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
argSSimilar to SYR_SALTY (P74871) Arginyl-tRNA synthetase from Salmonella typhimurium (577 aa). FASTA: opt: 1159 Z-score: 1408.5 E(): 1.5e-70 Smith-Waterman score: 1159; 34.841 identity in 597 aa overlap. (581 aa)    
Predicted Functional Partners:
guaA
GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.
  
  
 0.992
metG
tRNA-Ser; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
  
 0.955
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.
  
 0.923
proS
Transposase; 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 deacylation of [...]
  
 0.871
pheT
Similar to SYFB_ECOL6 (P59664) Phenylalanyl-tRNA synthetase beta from Escherichia coli (795 aa). FASTA: opt: 2214 Z-score: 2665.4 E(): 1.4e-140 Smith-Waterman score: 2214; 45.125 identity in 800 aa overlap.
  
  
 0.841
lysU
Similar to SYK2_ECOLI (P14825) Lysyl-tRNA synthetase, heat inducible, from E. coli (504 aa). FASTA: opt: 2003 Z-score: 2242.9 E(): 4.9e-117 Smith-Waterman score: 2003; 61.066 identity in 488 aa overlap; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 0.807
leuS
Similar to Q83DY1 Leucyl-tRNA synthetase from Coxiella burnetii (820 aa). FASTA: opt: 3351 Z-score: 3699.1 695.4 E(): 3.8e-198 Smith-Waterman score: 3351; 58.952 identity in 821 aa overlap; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 0.801
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).
  
 0.796
FTT_0900
Conserved hypothetical membrane protein; ORF ftt0900.
      
 0.780
rbn
Similar to RBN_ECOLI (P32146) tRNA processing ribonuclease BN from E. coli (290 aa). FASTA: opt: 535 Z-score: 578.5 E(): 2.5e-24 Smith-Waterman score: 535; 33.813 identity in 278 aa overlap.
  
  
 0.771
Your Current Organism:
Francisella tularensis SCHUS4
NCBI taxonomy Id: 177416
Other names: F. tularensis subsp. tularensis SCHU S4, Francisella tularensis Biovar A str. SCHU S4, Francisella tularensis Biovar A str. Schu 4, Francisella tularensis subsp. tularensis SCHU S4, Francisella tularensis subsp. tularensis Schu 4, Francisella tularensis subsp. tularensis str. SCHU S4, Francisella tularensis subsp. tularensis strain SCHU S4
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.