|sbcC||Exonuclease, dsDNA, ATP-dependent; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity. (1048 aa)|| |
Predicted Functional Partners:
Exonuclease, dsDNA, ATP-dependent; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity; Belongs to the SbcD family.
ATP-dependent DNA helicase; Involved in the RecF recombination pathway; its gene expression is under the regulation of the SOS system. It is a DNA helicase; Belongs to the helicase family. RecQ subfamily.
| || || ||0.966
5' to 3' DNA polymerase and 3' to 5'/5' to 3' exonuclease; In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. It is able to utilize nicked circular duplex DNA as a template and can unwind the parental DNA strand from its template.
| || || ||0.938
ssDNA exonuclease, 5' --> 3'-specific; Single-stranded-DNA-specific exonuclease. Required for many types of recombinational events, although the stringency of the requirement for RecJ appears to vary with the type of recombinational event monitored and the other recombination gene products which are available.
| || || || || || ||0.921
Exonuclease V (RecBCD complex), beta subunit; A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a rapid (>1 kb/second) and highly processive (>30 kb) ATP-dependent bidirectional helicase. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator, 5'-GCTGGTGG-3') sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to Chi site, by nicking one strand or switching the strand degraded (depending on the reaction conditions). The properties and activities of the enzyme are changed at Chi. The Chi-alte [...]
| || || || ||0.919
Exodeoxyribonuclease I; Degrades single-stranded DNA (ssDNA) in a highly processive manner. Also functions as a DNA deoxyribophosphodiesterase that releases deoxyribose-phosphate moieties following the cleavage of DNA at an apurinic/apyrimidinic (AP) site by either an AP endonuclease or AP lyase.
| || || || || || || ||0.899
Excinuclease UvrABC, endonuclease subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
| || || || || ||0.888
DNA recombination and repair protein; Required for homologous recombination and the bypass of mutagenic DNA lesions by the SOS response. Catalyzes ATP-driven homologous pairing and strand exchange of DNA molecules necessary for DNA recombinational repair. Catalyzes the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single- stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. The SOS response controls an apoptotic-like death (ALD) induced (in the absence of the mazE-mazF toxin-antitoxin module) in resp [...]
| || || ||0.875
Gap repair protein; The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
| || || || || || || ||0.862
Methyl-directed mismatch repair protein; This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of the final effector complex. The ATPase activity of MutL is stimulated by DNA.
| || || || ||0.815