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AIL77166.1 protein (Acinetobacter baumannii) - STRING interaction network
"AIL77166.1" - Lysine--tRNA ligase in Acinetobacter baumannii
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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[Homology]
Score
AIL77166.1Lysine--tRNA ligase; Derived by automated computational analysis using gene prediction method- Protein Homology (509 aa)    
Predicted Functional Partners:
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP (522 aa)
 
   
  0.945
argS
Arginine--tRNA ligase; Catalyzes a two-step reaction, first charging an arginine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; class-I aminoacyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method- Protein Homology (596 aa)
 
 
  0.921
AIL80271.1
Histidine--tRNA ligase; Derived by automated computational analysis using gene prediction method- Protein Homology (430 aa)
   
 
  0.877
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) (945 aa)
   
 
  0.873
pheT
Phenylalanine--tRNA ligase beta subunit; Catalyzes a two-step reaction, first charging a phenylalanine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; forms a tetramer of alpha(2)beta(2); binds two magnesium ions per tetramer; type 2 subfamily; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily (793 aa)
 
   
  0.863
metG
methionine--tRNA ligase; MetRS; adds methionine to tRNA(Met) with cleavage of ATP to AMP and diphosphate; some MetRS enzymes form dimers depending on a C-terminal domain that is also found in other proteins such as Trbp111 in Aquifex aeolicus and the cold-shock protein CsaA from Bacillus subtilis while others do not; four subfamilies exist based on sequence motifs and zinc content; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family (687 aa)
 
 
  0.843
thrS
Threonine--tRNA ligase; Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction- L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr) (640 aa)
   
 
  0.827
AIL80288.1
Leucine--tRNA ligase; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family (874 aa)
   
 
  0.798
AIL79124.1
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 [...] (571 aa)
     
 
  0.782
prfB
Peptide chain release factor 2; Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA (310 aa)
 
 
  0.769
Your Current Organism:
Acinetobacter baumannii
NCBI taxonomy Id: 470
Other names: A. baumannii, ATCC 19606, Acinetobacter baumannii, Acinetobacter genomosp. 2, Acinetobacter genomospecies 2, Bacterium anitratum, CCUG 19096, CIP 70.34, DSM 30007, JCM 6841, NCCB 85021, NCTC 12156
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