A0A013SG00 · A0A013SG00_9GAMM

  • 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

Lacks conserved residue(s) required for the propagation of feature annotation.
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 site121Proton acceptor
Binding site145[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site149[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site152[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site201-202S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site233S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site255-257S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site336S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site379S-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
      J690_0797

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 742879
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Acinetobacter > Acinetobacter calcoaceticus/baumannii complex

Accessions

  • Primary accession
    A0A013SG00

Proteomes

Subcellular Location

Keywords

PTM/Processing

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain131-374Radical SAM core

Sequence similarities

Belongs to the radical SAM superfamily. RlmN family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    411
  • Mass (Da)
    46,031
  • Last updated
    2014-06-11 v1
  • Checksum
    2482BE286CEECF3F
MSSAVVVSSENLDGQQQSSSTPVIPAAENKVNLLGMSRPELEKFFEDIGEKKFRAGQVMKWIHQYFVTDFAEMTNISGKLRAKLEQICEIKAPEVVHRHYSKDGTRKWVFRVGEGAGSLVETVLIPAEDKTGLRKTLCISSQVGCALDCSFCSTGKQGFQRDLTPDEIIGQLWMANYSYMEEVPVAERERSVTNVVMMGMGEPLLNYDAVLSSMQIMLDDFAYGMSKRRVTLSTSGVVPKIDQLAKDIDVALAISLHAPNDELRNELVPINKKYPLAQLIAACQRYIAKDGNESTRKHVTIEYVMLEGVNDQPEHAQQMIKLLKNLPSKINLIPFNPFPHAPYGRSSRNRIISFQKTLSDAGFVCTIRQTRGDDIDAACGQLVGQVADRTRRAEQWQKKVTQRQEILRTQG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JFYC01000002
EMBL· GenBank· DDBJ
EXS30072.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp