EC Number   |
Natural Substrates |
|---|
   5.6.2.3 | ATP + H2O |
- |
| 5.6.2.3 | ATP + H2O |
5' to 3' DNA helicase. ATPase/helicase activity of Pfh1p is essential. Maintenance of telomeric DNA is not the sole essential function of Pfh1p. Although mutant spores depleted for Pfh1p proceed through S phase, they arrest with a terminal cellular phenotype consistent with a postinitiation defect in DNA replication. Telomeric DNA is modestly shortened in the absence of Pfh1p |
| 5.6.2.3 | ATP + H2O |
5' to 3' DNA helicase. The ATPase/helicase activity of Rrm3p is required for its role in telomeric and subtelomeric DNA replication. Because Rrm3p is telomere-associated in vivo, it likely has a direct role in telomere replication |
| 5.6.2.3 | ATP + H2O |
PcrA is a chromosomally encoded DNA helicase of gram-positive bacteria involved in replication of rolling circle replicating plasmids |
| 5.6.2.3 | ATP + H2O |
TWINKLE is the helicase at the mitochondrial DNA replication fork |
| 5.6.2.3 | ATP + H2O |
can unwind a bubble substrate consistent with a role in nucleotide excision repair |
| 5.6.2.3 | ATP + H2O |
the archaeal Rad50-Mre11 complex might act in association with a 5' to 3' exonuclease (NurA) and a bipolar DNA helicase indicating a probable involvement in the initiation step of homologous recombination |
| 5.6.2.3 | ATP + H2O |
the enzyme physically interacts with StoHjc, the Holliday junction-specific endonuclease from Sulfolobus tokodaii. The unwinding activity of the helicase (StoHjm) is inhibited by StoHjc in vitro. These results may suggest that the Hjm/Hel308 family helicases, in association with Hjc endonucleases, are involved in processing of stalled replication forks |
| 5.6.2.3 | ATP + H2O |
the Hjm protein is essential for cell viability. The StoHjc protein regulates the helicase activity of StoHjm by inducing conformation change of the enzyme. Hjm/Hjc mediated resolution of stalled replication forks is of crucial importance in archaea. A tentative pathway with which Hjm/Hjc interaction could have occurred at stalled replication forks is discussed |
| 5.6.2.3 | more |
HDHB interacts with the N-terminal domain of replication protein A 70-kDa subunit |
