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
ileSisoleucine--tRNA ligase; 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. (941 aa)    
Predicted Functional Partners:
proS
proline--tRNA ligase; 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).
   
 0.991
pheT
KEGG: ral:Rumal_2370 3.2e-251 phenylalanyl-tRNA synthetase subunit beta; K01890 phenylalanyl-tRNA synthetase beta chain; Psort location: Cytoplasmic, score: 9.97.
  
 
 0.987
ERJ97098.1
methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
0.986
argS
arginine--tRNA ligase; KEGG: ral:Rumal_2414 5.5e-176 arginyl-tRNA synthetase K01887; Psort location: Cytoplasmic, score: 9.97.
 
 0.985
gltX
glutamate--tRNA ligase; 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.
  
 0.983
leuS
leucine--tRNA ligase; KEGG: ccl:Clocl_1028 0. leucyl-tRNA synthetase K01869; Psort location: Cytoplasmic, score: 9.97; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
0.979
lysS
lysine--tRNA ligase; KEGG: ral:Rumal_1087 8.4e-164 lysyl-tRNA synthetase; K04567 lysyl-tRNA synthetase, class II; Psort location: Cytoplasmic, score: 10.00; Belongs to the class-II aminoacyl-tRNA synthetase family.
 
 0.955
gatB-2
aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily.
   
 0.906
valS
valine--tRNA ligase; 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.
 
0.900
lspA
Signal peptidase II; This protein specifically catalyzes the removal of signal peptides from prolipoproteins; Belongs to the peptidase A8 family.
  
  
 0.877
Your Current Organism:
Ruminococcus callidus
NCBI taxonomy Id: 411473
Other names: R. callidus ATCC 27760, Ruminococcus callidus ATCC 27760
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