close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
trmDtRNA (guanine-N1)-methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family. (247 aa)    
Predicted Functional Partners:
rplS
Ribosomal protein L19; This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
 
  
 0.985
rpsP
Ribosomal protein S16; Identified by similarity to SP:P21474; match to protein family HMM PF00886; match to protein family HMM TIGR00002; Belongs to the bacterial ribosomal protein bS16 family.
 
  
 0.984
rimM
16S rRNA processing protein RimM; An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes; Belongs to the RimM family.
  
  
 0.974
rpoA
DNA-directed RNA polymerase, alpha subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
 
  
 0.893
nusA
Transcription termination factor NusA; Participates in both transcription termination and antitermination.
 
  
 0.887
rplC
Ribosomal protein L3; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit; Belongs to the universal ribosomal protein uL3 family.
  
  
 0.880
rpsB
Ribosomal protein S2; Identified by similarity to SP:P21464; match to protein family HMM PF00318; match to protein family HMM TIGR01011; Belongs to the universal ribosomal protein uS2 family.
 
  
 0.876
rpsH
Ribosomal protein S8; One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit; Belongs to the universal ribosomal protein uS8 family.
  
  
 0.871
rpsR
Ribosomal protein S18; Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit; Belongs to the bacterial ribosomal protein bS18 family.
 
  
 0.871
rpsC
Ribosomal protein S3; Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation; Belongs to the universal ribosomal protein uS3 family.
  
  
 0.865
Your Current Organism:
Myxococcus xanthus
NCBI taxonomy Id: 246197
Other names: M. xanthus DK 1622, Myxococcus xanthus DK 1622
Server load: very high (>100%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.