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:
some 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
pheTBelongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily (792 aa)    
Predicted Functional Partners:
pheS
Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily
 0.999
aspS
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Is 1.5 times more efficient at aminoacylating E.coli tRNA(Asp) over tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn)
   
 
 0.997
alaS
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
 
 
 0.996
thrS
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)
  
 
 0.988
glyQ
glyQ: glycine--tRNA ligase, alpha subunit
 
  
 0.970
guaA
Catalyzes the synthesis of GMP from XMP
  
 
 0.968
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).
  
 
 0.967
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)
  
 
 0.958
argS
argS: arginine--tRNA ligase
  
 
 0.956
trpS
Catalyzes the attachment of tryptophan to tRNA(Trp).
  
  
 0.955
Your Current Organism:
Pseudomonas aeruginosa
NCBI taxonomy Id: 287
Other names: ATCC 10145, ATCC 10145-U, Bacillus aeruginosus, Bacillus pyocyaneus, Bacterium aeruginosum, Bacterium pyocyaneum, CCEB 481, CCUG 28447, CCUG 29297, CCUG 551, CFBP 2466, CIP 100720, DSM 50071, IBCS 277, IFO 12689, JCM 5962, Micrococcus pyocyaneus, NBRC 12689, NCCB 76039, NCIB 8295, NCIMB 8295, NCTC 10332, NRRL B-771, P. aeruginosa, Pseudomonas polycolor, Pseudomonas pyocyanea, Pseudomonas sp. RV3, RH 815, VKM B-588, bacterium ASFP-37, bacterium ASFP-38, bacterium ASFP-45, bacterium ASFP-46, bacterium ASFP-48
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