STRINGSTRING
leuS leuS pheT pheT gltX gltX ileS ileS valS valS metS metS argS argS thrS thrS cysS cysS infB infB fus fus
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 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
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textmining
co-expression
protein homology
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Score
leuSleuS leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (967 aa)    
Predicted Functional Partners:
pheT
pheT phenylalanyl-tRNA synthetase, subunit beta.
 
  
 0.966
gltX
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).
 0.960
ileS
ileS isoleucyl-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.
 
0.952
valS
valS valyl-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 2 subfamily.
  
 
0.950
metS
metS 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.
  
0.950
argS
argS arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 0.937
thrS
thrS threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr) (Probable). Edits incorrectly charged L-seryl-tRNA(Thr) via its editing domain. Deacylates correctly charged glycyl-tRNA(Gly), but neither glycyl-tRNA(Gly)(2'-dA76) (the terminal 2'-OH of tRNA(Thr) adenine 76 has been replaced by hydrogen) nor the 2'-fluoro tRNA derivative do so, strongly suggesting the editing function is tRNA catalyzed. Belongs to the class-II aminoacyl-tR [...]
 
 
 0.937
cysS
cysS cysteinyl-tRNA synthetase.
  
 
 0.919
infB
infB intein containing translation initiation factor aIF-2; Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2 (By similarity).
 
 
 0.889
fus
Fus translation elongation factor EF-2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity); Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTP [...]
 
 
 0.874
Your Current Organism:
Pyrococcus abyssi
NCBI taxonomy Id: 272844
Other names: P. abyssi GE5, Pyrococcus abyssi GE5, Pyrococcus abyssi str. GE5, Pyrococcus abyssi str. Orsay, Pyrococcus abyssi strain GE5
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