes of restriction endonucleases: types I, II,III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. They differ in their recognition sequence, subunit composition, cleavage position, and cofactor requirements [, ], as summarised below:Type I enzymes () cleave at sites remote from recognition site; require both ATP and S-adenosyl-L-methionine to function; multifunctional protein with both restriction and methylase () activities.Type II enzymes () cleave within or at short specific distances from recognition site; most require magnesium; single function (restriction) enzymes independent of methylase.Type III enzymes () cleave at sites a short distance from recognition site; require ATP (but doesn't hydrolyse it); S-adenosyl-L-methionine stimulates reaction but is not required; exists as part of a complex with a modification methylase methylase ().Type IV enzymes target methylated DNA.Type I restriction endonucleases are components of prokaryotic DNA restriction-modification mechanisms that protects the organism against invading foreign DNA. Type I enzymes have three different subunits subunits - M (modification), S (specificity) and R (restriction) - that form multifunctional enzymes with restriction (), methylase () and ATPase activities [, ]. The S subunit is required for both restriction and modification and is responsible for recognition of the DNA sequence specific for the system. The M subunit is necessary for modification, and the R subunit is required for restriction. These enzymes use S-Adenosyl-L-methionine (AdoMet) as the methyl group donor in the methylation reaction, and have a requirement for ATP. They recognise asymmetric DNA sequences split into two domains of specific sequence, one 3-4 bp long and another 4-5 bp long, separated by a nonspecific spacer 6-8 bp in length. Cleavage occurs a considerable distance from the recognition sites, rarely less than 400 bp away and up to 7000 bp away. Adenosyl residues are methylated, one on each strand of the recognition sequence. These enzymes are widespread in eubacteria and archaea. In enteric bacteria they have been subdivide into four families: types IA, IB, IC and ID.This entry represents the R subunit (HsdR) of type I restriction endonucleases. The R protein (HsdR) is required for both nuclease and ATPase activity [, , ]. Members of this family are assumed to differ from each other in DNA site specificity.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

2 Contains

Id Name Short Name Type
IPR014001 Helicase superfamily 1/2, ATP-binding domain Helicase_ATP-bd Domain
IPR007409 Restriction endonuclease, type I, HsdR, N-terminal Restrct_endonuc_type1_HsdR_N Domain

0 Found In

0 Parent Features

6 Publications

First Author Title Year Journal Volume Pages
Sistla S S-Adenosyl-L-methionine-dependent restriction enzymes. 2004 Crit Rev Biochem Mol Biol 39 1-19
Bourniquel AA Complex restriction enzymes: NTP-driven molecular motors. 2002 Biochimie 84 1047-59
Williams RJ Restriction endonucleases: classification, properties, and applications. 2003 Mol Biotechnol 23 225-43
Piekarowicz A Analysis of type I restriction modification systems in the Neisseriaceae: genetic organization and properties of the gene products. 2001 Mol Microbiol 41 1199-210
Makovets S Regulation of endonuclease activity by proteolysis prevents breakage of unmodified bacterial chromosomes by type I restriction enzymes. 1999 Proc Natl Acad Sci U S A 96 9757-62
Murray NE Conservation of motifs within the unusually variable polypeptide sequences of type I restriction and modification enzymes. 1993 Mol Microbiol 9 133-43

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)