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trmL protein (Burkholderia cepacia) - STRING interaction network
"trmL" - tRNA in Burkholderia cepacia
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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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trmLtRNA (cytidine(34)-2’-O)-methyltransferase; Methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S- adenosyl-L-methionine to the 2’-OH of the wobble nucleotide (156 aa)    
Predicted Functional Partners:
WL94_22870
Uncharacterized protein (248 aa)
            0.730
DM42_2219
annotation not available (265 aa)
              0.720
mnmC
mnmC_Cterm- tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain (643 aa)
         
  0.675
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 (156 aa)
   
   
  0.669
bioC
Malonyl-[acyl-carrier protein] O-methyltransferase; Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl- L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway (321 aa)
         
  0.644
nnrD
Multifunctional fusion protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration; Belongs to the NnrD/CARKD family (514 aa)
         
  0.618
trmU
tRNA-specific 2-thiouridylase MnmA; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34 (391 aa)
   
 
  0.585
aspS
Aspartate--tRNA(Asp/Asn) ligase; 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 (600 aa)
 
        0.531
trmD
tRNA (guanine-N(1)-)-methyltransferase; Specifically methylates guanosine-37 in various tRNAs; Belongs to the RNA methyltransferase TrmD family (256 aa)
           
  0.531
rlmN
Dual-specificity RNA methyltransferase RlmN; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs (379 aa)
   
   
  0.512
Your Current Organism:
Burkholderia cepacia
NCBI taxonomy Id: 292
Other names: ATCC 25416, B. cepacia, Burkholderia cepacia, Burkholderia cepacia genomovar I, CCUG 12691, CCUG 13226, CFBP 2227, CIP 80.24, DSM 7288, ICMP 5796, IFO 14074, JCM 5964, NBRC 14074, NCCB 76047, NCPPB 2993, NCTC 10743, NRRL B-14810, Pseudomonas cepacia, Pseudomonas kingii, Pseudomonas multivorans, strain 717-ICPB 25, strain Ballard 717
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