Protein Family Models

This entry represents the central domain found in archaeal proteins such as DNA double-strand break repair helicase HerA (EC:3.6.4.12). HerA is a helicase which is able to utilise either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding [1]. It forms a complex with NurA nuclease, this complex has the 5'-3' DNA end resection activity and is essential for cell viability in the crenarchaeon Sulfolobus islandicus [2]. This domain includes the the central RecA-like catalytic core and a flanking four-helix bundle [3]. The function of this prokaryotic domain is unknown. It contains several conserved aspartates and histidines that could be metal ligands. [1]. 14990749. A bipolar DNA helicase gene, herA, clusters with rad50, mre11 and nurA genes in thermophilic archaea. Constantinesco F, Forterre P, Koonin EV, Aravind L, Elie C;. Nucleic Acids Res. 2004;32:1439-1447. [2]. 25880130. Efficient 5'-3' DNA end resection by HerA and NurA is essential for cell viability in the crenarchaeon Sulfolobus islandicus. Huang Q, Liu L, Liu J, Ni J, She Q, Shen Y;. BMC Mol Biol. 2015;16:2. [3]. 25420454. Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea. Rzechorzek NJ, Blackwood JK, Bray SM, Maman JD, Pellegrini L, Robinson NP;. Nat Commun. 2014;5:5506. (from Pfam)

Date:

2024-10-16

ATP-binding protein containing HAS-barrel and ATPase domains may function as an ATPase; similar to Methanocaldococcus jannaschii DNA double-strand break repair helicase HerA

Date:

2024-11-21