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STRINGSTRING
STRING protein interaction network
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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
tyrStyrosyl-tRNA synthetase TyrS; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily. (398 aa)    
Predicted Functional Partners:
pheT
phenylalanyl-tRNA synthetase beta subunit PheT; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
 
  
 0.926
metG
methionyl-tRNA synthetase MetG; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
  
 
 0.833
ydiA
Putative phosphotransferase YdiA; Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation.
      
 0.794
pheS
phenylalanyl-tRNA synthetase alpha subunit PheS; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
 
  
 0.768
argS
arginyl-tRNA synthetase ArgS.
  
  
 0.763
tsf
Translation elongation factor EF-Ts Tsf; Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. Belongs to the EF-Ts family.
  
 
 0.758
ileS
isoleucyl-tRNA synthetase IleS; 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.
  
  
 0.745
prfA
Peptide chain release factor 1 PrfA; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
  
  
 0.745
uvrD
DNA helicase II UvrD.
   
  
 0.735
proS
prolyl-tRNA synthetase ProS; 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 involve [...]
 
  
 0.728
Your Current Organism:
Shewanella oneidensis
NCBI taxonomy Id: 211586
Other names: S. oneidensis MR-1, Shewanella oneidensis ATCC 700550, Shewanella oneidensis MR-1, Shewanella oneidensis str. MR-1, Shewanella oneidensis strain MR-1, Shewanella sp. MR-1
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