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 2 subfamily. (1220 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).
  
 0.987
argS
arginine--tRNA ligase; KEGG: pmz:HMPREF0659_A6251 1.7e-282 argS; arginine--tRNA ligase K01887; Psort location: Cytoplasmic, score: 9.97.
 
 0.975
pheT
KEGG: pmz:HMPREF0659_A6941 0. pheT; phenylalanine--tRNA ligase, beta subunit K01890; Psort location: Cytoplasmic, score: 9.97; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
 
 0.974
metG
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.
 
 0.967
leuS
leucine--tRNA ligase; KEGG: pmz:HMPREF0659_A5028 0. leuS; leucine--tRNA ligase K01869; Psort location: Cytoplasmic, score: 9.97; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
0.961
lysS
lysine--tRNA ligase; KEGG: pmz:HMPREF0659_A6046 3.4e-286 lysS; lysine--tRNA ligase K04567; Psort location: Cytoplasmic, score: 10.00; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 0.901
lspA
Signal peptidase II family protein; This protein specifically catalyzes the removal of signal peptides from prolipoproteins; Belongs to the peptidase A8 family.
 
  
 0.898
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.
  
0.880
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.
 
 0.869
KXB78291.1
glutamine--tRNA ligase; KEGG: pmz:HMPREF0659_A6665 6.4e-285 glnS; glutamine--tRNA ligase K01886; Psort location: Cytoplasmic, score: 9.97.
 
 0.855
Your Current Organism:
Prevotella amnii
NCBI taxonomy Id: 419005
Other names: CCUG 53648, DSM 23384, JCM 14753, P. amnii, Prevotella amnii Lawson et al. 2008 emend. Hahnke et al. 2016
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.