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lysS protein (Methylobacter tundripaludum) - STRING interaction network
"lysS" - Lysyl-tRNA 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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Gene Fusion
Cooccurence
Coexpression
Experiments
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Textmining
[Homology]
Score
lysSLysyl-tRNA synthetase (499 aa)    
Predicted Functional Partners:
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)
 
  0.992
pheT
Phenylalanyl-tRNA synthetase beta subunit (791 aa)
 
  0.988
guaA
Glutamine amidotransferase ; Catalyzes the synthesis of GMP from XMP (528 aa)
 
   
  0.957
leuS
Leucyl-tRNA synthetase (832 aa)
   
  0.939
prfB
Peptide chain release factor 2 ; Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA (365 aa)
   
 
  0.935
argS
Arginyl-tRNA synthetase (586 aa)
   
  0.931
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)
   
  0.924
gltX
Glutamyl-tRNA synthetase ; 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) (467 aa)
   
  0.917
gluQ
Glutamyl-Q tRNA(Asp) synthetase ; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5- dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon (301 aa)
 
  0.909
hisS
Histidyl-tRNA synthetase (424 aa)
   
 
  0.900
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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