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
valS-2valyl-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. (872 aa)    
Predicted Functional Partners:
Sare_3871
TIGRFAM: FolC bifunctional protein; PFAM: cytoplasmic peptidoglycan synthetase domain protein; Mur ligase middle domain protein; KEGG: stp:Strop_3492 FolC bifunctional protein; Belongs to the folylpolyglutamate synthase family.
  
  
 0.956
glyQ
glycyl-tRNA synthetase, beta subunit; KEGG: fra:Francci3_1275 glycine--tRNA ligase; TIGRFAM: glycyl-tRNA synthetase, alpha subunit; glycyl-tRNA synthetase, beta subunit; PFAM: glycyl-tRNA synthetase alpha subunit; glycyl-tRNA synthetase beta subunit.
  
  
 0.925
valS
tRNA synthetase valyl/leucyl anticodon-binding; 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.
     
 
0.900
guaA
GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP.
  
  
 0.868
leuS
TIGRFAM: leucyl-tRNA synthetase; KEGG: stp:Strop_3225 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
   
 
 0.850
ileS
isoleucyl-tRNA synthetase; 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 2 subfamily.
  
 
0.819
Sare_3640
KEGG: stp:Strop_3397 seryl-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like.
 
  
 0.774
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.
  
  
 0.772
Sare_0784
TIGRFAM: threonyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; KEGG: stp:Strop_0841 tRNA synthetase, class II (G, H, P and S).
 
  
 0.765
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.
  
  
 0.765
Your Current Organism:
Salinispora arenicola
NCBI taxonomy Id: 391037
Other names: S. arenicola CNS-205, Salinispora arenicola CNS-205, Salinispora arenicola str. CNS-205, Salinispora arenicola strain CNS-205
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.