EC Number   |
General Information |
Reference |
|---|
   3.6.4.B8 | evolution |
most archaeal genomes also encode two RFC homologs, designated the RFC large (RFC-L) and small (RFC-S) subunits, that assemble to form a pentameric complex that contains one RFC-L and four RFC-S subunits |
-, 733807 |
| 3.6.4.B8 | evolution |
the clamp loader complex is a member of the AAA+ family of ATPases (adenosine 5'-triphosphatases) |
758480 |
| 3.6.4.B8 | evolution |
the enzyme complex belongs to the AAA+ ATPase family. The complex is composed of an ORC1/4/5 motor module lobe in an organization reminiscent of the DNA polymerase clamp loader complexes. The structure of HsORC reveals a remarkable similarity between two very different ATPases: the replication initiator ORC-CDC6 ATPase and the replication fork DNA polymerase clamp loader. Both ATPases function at different times during genome replication but load ring-shaped proteins onto double-stranded DNA so that the ring-shaped proteins become topologically linked to the DNA double helix. The ATPase motor module of HsORC is very reminiscent of the DNA polymerase clamp loader complexes such as replication factor C (RFC) in eukaryotes, the bacterial gamma-complex, and the T4 bacteriophage Gene44 clamp loader |
756573 |
| 3.6.4.B8 | evolution |
three RFC1 paralogues - RAD17, CTF18 (chromosome transmission fidelity 18), and ELG1 (enhanced level of genome instability 1, in human also called ATAD5, ATPase family, AAA domain containing 5 or FRAG1, FGF receptor activating protein 1) - have been identified in eukaryotes. Furthermore, three proteins that share significant amino acid sequence similarities with PCNA (RAD9, RAD1, and HUS1) are necessary for the checkpoint-response pathway, along with RAD17-RFC |
755750 |
| 3.6.4.B8 | malfunction |
ORC molecular defects are observed in Meier-Gorlin syndrome mutations |
756573 |
| 3.6.4.B8 | metabolism |
Poldelta alone can only incorporate several nucleotides at the primer end, whereas in the presence of proliferating cell nuclear antigen (PCNA), it can produce DNA strands longer than 200-300 nucleotides. The PCNA-RFC-Poldelta system can efficiently fill DNA gaps from short patches to lagging-strand sizes |
755750 |
| 3.6.4.B8 | metabolism |
Poldelta alone can only incorporate several nucleotides at the primer end, whereas in the presence of proliferating cell nuclear antigen (PCNA), it can produce DNA strands longer than 200-300 nucleotides. The PCNA-RFC-Poldelta system can efficiently fill DNA gaps from short patches to lagging-strand sizes. Physiological functions and dynamics of proliferating-cell-nuclear-antigen (PCNA), overview |
755750 |
| 3.6.4.B8 | more |
determination and analysis of the structure of human ORC (HsORC motor module) in a functionally active, ATP-hydrolysis ready state, providing insight into ATP-dependent protein loading as well as DNA and CDC6 binding, structure-function relationship, overview. In the context of the motor module, only the ORC1/4 interface is a functional ATPase. Binding of ORC2-ORC3 modulates the ATPase activity of the ORC motor |
756573 |
| 3.6.4.B8 | more |
Escherichia coli clamp loader complex is comprised of seven subunits, each of these has critical roles in the function of the clamp loader. Determination and analysis of the solution structure of the complete seven subunit clamp loader complex using small angle X-ray scattering, model of the dynamic nature of the clamp loader complex, overview |
758480 |
| 3.6.4.B8 | more |
mechanism of primary PCNA and 9-1-1 loading and unloading by RFC and homologues, secondary PCNA loading by CTF18-RFC, unloading by ELG1-RFC, detailed overview. DNA-sequence-specific PCNA loading occurs via interaction of RFC with a sequence-specific DNA-binding protein |
755750 |
