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
gatAAspartyl-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). (483 aa)    
Predicted Functional Partners:
pet112
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
asnS
Asparaginyl-tRNA synthetase; Sly1018280.
   
 0.971
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP.
  
 
 0.767
pyrA
Carbamoyl-phosphate synthase large chain; Sly3000730; Belongs to the CarB family.
   
 
  0.709
AIE73478.1
Hypothetical protein; Sly1028920.
  
 
 0.707
gltX
Glutamyl-tRNA synthetase / Glutamyl-tRNA(Gln) synthetase; 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.
  
 
 0.707
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.
  
 
 0.691
AIE74728.1
Cell wall endopeptidase, family M23/M37; Sly1014750.
       0.618
carA
Carbamoyl-phosphate synthase small chain; Sly1009050; Belongs to the CarA family.
  
 
  0.588
Your Current Organism:
Synechocystis sp. PCC6714
NCBI taxonomy Id: 1147
Other names: Aphanocapsa sp. (strain 5.3A), Aphanocapsa sp. 5-3A, Aphanocapsa sp. 5.3A, S. sp. PCC 6714, Synechocystis sp. (ATCC 27178), Synechocystis sp. (PCC 6714), Synechocystis sp. (strain PCC 6714), Synechocystis sp. ATCC 27178, Synechocystis sp. PCC 6714, Synechocystis sp. SAG 92.79, Synechocystis sp. UTCC 98, Synechocystis sp. UTEX 2470
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