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
rsmG16S rRNA (guanine(527)-N(7))-methyltransferase GidB; Specifically methylates the N7 position of a guanine in 16S rRNA; Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family. (224 aa)    
Predicted Functional Partners:
ANP28684.1
Hypothetical protein; Pfam: CobQ/CobB/MinD/ParA nucleotide binding domain.
  
  
 0.948
ANP28686.1
Hypothetical protein; Pfam: R3H domain; SMART: Putative single-stranded nucleic acids-binding domain.
  
  
 0.944
ANP28683.1
parB-like partition protein; Pfam: ParB-like nuclease domain; TIGRFAM: parB_part: ParB/RepB/Spo0J family partition protein; SMART: ParB-like nuclease domain; Belongs to the ParB family.
  
  
 0.943
ANP28689.1
Ribonuclease P protein component; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
  
  
 0.917
ANP28687.1
TIGRFAM: yidC_oxa1_cterm: membrane protein insertase, YidC/Oxa1 family; Pfam: 60Kd inner membrane protein.
  
  
 0.908
rsmA
Dimethyladenosine transferase; Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
     
 0.765
rpoB
DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
   
  
 0.748
rpsL
30S ribosomal protein S12; Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
      
 0.735
frr
Ribosome recycling factor; Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another; Belongs to the RRF family.
      
 0.735
ANP27780.1
Cytochrome c oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
      
 0.733
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.