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AAA family ATPase
Replication factor C C-terminal domain
This is the C-terminal domain of RFC (replication factor-C) protein of the clamp loader complex which binds to the DNA sliding clamp (proliferating cell nuclear antigen, PCNA). The five modules of RFC assemble into a right-handed spiral, which results in only three of the five RFC subunits (RFC-A, RFC-B and RFC-C) making contact with PCNA, leaving a wedge-shaped gap between RFC-E and the PCNA clamp-loader complex. The C-terminal is vital for the correct orientation of RFC-E with respect to RFC-A [1]. [1]. 15201901. Structural analysis of a eukaryotic sliding DNA clamp-clamp. loader complex.. Bowman GD, O'Donnell M, Kuriyan J;. Nature. 2004;429:724-730. (from Pfam)
DNA polymerase III, delta subunit
DNA polymerase III, delta subunit (EC 2.7.7.7) is required for, along with delta' subunit, the assembly of the processivity factor beta(2) onto primed DNA in the DNA polymerase III holoenzyme-catalysed reaction [1]. The delta subunit is also known as HolA. [1]. 11432857. The delta and delta ' subunits of the DNA polymerase III. holoenzyme are essential for initiation complex formation and. processive elongation.. Song MS, Pham PT, Olson M, Carter JR, Franden MA, Schaaper RM,. McHenry CS;. J Biol Chem 2001;276:35165-35175. (from Pfam)
AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2]. [1]. 7646486. A 200-amino acid ATPase module in search of a basic function.. Confalonieri F, Duguet M;. Bioessays 1995;17:639-650.. A large extension of the family. [2]. 9927482. AAA+: A class of chaperone-like ATPases associated with the. assembly, operation, and disassembly of protein complexes.. Neuwald AF, Aravind L, Spouge JL, Koonin EV;. Genome Res 1999;9:27-43. (from Pfam)
AAA family ATPase containing an AAA (ATPases Associated with various cellular Activities) domain, may function as an ATP-dependent endonuclease or the ATPase component of an ABC-type transporter
replication factor C small subunit 2
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