STRINGSTRING
tyrS protein (Methylobacter tundripaludum) - STRING interaction network
"tyrS" - Tyrosyl-tRNA synthetase in Methylobacter tundripaludum
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
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
tyrSTyrosyl-tRNA synthetase ; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction- tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr) (398 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)
   
  0.972
pheT
Phenylalanyl-tRNA synthetase beta subunit (791 aa)
   
  0.969
thrS
Threonyl-tRNA synthetase (635 aa)
     
 
  0.915
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)
 
   
  0.904
proS
Prolyl-tRNA synthetase ; Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction- proline is first activated by ATP to form Pro- AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as ’pretransfer’ editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated ’posttransfer’ editing and involves de [...] (569 aa)
   
   
  0.878
pheS
Phenylalanyl-tRNA synthetase alpha subunit (339 aa)
   
   
  0.863
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)
   
 
  0.856
cysS
Cysteinyl-tRNA synthetase (492 aa)
     
 
  0.855
hisS
Histidyl-tRNA synthetase (424 aa)
   
   
  0.849
serS
Seryl-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)
   
   
  0.833
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
Server load: low (16%) [HD]