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leuS protein (Deinococcus radiodurans) - STRING interaction network
"leuS" - Leucine--tRNA ligase in Deinococcus radiodurans
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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
leuSLeucine--tRNA ligase; Similar to PID-1652380 percent identity- 64.42; identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family (874 aa)    
Predicted Functional Partners:
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 (1078 aa)
   
 
0.938
cysS
Cysteine--tRNA ligase; Similar to PID-1877311 GB-AL123456 percent identity- 64.06; identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family (532 aa)
   
 
  0.917
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 (913 aa)
     
 
0.917
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 (890 aa)
 
 
  0.916
argS
Arginine--tRNA ligase; Similar to GB-Pyro_h percent identity- 62.62; identified by sequence similarity; putative (609 aa)
     
 
  0.901
glnS
Glutamine--tRNA ligase; Similar to GB-L42023 SP-P43831 PID-1007373 PID-1221487 PID-1205590 percent identity- 67.97; identified by sequence similarity; putative; In the C-terminal section; belongs to the GatB/GatE family (852 aa)
   
 
  0.900
thrS
Threonine--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) (649 aa)
 
 
  0.892
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; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily (681 aa)
   
 
  0.885
tyrS
Tyrosine--tRNA ligase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction- tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily (411 aa)
 
   
  0.885
aspS1
Aspartate--tRNA(Asp) ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction- L-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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily (577 aa)
 
   
  0.880
Your Current Organism:
Deinococcus radiodurans
NCBI taxonomy Id: 243230
Other names: D. radiodurans R1, Deinococcus radiodurans, Deinococcus radiodurans R1, Deinococcus radiodurans str. R1
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