InterPro : IPR019058

Name  Restriction endonuclease, type II, HaeII Short Name  Restrct_endonuc_II_HaeII
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 II restriction endonucleases () are components of prokaryotic DNA restriction-modification mechanisms that protect the organism against invading foreign DNA. These site-specific deoxyribonucleases catalyse the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. Of the 3000 restriction endonucleases that have been characterised, most are homodimeric or tetrameric enzymes that cleave target DNA at sequence-specific sites close to the recognition site. For homodimeric enzymes, the recognition site is usually a palindromic sequence 4-8 bp in length. Most enzymes require magnesium ions as a cofactor for catalysis. Although they can vary in their mode of recognition, many restriction endonucleases share a similar structural core comprising four beta-strands and one alpha-helix, as well as a similar mechanism of cleavage, suggesting a common ancestral origin []. However, there is still considerable diversity amongst restriction endonucleases [, ]. The target site recognition process triggers large conformational changes of the enzyme and the target DNA, leading to the activation of the catalytic centres. Like other DNA binding proteins, restriction enzymes are capable of non-specific DNA binding as well, which is the prerequisite for efficient target site location by facilitated diffusion. Non-specific binding usually does not involve interactions with the bases but only with the DNA backbone []. This family includes Type-2 restriction enzyme NgoBI, and HaeII. They recognise the double-stranded sequence RGCGCY and cleaves after C-5.
 Feedback

Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

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
Williams RJ Restriction endonucleases: classification, properties, and applications. 2003 Mol Biotechnol 23 225-43
Pingoud A Type II restriction endonucleases: structure and mechanism. 2005 Cell Mol Life Sci 62 685-707
Mucke M Diversity of type II restriction endonucleases that require two DNA recognition sites. 2003 Nucleic Acids Res 31 6079-84
Pingoud V Evolutionary relationship between different subgroups of restriction endonucleases. 2002 J Biol Chem 277 14306-14
Pingoud A Structure and function of type II restriction endonucleases. 2001 Nucleic Acids Res 29 3705-27



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)