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uvrC protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"uvrC" - UvrABC system protein C in Desulfovibrio vulgaris Hildenborough
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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uvrCUvrABC system protein C; 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 (702 aa)    
Predicted Functional Partners:
uvrB
UvrABC system protein B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and [...] (677 aa)
  0.993
uvrA
UvrABC system protein A; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate (956 aa)
 
 
  0.978
recR
Recombination protein RecR; May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO (201 aa)
 
     
  0.906
recD2
ATP-dependent RecD-like DNA helicase; DNA-dependent ATPase and ATP-dependent 5’-3’ DNA helicase. Has no activity on blunt DNA or DNA with 3’-overhangs, requires at least 10 bases of 5’-ssDNA for helicase activity (742 aa)
 
 
  0.877
ruvA
Holliday junction ATP-dependent DNA helicase RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB (202 aa)
 
   
  0.844
polA
DNA polymerase I; Identified by similarity to SP-P00582; match to protein family HMM PF00476; match to protein family HMM PF01367; match to protein family HMM PF02739; match to protein family HMM TIGR00593 (1015 aa)
 
   
  0.838
ruvC
Crossover junction endodeoxyribonuclease RuvC; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5’-terminal phosphate and a 3’-terminal hydroxyl group (166 aa)
   
 
  0.826
recA
Protein RecA; Can catalyze 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. It interacts with LexA causing its activation and leading to its autocatalytic cleavage (357 aa)
 
   
  0.810
recO
DNA repair protein RecO; Involved in DNA repair and RecF pathway recombination (251 aa)
         
  0.802
DVU_3257
DNA internalization-related competence protein ComEC/Rec2; Identified by similarity to SP-P39695; match to protein family HMM TIGR00360 (974 aa)
   
   
  0.756
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882
Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
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