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Links from Protein

Items: 5

1.

Eco57I restriction-modification methylase domain-containing protein

Homologues of the Escherichia coli Eco57I restriction-modification methylase are found in several phylogenetically diverse bacteria. The structure of TaqI has been solved [1]. [1]. 1334261. Cloning and sequence analysis of the genes coding for Eco57I. type IV restriction-modification enzymes.. Janulaitis A, Vaisvila R, Timinskas A, Klimasauskas S, Butkus V;. Nucleic Acids Res 1992;20:6051-6056.. [2]. 8995524. Differential binding of S-adenosylmethionine. S-adenosylhomocysteine and Sinefungin to the adenine-specific. DNA methyltransferase M.TaqI.. Schluckebier G, Kozak M, Bleimling N, Weinhold E, Saenger W;. J Mol Biol. 1997;265:56-67. (from Pfam)

GO Terms:
Molecular Function:
DNA binding (GO:0003677)
Molecular Function:
catalytic activity (GO:0003824)
Biological Process:
DNA modification (GO:0006304)
Date:
2024-08-14
Family Accession:
NF019291.5
Method:
HMM
2.

N-6 DNA methylase

Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The R-M system is a complex containing three polypeptides: M (this family), S (Pfam:PF01420), and R [1]. This family consists of N-6 adenine-specific DNA methylase EC:2.1.1.72 from Type I and Type IC restriction systems. These methylases have the same sequence specificity as their corresponding restriction enzymes. [1]. 9440532. A type IC restriction-modification system in Lactococcus lactis.. Schouler C, Clier F, Lerayer AL, Ehrlich SD, Chopin MC;. J Bacteriol 1998;180:407-411.. [2]. 9593305. Combinational variation of restriction modification. specificities in Lactococcus lactis.. Schouler C, Gautier M, Ehrlich SD, Chopin MC;. Mol Microbiol 1998;28:169-178.. [3]. 9108149. The specificity of sty SKI, a type I restriction enzyme, implies. a structure with rotational symmetry.. Thorpe PH, Ternent D, Murray NE;. Nucleic Acids Res 1997;25:1694-1700. (from Pfam)

GO Terms:
Molecular Function:
DNA binding (GO:0003677)
Molecular Function:
N-methyltransferase activity (GO:0008170)
Date:
2024-08-14
Family Accession:
NF014442.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.

class I SAM-dependent DNA methyltransferase

class I SAM-dependent DNA methyltransferase catalyzes the methylation of a specific DNA substrate using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor similar to type I restriction-modification system modification (M) subunit (HsdM), which together with specificity (S) subunit (HsdS), forms a methyltransferase that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence

Date:
2022-08-10
Family Accession:
11416313
Method:
Sparcle
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