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RuvB AAA lid domain
The RuvB protein makes up part of the RuvABC revolvasome which catalyses the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalysed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein [1]. This entry contains the AAA lid domain that is found to the C-terminus of the AAA domain. [1]. 12423347. The RuvABC resolvasome.. Dickman MJ, Ingleston SM, Sedelnikova SE, Rafferty JB, Lloyd RG,. Grasby JA, Hornby DP;. Eur J Biochem 2002;269:5492-5501. (from Pfam)
Holliday junction DNA helicase RuvB C-terminal domain-containing protein
The RuvB protein makes up part of the RuvABC revolvasome which catalyses the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalysed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein [1]. This family consists of the C-terminal region of the RuvB protein which is thought to be helicase DNA-binding domain. [1]. 12423347. The RuvABC resolvasome.. Dickman MJ, Ingleston SM, Sedelnikova SE, Rafferty JB, Lloyd RG,. Grasby JA, Hornby DP;. Eur J Biochem 2002;269:5492-5501. (from Pfam)
Holliday junction DNA helicase RuvB P-loop domain
The RuvB protein makes up part of the RuvABC revolvasome which catalyses the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalysed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein [1]. This family contains the N-terminal region of the protein. [1]. 12423347. The RuvABC resolvasome.. Dickman MJ, Ingleston SM, Sedelnikova SE, Rafferty JB, Lloyd RG,. Grasby JA, Hornby DP;. Eur J Biochem 2002;269:5492-5501. (from Pfam)
AAA family ATPase
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)
Holliday junction branch migration DNA helicase RuvB
Holliday junction branch migration DNA helicase RuvB is an ATPase that forms a complex with RuvA; the helicase RuvAB mediates the Holliday junction migration by localized denaturation and reannealing
All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions.
Promotes strand exchange during homologous recombination; RuvAB complex promotes branch migration; RuvABC complex scans the DNA during branch migration and resolves Holliday junctions at consensus sequences; forms hexameric rings around opposite DNA arms; requires ATP for branch migration and orientation of RuvAB complex determines direction of migration
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