STRUCTURE OF RUVB FROM THERMUS THERMOPHILUS HB8
External Resource: Annotation
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
A | SCOP2B Superfamily | Winged helix DNA-binding domain | 8058580 | 3000034 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | RecA-like P-loop NTPases | 8058578 | 3002019 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | DNA polymerases epsilon, N-terminal domain (Dpoe2NT)-like | 8104163 | 3002834 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | DNA polymerases epsilon, N-terminal domain (Dpoe2NT)-like | 8104163 | 3002834 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | Winged helix DNA-binding domain | 8058580 | 3000034 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | RecA-like P-loop NTPases | 8058578 | 3002019 | SCOP2B (2022-06-29) |
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | RuvB_C | e1hqcA1 | A: alpha arrays | X: HTH | H: HTH | T: winged | F: RuvB_C | ECOD (1.6) |
A | RuvB_N | e1hqcA2 | A: alpha arrays | X: Histone-like | H: Histone-related | T: AAA+ ATPase lid domain | F: RuvB_N | ECOD (1.6) |
A | Sigma54_activat | e1hqcA3 | A: a/b three-layered sandwiches | X: P-loop domains-like | H: P-loop domains-related | T: P-loop containing nucleoside triphosphate hydrolases | F: Sigma54_activat | ECOD (1.6) |
B | RuvB_C | e1hqcB1 | A: alpha arrays | X: HTH | H: HTH | T: winged | F: RuvB_C | ECOD (1.6) |
B | RuvB_N | e1hqcB2 | A: alpha arrays | X: Histone-like | H: Histone-related | T: AAA+ ATPase lid domain | F: RuvB_N | ECOD (1.6) |
B | Sigma54_activat | e1hqcB3 | A: a/b three-layered sandwiches | X: P-loop domains-like | H: P-loop domains-related | T: P-loop containing nucleoside triphosphate hydrolases | F: Sigma54_activat | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
A | 3.40.50.300 | Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | P-loop containing nucleotide triphosphate hydrolases | CATH (4.3.0) |
A | 1.10.8.60 | Mainly Alpha | Orthogonal Bundle | Helicase, Ruva Protein | domain 3 | CATH (4.3.0) |
A | 1.10.10.10 | Mainly Alpha | Orthogonal Bundle | Arc Repressor Mutant, subunit A | Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain | CATH (4.3.0) |
B | 3.40.50.300 | Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | P-loop containing nucleotide triphosphate hydrolases | CATH (4.3.0) |
B | 1.10.8.60 | Mainly Alpha | Orthogonal Bundle | Helicase, Ruva Protein | domain 3 | CATH (4.3.0) |
B | 1.10.10.10 | Mainly Alpha | Orthogonal Bundle | Arc Repressor Mutant, subunit A | Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF05491 | RuvB C-terminal winged helix domain (RuvB_C) | RuvB C-terminal winged helix 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 j ... | Domain | |
PF05496 | Holliday junction DNA helicase RuvB P-loop domain (RuvB_N) | 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 j ... | Domain | |
PF17864 | RuvB AAA lid domain (AAA_lid_4) | 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 j ... | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR036388 | Winged helix-like DNA-binding domain superfamily | Homologous Superfamily | |
IPR008824 | RuvB-like P-loop domain | Domain | |
IPR036390 | Winged helix DNA-binding domain superfamily | Homologous Superfamily | |
IPR041445 | RuvB, AAA lid domain | Domain | |
IPR003593 | AAA+ ATPase domain | Domain | |
IPR004605 | Holliday junction branch migration complex subunit RuvB | Family | |
IPR008823 | RuvB C-terminal winged helix domain | Domain | |
IPR027417 | P-loop containing nucleoside triphosphate hydrolase | Homologous Superfamily |
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage
Chains | Enzyme Name | Description | Catalytic Residues |
---|---|---|---|
DNA helicase M-CSA #780 | Recombination in bacteria requires the isomerisation of the Holliday junction in a process revolving around the activities of three enzymes each with specific functions. RuvB, the second of the three enzymes involved, catalyses the migration of the branches of DNA before the cleavage step occurs, so that the cleavage and rejoining can produce recombinant products. It works by using ATP hydrolysis to power conformational change in the DNA binding domain, restructuring the Holliday junction. The ATP binding domain shows homology to the AAA family (ATP associated activities) in that it has a Rossman fold and both Walker A and Walker B motifs. Here, the enzyme from Thermus thermophilus is analysed; it displays significant sequence identity with the E.coli enzyme and both share similar active sites and probable catalytic mechanisms, as well as the same overall fold. | Defined by 5 residues: LYS:A-51THR:A-52ASP:A-97THR:A-146ARG:A-205 | EC: 3.6.1.3 (PDB Primary Data) EC: 3.6.4 (UniProt) |