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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colored nodes:
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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from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
trpS-2tryptophan--tRNA ligase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (337 aa)    
Predicted Functional Partners:
trpS
tryptophan--tRNA ligase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family.
  
  
 
0.905
leuS
leucine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
 0.825
pheT
phenylalanine--tRNA ligase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
  
 0.783
ANB08139.1
Phosphoesterase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.757
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). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.
  
 
 0.723
trpE
Anthranilate synthase; Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.
     
 0.712
alaS
alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
  
 
 0.697
thrS
threonine--tRNA ligase; Catalyzes the formation of threonyl-tRNA(Thr) from threonine and tRNA(Thr); 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; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
  
 0.681
ANB08136.1
Glutathionylspermidine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.673
ANB08135.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.665
Your Current Organism:
Streptomyces ambofaciens
NCBI taxonomy Id: 1889
Other names: ATCC 23877, BCRC 11857, CBS 616.68, CCRC 11857, CCRC:11857, CECT 3101, DSM 40053, IFO 12836, ISP 5053, JCM 4204, JCM 4618, KCTC 9111, NBRC 12836, NRRL 2420, NRRL B-2516, NRRL-ISP 5053, S. ambofaciens
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