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leuS protein (Streptomyces griseus) - STRING interaction network
"leuS" - leucyl-tRNA synthetase in Streptomyces griseus
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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 (957 aa)    
Predicted Functional Partners:
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 [...] (567 aa)
   
  0.981
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) (1047 aa)
   
  0.980
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 (889 aa)
   
 
  0.930
pheT
phenylalanyl-tRNA synthetase subunit beta (837 aa)
   
  0.909
aspS
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) (599 aa)
 
   
  0.908
alaS2
alanyl-tRNA synthetase (388 aa)
   
 
  0.905
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) (504 aa)
 
  0.902
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 (873 aa)
   
 
0.902
argS
arginyl-tRNA synthetase (594 aa)
   
  0.879
lysS
lysyl-tRNA synthetase (590 aa)
     
 
  0.875
Your Current Organism:
Streptomyces griseus
NCBI taxonomy Id: 455632
Other names: Actinomyces griseus, Actinomyces setonii, Nocardia italica, S. griseus, S. griseus group, S. griseus subsp. griseus, S. griseus subsp. griseus NBRC 13350, Streptomyces cavourensis subsp. washingtonensis, Streptomyces griseus, Streptomyces griseus group, Streptomyces griseus subsp. griseus, Streptomyces griseus subsp. griseus IFO 13350, Streptomyces griseus subsp. griseus NBRC 13350, Streptomyces griseus subsp. griseus str. NBRC 13350, Streptomyces griseus subsp. griseus strain NBRC 13350, Streptomyces setonii, Streptomyces sp. AP19-1, Streptomyces sp. AP19-2, Streptomyces sp. WXC19-1
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