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
glySSimilar to Escherichia coli glycyl-tRNA synthetase beta chain subunit GlyS SW:SYGB_ECOLI (P00961) (688 aa) fasta scores: E(): 0, 85.6% id in 688 aa, and to Haemophilus influenzae glycyl-tRNA synthetase beta chain subunit GlyS SW:SYGB_HAEIN (P43822) (688 aa) fasta scores: E(): 0, 68.9% id in 689 aa. (689 aa)    
Predicted Functional Partners:
glyQ
Similar to Escherichia coli glycyl-tRNA synthetase alpha subunit GlyQ SW:SYGA_ECOLI (P00960) (303 aa) fasta scores: E(): 0, 93.7% id in 303 aa, and to Vibrio cholerae glycyl-tRNA synthetase alpha subunit GlyQ TR:Q9KVW7 (EMBL:AE004094) (330 aa) fasta scores: E(): 0, 88.8% id in 303 aa.
 0.999
b0026
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.
 
  
 0.898
leuS
Similar to Escherichia coli leucyl-tRNA synthetase LeuS SW:SYL_ECOLI (P07813) (860 aa) fasta scores: E(): 0,84.8% id in 860 aa, and to Vibrio cholerae leucyl-tRNA synthetase VC0956 TR:Q9KTE6 (EMBL:AE004177) (894 aa) fasta scores: E(): 0, 74.5% id in 858 aa; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
  
 0.887
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 1 subfamily.
  
  
 0.873
drpA
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 [...]
  
  
 0.870
alaS
alanyl-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; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
  
 0.838
aspS
aspartyl-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.
  
  
 0.790
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). Also edits incorrectly charged L-seryl-tRNA(Thr).
 
  
 0.778
far
Elongation factor G; 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; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
   
    0.745
atpA
ATP synthase alpha subunit protein; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family.
   
    0.717
Your Current Organism:
Yersinia pestis
NCBI taxonomy Id: 214092
Other names: Y. pestis CO92, Yersinia pestis CO92, Yersinia pestis str. CO92, Yersinia pestis strain CO92
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