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JG24_28735 protein (Klebsiella pneumoniae) - STRING interaction network
"JG24_28735" - Tryptophanyl-tRNA synthetase in Klebsiella pneumoniae
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second shell of interactors
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proteins of unknown 3D structure
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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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[Homology]
Score
JG24_28735Tryptophanyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family (335 aa)    
Predicted Functional Partners:
JG24_23685
Tryptophanyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family (334 aa)
         
 
0.800
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 (795 aa)
   
   
  0.769
JG24_09510
Monomeric bifunctional protein; functions in tryptophan biosynthesis pathway; phosphoribosylanthranilate is rearranged to carboxyphenylaminodeoxyribulosephosphate which is then closed to form indole-3-glycerol phosphate; Derived by automated computational analysis using gene prediction method- Protein Homology (452 aa)
   
   
  0.683
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; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily (677 aa)
   
   
  0.672
argS
Arginine--tRNA ligase; Derived by automated computational analysis using gene prediction method- Protein Homology (577 aa)
   
   
  0.665
ribD
5-amino-6-(5-phosphoribosylamino)uracil reductase; Riboflavin biosynthesis protein which catalyzes the deamination and reduction steps in the riboflavin biosynthesis pathway; catalyzes the formation of 5-amino-6-(5-phosphoribosylamino)uracil from 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine and the formation of 5-amino-6-(5-phosphoribosylamino)uracil from 5-amino-6-(5-phosphoribitylamino)uracil; Derived by automated computational analysis using gene prediction method- Protein Homology (367 aa)
         
  0.654
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (930 aa)
   
   
  0.566
serS
Serine--tRNA ligase; 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) (430 aa)
   
 
  0.563
leuS
Leucyl-tRNA synthetase; leucine--tRNA ligase; LeuRS; class-I aminoacyl-tRNA synthetase; charges leucine by linking carboxyl group to alpha-phosphate of ATP and then transfers aminoacyl-adenylate to its tRNA; due to the large number of codons that tRNA(Leu) recognizes, the leucyl-tRNA synthetase does not recognize the anticodon loop of the tRNA, but instead recognition is dependent on a conserved discriminator base A37 and a long arm; an editing domain hydrolyzes misformed products; in Methanothermobacter thermautotrophicus this enzyme associates with prolyl-tRNA synthetase; Derived by [...] (860 aa)
   
   
  0.557
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 [...] (572 aa)
     
   
  0.556
Your Current Organism:
Klebsiella pneumoniae
NCBI taxonomy Id: 573
Other names: ATCC 13883, Bacillus pneumoniae, Bacterium pneumoniae crouposae, CCUG 225, CIP 82.91, DSM 30104, HAMBI 450, Hyalococcus pneumoniae, IFO 14940, K. pneumoniae, Klebsiella pneumoniae, Klebsiella sp. M-AI-2, Klebsiella sp. PB12, Klebsiella sp. RCE-7, LMG 2095, NBRC 14940, NCTC 9633
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