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prmA protein (Methylobacter tundripaludum) - STRING interaction network
"prmA" - Ribosomal protein L11 methyltransferase in Methylobacter tundripaludum
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.
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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:
some 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 each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Gene Fusion
Cooccurence
Coexpression
Experiments
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[Homology]
Score
prmARibosomal protein L11 methyltransferase; Methylates ribosomal protein L11 (292 aa)    
Predicted Functional Partners:
aroQ
3-dehydroquinate dehydratase; Catalyzes a trans-dehydration via an enolate intermediate; Belongs to the type-II 3-dehydroquinase family (148 aa)
            0.904
Mettu_2632
KEGG- mca-MCA1048 hypothetical protein (172 aa)
   
        0.890
Mettu_2631
PFAM- Methyltransferase small; KEGG- mca-MCA1049 hypothetical protein (398 aa)
         
  0.866
Mettu_3413
KEGG- hiq-CGSHiGG_00130 Sel1 domain-containing protein; PFAM- Heat shock protein DnaJ, N-terminal; Sel1-like; SMART- Heat shock protein DnaJ, N-terminal; Sel1-like (222 aa)
   
   
  0.836
Mettu_3149
KEGG- aas-Aasi_0854 hypothetical protein; PFAM- Heat shock protein DnaJ, N-terminal; Sel1-like; SMART- Heat shock protein DnaJ, N-terminal; Sel1-like (362 aa)
   
   
  0.836
dnaJ
Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] (376 aa)
   
   
  0.830
Mettu_1896
KEGG- noc-Noc_1382 heat shock protein DnaJ-like; PFAM- Heat shock protein DnaJ, N-terminal; Chaperone DnaJ, C-terminal; SMART- Heat shock protein DnaJ, N-terminal (318 aa)
   
   
  0.830
rlmH
Ribosomal RNA large subunit methyltransferase H; Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA; Belongs to the RNA methyltransferase RlmH family (155 aa)
 
     
  0.827
Mettu_2630
annotation not available (62 aa)
              0.811
Mettu_2629
KEGG- mca-MCA2501 hypothetical protein (175 aa)
              0.793
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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