STRINGSTRING
pheT pheT pheS pheS rpsB rpsB leuS leuS ileS ileS purL purL rplO rplO rpoB rpoB guaB guaB metG metG thrS thrS
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
pheTphenylalanyl-tRNA synthetase, beta subunit; Product name confidence: Class 2 (High similarity to functionally studied protein); Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (792 aa)    
Predicted Functional Partners:
pheS
phenylalanyl-tRNA synthetase, alpha-subunit; Product name confidence: Class 2 (High similarity to functionally studied protein); Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
 
 0.999
rpsB
30S ribosomal protein S2; Product name confidence: Class 2 (High similarity to functionally studied protein); Belongs to the universal ribosomal protein uS2 family.
 
 
 0.973
leuS
leucyl-tRNA synthetase; Product name confidence: Class 2 (High similarity to functionally studied protein); Belongs to the class-I aminoacyl-tRNA synthetase family.
 
  
 0.973
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.
  
 
 0.969
purL
Phosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.
  
  
 0.966
rplO
50S ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
  
  
 0.954
rpoB
DNA-directed RNA polymerase beta chain; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
 
  
 0.947
guaB
Inosine-5'-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
  
  
 0.942
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.
  
  
 0.937
thrS
threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
 
 
 0.933
Your Current Organism:
Pseudomonas aeruginosa
NCBI taxonomy Id: 208964
Other names: P. aeruginosa PAO1, Pseudomonas aeruginosa PAO1, Pseudomonas sp. PAO1
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