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
glySglycyl-tRNA synthetase, beta subunit; KEGG: tgr:Tgr7_3255 glycine--tRNA ligase; TIGRFAM: glycyl-tRNA synthetase, beta subunit. (691 aa)    
Predicted Functional Partners:
glyQ
KEGG: hna:Hneap_2050 glycyl-tRNA synthetase, alpha subunit; TIGRFAM: glycyl-tRNA synthetase, alpha subunit; PFAM: glycyl-tRNA synthetase alpha subunit.
 0.999
ileS
isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.
 
  
 0.827
leuS
TIGRFAM: leucyl-tRNA synthetase; KEGG: aeh:Mlg_0400 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family.
   
  
 0.820
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.
  
  
 0.796
ADC63905.1
TIGRFAM: histidinol-phosphate phosphatase family protein; hydrolase, HAD-superfamily, subfamily IIIA; PFAM: Haloacid dehalogenase domain protein hydrolase; KEGG: pag:PLES_00051 D,D-heptose 1,7-bisphosphate phosphatase.
  
    0.751
ADC63906.1
PFAM: phospholipid/glycerol acyltransferase; SMART: phospholipid/glycerol acyltransferase; KEGG: noc:Noc_0375 phospholipid/glycerol acyltransferase.
  
    0.749
aspS
aspartyl-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.
  
  
 0.707
proS
prolyl-tRNA synthetase; 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...]
   
  
 0.692
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.
  
  
 0.691
thrS
threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr).
 
  
 0.670
Your Current Organism:
Allochromatium vinosum
NCBI taxonomy Id: 572477
Other names: A. vinosum DSM 180, Allochromatium vinosum DSM 180, Allochromatium vinosum str. DSM 180, Allochromatium vinosum strain DSM 180
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