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
gatBaspartyl/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. (476 aa)    
Predicted Functional Partners:
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).
 
 0.999
KXB66645.1
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.
 
 0.999
aspS
aspartate--tRNA ligase; 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). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
 
 0.997
asnS
asparagine--tRNA ligase; KEGG: cth:Cthe_0070 1.3e-176 asnC; asparaginyl-tRNA synthetase K01893; Psort location: Cytoplasmic, score: 10.00.
  
 0.989
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.
 
 0.989
guaA
GMP synthase domain protein; Catalyzes the synthesis of GMP from XMP.
  
  
 0.889
ligA
DNA ligase; DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
  
    0.882
KXB66647.1
KEGG: ttm:Tthe_2091 7.7e-186 ATP-dependent DNA helicase PcrA; K03657 DNA helicase II / ATP-dependent DNA helicase PcrA; Psort location: Cytoplasmic, score: 9.97.
  
    0.846
KXB66642.1
SNARE-like domain protein; KEGG: ljf:FI9785_1143 4.5e-39 apl; alkaline phosphatase-like protein; Psort location: CytoplasmicMembrane, score: 10.00.
   
   0.787
KXB66648.1
ThiF family protein; KEGG: bpb:bpr_I2644 6.7e-52 thiF; thiamine biosynthesis protein ThiF; Psort location: Cytoplasmic, score: 9.97.
       0.776
Your Current Organism:
Peptoniphilus coxii
NCBI taxonomy Id: 755172
Other names: ATCC BAA-2106, CCUG 59622, JCM 16892, P. coxii, Peptoniphilus coxii Citron et al. 2013, Peptoniphilus sp. RMA 16757, strain RMA 16757
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