PROSITE documentation PDOC51737 [for PROSITE entry PS51737]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.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Rutherford K. Yuan P. Perry K. Sharp R. Van Duyne G.D. |
| Title | Attachment site recognition and regulation of directionality by the serine integrases. | |
| Source | Nucleic Acids Res. 41:8341-8356(2013). | |
| PubMed ID | 23821671 | |
| DOI | 10.1093/nar/gkt580 |
| 2 | Authors | Van Duyne G.D. Rutherford K. |
| Title | Large serine recombinase domain structure and attachment site binding. | |
| Source | Crit. Rev. Biochem. Mol. Biol. 48:476-491(2013). | |
| PubMed ID | 23980849 | |
| DOI | 10.3109/10409238.2013.831807 |
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