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
metGmethionyl-tRNA synthetase (metS); Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (658 aa)    
Predicted Functional Partners:
leuS
leucyl-tRNA synthetase (leuS); Similar to GB:L77117 SP:Q58050 PID:1591345 percent identity: 49.68; identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
0.986
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.
 
 0.981
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).
 
 0.966
gltX
glutamyl-tRNA synthetase (gltX); Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
 
 0.964
ileS
isoleucyl-tRNA synthetase (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). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.
 
0.964
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.
 
 
 0.928
AF_2112
5-methyltetrahydropteroyltriglutamate- homocysteine methyltransferase (metE); Similar to PID:1103707 SP:P55299 percent identity: 28.08; identified by sequence similarity; putative.
    
 0.916
proS
prolyl-tRNA synthetase (proS); Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
 
 0.912
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.
 
 0.873
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). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain.
 
  
 0.863
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: low (34%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.