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valS protein (Methylobacter tundripaludum) - STRING interaction network
"valS" - Valine--tRNA ligase in Methylobacter tundripaludum
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query proteins and first shell of interactors
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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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Score
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; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily (931 aa)    
Predicted Functional Partners:
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 1 subfamily (672 aa)
 
 
  0.937
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) (943 aa)
 
0.918
leuS
Leucine--tRNA ligase; TIGRFAM- Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; KEGG- tgr-Tgr7_2279 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family (832 aa)
     
0.900
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP (528 aa)
   
   
  0.879
cysS
Cysteine--tRNA ligase; TIGRFAM- Cysteinyl-tRNA synthetase, class Ia; KEGG- mca-MCA0509 cysteinyl-tRNA synthetase; PFAM- Cysteinyl-tRNA synthetase, class Ia, N-terminal; Cysteinyl-tRNA synthetase, class Ia, DALR; Belongs to the class-I aminoacyl-tRNA synthetase family (492 aa)
 
   
  0.868
pheS
TIGRFAM- Phenylalanyl-tRNA synthetase, class IIc, alpha subunit; HAMAP- Phenylalanyl-tRNA synthetase alpha chain; KEGG- mca-MCA0697 phenylalanyl-tRNA synthetase subunit alpha; PFAM- Phenylalanyl-tRNA synthetase alpha chain; Phenylalanyl-tRNA synthetase, class II, N-terminal; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily (339 aa)
   
   
  0.862
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) (635 aa)
 
   
  0.852
argS
Arginine--tRNA ligase; TIGRFAM- Arginyl-tRNA synthetase, class Ic; HAMAP- Arginyl-tRNA synthetase, class Ic; KEGG- mca-MCA3089 arginyl-tRNA synthetase (586 aa)
   
   
  0.851
pepA
Probable cytosol aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides; Belongs to the peptidase M17 family (501 aa)
 
      0.833
aspS
Aspartate--tRNA(Asp/Asn) ligase; 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- L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily (596 aa)
 
   
  0.816
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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