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serS serS valS valS pheT pheT lysS lysS glnS glnS leuS leuS metG metG gltX gltX argS argS proS proS ileS ileS
"argS" - arginyl-tRNA synthetase in Buchnera aphidicola APS
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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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[Homology]
Score
argSarginyl-tRNA synthetase (574 aa)    
Predicted Functional Partners:
pheT
phenylalanyl-tRNA synthetase subunit beta (795 aa)
   
  0.995
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) (940 aa)
   
  0.990
metG
methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation (547 aa)
 
  0.984
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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as ’pretransfer’ editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated ’posttransfer’ editing and involves dea [...] (572 aa)
   
  0.979
glnS
glutaminyl-tRNA synthetase (571 aa)
   
  0.977
gltX
glutamyl-tRNA synthetase; 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) (467 aa)
   
  0.975
lysS
lysyl-tRNA synthetase (506 aa)
   
  0.972
leuS
leucyl-tRNA synthetase (859 aa)
   
  0.966
serS
seryl-tRNA synthetase; 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) (427 aa)
   
   
  0.959
valS
valyl-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 (955 aa)
   
   
  0.941
Your Current Organism:
Buchnera aphidicola APS
NCBI taxonomy Id: 107806
Other names: Acyrthosiphon pisum endosymbiont, Acyrthosiphon pisum primary endosymbiont, Acyrthosiphon pisum symbiotic bacterium, B. aphidicola (Acyrthosiphon pisum), B. aphidicola str. APS (Acyrthosiphon pisum), Buchnera aphidicola (Acyrthosiphon pisum), Buchnera aphidicola APS, Buchnera aphidicola str. APS (Acyrthosiphon pisum), Buchnera aphidicola strain APS (Acyrthosiphon pisum), Buchnera sp. (Acyrthosiphon pisum symbiont), Buchnera sp. APS, primary endosymbiont of Acyrthosiphon pisum
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