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Arm DNA-binding domain-containing protein
This domain is found at the N-terminus of various phage integrases. The domain binds to DNA. (from Pfam)
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)
tyrosine-type recombinase/integrase is a tyrosine based site-specific recombinase (integrase) 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
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