A0A1B9VEF9 · A0A1B9VEF9_9PROT

  • Protein
    Dual-specificity RNA methyltransferase RlmN
  • Gene
    rlmN
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

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.

Miscellaneous

Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site129Proton acceptor
Binding site151[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site155[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site158[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site207-208S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site239S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site261-263S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site338S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site381S-methylcysteine intermediate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionmetal ion binding
Molecular FunctionrRNA (adenine(2503)-C2-)-methyltransferase activity
Molecular FunctionrRNA binding
Molecular FunctiontRNA (adenine(37)-C2)-methyltransferase activity
Molecular FunctiontRNA binding
Biological ProcessrRNA base methylation
Biological ProcesstRNA methylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Dual-specificity RNA methyltransferase RlmN
  • EC number
  • Alternative names
    • 23S rRNA (adenine(2503)-C(2))-methyltransferase
    • 23S rRNA m2A2503 methyltransferase
    • Ribosomal RNA large subunit methyltransferase N
    • tRNA (adenine(37)-C(2))-methyltransferase
    • tRNA m2A37 methyltransferase

Gene names

    • Name
      rlmN
    • ORF names
      KO164_1033

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • KO164
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Thalassospiraceae > Thalassospira

Accessions

  • Primary accession
    A0A1B9VEF9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for disulfide bond.

TypeIDPosition(s)Description
Disulfide bond144↔381(transient)

Keywords

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-25Disordered
Domain137-370Radical SAM core
Region388-414Disordered

Sequence similarities

Belongs to the radical SAM superfamily. RlmN family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    414
  • Mass (Da)
    46,199
  • Last updated
    2016-11-02 v1
  • Checksum
    308B0270E98B785C
MTDVLSENVTQNAENGATPSGPTLTDFVTRAANGQAADGRRDLVGLSRDQLTELLGEMGESKFRVKQMWNWIYNRGVKDIEDMTNISKKLRDRLSQDFYIGRPVLTADQKSSDDTHKWLMKFHDGNEAETVYIPDRNEDRGAVCISSQVGCTLTCKFCHTGTQLLVRNLTPGEIISQFMVARDSYGEWPTPANGIRRLSNIVMMGMGEPLFNYENVREALKIAMDGEGISISRRRVTLSTSGVVPEIVRCGEELGVGLAISLHAPDDDLRNEIMPINKKYPLKELMDACRHYPGMSNSRPITMEYVMLKGVNDKPEHARALAKLVKGVHCKFNLIPFNKWPGSDYECTPTNDIKKFAHTLLELGYEAPIRWPRGRDILAACGQLKSESQRQRKSRVGDCGNASDAENANVVAAQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MAJC01000002
EMBL· GenBank· DDBJ
OCK06856.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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