STRINGSTRING
ileS ileS proS proS argS argS pheT pheT valS valS tyrS tyrS lspA lspA leuS leuS ribF ribF gltX gltX asnS asnS
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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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ileSIsoleucine 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 1 subfamily. (938 aa)    
Predicted Functional Partners:
proS
Proline 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). 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 involves de [...]
  
 0.989
argS
Arginine tRNA synthetase; Code: J; COG: COG0018.
  
 0.953
pheT
Phenylalanine tRNA synthetase, beta-subunit; Code: J; COG: COG0072; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
 
 0.946
valS
Valine tRNA synthetase; 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 1 subfamily.
 
 
0.919
tyrS
Tyrosine tRNA synthetase; 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.
  
  
 0.918
lspA
Prolipoprotein signal peptidase; This protein specifically catalyzes the removal of signal peptides from prolipoproteins; Belongs to the peptidase A8 family.
 
  
 0.916
leuS
Leucine tRNA synthetase; Code: J; COG: COG0495; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
0.916
ribF
Putative regulator; Code: H; COG: COG0196; Belongs to the ribF family.
 
   0.893
gltX
Glutamate tRNA synthetase, catalytic subunit; 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).
 
 0.890
asnS
Asparagine tRNA synthetase; Code: J; COG: COG0017.
   
 0.888
Your Current Organism:
Shigella dysenteriae
NCBI taxonomy Id: 300267
Other names: S. dysenteriae Sd197, Shigella dysenteriae Sd197, Shigella dysenteriae str. Sd197, Shigella dysenteriae strain Sd197
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