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recQ protein (Yersinia pseudotuberculosis) - STRING interaction network
recQ: ATP-dependent DNA helicase RecQ in Yersinia pseudotuberculosis
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second shell of interactors
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proteins of unknown 3D structure
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some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Score
recQrecQ- ATP-dependent DNA helicase RecQ (597 aa)    
Predicted Functional Partners:
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (932 aa)
   
 
  0.852
deaD
ATP-dependent RNA helicase DeaD; DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation (664 aa)
 
 
0.848
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 (356 aa)
     
 
  0.847
recJ
SsDNA exonuclease RecJ; recJ- single-stranded-DNA-specific exonuclease RecJ (577 aa)
 
   
  0.828
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 (204 aa)
   
   
  0.799
radA
DNA repair protein RadA; DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3’ invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA’s homology-searching function (460 aa)
           
  0.794
holB
holB- DNA polymerase III, delta’ subunit (340 aa)
     
 
  0.793
xseA
Exodeoxyribonuclease 7 large subunit; Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides; Belongs to the XseA family (459 aa)
   
   
  0.779
topB
DNA topoisomerase 3; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5’-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3’-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA super [...] (641 aa)
 
 
 
  0.739
dinB
DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3’-5’ exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII (352 aa)
   
 
  0.692
Your Current Organism:
Yersinia pseudotuberculosis
NCBI taxonomy Id: 633
Other names: ATCC 29833, Bacillus pseudotuberkulosis, Bacterium pseudotuberculosis, CCUG 5855, CIP 55.85, DSM 8992, NCTC 10275, Pasteurella pseudotuberculosis, Shigella pseudotuberculosis, Y. pseudotuberculosis, Yersinia pseudotuberculosis
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