Protein Family Models for Protein (Select 502374875) - Protein Family Models

Select item 4230961.

type I restriction-modification system subunit M N-terminal domain-containing protein

This domain is found at the N-terminus of the methylase subunit of Type I DNA methyltransferases. This domain family is found in bacteria and archaea, and is typically between 123 and 138 amino acids in length. The family is found in association with Pfam:PF02384. Mutations in this region of EcoKI methyltransferase Swiss:P08957 abolish the normally strong preference of this system for methylating hemimethylated substrate [1]. The structure of this domain has been shown to be all alpha-helical. [1]. 1833555. Mutations that confer de novo activity upon a maintenance. methyltransferase.. Kelleher JE, Daniel AS, Murray NE;. J Mol Biol. 1991;221:431-440. (from Pfam)

Date:: 2024-08-14

Family Accession:: NF023583.5
Method:: HMM

Select item 4182772.

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

Select item 4156093.

methyltransferase

This domain is found in ribosomal RNA small subunit methyltransferase C (eg Swiss:P44453) as well as other methyltransferases (eg Swiss:Q53742). (from Pfam)

GO Terms:

Molecular Function:: methyltransferase activity (GO:0008168)

Date:: 2024-08-14

Family Accession:: NF017026.5
Method:: HMM

Select item 4129224.

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

Select item 3978245.