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
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
valSvalyl-tRNA synthetase; 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. (891 aa)    
Predicted Functional Partners:
guaA
GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP.
  
  
 0.908
Tter_0977
TIGRFAM: isoleucyl-tRNA synthetase; KEGG: bcb:BCB4264_A2186 isoleucyl-tRNA synthetase.
  
 
 0.863
leuS
TIGRFAM: leucyl-tRNA synthetase; KEGG: glo:Glov_2116 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
   
 
 0.856
alaS
alanyl-tRNA synthetase; 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.
 
  
 0.812
aspS
aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
  
 0.804
thrS
TIGRFAM: threonyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; Threonyl/alanyl tRNA synthetase SAD; KEGG: bsu:BSU28950 threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family.
 
 
 0.796
pheT
KEGG: dol:Dole_3039 phenylalanyl-tRNA synthetase, beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
  
 0.770
lysS
TIGRFAM: lysyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); tRNA synthetase class II (G H P and S); nucleic acid binding OB- fold tRNA/helicase-type; KEGG: bsu:BSU00820 lysyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 
 0.705
proS
prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
  
 
 0.689
nadA
Quinolinate synthetase complex, A subunit; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
      0.674
Your Current Organism:
Thermobaculum terrenum
NCBI taxonomy Id: 525904
Other names: T. terrenum ATCC BAA-798, Thermobaculum terrenum ATCC BAA-798, Thermobaculum terrenum YNP1, Thermobaculum terrenum str. ATCC BAA-798, Thermobaculum terrenum strain ATCC BAA-798
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.