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
prmCprotein-(glutamine-N5) methyltransferase, release factor-specific; Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif; Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily. (283 aa)    
Predicted Functional Partners:
prfA
ATPase; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
 
 0.997
OLU47848.1
Rossman fold protein, TIGR00730 family; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the LOG family.
      0.891
map
Type I methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
   
 
 0.812
atpE
ATP synthase F0 subunit C; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
  
   0.776
atpC
Hypothetical protein; Produces ATP from ADP in the presence of a proton gradient across the membrane.
 
   0.775
OLU45595.1
threonylcarbamoyl-AMP synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SUA5 family.
 
  
 0.772
atpH
ATP synthase F1 subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
  
   0.762
atpG
ATP synthase F1 subunit gamma; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
  
   0.748
atpA
F0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
  
   0.747
atpD
F0F1 ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
  
   0.740
Your Current Organism:
Dubosiella newyorkensis
NCBI taxonomy Id: 1862672
Other names: ATCC TSD-64, D. newyorkensis, DSM 103457, Dubosiella newyorkensis Cox et al. 2017, Erysipelotrichaceae bacterium NYU-BL-A4, strain NYU-BL-A4
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