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rluB protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"rluB" - Pseudouridine synthase in Desulfovibrio vulgaris Hildenborough
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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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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rluBPseudouridine synthase; Identified by similarity to SP-P35159; match to protein family HMM PF00849; match to protein family HMM PF01479; match to protein family HMM TIGR00093; Belongs to the pseudouridine synthase RsuA family (267 aa)    
Predicted Functional Partners:
DVU_1531
Methyltransferase, putative; Identified by match to protein family HMM PF03602; match to protein family HMM TIGR00095 (190 aa)
        0.843
engA
GTPase Der; GTPase that plays an essential role in the late steps of ribosome biogenesis (491 aa)
 
   
  0.771
DVU_1670
Uncharacterized protein; Identified by similarity to OMNI-NTL03CP2236; Belongs to the sulfur carrier protein TusA family (212 aa)
              0.731
pheT
Phenylalanine--tRNA ligase beta subunit; Identified by match to protein family HMM PF01588; match to protein family HMM PF03147; match to protein family HMM PF03483; match to protein family HMM PF03484; match to protein family HMM TIGR00472 (798 aa)
         
  0.652
rplA
50S ribosomal protein L1; Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (235 aa)
   
      0.645
era
GTPase Era; An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism (308 aa)
 
   
  0.635
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 [...] (375 aa)
   
 
  0.621
polA
DNA polymerase I; Identified by similarity to SP-P00582; match to protein family HMM PF00476; match to protein family HMM PF01367; match to protein family HMM PF02739; match to protein family HMM TIGR00593 (1015 aa)
 
        0.616
rlmN
Dual-specificity RNA methyltransferase RlmN; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family (364 aa)
 
 
  0.609
cdsA
Phosphatidate cytidylyltransferase; Identified by match to protein family HMM PF01148; Belongs to the CDS family (268 aa)
 
        0.605
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882
Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
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