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
ruvAHolliday 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. (200 aa)    
Predicted Functional Partners:
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.
 
 
 0.995
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.
 
 
 0.923
ACE03388.1
TIGRFAM: FolC bifunctional protein; PFAM: cytoplasmic peptidoglycan synthetase domain protein; Mur ligase middle domain protein; KEGG: pvi:Cvib_1538 FolC bifunctional protein; Belongs to the folylpolyglutamate synthase family.
       0.795
queA
S-adenosylmethionine/tRNA-ribosyltransferase- isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
 
    0.601
ACE03553.1
DNA repair protein RecN; May be involved in recombinational repair of damaged DNA.
 
  
 0.567
rpsT
Ribosomal protein S20; Binds directly to 16S ribosomal RNA.
       0.562
queA-2
S-adenosylmethionine/tRNA-ribosyltransferase- isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
  
    0.547
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.
 
   
 0.544
pheT
KEGG: cte:CT0730 phenylalanyl-tRNA synthetase beta chain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
 
   
 0.536
ligA
DNA ligase, NAD-dependent; DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
  
   
 0.485
Your Current Organism:
Chlorobium phaeobacteroides BS1
NCBI taxonomy Id: 331678
Other names: C. phaeobacteroides BS1, Chlorobium phaeobacteroides MN1, Chlorobium phaeobacteroides str. BS1, Chlorobium phaeobacteroides strain BS1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.