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
Deba_3239Protein of unknown function DUF28; COGs: COG0217 conserved hypothetical protein; InterPro IPR002876:IPR017856; KEGG: dat:HRM2_04000 hypothetical protein; PFAM: protein of unknown function DUF28; SPTR: C0QGP3 UPF0082 protein HRM2_04000; PFAM: Domain of unknown function DUF28; TIGRFAM: conserved hypothetical protein TIGR01033. (250 aa)    
Predicted Functional Partners:
ruvC
Crossover junction endodeoxyribonuclease RuvC; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
 
  
 0.859
ruvA
Holliday junction DNA helicase RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
 
   
 0.841
rlmE
Ribosomal RNA methyltransferase RrmJ/FtsJ; Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
  
    0.807
ruvB
Holliday junction DNA helicase RuvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
 
   
 0.740
metG
methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
  
   0.716
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.
  
   0.716
nadE
NAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
   
   0.709
Deba_3242
NAD-dependent epimerase/dehydratase; COGs: COG0451 Nucleoside-diphosphate-sugar epimerase; InterPro IPR016040:IPR001509; KEGG: dal:Dalk_1637 NAD-dependent epimerase/dehydratase; PFAM: NAD-dependent epimerase/dehydratase; SPTR: B8FAN9 NAD-dependent epimerase/dehydratase; PFAM: NAD dependent epimerase/dehydratase family.
   
   0.661
rpmF
COGs: COG0333 Ribosomal protein L32; InterPro IPR002677; KEGG: dal:Dalk_3305 ribosomal protein L32; PFAM: ribosomal L32p protein; SPTR: B8FJ67 50S ribosomal protein L32; TIGRFAM: ribosomal protein L32; PFAM: Ribosomal L32p protein family; TIGRFAM: ribosomal protein L32; Belongs to the bacterial ribosomal protein bL32 family.
  
  
 0.657
aspS
aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
  
 0.645
Your Current Organism:
Desulfarculus baarsii
NCBI taxonomy Id: 644282
Other names: D. baarsii DSM 2075, Desulfarculus baarsii 2st 14, Desulfarculus baarsii DSM 2075, Desulfarculus baarsii str. DSM 2075, Desulfarculus baarsii strain DSM 2075
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.