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
thrSthrS 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charged glycyl-tRNA(Gly), but neither glycyl-tRNA(Gly)(2'-dA76) (the terminal 2'-OH of tRNA(Thr) adenine 76 has been replaced by hydrogen) nor the 2'-fluoro tRNA derivative do so, strongly suggesting the editing function is tRNA catalyzed.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 [...] (625 aa)    
Predicted Functional Partners:
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).
 
 
 0.953
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.
 
  
 0.939
leuS
leuS leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 
 0.937
hisS
hisS histidyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family.
 
 
 0.923
rpl11
rpl11P LSU ribosomal protein L11P; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors; Belongs to the universal ribosomal protein uL11 family.
 
 
 0.896
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.
 
 
 0.893
pheS
pheS phenylalanyl-tRNA synthetase, subunit alpha; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
 
 
 0.887
pheT
pheT phenylalanyl-tRNA synthetase, subunit beta.
 
 
 0.885
rps15P
rps15P SSU ribosomal protein S15P.
  
 
 0.880
ndk
Ndk nucleoside diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
  
 
 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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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.