Protein Family Models

The PcrA/UvrD helicase binds directly to RNA polymerase (RNAP). This entry represents the C-terminal tudor domain that mediates interaction with RNA polymerase [1-5]. Paper describing PDB structure 1pjr. [1]. 8934527. Crystal structure of a DExx box DNA helicase. Subramanya HS, Bird LE, Brannigan JA, Wigley DB;. Nature. 1996;384:379-383. Paper describing PDB structure 1qhh. [2]. 10388562. DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase. Soultanas P, Dillingham MS, Velankar SS, Wigley DB;. J Mol Biol. 1999;290:137-148. Paper describing PDB structure 4c2t. [3]. 24143224. Structural and mechanistic insight into DNA unwinding by Deinococcus radiodurans UvrD. Stelter M, Acajjaoui S, McSweeney S, Timmins J;. PLoS One. 2013;8:e77364. Paper describing PDB structure 5dma. [4]. 28160601. The structure and function of an RNA polymerase interaction domain in the PcrA/UvrD helicase. Sanders K, Lin CL, Smith AJ, Cronin N, Fisher G, Eftychidis V, McGlynn P, Savery NJ, Wigley DB, Dillingham MS;. Nucleic Acids Res. 2017;45:3875-3887. Paper describing PDB structure 6yi2. [5]. 33097771. UvrD helicase-RNA polymerase interactions are governed by UvrD's carboxy-terminal Tudor domain. Kawale AA, Burmann BM;. Commun Biol. 2020;3:607. (from Pfam)

Date:

2024-10-16

This domain is found at the C-terminus of a wide variety of helicase enzymes. This domain has a AAA-like structural fold. (from Pfam)

Date:

2024-08-14

This domain is found at the C-terminus of a wide variety of helicase enzymes. This domain has a AAA-like structural fold. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

The Rep family helicases are composed of four structural domains. The Rep family function as dimers. REP helicases catalyse ATP dependent unwinding of double stranded DNA to single stranded DNA. Swiss:P23478, Swiss:P08394 have large insertions near to the carboxy-terminus relative to other members of the family. Structure of Swiss:P09980. [1]. 9288744. Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Korolev S, Hsieh J, Gauss GH, Lohman TM, Waksman G;. Cell 1997;90:635-647. (from Pfam)

Date:

2024-10-16

Unwinds DNA duplexes with 3' to 5' polarity with respect to the bound strand and initiates unwinding most effectively when a single-stranded region is present; involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair.

Gene:

uvrD

Date:

2021-08-23

ATP-dependent DNA helicase utilizes the energy from ATP hydrolysis to unwind double-stranded DNA; similar to DNA helicase II (UvrD), which displays DNA-dependent ATPase activity and is involved in post-incision events of nucleotide excision repair and methyl-directed mismatch repair

Date:

2023-02-23

Designed to identify uvrD members of the uvrD/rep subfamily.

Gene:

uvrD

Date:

2024-05-30