Protein Family Models

DNA polymerase III subunit delta' is part of the beta sliding clamp loading complex, which hydrolyses ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex [1,2]. It consists of three domains, of which the N-terminal domain contains a nonfunctional nucleotide binding site. This entry represents the lid domain (or domain 2 in [1]). Paper describing PDB structure 1a5t. [1]. 9363942. Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III. Guenther B, Onrust R, Sali A, O'Donnell M, Kuriyan J;. Cell. 1997;91:335-345. Paper describing PDB structure 1jr3. [2]. 11525729. Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III. Jeruzalmi D, O'Donnell M, Kuriyan J;. Cell. 2001;106:429-441. (from Pfam)

Date:

2024-10-16

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)

Date:

2024-10-16

Members of this family, which are predominantly found in prokaryotic DNA polymerase III, assume an alpha helical structure, with a core of five alpha helices, and an additional small helix. They are essential for the formation of the polymerase clamp loader [1]. [1]. 9363942. Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III. Guenther B, Onrust R, Sali A, O'Donnell M, Kuriyan J;. Cell. 1997;91:335-345. (from Pfam)

Date:

2024-10-16

DNA polymerase III subunit delta' interacts with the delta and gamma subunits and is part of the clamp-loading complex, which assembles the beta processivity factor onto the primer template and plays a central role in the organization and communication at the replication fork

Date:

2017-05-22

Catalyzes the DNA-template-directed extension of the 3'-end of a DNA strand; the delta' subunit seems to interact with the gamma subunit to transfer the beta subunit on the DNA

Gene:

holB

Date:

2021-09-10

This model describes the N-terminal half of the delta' subunit of DNA polymerase III. Delta' is homologous to the gamma and tau subunits, which form an outgroup for phylogenetic comparison. The gamma/tau branch of the tree is much more tighly conserved than the delta' branch, and some members of that branch score more highly against this model than some proteins classisified as delta'. The noise cutoff is set to detect weakly scoring delta' subunits rather than to exclude gamma/tau subunits. At position 126-127 of the seed alignment, this family lacks the HM motif of gamma/tau; at 132 it has a near-invariant A vs. an invariant F in gamma/tau.

Gene:

holB

Date:

2024-06-04