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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
leuS2TIGRFAM: leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (950 aa)    
Predicted Functional Partners:
Msed_0089
TIGRFAM: isoleucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 0.980
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).
 0.980
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; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily.
 
 0.977
argS
TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 0.971
aspS
aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
 
 0.967
proS
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).
 
 0.941
lysS
TIGRFAM: lysyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); tRNA synthetase, class II (D, K and N); nucleic acid binding, OB-fold, tRNA/helicase-type; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 0.937
Msed_2213
TIGRFAM: glycyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein.
 
 
 0.907
leuS1
leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
  
 
0.904
thrS-cat
threonyl-tRNA synthetase / Ser-tRNA(Thr) hydrolase; 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 activates L-serine and transfers it to tRNA(Thr) but cannot deacylate incorrectly charged amino acid; unlike most archaea the editing function is found in a freestanding protein.
  
 
 0.899
Your Current Organism:
Metallosphaera sedula
NCBI taxonomy Id: 399549
Other names: M. sedula DSM 5348, Metallosphaera sedula DSM 5348, Metallosphaera sedula IFO 15509, Metallosphaera sedula JCM 9185, Metallosphaera sedula NBRC 15509, Metallosphaera sedula str. DSM 5348, Metallosphaera sedula strain DSM 5348
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