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
aspSAspartyl-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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. (596 aa)    
Predicted Functional Partners:
hisS
Histidyl-tRNA synthetase.
 
  
 0.992
gatB
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.
 
 0.992
alaS
Alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
  
 0.928
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.
  
 
 0.877
valS
Valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
 
  
 0.848
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP.
  
  
 0.847
SFV40322.1
FIG000859: hypothetical protein YebC.
  
 0.837
pheT
Phenylalanyl-tRNA synthetase beta chain; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
 
  
 0.792
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.
 
  
 0.729
leuS
Leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
 
  
 0.710
Your Current Organism:
Lactobacillus acidipiscis
NCBI taxonomy Id: 89059
Other names: CCUG 42961 [[Lactobacillus cypricasei]], CCUG 46556, CIP 106393 [[Lactobacillus cypricasei]], CIP 106750, DSM 15353 [[Lactobacillus cypricasei]], DSM 15836, JCM 10692, KCTC 13900 [[Lactobacillus cypricasei]], L. acidipiscis, Lactobacillus acidipiscis Tanasupawat et al. 2000, Lactobacillus cypricasei, Lactobacillus cypricasei Lawson et al. 2001, Lactobacillus sp. FS60-1, Lactobacillus sp. FS60-1T, Lactobacillus sp. LMG 17676, Lactobacillus sp. LMK3, NBRC 102163, NRIC 0300, PCU 207, PCU:207, strain FS60-1, strain LMK3 [[Lactobacillus cypricasei]]
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