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phage integrase N-terminal SAM-like domain-containing protein
tyrosine-type recombinase/integrase
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)
site-specific integrase
tyrosine based site-specific recombinase (integrase) is involved in cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct
class 1 integron integrase IntI1
integron integrase
Members of this family are integrases associated with integrons (and super-integrons), which are systems for incorporating and expressing cassettes of laterally transferred DNA. Incorporation occurs at an attI site. A super-integron, as in Vibrio sp., may include over 100 cassettes. This family belongs to the phage integrase family (PF00589) that also includes recombinases XerC (TIGR02224) and XerD (TIGR02225), which are bacterial housekeeping proteins. Within this family of integron integrases, some are designated by class, e.g. IntI4, a class 4 integron integrase from Vibrio cholerae N16961.
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