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
lysSlysine--tRNA ligase; KEGG: bbc:BLC1_0418 3.6e-227 lysyl-tRNA synthetase; K04567 lysyl-tRNA synthetase, class II; Psort location: Cytoplasmic, score: 10.00; Belongs to the class-II aminoacyl-tRNA synthetase family. (574 aa)    
Predicted Functional Partners:
guaA
GMP synthase domain protein; Catalyzes the synthesis of GMP from XMP.
  
  
 0.954
gltX
glutamate--tRNA ligase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
 
 0.930
argS
arginine--tRNA ligase; KEGG: bad:BAD_1418 2.2e-243 argS; arginyl-tRNA synthetase K01887; Psort location: Cytoplasmic, score: 9.97.
 
 0.865
metG
methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
   
 0.864
proS
proline--tRNA ligase; 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 deacy [...]
  
 0.863
KWZ74106.1
Hypothetical protein; KEGG: bad:BAD_1187 2.0e-91 ileS; isoleucyl-tRNA synthetase K01870; Psort location: Cytoplasmic, score: 9.97.
  
 0.829
ileS
Anticodon-binding domain protein; 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.
  
 0.829
rpsB
Ribosomal protein S2; KEGG: apb:SAR116_0519 4.3e-57 30S ribosomal protein S2 K02967; Psort location: Cytoplasmic, score: 9.97; Belongs to the universal ribosomal protein uS2 family.
  
 
 0.797
KWZ73405.1
Hypothetical protein.
       0.773
thrS
threonine--tRNA ligase; KEGG: gvh:HMPREF9231_0875 6.6e-299 thrS; threonine--tRNA ligase K01868; Psort location: Cytoplasmic, score: 10.00; Belongs to the class-II aminoacyl-tRNA synthetase family.
 
 
 0.763
Your Current Organism:
Alloscardovia omnicolens
NCBI taxonomy Id: 419015
Other names: A. omnicolens, Alloscardovia omnicolens Huys et al. 2007, CCUG 31649, DSM 21503, LMG 23792, LMG:23792
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.