Protein Family Models

The Ku heterodimer (composed of Ku70 Swiss:P12956 and Ku80 Swiss:P13010) contributes to genomic integrity through its ability to bind DNA double-strand breaks and facilitate repair by the non-homologous end-joining pathway. This is the central DNA-binding beta-barrel domain. This domain is found in both the Ku70 Swiss:P12956 and Ku80 Swiss:P13010 proteins that form a DNA binding heterodimer [1]. [1]. 11493912. Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair. Walker JR, Corpina RA, Goldberg J;. Nature 2001;412:607-614. [2]. 11483577. Prokaryotic homologs of the eukaryotic DNA-end-binding protein Ku, novel domains in the Ku protein and prediction of a prokaryotic double-strand break repair system. Aravind L, Koonin EV;. Genome Res 2001;11:1365-1374. (from Pfam)

Date:

2024-10-16

Ku protein, together with LigD, forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity; binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA; recruits and stimulates the ligase activity of LigD

Date:

2024-10-22

Members of this protein family are Ku proteins of non-homologous end joining (NHEJ) DNA repair in bacteria and in at least one member of the archaea (Archaeoglobus fulgidus). Most members are encoded by a gene adjacent to the gene for the DNA ligase that completes the repair. The NHEJ system is broadly but rather sparsely distributed, being present in about one fifth of the first 250 completed prokarytotic genomes. A few species (e.g. Archaeoglobus fulgidus and Bradyrhizobium japonicum) have multiple copies that appear to represent recent paralogous family expansion.

Date:

2021-04-27