Protein Domain : IPR004473

Type:  Family Name:  Restriction endonuclease, type I, HsdR
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. Short Name:  Restrct_endonuc_typeI_HsdR

0 Child Features

2 Contains

DB identifier Type Name
IPR014001 Domain Helicase superfamily 1/2, ATP-binding domain
IPR007409 Domain Restriction endonuclease, type I, HsdR, N-terminal

1 Cross References

Identifier
TIGR00348

0 Found In

4 GO Annotations

GO Term Gene Name
GO:0003677 IPR004473
GO:0005524 IPR004473
GO:0009035 IPR004473
GO:0009307 IPR004473

4 Ontology Annotations

GO Term Gene Name
GO:0003677 IPR004473
GO:0005524 IPR004473
GO:0009035 IPR004473
GO:0009307 IPR004473

0 Parent Features

1 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
27596.m000014 B9TB59 PAC:16798776 Ricinus communis 903  

6 Publications

First Author Title Year Journal Volume Pages PubMed ID
            15121719
            12595133
            12665693
            11555298
            10449767
            8412658