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
valSvaline--tRNA ligase ValS; 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; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. (947 aa)    
Predicted Functional Partners:
guaA
GMP synthase; Catalyzes the synthesis of GMP from XMP.
  
  
 0.902
ileS
isoleucine--tRNA ligase 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).
 
 
0.901
alaS
alanine--tRNA ligase 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.
 
  
 0.901
leuS
leucine--tRNA ligase LeuS; Region:COG0495J; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
0.888
aspS
aspartate--tRNA ligase AspS; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
  
 0.875
thrS
threonine--tRNA ligase 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).
 
  
 0.847
serS
serine--tRNA ligase SerS; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec).
 
  
 0.828
glyS
glycine--tRNA ligase beta subunit GlyS; Region:COG0751J.
  
  
 0.826
pheT
phenylalanine--tRNA ligase subunit beta; Region:COG0072J; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
  
 0.792
argS
arginine--tRNA ligase ArgS; Region:COG0018J.
  
  
 0.767
Your Current Organism:
Sinorhizobium americanum
NCBI taxonomy Id: 194963
Other names: ATCC BAA-532, CIP 108390, DSM 15007, Ensifer americanum, Ensifer americanus, Ensifer americanus corrig. (Toledo et al. 2003) Wang et al. 2015, Ensifer sp. AC14c, Ensifer sp. CFNEI 156, S. americanum, Sinorhizobium americanum Toledo et al. 2004, Sinorhizobium americanus, Sinorhizobium sp. CFNEI 156, Sinorhizobium sp. CFNEI 54, strain CFNEI 156
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.