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InterPro: IPR001091 Site-specific DNA-methyltransferase (cytosine-N4-specific)

Protein matchesHelp
UniProtKB
Matches:
1768 proteins
AccessionHelp IPR001091 MeTrfase_CN4
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR002941 DNA methylase N-4/N-6
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

Synonym(s): N-4 cytosine-specific DNA methylase, Modification methylase

Site-specific DNA-methyltransferase (cytosine-N4-specific) (EC:2.1.1.113) are enzymes that specifically methylate the amino group at the C-4 position of cytosines in DNA. In prokaryotes, the major role of DNA methylation is to protect host DNA against degradation by restriction enzymes. There are two major classes of DNA methyltransferase that differ in the nature of the modifications they effect. The members of one class (C-MTases) methylate a ring carbon and form C5-methylcytosine and members of the second class (N-MTases) methylate exocyclic nitrogens and form either N4-methylcytosine (N4-MTases) or N6-methyladenine (N6-MTases). Both classes of MTase utilise the cofactor S-adenosyl-L-methionine (SAM) as the methyl donor and are active as monomeric enzymes [1].

Structural linksHelp
SCOP: c.66.1.11
CATH: 3.40.50.150
Database linksHelp
PDBe-motif: PS00093
Enzyme: EC:2.1.1
PROSITE doc: PDOC00088
Blocks: IPB001091

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001091 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O59647 Modification methylase MwoI

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
IPR001091 Site-specific DNA-methyltransferase (cytosine-N4-specific)
SWISS-MODEL
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp
1. Cheng X.
Structure and function of DNA methyltransferases.
24 293-318 1995 [PubMed: 7663118]
http://dx.doi.org/10.1146/annurev.bb.24.060195.001453

Additional ReadingHelp
Willcock DF, Dryden DT, Murray NE.
A mutational analysis of the two motifs common to adenine methyltransferases.
EMBO J. 13 1994 3902-8 [PubMed: 8070417]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=8070417&action=stream&blobtype=pdf
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 1995 3-11 [PubMed: 7607512]
http://dx.doi.org/10.1016/0378-1119(94)00783-O
Labahn J, Granzin J, Schluckebier G, Robinson DP, Jack WE, Schildkraut I, Saenger W.
Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine.
Proc. Natl. Acad. Sci. U.S.A. 91 1994 10957-61 [PubMed: 7971991]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7971991&action=stream&blobtype=pdf
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
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
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InterPro 23.1