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
alaSalanyl-tRNA synthetase; 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. (868 aa)    
Predicted Functional Partners:
PSHAa2902
Homologs of previously reported genes of unknown function; 11347268, 14672542.
   
 0.955
aspS
Aspartate tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
 0.899
lysC
Aspartokinase; Function of strongly homologous gene; enzyme; Belongs to the aspartokinase family.
  
    0.893
valS
Valine 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 1 subfamily.
 
  
 0.887
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).
  
 
 0.878
pheT
Phenylalanine tRNA synthetase, beta-subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
 
 
 0.873
recX
Putative regulatory protein, inhibitor of RecA recombinase and coprotease activities; Modulates RecA activity; Belongs to the RecX family.
       0.867
leuS
leucyl-tRNA synthetase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 
 0.843
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.
  
  
 0.835
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 1 subfamily.
 
 
 0.802
Your Current Organism:
Pseudoalteromonas haloplanktis
NCBI taxonomy Id: 326442
Other names: P. haloplanktis TAC125, Pseudoalteromonas haloplanktis TAC125, Pseudoalteromonas haloplanktis str. TAC125, Pseudoalteromonas haloplanktis strain TAC125
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.