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
hisShistidine--tRNA ligase; KEGG: ols:Olsu_1380 1.8e-161 histidyl-tRNA synthetase K01892; Psort location: Cytoplasmic, score: 10.00. (439 aa)    
Predicted Functional Partners:
valS
valine--tRNA ligase; 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.
 
 
 0.823
aspS
aspartate--tRNA ligase; 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.
 
  
 0.820
lysS
lysine--tRNA ligase; KEGG: ols:Olsu_1638 7.5e-211 lysyl-tRNA synthetase K04567; Psort location: Cytoplasmic, score: 10.00; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 
 0.817
thrS
threonine--tRNA ligase; KEGG: ols:Olsu_0800 9.5e-259 Ser-tRNA(Thr) hydrolase; threonyl-tRNA synthetase K01868; Psort location: Cytoplasmic, score: 10.00; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 
 0.806
KXG88350.1
KEGG: ols:Olsu_1566 2.5e-148 ribose-phosphate pyrophosphokinase K00948; Psort location: Cytoplasmic, score: 9.97.
  
 
 0.787
fmt
methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family.
 
  
 0.763
guaA
GMP synthase domain protein; Catalyzes the synthesis of GMP from XMP.
  
  
 0.739
KXG88858.1
KEGG: pdn:HMPREF9137_0030 1.9e-166 class I/II aminotransferase; Psort location: Cytoplasmic, score: 7.50.
  
 
 0.723
glyQ
glycine--tRNA ligase, alpha subunit; KEGG: apv:Apar_0693 2.9e-138 glyQ; glycyl-tRNA synthetase subunit alpha K01878; Psort location: Cytoplasmic, score: 9.97.
  
  
 0.700
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.
  
 
 0.698
Your Current Organism:
Atopobium vaginae
NCBI taxonomy Id: 82135
Other names: A. vaginae, ATCC BAA-55, ATCC:BAA 55, ATCC:BAA:55, CCUG 38953, CIP 106431, DSM 15829, NCTC 13935
Server load: low (40%) [HD]