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InterPro: IPR003356 DNA methylase, adenine-specific
Protein matches
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UniProtKB Matches: 2575 proteins |
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Accession
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IPR003356 DNA_methylase_A-5 |
Type
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Domain |
Signatures
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InterPro Relationships
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Found in
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IPR002296 N6 adenine-specific DNA methyltransferase, N12 class
IPR004546 Restriction endonuclease, type I, EcoRI, M subunit
IPR016843 S-adenosyl-L-methionine dependent adenine methyltransferase, bacteria, predicted
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GO Term annotation
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Process
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GO:0006306 DNA methylation
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Function
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GO:0003677 DNA binding
GO:0008170 N-methyltransferase activity
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InterPro annotation
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Entry Details in BioMart
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Abstract
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This domain is fpound in N-6 adenine-specific DNA methylase (EC:2.1.1.72) from Type I and Type IC restriction systems.
These enzymes are responsible for the methylation of specific DNA sequences in order to prevent the host from digesting its own genome via its restriction enzymes. These methylases have the same sequence specificity as their corresponding restriction enzymes. The type I restriction and modification system is composed of three polypeptides R, M and S. The M and S subunits together form a methyltransferase that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit, the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance methyltransferase, modifying the DNA so that both strands become methylated.
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Structural links
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Database links
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Pfam Clan: CL0102.19
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Additional Reading
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Schouler C, Clier F, Lerayer AL, Ehrlich SD, Chopin MC.
A type IC restriction-modification system in Lactococcus lactis.
J. Bacteriol. 180 1998 407-11
[PubMed: 9440532]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=9440532&action=stream&blobtype=pdf
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Thorpe PH, Ternent D, Murray NE.
The specificity of sty SKI, a type I restriction enzyme, implies a structure with rotational symmetry.
Nucleic Acids Res. 25 1997 1694-700
[PubMed: 9108149]
http://dx.doi.org/10.1093/nar/25.9.1694
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Schouler C, Gautier M, Ehrlich SD, Chopin MC.
Combinational variation of restriction modification specificities in Lactococcus lactis.
Mol. Microbiol. 28 1998 169-78
[PubMed: 9593305]
http://dx.doi.org/10.1046/j.1365-2958.1998.00787.x
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InterPro 23.1
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