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
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[Homology]
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ruvCCrossover 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. (169 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.
 
 0.999
ruvB
Holliday junction ATP-dependent 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.
 
 
 0.994
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; Belongs to the RecA family.
   
  
 0.793
ANP27492.1
Pfam: Transcriptional regulator; TIGRFAM: TIGR01033: DNA-binding regulatory protein, YebC/PmpR family.
 
  
 0.774
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.
     
 0.711
recX
Hypothetical protein; Modulates RecA activity; Belongs to the RecX family.
  
  
 0.698
ANP27496.1
TIGRFAM: yajC: preprotein translocase, YajC subunit; Pfam: Preprotein translocase subunit.
     
 0.681
uvrC
Excinuclease ABC subunit 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.
      
 0.646
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 [...]
     
 0.645
thrS
threonyl-tRNA synthetase; Pfam: Anticodon binding domain; Pfam: Threonyl and Alanyl tRNA synthetase second additional domain; Pfam: tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: thrS: threonine--tRNA ligase; SMART: Threonyl and Alanyl tRNA synthetase second additional domain; PRINTS: Threonyl-tRNA synthetase signature; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
    0.644
Your Current Organism:
Dermabacter vaginalis
NCBI taxonomy Id: 1630135
Other names: D. vaginalis, DSM 100050, Dermabacter sp. AD1-86, Dermabacter vaginalis Chang et al. 2016, KCTC 39585, strain AD1-86
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