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argS protein (Acidovorax citrulli) - STRING interaction network
"argS" - Arginine--tRNA ligase in Acidovorax citrulli
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second shell of interactors
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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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argSArginine--tRNA ligase; KEGG- rfr-Rfer_0773 arginyl-tRNA synthetase; TIGRFAM- arginyl-tRNA synthetase (569 aa)    
Predicted Functional Partners:
pheT
KEGG- pol-Bpro_2107 phenylalanyl-tRNA synthetase, beta subunit; TIGRFAM- phenylalanyl-tRNA synthetase, beta subunit; PFAM- t-RNA-binding domain protein; B3/4 domain protein; tRNA synthetase, B5 (812 aa)
   
 
  0.941
lysS
Lysine--tRNA ligase; TIGRFAM- lysyl-tRNA synthetase; PFAM- tRNA synthetase, class II (D, K and N); nucleic acid binding, OB-fold, tRNA/helicase-type; KEGG- pol-Bpro_3620 lysyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family (518 aa)
   
 
  0.941
Aave_0415
PFAM- Sporulation domain protein; KEGG- rfr-Rfer_0774 sporulation related (218 aa)
 
          0.917
metG
Methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation (706 aa)
   
 
  0.907
proS
Proline--tRNA ligase; 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 deacy [...] (581 aa)
      
 
  0.892
ileS
Isoleucine--tRNA ligase; 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) (959 aa)
 
 
  0.892
leuS
Leucine--tRNA ligase; TIGRFAM- leucyl-tRNA synthetase; KEGG- rfr-Rfer_0758 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family (897 aa)
      
 
  0.876
pyrG
CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates (559 aa)
   
        0.857
purL
Phosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (1347 aa)
   
   
  0.848
valS
Valine--tRNA ligase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a "posttransfer" editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily (963 aa)
   
   
  0.826
Your Current Organism:
Acidovorax citrulli
NCBI taxonomy Id: 397945
Other names: A. citrulli AAC00-1, Acidovorax avenae subsp. citrulli AAC00-1, Acidovorax citrulli, Acidovorax citrulli AAC00-1, Acidovorax citrulli str. AAC00-1, Acidovorax citrulli strain AAC00-1
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