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
valSValine-tRNA ligase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. (875 aa)    
Predicted Functional Partners:
folC
Most examples are bifunctional (folate pathway), active as both folylpolyglutamate synthetase and dihydrofolate synthetase; High confidence in function and specificity; Belongs to the folylpolyglutamate synthase family.
 
  
 0.895
guaA
GMP synthase; Catalyzes the synthesis of GMP from XMP.
  
  
 0.880
ileS
Isoleucine-tRNA ligase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.
 
 
0.871
leuS
Leucine-tRNA ligase; High confidence in function and specificity; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
0.858
aspS
Aspartate-tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
  
 0.824
pheT
phenylalanyl-tRNA synthetase subunit beta; High confidence in function and specificity; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
  
 0.774
alaS1
Alanine-tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
 
  
 0.763
thrS
threonyl-tRNA ligase; Catalyses: ATP + L-threonine + tRNA(Thr) <=> AMP + diphosphate + L-threonyl-tRNA(Thr); High confidence in function and specificity; Belongs to the class-II aminoacyl-tRNA synthetase family.
 
  
 0.756
ruvA
Holliday junction DNA helicase; 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.
       0.749
glyS
glycyl-tRNA synthetase subunit beta; High confidence in function and specificity.
  
  
 0.748
Your Current Organism:
Defluviitoga tunisiensis
NCBI taxonomy Id: 1006576
Other names: D. tunisiensis, DSM 23805, Defluviitoga tunisiensis Ben Hania et al. 2012, JCM 17210, Thermotogaceae bacterium SulfLac1, strain SulfLac1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.