InterPro domain: IPR027421

DNA polymerase lambda is a repair polymerase that has both DNA polymerase and terminal transferase activities. It has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity [ 1 , 2 ]. Structural modeling suggests that pol lambda contains the palm, fingers, thumb, and lyase domains present in pol beta, as well as an additional N-terminal BRCT domain and a serine-proline-rich linker that are presumably involved in protein-protein interactions [ 3 ].

This superfamily represents the lyase domain of pol lambda which is also known as the 8kDa domain [ 4 , 5 ].

1. Identification of an intrinsic 5'-deoxyribose-5-phosphate lyase activity in human DNA polymerase lambda: a possible role in base excision repair. J. Biol. Chem. 276, 34659-63
2. DNA elongation by the human DNA polymerase lambda polymerase and terminal transferase activities are differentially coordinated by proliferating cell nuclear antigen and replication protein A. J. Biol. Chem. 280, 1971-81
3. Solution structure of the lyase domain of human DNA polymerase lambda. Biochemistry 42, 9564-74
4. The structural basis of the kinetic mechanism of a gap-filling X-family DNA polymerase that binds Mg(2+)-dNTP before binding to DNA. J. Mol. Biol. 417, 179-96
5. Crystal structures of a template-independent DNA polymerase: murine terminal deoxynucleotidyltransferase. EMBO J. 21, 427-39