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 subsequ ...
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.