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dtd protein (Desulfotomaculum reducens) - STRING interaction network
"dtd" - D-aminoacyl-tRNA deacylase in Desulfotomaculum reducens
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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dtdD-aminoacyl-tRNA deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl- tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality; Belongs to the DTD family (149 aa)    
Predicted Functional Partners:
Dred_0735
PFAM- beta-lactamase domain protein; KEGG- mta-Moth_1678 beta-lactamase-like (205 aa)
              0.869
Dred_0733
(P)ppGpp synthetase I, SpoT/RelA; In eubacteria ppGpp (guanosine 3’-diphosphate 5-’ diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance (721 aa)
   
   
  0.853
apt
Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis (172 aa)
              0.770
Dred_0731
Exonuclease RecJ; TIGRFAM- single-stranded-DNA-specific exonuclease RecJ; PFAM- phosphoesterase, RecJ domain protein; phosphoesterase, DHHA1; KEGG- chy-CHY_2224 single-stranded DNA-specific exonuclease RecJ (885 aa)
              0.770
tgt
Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1’ of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1’ of the ribose to form th [...] (370 aa)
   
   
  0.742
xseB
Exodeoxyribonuclease 7 small subunit; Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides; Belongs to the XseB family (81 aa)
         
  0.570
Dred_1131
Polynucleotide adenylyltransferase region; PFAM- CBS domain containing protein; phosphoesterase, RecJ domain protein; Polynucleotide adenylyltransferase region; phosphoesterase, DHHA1; KEGG- swo-Swol_1420 polyA polymerase family protein (907 aa)
   
      0.556
rpsR
30S 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 (77 aa)
           
  0.550
rimM
Ribosome maturation factor 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 (169 aa)
           
  0.550
rsmG
Ribosomal RNA small subunit methyltransferase G; Specifically methylates the N7 position of a guanine in 16S rRNA (240 aa)
         
  0.526
Your Current Organism:
Desulfotomaculum reducens
NCBI taxonomy Id: 349161
Other names: D. reducens MI-1, Desulfotomaculum reducens, Desulfotomaculum reducens MI-1, Desulfotomaculum reducens str. MI-1, Desulfotomaculum reducens strain MI-1
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