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
gatCgatC: aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; 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. (93 aa)    
Predicted Functional Partners:
gatB
gatB: aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit; 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
gatA
gatA: aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, A subunit; 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).
 
 0.998
AHY46237.1
COG:COG0154: Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidases [Translation ribosomal structure and biogenesis]; Pfam:PF01425:Amidase; Pfam:PF01425:Amidase; ProSitePatterns:PS00571:Amidase, conserved site; SUPERFAMILY:SSF75304:Amidase signature domain; Belongs to the amidase family.
 
 
 0.899
AHY46959.1
COG:COG0154: Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidases [Translation ribosomal structure and biogenesis]; Pfam:PF01425:Amidase; Pfam:PF01425:Amidase; ProSitePatterns:PS00571:Amidase, conserved site; SUPERFAMILY:SSF75304:Amidase signature domain; Belongs to the amidase family.
 
 
 0.883
aspS
aspartate--tRNA ligase; 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.
  
 
 0.881
AHY45362.1
COG:COG0154: Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidases [Translation ribosomal structure and biogenesis]; Pfam:PF01425:Amidase; Pfam:PF01425:Amidase; ProSitePatterns:PS00571:Amidase, conserved site; SUPERFAMILY:SSF75304:Amidase signature domain; Belongs to the amidase family.
 
 
 0.875
AHY47837.1
COG:COG0069: Glutamate synthase domain 2 [Amino acid transport and metabolism]; Pfam:PF01645:Glutamate synthase, central-C; ProSiteProfiles:PS51278:Glutamine amidotransferase type 2 domain; SUPERFAMILY:SSF51395:No Description;UniPathway: UPA00045.
   
 
 0.675
dapA
dapA: dihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
  
  
 0.670
guaA
GMP synthase (glutamine-hydrolyzing), C-terminal domain; Catalyzes the synthesis of GMP from XMP.
  
 
 0.651
AHY45998.1
DHHA2 domain; COG:COG1227: Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion]; Pfam:PF02833:DHHA2; ProSiteProfiles:PS51371:Cystathionine beta-synthase, core; SMART:SM00116:Cystathionine beta-synthase, core; SUPERFAMILY:SSF64182:No Description.
       0.651
Your Current Organism:
Rubrobacter radiotolerans
NCBI taxonomy Id: 42256
Other names: ATCC 51242, Arthrobacter radiotolerans, CIP 106991, DSM 46359, DSM 5868, IAM 12072, IFO 14777, JCM 2153, NBRC 14777, R. radiotolerans, strain P-1
Server load: low (24%) [HD]
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