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ileS protein (Streptomyces avermitilis) - STRING interaction network
"ileS" - Isoleucine--tRNA ligase in Streptomyces avermitilis
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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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ileSIsoleucine--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 (1047 aa)    
Predicted Functional Partners:
leuS
Leucine--tRNA ligase; PF00133- tRNA synthetases class I (I, L, M and V); Belongs to the class-I aminoacyl-tRNA synthetase family (962 aa)
   
 
  0.985
pheT
Phenylalanine--tRNA ligase beta subunit; PF03483- B3/4 domain; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily (833 aa)
   
 
  0.979
glyS
Glycine--tRNA ligase; Catalyzes the attachment of glycine to tRNA(Gly); Belongs to the class-II aminoacyl-tRNA synthetase family (460 aa)
 
 
  0.924
lysS2
Lysine--tRNA ligase; PF00152- tRNA synthetases class II (D, K and N); Belongs to the class-II aminoacyl-tRNA synthetase family (1093 aa)
   
 
  0.924
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)
   
 
  0.919
proS2
Proline--tRNA ligase 2; 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) (471 aa)
   
 
  0.900
gltS
Glutamate--tRNA ligase; 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)
   
 
  0.880
metS
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 (574 aa)
 
 
  0.875
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 (874 aa)
   
 
0.871
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) (658 aa)
   
 
  0.867
Your Current Organism:
Streptomyces avermitilis
NCBI taxonomy Id: 227882
Other names: S. avermitilis MA-4680 = NBRC 14893, Streptomyces avermitilis, Streptomyces avermitilis MA-4680, Streptomyces avermitilis MA-4680 = NBRC 14893, Streptomyces avermitilis NBRC 14893, Streptomyces avermitilis NBRC 14893 = MA-4680
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