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InterPro: IPR002941 DNA methylase N-4/N-6

Protein matchesHelp
UniProtKB
Matches:
2781 proteins
AccessionHelp IPR002941 DNA_methylase_N4/N6
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR001091 Site-specific DNA-methyltransferase (cytosine-N4-specific)
Contains IPR017985 DNA methylase, N-4 cytosine-specific, conserved site
GO Term annotationHelp
Process GO:0006306 DNA methylation
Function GO:0003677 DNA binding
GO:0008170 N-methyltransferase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This domain is found in DNA methylases. In prokaryotes, the major role of DNA methylation is to protect host DNA against degradation by restriction enzymes. This family contains both N-4 cytosine-specific DNA methylases and N-6 Adenine-specific DNA methylases. N-4 cytosine-specific DNA methylases (EC:2.1.1.113) [1] are enzymes that specifically methylate the amino group at the C-4 position of cytosines in DNA. Such enzymes are found as components of type II restriction-modification systems in prokaryotes. Such enzymes recognise a specific sequence in DNA and methylate a cytosine in that sequence. By this action they protect DNA from cleavage by type II restriction enzymes that recognise the same sequence. N-6 adenine-specific DNA methylases (EC:2.1.1.72) (A-Mtase) are enzymes that specifically methylate the amino group at the C-6 position of adenines in DNA. Such enzymes are found in the three existing types of bacterial restriction-modification systems (in type I system the A-Mtase is the product of the hsdM gene, and in type III it is the product of the mod gene). All of these enzymes recognise a specific sequence in DNA and methylate an adenine in that sequence.

Structural linksHelp
SCOP: c.66.1.11
CATH: 3.40.50.150
Database linksHelp
Enzyme: EC:2.1.1
PANDIT: PF01555
Blocks: IPB002941
Pfam Clan: CL0102.19

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR002941 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O59647 Modification methylase MwoI

P08763 Type III restriction-modification system EcoPI enzyme mod

P11409 Modification methylase PvuII

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR017985 DNA methylase, N-4 cytosine-specific, conserved site
IPR002941 DNA methylase N-4/N-6
IPR002295 N6 adenine-specific DNA methyltransferase, D21 class
IPR002052 DNA methylase, N-6 adenine-specific, conserved site
IPR001091 Site-specific DNA-methyltransferase (cytosine-N4-specific)
SWISS-MODEL
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp
1. Timinskas A, Butkus V, Janulaitis A.
Sequence motifs characteristic for DNA [cytosine-N4] and DNA [adenine-N6] methyltransferases. Classification of all DNA methyltransferases.
Gene 157 3-11 1995 [PubMed: 7607512]
http://dx.doi.org/10.1016/0378-1119(94)00783-O

Additional ReadingHelp
Osipiuk J, Walsh MA, Joachimiak A.
Crystal structure of MboIIA methyltransferase.
Nucleic Acids Res. 31 2003 5440-8 [PubMed: 12954781]
http://dx.doi.org/10.1093/nar/gkg713
Thomas CB, Scavetta RD, Gumport RI, Churchill ME.
Structures of liganded and unliganded RsrI N6-adenine DNA methyltransferase: a distinct orientation for active cofactor binding.
J. Biol. Chem. 278 2003 26094-101 [PubMed: 12732637]
http://dx.doi.org/10.1074/jbc.M303751200
Gong W, O'Gara M, Blumenthal RM, Cheng X.
Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment.
Nucleic Acids Res. 25 1997 2702-15 [PubMed: 9207015]
http://dx.doi.org/10.1093/nar/25.14.2702
Scavetta RD, Thomas CB, Walsh MA, Szegedi S, Joachimiak A, Gumport RI, Churchill ME.
Structure of RsrI methyltransferase, a member of the N6-adenine beta class of DNA methyltransferases.
Nucleic Acids Res. 28 2000 3950-61 [PubMed: 11024175]
http://dx.doi.org/10.1093/nar/28.20.3950
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InterPro 23.1