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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
xseAExodeoxyribonuclease VII; 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. (439 aa)    
Predicted Functional Partners:
xseB
Exodeoxyribonuclease VII; 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.
 
 0.997
KJA12394.1
Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family.
       0.601
KJA09906.1
DNA repair protein; May be involved in recombinational repair of damaged DNA.
 
   
 0.592
fliG
One of three proteins involved in switching the direction of the flagellar rotation; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
   0.575
KJA11331.1
Helicase UvrD; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
   
 0.541
KJA10486.1
Polyprenyl synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the FPP/GGPP synthase family.
 
  
 0.538
ruvA
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.
 
   
 0.531
folD
Methenyltetrahydrofolate cyclohydrolase; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate.
 
    0.520
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.
  
  
 0.501
uvrB
Excinuclease ABC subunit 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 [...]
 
  
 0.495
Your Current Organism:
Acidovorax temperans
NCBI taxonomy Id: 80878
Other names: A. temperans, ATCC 49665, Acidivorax temperans, CCUG 11779, CCUG 29362, CFBP 3610, CIP 103457, DSM 7270, LMG 7169, LMG:7169
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