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
ileSisoleucyl-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. (1050 aa)    
Predicted Functional Partners:
proS
prolyl-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 dea [...]
   
 0.994
leuS
TIGRFAM: leucyl-tRNA synthetase; KEGG: gsu:GSU2209 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
0.988
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).
  
 0.981
pheT
KEGG: ade:Adeh_1971 phenylalanyl-tRNA synthetase beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit.
  
 
 0.978
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.
  
 0.974
argS
arginyl-tRNA synthetase; KEGG: scl:sce7660 hypothetical protein; TIGRFAM: arginyl-tRNA synthetase.
 
 0.964
lysS
TIGRFAM: lysyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; KEGG: bsu:BSU00820 lysyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 0.957
Tbis_0877
DALR anticodon binding domain protein; KEGG: mno:Mnod_2178 arginyl-tRNA synthetase.
  
 0.949
thrS
TIGRFAM: threonyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); TGS domain protein; Anticodon-binding domain protein; Threonyl/alanyl tRNA synthetase SAD; KEGG: mgm:Mmc1_0363 threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family.
 
 
 0.865
tyrS
tyrosyl-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.
  
  
 0.850
Your Current Organism:
Thermobispora bispora
NCBI taxonomy Id: 469371
Other names: T. bispora DSM 43833, Thermobispora bispora ATCC 19993, Thermobispora bispora DSM 43833, Thermobispora bispora str. DSM 43833, Thermobispora bispora strain DSM 43833
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