Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
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)
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)
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)
RMKL-like, methyltransferase domain
This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains [1]. [1]. 11295541. THUMP - a predicted RNA-binding domain shared by 4-thiouridine,. pseudouridine synthases and RNA methylases.. Aravind L, Koonin EV;. Trends Biochem Sci 2001;26:215-217. (from Pfam)
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on