Protein Family Models

Date:

2024-08-14

Members of this family cleave DNA substrates by a series of staggered cuts, during which the protein becomes covalently linked to the DNA through a catalytic tyrosine residue at the carboxy end of the alignment. The catalytic site residues in CRE recombinase (Swiss:P06956) are Arg-173, His-289, Arg-292 and Tyr-324. [1]. 9082984. Flexibility in DNA recombination: structure of the lambda. integrase catalytic core.. Kwon HJ, Tirumalai R, Landy A, Ellenberger T;. Science 1997;276:126-131.. [2]. 9288963. Structure of Cre recombinase complexed with DNA in a. site-specific recombination synapse.. Guo F, Gopaul DN, van Duyne GD;. Nature 1997;389:40-46. (from Pfam)

Date:

2024-08-14

Date:

2020-10-26

site-specific tyrosine recombinase XerC acts by catalyzing the cutting and rejoining of recombining DNA molecules

Date:

2023-02-23

The phage integrase family describes a number of recombinases with tyrosine active sites that transiently bind covalently to DNA. Many are associated with mobile DNA elements, including phage, transposons, and phase variation loci. This model represents XerC, one of two closely related chromosomal proteins along with XerD (TIGR02225). XerC and XerD are site-specific recombinases which help resolve chromosome dimers to monomers for cell division after DNA replication. In species with a large chromosome and homologs of XerC on other replicons, the chomosomal copy was preferred for building this model. This model does not detect all XerC, as some apparent XerC examples score in the gray zone between trusted (450) and noise (410) cutoffs, along with some XerD examples. XerC and XerD interact with cell division protein FtsK.

Gene:

xerC

Date:

2024-05-17