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aspS protein (Thermococcus kodakarensis) - STRING interaction network
"aspS" - aspartyl-tRNA synthetase in Thermococcus kodakarensis
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Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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aspSaspartyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Asp) in a two-step reaction- aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp). Is specific for tRNA(Asp) since it aspartylates tRNA(Asn) 3 orders of magnitude less efficiently than tRNA(Asp) (438 aa)    
Predicted Functional Partners:
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 (741 aa)
   
  0.999
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) (573 aa)
 
  0.979
leuS
leucyl-tRNA synthetase (967 aa)
 
  0.966
argS
arginyl-tRNA synthetase (642 aa)
 
  0.955
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) (1065 aa)
 
  0.954
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) (481 aa)
 
  0.945
TK0239
Putative tRNA-binding protein (109 aa)
 
  0.903
gatE
glutamyl-tRNA(Gln) amidotransferase subunit E; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate (629 aa)
         
  0.900
gatD
glutamyl-tRNA(Gln) amidotransferase subunit D; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate (440 aa)
   
 
  0.882
TK1656
L-asparaginase (328 aa)
   
 
  0.867
Your Current Organism:
Thermococcus kodakarensis
NCBI taxonomy Id: 69014
Other names: Pyrococcus kodadaraensis (sic), Pyrococcus kodakaraensis, Pyrococcus sp. (strain KOD1), Pyrococcus sp. KOD1, T. kodakarensis, T. kodakarensis KOD1, Thermococcus kodakaraensis, Thermococcus kodakaraensis KOD1, Thermococcus kodakarensis, Thermococcus kodakarensis KOD1, Thermococcus kodakarensis corrig. Atomi et al. 2005, Thermococcus kodakarensis str. KOD1, Thermococcus kodakarensis strain KOD1
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