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gatA protein (Acidaminococcus intestini) - STRING interaction network
"gatA" - glutamyl-tRNA(Gln) amidotransferase in Acidaminococcus intestini
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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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gatAglutamyl-tRNA(Gln) amidotransferase; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln) (488 aa)    
Predicted Functional Partners:
gatB
aspartyl/glutamyl-tRNA amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp- tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (481 aa)
 
  0.999
gatC
glutamyl-tRNA(Gln) amidotransferase; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp- tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (77 aa)
 
  0.999
gltX1
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) (490 aa)
   
  0.971
pth
peptidyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl- tRNAs which drop off the ribosome during protein synthesis (224 aa)
   
 
    0.904
pncB
Nicotinic acid phosphoribosyltransferase; Catalyzes the synthesis of beta-nicotinate D- ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP (478 aa)
   
 
    0.903
aspS
aspartyl-tRNA synthetase (596 aa)
 
 
  0.792
Acin_0418
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) (472 aa)
   
 
  0.730
polA
DNA polymerase I (873 aa)
   
   
  0.548
Acin_0269
Hypothetical protein (335 aa)
 
   
  0.534
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 dea [...] (571 aa)
   
 
  0.532
Your Current Organism:
Acidaminococcus intestini
NCBI taxonomy Id: 568816
Other names: A. intestini, A. intestini RyC-MR95, Acidaminococcus intestini, Acidaminococcus intestini Jumas-Bilak et al. 2007, Acidaminococcus intestini RyC-MR95, Acidaminococcus intestini strain RyC-MR95, Acidaminococcus sp. ADV 255.99
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