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glyQ protein (Methylobacter tundripaludum) - STRING interaction network
"glyQ" - Glycyl-tRNA synthetase alpha subunit in Methylobacter tundripaludum
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query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Edges represent protein-protein associations
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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
glyQGlycyl-tRNA synthetase alpha subunit (304 aa)    
Predicted Functional Partners:
glyS
Glycyl-tRNA synthetase beta subunit (688 aa)
  0.999
Mettu_3946
Putative uncharacterized protein (185 aa)
              0.859
Mettu_3945
ATPase-like protein (350 aa)
              0.859
Mettu_3949
Phospholipid/glycerol acyltransferase (248 aa)
   
        0.760
pheS
Phenylalanyl-tRNA synthetase alpha subunit (339 aa)
     
   
  0.751
Mettu_3948
D,D-heptose 1,7-bisphosphate phosphatase (183 aa)
              0.721
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)
 
   
  0.662
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)
     
   
  0.650
pheT
Phenylalanyl-tRNA synthetase beta subunit (791 aa)
     
   
  0.643
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)
 
   
  0.629
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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