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
gatDGlutamyl-tRNA(Gln) amidotransferase subunit D; 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). The GatDE system is specific for glutamate and does not act on aspartate. (437 aa)    
Predicted Functional Partners:
gatE
Glutamyl-tRNA(Gln) amidotransferase subunit E; 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). The GatDE system is specific for glutamate and does not act on aspartate.
 
 0.999
gatA
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).
  
 
 0.965
gatB
Aspartyl/glutamyl-tRNA(Asn/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.
    
 0.957
ADZ10330.1
KEGG: gtn:GTNG_2275 aspartate ammonia-lyase; PFAM: Lyase 1, N-terminal; Fumarase C, C-terminal.
 
  
 0.772
ADZ10659.1
KEGG: mmg:MTBMA_c10960 thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase.
     
 0.752
ADZ09420.1
KEGG: mst:Msp_0490 putative asparagine synthetase; TIGRFAM: Asparagine synthase, glutamine-hydrolyzing; PFAM: Asparagine synthase; Glutamine amidotransferase, class-II.
 
  
 0.693
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).
 
  
 0.686
guaAB
GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP.
  
 
 0.644
carA
TIGRFAM: Carbamoyl-phosphate synthase, small subunit; KEGG: mmg:MTBMA_c13800 carbamoyl-phosphate synthase, small subunit; PFAM: Carbamoyl-phosphate synthase, small subunit, N-terminal; Glutamine amidotransferase class-I, C-terminal; Belongs to the CarA family.
 
  
 0.627
ADZ10667.1
PFAM: 4Fe-4S binding domain; KEGG: mmq:MmarC5_0318 ketoisovalerate ferredoxin oxidoreductase, delta subunit.
  
    0.604
Your Current Organism:
Methanobacterium lacus
NCBI taxonomy Id: 877455
Other names: DSM 24406, JCM 17760, M. lacus, Methanobacterium lacus Borrel et al. 2012, Methanobacterium sp. 17A1, Methanobacterium sp. AL-21, strain 17A1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.