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aspS protein (Lactobacillus reuteri DSM20016) - STRING interaction network
"aspS" - Aspartate--tRNA ligase in Lactobacillus reuteri DSM20016
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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aspSAspartate--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 (600 aa)    
Predicted Functional Partners:
gatB
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp- tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily (474 aa)
 
  0.918
pheS
TIGRFAM- phenylalanyl-tRNA synthetase, alpha subunit; PFAM- phenylalanyl-tRNA synthetase, class IIc; aminoacyl tRNA synthetase, class II domain protein; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily (348 aa)
     
   
  0.908
valS
Valine--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 (884 aa)
 
   
  0.894
leuS
Leucine--tRNA ligase; TIGRFAM- leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family (806 aa)
 
   
  0.878
Lreu_1848
Histidine--tRNA ligase; TIGRFAM- histidyl-tRNA synthetase; PFAM- tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein (425 aa)
 
   
  0.844
Lreu_1830
Histidine--tRNA ligase; TIGRFAM- histidyl-tRNA synthetase; PFAM- tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein (433 aa)
 
   
  0.843
cysS
Cysteine--tRNA ligase; TIGRFAM- cysteinyl-tRNA synthetase; PFAM- Cysteinyl-tRNA synthetase, class Ia, DALR; tRNA synthetase class I (M); Cysteinyl-tRNA synthetase, class Ia-like; Belongs to the class-I aminoacyl-tRNA synthetase family (470 aa)
 
   
  0.817
gltX
Glutamate--tRNA ligase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction- glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily (501 aa)
 
   
  0.817
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (888 aa)
   
   
  0.797
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) (960 aa)
   
   
  0.787
Your Current Organism:
Lactobacillus reuteri DSM20016
NCBI taxonomy Id: 557436
Other names: L. reuteri DSM 20016, Lactobacillus reuteri DSM 20016, Lactobacillus reuteri DSM20016, Lactobacillus reuteri str. DSM 20016, Lactobacillus reuteri strain DSM 20016
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