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serS protein (Methylobacter tundripaludum) - STRING interaction network
"serS" - Seryl-tRNA(Ser/Sec) synthetase 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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[Homology]
Score
serSSeryl-tRNA(Ser/Sec) synthetase ; 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) (423 aa)    
Predicted Functional Partners:
cysS
Cysteinyl-tRNA synthetase (492 aa)
 
   
  0.975
thrS
Threonyl-tRNA synthetase (635 aa)
 
 
  0.959
hisS
Histidyl-tRNA synthetase (424 aa)
   
 
  0.942
argS
Arginyl-tRNA synthetase (586 aa)
   
   
  0.929
trpS
Tryptophanyl-tRNA synthetase (337 aa)
   
 
  0.914
pheT
Phenylalanyl-tRNA synthetase beta subunit (791 aa)
 
   
  0.903
pheS
Phenylalanyl-tRNA synthetase alpha subunit (339 aa)
 
   
  0.899
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) (943 aa)
 
   
  0.886
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 (931 aa)
   
   
  0.875
metG
Methionyl-tRNA synthetase ; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation (672 aa)
     
   
  0.871
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum, M. tundripaludum SV96, Methylobacter, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum Wartiainen et al. 2006, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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