v5.1.0.3
Cicer data from the Legume Information System
| Type | Homologous_superfamily |
| Description | Primosomal protein N', also known as ATP-dependent helicase PriA, is a component of the primosome, involved in replication, repair and recombination. PriA is a multifunctional enzyme that mediates the essential process of restarting prematurely terminated DNA replication reactions in bacteria [ , ]. PriA presents a two-domain architecture, with an N-terminal DNA-binding domain (DBD) and a C-terminal helicase domain (HD). Structural studies reveal a central helicase core surrounded by an array of DNA-binding elements. These elements include two domains within the DBD, a 3' DNA-binding domain (3'BD) and an unusual circularly permuted winged helix (WH) domain, and two domains within the HD, a Cys-rich region (CRR) that binds two Zn2+ ions and a C-terminal domain (CTD) which shows unexpected similarity to the S10 subunit of the bacterial ribosome [].This superfamily represents the 3' DNA binding domain. |
| Short Name | PriA_3primeBD_sf |