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
alaSAlanyl-tRNA synthetase (Alanine--tRNA ligase) (AlaRS); 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. (895 aa)    
Predicted Functional Partners:
CBL56891.1
6 Protein of unknown function, without similarity to other proteins.
   
 0.978
pheT
Phenylalanyl-tRNA synthetase beta chain (Phenylalanine--tRNA ligase beta chain) (PheRS); ATP + L-Phenylalanine + tRNA(Phe) <=> AMP + Pyrophosphate + L-Phenylalanyl-tRNA(Phe); Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
 
 
 0.966
CBL56677.1
Holliday junction resolvase; Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA; Belongs to the YqgF HJR family.
  
  
 0.962
mltG
Aminodeoxychorismate lyase; Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. Belongs to the transglycosylase MltG family.
  
    0.887
aspS
Aspartyl-tRNA synthetase (Aspartate--tRNA ligase) (AspRS); 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.
 
  
 0.852
valS
Valyl-tRNA synthetase (Valine--tRNA ligase) (ValRS); 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.
 
  
 0.825
leuS
Leucyl-tRNA synthetase (Leucine--tRNA ligase) (LeuRS); Belongs to the class-I aminoacyl-tRNA synthetase family.
 
 
 0.821
thrS
Threonyl-tRNA synthetase (Threonine--tRNA ligase) (ThrRS); ATP + L-Threonine + tRNA(Thr) <=> AMP + Pyrophosphate + L-Threonyl-tRNA(Thr); Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 
 0.790
ileS
Isoleucyl-tRNA synthetase (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.
  
 
 0.759
gmk
Guanylate kinase, Guanosine monophosphate kinase (GMP kinase); Essential for recycling GMP and indirectly, cGMP.
 
 
 
 0.754
Your Current Organism:
Propionibacterium freudenreichii
NCBI taxonomy Id: 754252
Other names: P. freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii ATCC 9614, Propionibacterium freudenreichii subsp. shermanii CIP 103027, Propionibacterium freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii str. CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii strain CIRM-BIA1
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