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
glyQglycyl-tRNA synthetase alpha subunit (glyQ); Psort: bacterial cytoplasm --- Certainty= 0.269(Affirmative); COG0752 GlyQ glycyl-tRNA synthetase, alpha subunit. (283 aa)    
Predicted Functional Partners:
glyS
glycyl-tRNA synthetase beta chain (glyS); Psort: bacterial inner membrane --- Certainty= 0.179(Affirmative); COG0751 GlyS glycyl-tRNA synthetase, beta subunit.
  0.999
hisS
Histidyl tRNA synthetase (hisS); Psort: bacterial cytoplasm --- Certainty= 0.492(Affirmative); COG0124 hisS histidyl-tRNA synthetase.
  
  
 0.788
pheS
Phenylalanyl tRNA synthetase alpha subunit (pheS); Psort: bacterial cytoplasm --- Certainty= 0.102(Affirmative); COG0016 PheS phenylalanyl-tRNA synthetase alpha subunit.
   
  
 0.707
alaS
alanyl-tRNA synthetase (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.
   
  
 0.692
guaA
GMP synthase (glutamine-hydrolyzing) (guaA); Catalyzes the synthesis of GMP from XMP.
  
    0.649
aspS
aspartyl-tRNA synthetase (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.
  
  
 0.628
dnaJ
DNAJ protein (dnaJ); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK [...]
     
 0.618
valS
valyl-tRNA synthetase (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.
   
  
 0.616
trmD
tRNA (guanine-N1)-methyltransferase (trmD); Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family.
  
    0.599
pheT
phenylalanyl-tRNA synthetase beta chain (pheT); Psort: bacterial inner membrane --- Certainty= 0.193(Affirmative); COG0072 PheT phenylalanyl-tRNA synthetase beta subunit.
   
  
 0.582
Your Current Organism:
Anaplasma marginale
NCBI taxonomy Id: 320483
Other names: A. marginale str. Florida, Anaplasma marginale str. Florida, Anaplasma marginale strain Florida
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.