Pathways & interactions
Resolvase, N-terminal catalytic domain (IPR006119)
Short name: Resolv_N
Overlapping homologous superfamilies
- Resolvase, N-terminal catalytic domain (IPR006119)
- IS607-like transposase, catalytic domain (IPR041718)
Site-specific recombination plays an important role in DNA rearrangement in prokaryotic organisms. Two types of site-specific recombination are known to occur:
- Recombination between inverted repeats resulting in the reversal of a DNA segment.
- Recombination between repeat sequences on two DNA molecules resulting in their cointegration, or between repeats on one DNA molecule resulting in the excision of a DNA fragment.
Site-specific recombination is characterised by a strand exchange mechanism that requires no DNA synthesis or high energy cofactor; the phosphodiester bond energy is conserved in a phospho-protein linkage during strand cleavage and re-ligation.
Two unrelated families of recombinases are currently known [PMID: 3011407]. The first, called the 'phage integrase' family, groups a number of bacterial phage and yeast plasmid enzymes. The second [PMID: 2896291], called the 'resolvase' family, groups enzymes which share the following structural characteristics: an N-terminal catalytic and dimerization domain that contains a conserved serine residue involved in the transient covalent attachment to DNA, and a C-terminal helix-turn-helix DNA-binding domain (IPR006120).
The N-terminal resolvase/invertase-type recombinase catalytic domain has an alpha/beta fold and consists of a five-stranded mixed beta-sheet surrounded by three alpha helices on one side and one helix on the other [PMID: 7628011].