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
argSarginine-tRNA ligase; PRINTS: Arginyl-tRNA synthetase signature; TIGRFAM: argS: arginine--tRNA ligase; Pfam: tRNA synthetases class I (R); SMART: DALR anticodon binding domain; SMART: Arginyl tRNA synthetase N terminal dom; Pfam: Arginyl tRNA synthetase N terminal domain; Pfam: DALR anticodon binding domain. (585 aa)    
Predicted Functional Partners:
ileS
isoleucine-tRNA ligase; 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 2 subfamily.
  
 0.954
guaA
GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.
  
  
 0.938
leuS
leucine-tRNA ligase; Pfam: tRNA synthetases class I (M); Pfam: Leucyl-tRNA synthetase, Domain 2; TIGRFAM: leuS_bact: leucine--tRNA ligase; PRINTS: Leucyl-tRNA synthetase signature; Pfam: Anticodon-binding domain of tRNA; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 0.933
pheT
phenylalanine-tRNA ligase, beta subunit; SMART: Ferredoxin-fold anticodon binding domain; SMART: tRNA synthetase B5 domain; TIGRFAM: pheT_bact: phenylalanine--tRNA ligase, beta subunit; SMART: B3/4 domain; Pfam: B3/4 domain; Pfam: Putative tRNA binding domain; Pfam: Ferredoxin-fold anticodon binding domain; Pfam: tRNA synthetase B5 domain; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
  
 0.912
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.
  
 0.908
proS
proline-tRNA ligase; 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 deacyl [...]
  
 0.905
valS
valine-tRNA ligase; 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.
 
  
 0.896
tyrS
tyrosine-tRNA ligase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily.
  
  
 0.882
metG
methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
  
 0.866
lysS
lysine-tRNA ligase; TIGRFAM: lysS_bact: lysine--tRNA ligase; Pfam: tRNA synthetases class II (D, K and N); Pfam: OB-fold nucleic acid binding domain; PRINTS: Lysyl-tRNA synthetase signature; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 0.849
Your Current Organism:
Dermabacter vaginalis
NCBI taxonomy Id: 1630135
Other names: D. vaginalis, DSM 100050, Dermabacter sp. AD1-86, Dermabacter vaginalis Chang et al. 2016, KCTC 39585, strain AD1-86
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.