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ileS protein (Methylobacter tundripaludum) - STRING interaction network
"ileS" - Isoleucine--tRNA ligase in Methylobacter tundripaludum
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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 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) (943 aa)    
Predicted Functional Partners:
lspA
Lipoprotein signal peptidase; This protein specifically catalyzes the removal of signal peptides from prolipoproteins; Belongs to the peptidase A8 family (169 aa)
 
   
  0.986
Mettu_1554
Riboflavin biosynthesis protein; TIGRFAM- Riboflavin kinase/FAD synthetase; Cytidyltransferase-related; KEGG- saz-Sama_0923 riboflavin biosynthesis protein RibF; PFAM- FAD synthetase; Riboflavin kinase; Belongs to the ribF family (327 aa)
 
   
  0.981
leuS
Leucine--tRNA ligase; TIGRFAM- Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; KEGG- tgr-Tgr7_2279 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family (832 aa)
 
0.973
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). 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 deacy [...] (569 aa)
   
  0.955
lysS
Lysine--tRNA ligase; PFAM- Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; TIGRFAM- Lysyl-tRNA synthetase, class II; HAMAP- Lysyl-tRNA synthetase; KEGG- nhl-Nhal_2437 lysyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family (499 aa)
   
  0.954
alaS
Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain (870 aa)
 
 
  0.953
pheT
TIGRFAM- Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; HAMAP- Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG- mca-MCA0698 phenylalanyl-tRNA synthetase, beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily (791 aa)
   
 
  0.946
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; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily (672 aa)
   
  0.943
argS
Arginine--tRNA ligase; TIGRFAM- Arginyl-tRNA synthetase, class Ic; HAMAP- Arginyl-tRNA synthetase, class Ic; KEGG- mca-MCA3089 arginyl-tRNA synthetase (586 aa)
 
  0.943
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 (931 aa)
 
0.918
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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