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leuS leuS ileS ileS metG metG pheT pheT argS argS gltX2 gltX2 proS proS valS valS gltX1 gltX1 Dshi_1474 Dshi_1474 gst2 gst2
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query proteins and first shell of interactors
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second shell of interactors
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Known Interactions
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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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leuSTIGRFAM: leucyl-tRNA synthetase KEGG: sil:SPO3432 leucyl-tRNA synthetase; tRNA synthetases class I (I, L, M and V); Belongs to the class-I aminoacyl-tRNA synthetase family. (869 aa)    
Predicted Functional Partners:
ileS
isoleucyl-tRNA synthetase; 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 1 subfamily.
 
0.974
metG
methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
  
 0.973
pheT
KEGG: rde:RD1_1013 phenylalanyl-tRNA synthetase, beta subunit TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit.
  
  
 0.936
argS
SWISSPROT Q5LQI6: Arginyl-tRNA synthetase; TIGRFAM: TIGR00456 arginyl-tRNA synthetase; PFAM: PF03485, PF05746, PF00750; PROSITE: PS00177, PS00178.
  
 0.931
gltX2
glutamyl-tRNA synthase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
  
 0.926
proS
prolyl-tRNA synthetase; 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); Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 2 subfamily.
 
 0.915
valS
valyl-tRNA synthetase; 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.
   
 
0.910
gltX1
glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
  
 0.902
Dshi_1474
Similar to Glutamyl-Q tRNA(Asp) synthetase which catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp); Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 0.892
gst2
PFAM: Glutathione S-transferase domain KEGG: pde:Pden_2769 glutathione S-transferase, N-terminal domain and C-terminal domain; Thioredoxin fold.
  
 0.876
Your Current Organism:
Dinoroseobacter shibae
NCBI taxonomy Id: 398580
Other names: D. shibae DFL 12 = DSM 16493, Dinoroseobacter shibae DFL 12, Dinoroseobacter shibae DFL 12 = DSM 16493, Dinoroseobacter shibae DSM 16493, Dinoroseobacter shibae DSM 16493 = DFL 12, Jannaschia sp. DFL-12
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