Protein Family Models

Date:

2024-08-14

This is the C-terminal domain of Type ISP restriction-modification enzyme LLaBIII present in Lactococcus lactis subsp. cremoris. Type ISP restriction-modification (RM) enzymes provide a potent defence against infection by foreign and bacteriophage DNA. This domain interacts extensively with DNA and is known as the target recognition domain (TRD). TRD works by recognising 6/7 base pairs of asymmetric sequence [1]. [1]. 26389736. Translocation-coupled DNA cleavage by the Type ISP. restriction-modification enzymes.. Chand MK, Nirwan N, Diffin FM, van Aelst K, Kulkarni M,. Pernstich C, Szczelkun MD, Saikrishnan K;. Nat Chem Biol. 2015;11:870-877. (from Pfam)

Date:

2024-08-14

Prokaryotic family found in type II restriction enzymes containing the hallmark (D/E)-(D/E)XK active site. Presence of catalytic residues implicates this region in the enzymatic cleavage of DNA [1,2] [1]. 1650347. Characterization and expression of the Escherichia coli Mrr. restriction system.. Waite-Rees PA, Keating CJ, Moran LS, Slatko BE, Hornstra LJ,. Benner JS;. J Bacteriol 1991;173:5207-5219.. [2]. 11313145. Identification of a PD-(D/E)XK-like domain with a novel. configuration of the endonuclease active site in the. methyl-directed restriction enzyme Mrr and its homologs.. Bujnicki JM, Rychlewski L;. Gene 2001;267:183-191. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

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)

Date:

2024-08-14

Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression. [1]. 10322435. Unwinding RNA in Saccharomyces cerevisiae: DEAD-box proteins and. related families.. de la Cruz J, Kressler D, Linder P;. Trends Biochem Sci 1999;24:192-198.. [2]. 9862990. The DEAD box RNA helicase family in Arabidopsis thaliana.. Aubourg S, Kreis M, Lecharny A;. Nucleic Acids Res 1999;27:628-636. (from Pfam)

Date:

2024-08-14

The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase. (from Pfam)

Date:

2024-08-14

DEAD/DEAH box-containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA

Date:

2019-07-15