Structural highlights
Function
[RFC1_HUMAN] The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. This subunit binds to the primer-template junction. Binds the PO-B transcription element as well as other GA rich DNA sequences. Could play a role in DNA transcription regulation as well as DNA replication and/or repair. Can bind single- or double-stranded DNA.[1] Interacts with C-terminus of PCNA. 5' phosphate residue is required for binding of the N-terminal DNA-binding domain to duplex DNA, suggesting a role in recognition of non-primer template DNA structures during replication and/or repair.[2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Mossi R, Jonsson ZO, Allen BL, Hardin SH, Hubscher U. Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen. J Biol Chem. 1997 Jan 17;272(3):1769-76. PMID:8999859
- ↑ Mossi R, Jonsson ZO, Allen BL, Hardin SH, Hubscher U. Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen. J Biol Chem. 1997 Jan 17;272(3):1769-76. PMID:8999859
