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valS protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"valS" - Valine--tRNA ligase in Desulfovibrio vulgaris Hildenborough
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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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valSValine--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 (884 aa)    
Predicted Functional Partners:
pheS
Phenylalanine--tRNA ligase alpha subunit; Identified by similarity to SP-P08312; match to protein family HMM PF01409; match to protein family HMM PF02912; match to protein family HMM TIGR00468 (345 aa)
   
   
  0.925
argS
Arginine--tRNA ligase; Identified by similarity to SP-P35868; match to protein family HMM PF00750; match to protein family HMM PF03485; match to protein family HMM PF05746; match to protein family HMM TIGR00456 (551 aa)
   
   
  0.923
leuS
Leucine--tRNA ligase; Identified by similarity to SP-P07813; match to protein family HMM PF00133; match to protein family HMM TIGR00396; Belongs to the class-I aminoacyl-tRNA synthetase family (829 aa)
     
 
0.904
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) (938 aa)
 
 
0.889
gltX-2
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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily (463 aa)
   
 
  0.868
serS
Serine--tRNA ligase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) (424 aa)
   
   
  0.864
cysS
Cysteine--tRNA ligase; Identified by similarity to SP-Q06752; match to protein family HMM PF01406; match to protein family HMM TIGR00435; Belongs to the class-I aminoacyl-tRNA synthetase family (485 aa)
 
   
  0.858
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) (644 aa)
 
   
  0.855
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP (515 aa)
   
   
  0.855
trpS
Tryptophanyl-tRNA synthetase; Identified by match to protein family HMM PF00579; match to protein family HMM TIGR00233; Belongs to the class-I aminoacyl-tRNA synthetase family (329 aa)
   
   
  0.843
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882
Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
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