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Conserved domains on  [gi|487730642|ref|WP_001814874|]
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MULTISPECIES: 23S rRNA methyltransferase attenuation leader peptide [Bacteria]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ErmC super family cl05681
23S rRNA methylastransferase leader peptide (ErmCL); This family consists of several very ...
4-27 4.36e-03

23S rRNA methylastransferase leader peptide (ErmCL); This family consists of several very short bacterial 23S rRNA methylase leader peptide (ErmCL) sequences. ermC confers resistance to macrolide-lincosamide streptogramin B antibiotics by specifying a ribosomal RNA methylase, which results in decreased ribosomal affinity for these antibiotics. ermC expression is induced by exposure to erythromycin and is controlled by an uORF encoding the leader peptide ErmCL. It has been shown that the four C-terminal ErmCL residues I6F7V8I9 are crucial for ribosome stalling and that translation is arrested likely due to the PTC adopting an inactive conformation that prevents peptide bond formation with the incoming Ser-tRNASer at the 10th ermCL codon position.


The actual alignment was detected with superfamily member pfam06308:

Pssm-ID: 368836  Cd Length: 31  Bit Score: 29.49  E-value: 4.36e-03
                         10        20
                 ....*....|....*....|....
gi 487730642   4 FQMRNVDKTSTVLKQTKNSDYADK 27
Cdd:pfam06308  8 YQMRNVDKTSTVLKQTKNSDYADK 31
 
Name Accession Description Interval E-value
ErmC pfam06308
23S rRNA methylastransferase leader peptide (ErmCL); This family consists of several very ...
4-27 4.36e-03

23S rRNA methylastransferase leader peptide (ErmCL); This family consists of several very short bacterial 23S rRNA methylase leader peptide (ErmCL) sequences. ermC confers resistance to macrolide-lincosamide streptogramin B antibiotics by specifying a ribosomal RNA methylase, which results in decreased ribosomal affinity for these antibiotics. ermC expression is induced by exposure to erythromycin and is controlled by an uORF encoding the leader peptide ErmCL. It has been shown that the four C-terminal ErmCL residues I6F7V8I9 are crucial for ribosome stalling and that translation is arrested likely due to the PTC adopting an inactive conformation that prevents peptide bond formation with the incoming Ser-tRNASer at the 10th ermCL codon position.


Pssm-ID: 368836  Cd Length: 31  Bit Score: 29.49  E-value: 4.36e-03
                         10        20
                 ....*....|....*....|....
gi 487730642   4 FQMRNVDKTSTVLKQTKNSDYADK 27
Cdd:pfam06308  8 YQMRNVDKTSTVLKQTKNSDYADK 31
 
Name Accession Description Interval E-value
ErmC pfam06308
23S rRNA methylastransferase leader peptide (ErmCL); This family consists of several very ...
4-27 4.36e-03

23S rRNA methylastransferase leader peptide (ErmCL); This family consists of several very short bacterial 23S rRNA methylase leader peptide (ErmCL) sequences. ermC confers resistance to macrolide-lincosamide streptogramin B antibiotics by specifying a ribosomal RNA methylase, which results in decreased ribosomal affinity for these antibiotics. ermC expression is induced by exposure to erythromycin and is controlled by an uORF encoding the leader peptide ErmCL. It has been shown that the four C-terminal ErmCL residues I6F7V8I9 are crucial for ribosome stalling and that translation is arrested likely due to the PTC adopting an inactive conformation that prevents peptide bond formation with the incoming Ser-tRNASer at the 10th ermCL codon position.


Pssm-ID: 368836  Cd Length: 31  Bit Score: 29.49  E-value: 4.36e-03
                         10        20
                 ....*....|....*....|....
gi 487730642   4 FQMRNVDKTSTVLKQTKNSDYADK 27
Cdd:pfam06308  8 YQMRNVDKTSTVLKQTKNSDYADK 31
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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