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thrS protein (Chlamydia muridarum) - STRING interaction network
"thrS" - Threonine--tRNA ligase in Chlamydia muridarum
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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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thrSThreonine--tRNA ligase; 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) (635 aa)    
Predicted Functional Partners:
pheT
Phenylalanine--tRNA ligase beta subunit; Similar to GB-J04809, SP-P00568, and PID-178322; identified by sequence similarity; putative; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily (790 aa)
   
 
  0.966
lysS
Lysine--tRNA ligase; Similar to SP-P80105; identified by sequence similarity; putative; Belongs to the class-II aminoacyl-tRNA synthetase family (524 aa)
   
 
  0.950
pheS
Phenylalanine--tRNA ligase alpha subunit; Similar to SP-P37279, and PID-435125; identified by sequence similarity; putative; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily (341 aa)
   
 
  0.944
leuS
Leucine--tRNA ligase; Similar to SP-P14878, GB-X06083, and PID-43373; identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family (819 aa)
   
 
  0.915
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 (875 aa)
   
 
  0.911
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 (939 aa)
 
   
  0.889
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 2 subfamily (1036 aa)
   
 
  0.888
metG
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 (550 aa)
   
 
  0.872
trpS
Tryptophan--tRNA ligase; Catalyzes the attachment of tryptophan to tRNA(Trp); Belongs to the class-I aminoacyl-tRNA synthetase family (346 aa)
   
   
  0.866
fusA
Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity) (694 aa)
     
 
  0.850
Your Current Organism:
Chlamydia muridarum
NCBI taxonomy Id: 243161
Other names: C. muridarum str. Nigg, Chlamydia muridarum, Chlamydia muridarum Nigg, Chlamydia muridarum str. Nigg, Chlamydia muridarum strain Nigg, Chlamydia trachomatis MoPn strain Nigg
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