STRINGSTRING
ruvC ruvC ruvA ruvA ruvB ruvB polC polC THA_1317 THA_1317 polA polA recX recX THA_559 THA_559 THA_1246 THA_1246 topA topA def def
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
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. (157 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.
 
 
 0.971
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.
 
 
 0.935
polC
DNA polymerase III, alpha subunit, Gram-positive type; Required for replicative DNA synthesis. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
     
 0.787
THA_1317
Transporter, major facilitator family.
     
 0.778
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.
     
 0.668
recX
Regulatory protein RecX; Modulates RecA activity; Belongs to the RecX family.
  
  
 0.618
THA_559
Single-stranded DNA-specific exonuclease.
   
 
 0.544
THA_1246
Conserved hypothetical protein.
 
  
 0.530
topA
DNA topoisomerase I; 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 supe [...]
     
 0.491
def
Def peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
 
 
 
 0.489
Your Current Organism:
Thermosipho africanus
NCBI taxonomy Id: 484019
Other names: T. africanus TCF52B, Thermosipho africanus TCF52B, Thermosipho africanus str. TCF52B, Thermosipho africanus strain TCF52B
Server load: low (22%) [HD]