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pheT protein (Methylobacter tundripaludum) - STRING interaction network
"pheT" - Phenylalanyl-tRNA synthetase beta subunit in Methylobacter tundripaludum
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query proteins and first shell of interactors
white nodes:
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
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
pheTPhenylalanyl-tRNA synthetase beta subunit (791 aa)    
Predicted Functional Partners:
pheS
Phenylalanyl-tRNA synthetase alpha subunit (339 aa)
 
  0.999
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)
   
  0.999
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)
 
  0.995
lysS
Lysyl-tRNA synthetase (499 aa)
 
  0.988
argS
Arginyl-tRNA synthetase (586 aa)
   
  0.988
alaS
Alanyl-tRNA synthetase ; 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 (870 aa)
 
 
  0.986
thrS
Threonyl-tRNA synthetase (635 aa)
 
 
  0.982
glnS
Glutaminyl-tRNA synthetase (554 aa)
   
  0.980
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)
   
  0.980
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)
   
  0.980
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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