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leuS protein (Idiomarina loihiensis) - STRING interaction network
"leuS" - Leucyl-tRNA synthetase in Idiomarina loihiensis
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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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Cooccurence
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[Homology]
Score
leuSLeucyl-tRNA synthetase (858 aa)    
Predicted Functional Partners:
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). 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 dea [...] (567 aa)
 
  0.982
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 (677 aa)
   
  0.978
argS
Arginyl-tRNA synthetase (580 aa)
   
  0.949
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) (944 aa)
 
0.942
alaS
Alanyl-tRNA synthetase; 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 (865 aa)
   
 
  0.928
fusA
Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (707 aa)
 
   
  0.915
lysS
lysyl-tRNA synthetase (503 aa)
   
  0.911
lptE
Rare lipoprotein B; Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane (164 aa)
   
   
  0.908
holA
DNA polymerase III subunit delta (360 aa)
   
   
  0.905
thrS
Threonyl-tRNA synthetase (638 aa)
   
   
  0.902
Your Current Organism:
Idiomarina loihiensis
NCBI taxonomy Id: 283942
Other names: I. loihiensis, I. loihiensis L2TR, Idiomarina loihiensis, Idiomarina loihiensis Donachie et al. 2003, Idiomarina loihiensis L2TR, Idiomarina loihiensis str. L2TR, Idiomarina loihiensis strain L2TR
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