STRINGSTRING
trpS trpS ileS ileS thrS thrS leuS leuS trpA trpA pheT pheT aspS aspS serS serS trpB trpB amn amn argS argS
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
trpSTRYPTOPHAN TRNA SYNTHETASE; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (345 aa)    
Predicted Functional Partners:
ileS
ISOLEUCINE-TRNA LIGASE-LIKE PROTEIN; 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.
 
 
 0.911
thrS
THREONYL-TRNA SYNTHETASE; 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).
  
  
 0.841
leuS
LEUCYL-TRNA SYNTHETASE; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
 0.835
trpA
TRYPTOPHAN SYNTHASE ALPHA CHAIN; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family.
  
  
 0.831
pheT
PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
  
 0.815
aspS
PROBABLE ASPARTYL-TRNA SYNTHETASE PROTEIN; 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.
  
  
 0.777
serS
SERYL-TRNA SYNTHETASE; 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).
  
 
 0.762
trpB
TRYPTOPHAN SYNTHASE BETA CHAIN; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
  
  
 0.726
amn
AMP NUCLEOSIDASE; Catalyzes the hydrolysis of the N-glycosidic bond of AMP to form adenine and ribose 5-phosphate. Involved in regulation of AMP concentrations.
  
  
 0.724
argS
ARGINYL-TRNA SYNTHETASE; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
  
 0.703
Your Current Organism:
Corynebacterium glutamicum
NCBI taxonomy Id: 196627
Other names: C. glutamicum ATCC 13032, Corynebacterium glutamicum ATCC 13032, Corynebacterium glutamicum str. ATCC 13032, Corynebacterium glutamicum strain ATCC 13032
Server load: low (8%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.