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leuS protein (Deinococcus radiodurans) - STRING interaction network
"leuS" - leucyl-tRNA synthetase in Deinococcus radiodurans
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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
leuSleucyl-tRNA synthetase (874 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 (681 aa)
   
  0.988
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). Can inadvertently accommodate and process cysteine (499 aa)
   
  0.983
alaS
alanyl-tRNA synthetase; 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 (890 aa)
 
 
  0.961
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) (1078 aa)
   
0.941
pheT
phenylalanyl-tRNA synthetase subunit beta (820 aa)
   
  0.926
cysS
cysteinyl-tRNA synthetase (532 aa)
   
 
  0.924
argS
arginyl-tRNA synthetase (609 aa)
   
  0.922
lysS
lysyl-tRNA synthetase (525 aa)
   
  0.914
aspS2
aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps- aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn). Is slightly more efficient at aminoacylating tRNA(Asn) over tRNA(Asp) (435 aa)
   
  0.908
aspS1
aspartyl-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 cannot aspartylate tRNA(Asn) (577 aa)
 
   
  0.900
Your Current Organism:
Deinococcus radiodurans
NCBI taxonomy Id: 243230
Other names: D. radiodurans, D. radiodurans R1, Deinococcus radiidurans, Deinococcus radiodurans, Deinococcus radiodurans R1, Deinococcus radiodurans str. R1, Micrococcus radiodurans
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