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thrS protein (Bacillus subtilis) - STRING interaction network
"thrS" - Threonine--tRNA ligase 1 in Bacillus subtilis
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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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Score
thrSThreonine--tRNA ligase 1; Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction- L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr); Belongs to the class-II aminoacyl-tRNA synthetase family (643 aa)    
Predicted Functional Partners:
pheT
Phenylalanine--tRNA ligase beta subunit; Evidence 1a- Function experimentally demonstrated in the studied strain; Product type e- enzyme; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily (804 aa)
   
 
  0.935
alaS
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 (878 aa)
   
 
  0.918
tyrS
Tyrosine--tRNA ligase 1; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction- tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr) (422 aa)
   
 
  0.909
metS
Methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily (664 aa)
 
 
  0.907
lysS
Lysine--tRNA ligase; Evidence 1a- Function experimentally demonstrated in the studied strain; Product type e- enzyme; Belongs to the class-II aminoacyl-tRNA synthetase family (499 aa)
 
 
  0.904
serS
Serine--tRNA ligase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) (425 aa)
 
 
  0.898
valS
Valine--tRNA ligase; 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 (By similarity). Catalyzes the attachment of valine to tRNA(Val); Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily (880 aa)
 
   
  0.888
rplC
50S ribosomal protein L3; One of the primary rRNA binding proteins, it binds directly near the 3’-end of the 23S rRNA, where it nucleates assembly of the 50S subunit (By similarity). Strongly stimulates 23S rRNA precursor processing by mini-ribonuclease 3 (MrnC); 20- 30% DMSO can replace L3, suggesting the protein may alter rRNA conformation (209 aa)
   
 
  0.886
cysS
Cysteine--tRNA ligase; Evidence 1a- Function experimentally demonstrated in the studied strain; Product type e- enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family (466 aa)
 
   
  0.878
rpsO
30S ribosomal protein S15; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA (89 aa)
 
 
  0.864
Your Current Organism:
Bacillus subtilis
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis, Bacillus subtilis 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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