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
serSseryl-tRNA synthetase (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). (453 aa)    
Predicted Functional Partners:
sepS
Conserved hypothetical protein; Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys); Belongs to the class-II aminoacyl-tRNA synthetase family. O-phosphoseryl-tRNA(Cys) synthetase subfamily.
  
 
 0.971
argS
arginyl-tRNA synthetase (argS); Similar to GB:L77117 SP:Q57689 PID:1590971 percent identity: 48.77; identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 
 0.924
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; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 2 subfamily.
 
  
 0.919
cysS
cysteinyl-tRNA synthetase (cysS); Similar to GB:D26185 SP:Q06752 GB:L14580 GB:X73989 PID:289284 percent identity: 46.12; identified by sequence similarity; putative.
 
 
 0.917
trpS
tryptophanyl-tRNA synthetase (trpS); Similar to GB:L77117 SP:Q58810 PID:1592065 percent identity: 52.41; identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
 0.908
thrS
threonyl-tRNA synthetase (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). Also edits incorrectly charged L-seryl-tRNA(Thr) (By similarity); Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 
 0.865
hisS
histidyl-tRNA synthetase (hisS); Similar to GB:L77117 SP:Q58406 PID:1591660 percent identity: 45.97; identified by sequence similarity; putative; Belongs to the class-II aminoacyl-tRNA synthetase family.
 
 
 0.861
tyrS
tyrosyl-tRNA synthetase (tyrS); 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 3 subfamily.
  
  
 0.860
glyS
glycyl-tRNA synthetase (glyS); Catalyzes the attachment of glycine to tRNA(Gly).
   
  
 0.853
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).
 
 
 0.853
Your Current Organism:
Archaeoglobus fulgidus
NCBI taxonomy Id: 224325
Other names: A. fulgidus DSM 4304, Archaeoglobus fulgidus DSM 4304, Archaeoglobus fulgidus VC-16, Archaeoglobus fulgidus str. DSM 4304, Archaeoglobus fulgidus strain DSM 4304
Server load: medium (44%) [HD]