close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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; ValRS; converts valine ATP and tRNA(Val) to AMP PPi and valyl-tRNA(Val); class-I aminoacyl-tRNA synthetase type 1 subfamily; has a posttransfer editing process to hydrolyze mischarged Thr-tRNA(Val) which is done by the editing domain; Derived by automated computational analysis using gene prediction method: Protein Homology. (876 aa)    
Predicted Functional Partners:
fgs_1
Folylpolyglutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.920
leuS_4
leucyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
0.907
ileS
isoleucine--tRNA ligase; IleRS; catalyzes the formation of isoleucyl-tRNA(Ile) from isoleucine and tRNA(Ile); since isoleucine and other amino acids such as valine are similar, there are additional editing function in this enzyme; one is involved in hydrolysis of activated valine-AMP and the other is involved in deacylation of mischarged Val-tRNA(Ile); there are two active sites, one for aminoacylation and one for editing; class-I aminoacyl-tRNA synthetase family type 1 subfamily; some organisms carry two different copies of this enzyme; Derived by automated computational analysis usin [...]
 
0.905
guaA_1
GMP synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.878
aspS
aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
 
  
 0.874
alaS
alanine--tRNA ligase; 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; Belongs to the class-II aminoacyl-tRNA synthetase family.
 
  
 0.867
KIR10772.1
Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
  
   0.785
pheT_3
phenylalanyl-tRNA synthase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.745
hisS_1
histidyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.743
thrS
threonyl-tRNA synthase; 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).
 
  
 0.741
Your Current Organism:
Staphylococcus gallinarum
NCBI taxonomy Id: 1293
Other names: ATCC 35539, CCM 3572, CCUG 15600, CIP 103504, DSM 20610, LMG 19121, LMG:19121, NCTC 12195, NRRL B-14763, S. gallinarum, strain VIII1
Server load: low (30%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.