LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | This entry represents the central DNA-binding core domain of Ku70, which folds as a β-barrel [ ]. Ku70 (also known as XRCC6 in animals), a single-stranded DNA-dependent ATP-dependent helicase, is a subunit of the Ku protein, which plays a key role in multiple nuclear processes such as DNA repair, chromosome maintenance, transcription regulation, DNA non-homologous end joining (NHEJ) and V(D)J recombination [ , , , , , , ].Some findings have implicated yeast Ku in telomeric structure maintenance in addition to non-homologous end-joining. Some of the phenotypes of Ku-knockout mice may indicate a similar role for Ku at mammalian telomeres [ ]. Ku70 also plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway [].Both subunits of the eukaryotic Ku heterodimer (Ku70 and Ku80) share a topology comprised of three domains: an α/β N-terminal, a central β-barrel domain and a helical C-terminal arm [ ]. Structural analysis of the Ku70/80 heterodimer bound to DNA indicates that subunit contacts lead to the formation of a highly charged channel through which the DNA passes without making any contacts with the DNA bases []. |
| Short Name | KU70_core_dom |
