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
proSprolyl-tRNA synthetase; 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). (478 aa)    
Predicted Functional Partners:
ileS
isoleucyl-tRNA synthetase; 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.
  
 0.987
glnS
glutaminyl-tRNA synthetase; Identified by match to protein family HMM PF00749; match to protein family HMM PF03950; match to protein family HMM TIGR00440.
 
 0.980
metG
methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
  
 0.966
argS
arginyl-tRNA synthetase; Identified by match to protein family HMM PF00750; match to protein family HMM PF03485; match to protein family HMM PF05746; match to protein family HMM TIGR00456.
 
 0.961
ABK61949.1
Flagellar switch protein FliY, contains CheC-like domain; Identified by match to protein family HMM PF01052; match to protein family HMM PF04509.
   
   0.919
asnS
asparaginyl-tRNA synthetase; Identified by match to protein family HMM PF00152; match to protein family HMM PF01336; match to protein family HMM TIGR00457.
  
 0.917
leuS
leucyl-tRNA synthetase; Identified by match to protein family HMM PF00133; match to protein family HMM TIGR00396; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 0.891
gltX
glutamyl-tRNA synthetase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
  
 0.869
lysS
lysyl-tRNA synthetase; Identified by match to protein family HMM PF00152; match to protein family HMM PF01336; match to protein family HMM TIGR00499; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 0.841
pheT
phenylalanyl-tRNA synthetase, beta subunit; Identified by match to protein family HMM PF01588; match to protein family HMM PF03147; match to protein family HMM PF03483; match to protein family HMM PF03484; match to protein family HMM TIGR00472; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
 
 0.802
Your Current Organism:
Clostridium novyi
NCBI taxonomy Id: 386415
Other names: C. novyi NT, Clostridium novyi NT, Clostridium novyi str. NT, Clostridium novyi strain NT, Clostridium novyi-NT
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.