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
gatA_2Aspartyl-tRNA(Asn) amidotransferase subunit A, Glutamyl-tRNA(Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). (511 aa)    
Predicted Functional Partners:
gatB
Aspartyl-tRNA(Asn) amidotransferase subunit B, Glutamyl-tRNA(Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily.
 0.999
gatC
Aspartyl-tRNA(Asn) amidotransferase subunit C, Glutamyl-tRNA(Gln) amidotransferase subunit C; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family.
 
 0.998
AIY19381.1
Methylcrotonyl-CoA carboxylase biotin-containing subunit.
   
 0.947
AIY17090.1
Allophanate hydrolase 2 subunit 2.
    
 0.907
AIY15692.1
Methylcrotonyl-CoA carboxylase biotin-containing subunit.
    
 0.883
AIY18491.2
Biotin carboxylase of acetyl-CoA carboxylase.
    
 0.804
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP.
  
 
 0.694
carB
Carbamoyl-phosphate synthase large chain; Belongs to the CarB family.
   
 
 0.690
lepA
Translation elongation factor LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner.
   
  
 0.651
aspS
Aspartyl-tRNA synthetase, Aspartyl-tRNA(Asn) 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
 
 
 0.640
Your Current Organism:
Pimelobacter simplex
NCBI taxonomy Id: 2045
Other names: ATCC 6946, Arthrobacter simplex, CCUG 23611, CIP 82.106, Corynebacterium simplex, DSM 20130, HAMBI 90, IFO 12069, KCTC 9106, LMG 16261, LMG:16261, NBRC 12069, NCIB 8929, NCIB:8929, Nocardioides simplex, P. simplex
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