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
valSValyl-tRNA synthetase (Valine--tRNA ligase) (ValRS); 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. (872 aa)    
Predicted Functional Partners:
leuS
Leucyl-tRNA synthetase (Leucine--tRNA ligase) (LeuRS); Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
0.934
thrS
Threonyl-tRNA synthetase (Threonine--tRNA ligase) (ThrRS); ATP + L-Threonine + tRNA(Thr) <=> AMP + Pyrophosphate + L-Threonyl-tRNA(Thr); Belongs to the class-II aminoacyl-tRNA synthetase family.
 
  
 0.891
argS
Arginyl-tRNA synthetase (Arginine--tRNA ligase) (ArgRS); ATP + L-Arginine + tRNA(Arg) <=> AMP + Pyrophosphate + L-Arginyl-tRNA(Arg).
 
  
 0.885
guaA
GMP synthase [glutamine-hydrolyzing] (Glutamine amidotransferase) (GMP synthetase); Catalyzes the synthesis of GMP from XMP.
  
  
 0.862
ileS
Isoleucyl-tRNA synthetase (Isoleucine--tRNA ligase); 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 2 subfamily.
  
 
0.859
pheT
Phenylalanyl-tRNA synthetase beta chain (Phenylalanine--tRNA ligase beta chain) (PheRS); ATP + L-Phenylalanine + tRNA(Phe) <=> AMP + Pyrophosphate + L-Phenylalanyl-tRNA(Phe); Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
  
 0.856
hisS
Histidyl-tRNA synthetase (Histidine--tRNA ligase) (HisRS).
 
 
 0.852
cysS2
Cysteinyl-tRNA synthetase (Cysteine--tRNA ligase); ATP + L-Cysteine + tRNA(Cys) <=> AMP + Pyrophosphate + L-Cysteinyl-tRNA(Cys); Belongs to the class-I aminoacyl-tRNA synthetase family.
 
  
 0.834
tyrS
Tyrosyl-tRNA synthetase (Tyrosine--tRNA ligase) (TyrRS); 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 1 subfamily.
 
  
 0.832
alaS
Alanyl-tRNA synthetase (Alanine--tRNA ligase) (AlaRS); 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.
 
  
 0.825
Your Current Organism:
Propionibacterium freudenreichii
NCBI taxonomy Id: 754252
Other names: P. freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii ATCC 9614, Propionibacterium freudenreichii subsp. shermanii CIP 103027, Propionibacterium freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii str. CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii strain CIRM-BIA1
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