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
ycgJPutative methyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the methyltransferase superfamily. (253 aa)    
Predicted Functional Partners:
ycgI
Putative methyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
   
  
 0.979
yodH
Putative S-adenosylmethionine-dependent methyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the methyltransferase superfamily.
 
   
 0.942
yrrM
Putative acyl-CoA O-methyltransferase; Catalyzes the methylation of 5-hydroxyuridine (ho5U) to form 5-methoxyuridine (mo5U) at position 34 in tRNAs.
     
 0.788
yerO
Putative transcriptional regulator (TetR/AcrR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator.
    
 
 0.700
ydaC
Putative methyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the methyltransferase superfamily.
  
  
 0.643
ycgK
Putative transcriptional regulator (LysR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator; Belongs to the LysR transcriptional regulatory family.
  
    0.603
gatA
glutamyl-tRNA(Gln) amidotransferase (subunit A); Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln).
      
 0.510
bioI
Cytochrome P450 for pimelic acid formation for biotin biosynthesis; Catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. It has high affinity for long-chain fatty acids with the greatest affinity for myristic acid; Belongs to the cytochrome P450 family.
    
 
 0.510
yrrT
Putative AdoMet-dependent methyltransferase; Could be a S-adenosyl-L-methionine-dependent methyltransferase; Belongs to the methyltransferase superfamily. YrrT family.
      
 0.507
rlmB
23S rRNA methyltransferase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
   
  
 0.499
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.