Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
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[Homology]
Score
glySglycine-tRNA synthetase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology. (688 aa)    
Predicted Functional Partners:
KOH23762.1
glycyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.999
ileS
isoleucine--tRNA ligase; IleRS; catalyzes the formation of isoleucyl-tRNA(Ile) from isoleucine and tRNA(Ile); since isoleucine and other amino acids such as valine are similar, there are additional editing function in this enzyme; one is involved in hydrolysis of activated valine-AMP and the other is involved in deacylation of mischarged Val-tRNA(Ile); there are two active sites, one for aminoacylation and one for editing; class-I aminoacyl-tRNA synthetase family type 1 subfamily; some organisms carry two different copies of this enzyme; Derived by automated computational analysis usin [...]
 
  
 0.877
leuS
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 automated computational [...]
  
  
 0.876
KOH20658.1
valyl-tRNA synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.848
KOH18567.1
alanyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.848
KOH21229.1
aspartyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.769
proS
proline--tRNA ligase; Catalyzes the formation of prolyl-tRNA(Pro) from proline and tRNA(Pro); Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.767
thrS
threonine--tRNA ligase; Catalyzes a two-step reaction, first charging a threonine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; catalyzes the formation of threonyl-tRNA(Thr) from threonine and tRNA(Thr); Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.738
trmD
Methylates guanosine-37 in various tRNAs; uses S-adenosyl-L-methionine to transfer methyl group to tRNA; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.671
pheT
phenylalanine--tRNA ligase; 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.
  
  
 0.651
Your Current Organism:
Vibrio parahaemolyticus
NCBI taxonomy Id: 670
Other names: ATCC 17802, Beneckea parahaemolytica, CAIM 320, CCUG 14474, CCUG 15657, CCUG 4224, CIP 75.2, DSM 10027, IFO 12711, LMG 2850, LMG:2850, NBRC 12711, NCCB 77010, NCCB 77018, NCTC 10903, NRRL B-4167, Oceanomonas parahaemolytica, Pasteurella parahaemolytica, V. parahaemolyticus
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