Q727F1 · RLMN_NITV2

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.

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 site91Proton acceptor
Binding site116[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site120[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site123[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site169-170S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site201S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site223-225S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site299S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site342S-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
    • Ordered locus names
      DVU_2904

Organism names

Accessions

  • Primary accession
    Q727F1

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00003501551-364Dual-specificity RNA methyltransferase RlmN
Disulfide bond109↔342(transient)

Keywords

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain102-337Radical SAM core

Sequence similarities

Belongs to the radical SAM superfamily. RlmN family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    364
  • Mass (Da)
    40,471
  • Last updated
    2004-07-05 v1
  • Checksum
    EEDEAF42CE5170B6
MTDILNLTYEELEAFMTAELGEPRFRARQVWQWLWQKCARSFDEMTNVSKATRARLAEKAVITWPEVETVQKSADGTTKFLLRLADGALVETVLIPSASREGTLRITQCLSCQVGCAMGCTFCSTGTMGFERNMTMGEILGQVLVARAHLGDSRPDHPILRNLVFMGMGEPLLNLNEVMRSLRTLNDEFGLSFSPRRITVSTCGIEKGLRELGESGLAFLAVSLHAPNQEIRKRIMPKAAHWHLDDLITALESYPLKTRERVTFEYLLLGGVNDGIEHARELVRLVSRTKGKLNLIVYNPAEGDPYDAPTPERILAFEQYLWSKNITAIIRKSKGQDIKAACGQLKASELQRGTASAGADAPEA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE017285
EMBL· GenBank· DDBJ
AAS97376.1
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