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uvrA uvrA uvrB uvrB uvrC uvrC ACS38066.1 ACS38066.1 uvrD uvrD mfd-2 mfd-2 mfd mfd recA recA rho rho dnaK dnaK gltB gltB
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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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uvrADNA excision repair enzyme subunit, with UvrBC; 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. (1029 aa)    
Predicted Functional Partners:
uvrB
UvrABC system protein B (UvrB protein) (Excinuclease ABC subunit 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 lesi [...]
 
 0.997
uvrC
DNA exisiton repair enzyme together with UvrAB; 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.
 
 0.956
ACS38066.1
Excinuclease ABC, A subunit; Function of strongly homologous gene; enzyme.
  
  
 
0.913
uvrD
DNA-dependent ATPase I and helicase II; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
 
 
 0.876
mfd-2
DEAD/DEAH box helicase domain protein; Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site; In the C-terminal section; belongs to the helicase family. RecG subfamily.
   
 
 0.741
mfd
Transcription repair coupling protein, ATP-dependent helicase; Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site; In the C-terminal section; belongs to the helicase family. RecG subfamily.
   
 
 0.741
recA
DNA strand exchange and recombination protein with protease and nuclease activity; 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; Belongs to the RecA family.
 
  
 0.723
rho
Transcription termination factor Rho; Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA- dependent ATPase activity, and release of the mRNA from the DNA template.
  
  
 0.718
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
  
 0.613
gltB
Glutamate synthase, large subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
     
 0.610
Your Current Organism:
Methylorubrum extorquens
NCBI taxonomy Id: 272630
Other names: M. extorquens AM1, Methylobacterium extorquens AM1, Methylorubrum extorquens AM1, Pseudomonas sp. AM1
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