PROSITE documentation PDOC51737
DNA-binding recombinase domain profile


The large serine recombinases (LSRs) are DNA-rearranging enzymes that are members of the serine recombinase or resolvase/invertase superfamily. Most resolvases/invertases have a catalytic domain of ~150 residues at their amino terminus (see <PDOC00334>), followed by a small, helix-turn-helix (HTH) DNA-binding domain. The LSRs share a similar amino-terminal catalytic domain, but have much larger carboxyl-terminal regions that range in size from ~300 residues to ~550 residues. The C-terminal region of the LSRs is comprised of multiple structural domains and is responsible for coordination of unique LSRs activities. The LSR C-terminal region is composed of two structural domains: a mixed α/β DNA-binding "recombinase domain" linked to an unusual DNA-binding zinc ribbon domain [1,2].

The DNA-binding recombinase domain is moderately well conserved among the LSRs and consists of a four stranded β-sheet embedded in a core 4-helix bundle (see <PDB:4KIS>) [1,2].

The profile we developed covers the entire DNA-binding recombinase domain.

Last update:

November 2014 / New entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

RECOMBINASE_DNA_BIND, PS51737; DNA-binding recombinase domain profile  (MATRIX)


1AuthorsRutherford K. Yuan P. Perry K. Sharp R. Van Duyne G.D.
TitleAttachment site recognition and regulation of directionality by the serine integrases.
SourceNucleic Acids Res. 41:8341-8356(2013).
PubMed ID23821671

2AuthorsVan Duyne G.D. Rutherford K.
TitleLarge serine recombinase domain structure and attachment site binding.
SourceCrit. Rev. Biochem. Mol. Biol. 48:476-491(2013).
PubMed ID23980849

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