STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ruvCHolliday junction nuclease (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 (By similarity). (196 aa)    
Predicted Functional Partners:
ruvA
Holliday junction 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.
 
 
 0.997
ruvB
Holliday junction DNA helicase (ruvB); 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.
 
 
 0.989
TP_0518
Conserved hypothetical protein; Similar to GB:AL009126 percent identity: 32.48; identified by sequence similarity; putative.
 
 
   0.879
recJ
single-stranded-DNA-specific exonuclease (recJ); Similar to GB:AE000783 percent identity: 24.42; identified by sequence similarity; putative.
   
 
 0.846
murJ
Virulence factor (mviN); Involved in peptidoglycan biosynthesis. Transports lipid- linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
 
    0.826
recX
recX protein (recX); Modulates RecA activity; Belongs to the RecX family.
  
  
 0.780
TP_0519
Response regulatory protein (atoC); Similar to GB:AE000783 percent identity: 54.34; identified by sequence similarity; putative.
       0.774
recG
DNA recombinase (recG); Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y- DNA) (By similarity); Belongs to the helicase family. RecG subfamily.
     
 0.731
sbcC
Exonuclease (sbcC); 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 (By similarity); Belongs to the SMC family. SbcC subfamily.
     
 0.717
recO
Conserved hypothetical protein; Involved in DNA repair and RecF pathway recombination.
  
  
 0.708
Your Current Organism:
Treponema pallidum
NCBI taxonomy Id: 243276
Other names: T. pallidum subsp. pallidum str. Nichols, Treponema pallidum Nichols, Treponema pallidum subsp. pallidum str. Nichols
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.