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
tyrStyrosyl-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 1 subfamily. (416 aa)    
Predicted Functional Partners:
metG
methionyl-tRNA synthetase (metG); Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
  
 0.993
argS
arginyl-tRNA synthetase (argS); Similar to GB:AE000783 percent identity: 43.07; identified by sequence similarity; putative.
 
  
 0.913
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.
  
  
 0.887
pheT
phenylalanyl-tRNA synthetase beta subunit (pheT); Similar to GP:1785608 percent identity: 39.93; identified by sequence similarity; putative.
  
  
 0.855
pheS
phenylalanyl-tRNA synthetase alpha subunit (pheS); Similar to SP:P94282 PID:1785607 GB:AE000783 percent identity: 49.61; identified by sequence similarity; putative; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
  
  
 0.840
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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and invol [...]
  
  
 0.827
glyQS
glycyl-tRNA synthetase (glyS); Catalyzes the attachment of glycine to tRNA(Gly). Belongs to the class-II aminoacyl-tRNA synthetase family.
  
  
 0.825
prfA
Peptide chain release factor 1 (prfA); Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
  
  
 0.818
tsf
Translation elongation factor TS (tsf); Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity); Belongs to the EF-Ts family.
  
 
 0.806
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).
  
  
 0.794
Your Current Organism:
Treponema pallidum
NCBI taxonomy Id: 243276
Other names: T. pallidum subsp. pallidum str. Nichols, Treponema pallidum Nichols, Treponema pallidum subsp. pallidum str. Nichols
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