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
xseAExodeoxyribonuclease 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. (526 aa)    
Predicted Functional Partners:
xseB
Exodeoxyribonuclease 7 small subunit; Bidirectionally degrades single-stranded DNA into large acid- insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides; Belongs to the XseB family.
 
 0.994
ANL57752.1
Protein involved in electron carrier activity, oxidoreductase activity and coenzyme binding.
       0.791
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.
 
   
 0.747
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.
 
   
 0.703
mutL
DNA mismatch repair protein MutL; This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
 
   
 0.702
recJ
Protein involved in 5'-3' exonuclease activity, manganese ion binding, DNA repair and DNA recombination.
 
  
 0.701
recN
DNA repair protein RecN; May be involved in recombinational repair of damaged DNA.
 
   
 0.689
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.
 
   
 0.663
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.
 
  
 0.662
folD-1
Bifunctional 5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase FolD 1; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate.
 
    0.639
Your Current Organism:
Rhizobium phaseoli
NCBI taxonomy Id: 396
Other names: ATCC 14482, DSM 30137, IFO 14785, JCM 20683, NBRC 14785, NRRL L-321, R. phaseoli
Server load: medium (44%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.