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recombinase family protein
recombinase family protein is a serine recombinase that catalyzes the site-specific recombination of DNA molecules by a concerted, four-strand cleavage and rejoining mechanism which involves a transient phosphoserine linkage between DNA and the enzyme
helix-turn-helix domain-containing protein
This helix-turn-helix domain is often found in transferases and is likely to be DNA-binding. (from Pfam)
This helix-turn-helix domain is often found in transposases and is likely to be DNA-binding. (from Pfam)
The N-terminal domain of the resolvase family (this family) contains the active site and the dimer interface. The extended arm at the C-terminus of this domain connects to the C-terminal helix-turn-helix domain of resolvase - see Pfam:PF02796. [1]. 7628011. Crystal structure of the site-specific recombinase gamma delta resolvase complexed with a 34 bp cleavage site. Yang W, Steitz TA;. Cell 1995;82:193-207. (from Pfam)
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