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
NEQ360NEQ360; Glu-tRNA amidotransferase, subunit A [Archaeoglobus fulgidus]; COG0154: Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidases; IPR000120: Amidase. (432 aa)    
Predicted Functional Partners:
gatB
NEQ185; 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
NEQ513
NEQ513.
  
 0.999
aspS
NEQ535; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp).
  
 0.996
gatD
NEQ126; 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 (By similarity).
    
 0.974
gatE
NEQ245; 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.
     
 0.940
NEQ396
NEQ396; Glu-tRNA amidotransferase [Methanococcus jannaschii] SPLIT; COG2511: Archaeal Glu-tRNAGln amidotransferase subunit E (contains GAD domain); IPR001472: Bipartite nuclear localization signal.
     
 0.940
gltX
NEQ302; 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).
  
 
 0.925
proS
NEQ210; 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).
  
 
 0.860
NEQ306
NEQ306; 3-oxoacyl- reductase [Aquifex aeolicus]; COG1028: Dehydrogenases with different specificities (related to short-chain alcohol dehydrogenases); IPR002198: Short-chain dehydrogenase/reductase (SDR) superfamily; IPR003560: 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (EntA); IPR002347: Glucose/ribitol dehydrogenase.
  
  
 0.844
hisS
NEQ102; histidyl-tRNA synthetase [Aeropyrum pernix]; COG0124: Histidyl-tRNA synthetase; IPR002106: Aminoacyl-transfer RNA synthetases class-II; IPR002314: tRNA synthetases, class-II (G, H, P and S); Belongs to the class-II aminoacyl-tRNA synthetase family.
  
  
 0.799
Your Current Organism:
Nanoarchaeum equitans
NCBI taxonomy Id: 228908
Other names: Microarchaeum sp. Kin4-M, N. equitans Kin4-M, Nanoarchaeum equitans Kin4-M, Nanoarchaeum equitans str. Kin4-M
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