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
glyQglycine--tRNA ligase, alpha subunit; Identified by similarity to SP:P00960; match to protein family HMM PF02091; match to protein family HMM TIGR00388. (317 aa)    
Predicted Functional Partners:
glyS
glycine--tRNA ligase, beta subunit; Identified by similarity to SP:P00961; match to protein family HMM PF02092; match to protein family HMM PF05746; match to protein family HMM TIGR00211.
 0.999
hisS
histidine--tRNA ligase; Identified by similarity to SP:P04804; match to protein family HMM PF00587; match to protein family HMM PF03129; match to protein family HMM TIGR00442.
 
  
 0.774
gmhB
Putative D,D-heptose 1,7-bisphosphate phosphatase; Identified by similarity to SP:P63228; match to protein family HMM TIGR01656; match to protein family HMM TIGR01662.
       0.766
alaS
alanine--tRNA ligase; 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.
 
  
 0.764
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 1 subfamily.
 
  
 0.740
pheS
phenylalanyl-tRNA synthetase, alpha subunit; Identified by similarity to SP:P08312; match to protein family HMM PF01409; match to protein family HMM PF02912; match to protein family HMM TIGR00468; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
   
  
 0.689
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; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
  
  
 0.663
glmU
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. In the C-terminal section; belongs to the trans [...]
 
  
 0.662
PFL_2299
tRNA synthetase class II family protein; Identified by match to protein family HMM PF00587.
  
  
 0.660
aspS
aspartate--tRNA ligase; 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.
  
  
 0.632
Your Current Organism:
Pseudomonas protegens
NCBI taxonomy Id: 220664
Other names: P. protegens Pf-5, Pseudomonas fluorescens Pf-5, Pseudomonas protegens Pf-5, Pseudomonas protegens str. Pf-5, Pseudomonas protegens strain Pf-5, Pseudomonas sp. Pf-5
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