A0A5B7WY14 · A0A5B7WY14_9MICC

Function

function

Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.

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.

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 site166Proton acceptor
Binding site186[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site190[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site193[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site244-245S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site278S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site301-303S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site380S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site423S-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
    Probable 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
      GcLGCM259_2568

Organism names

Accessions

  • Primary accession
    A0A5B7WY14

Proteomes

Subcellular Location

Keywords

PTM/Processing

Keywords

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-57Disordered
Compositional bias22-41Polar residues
Domain172-418Radical SAM core

Sequence similarities

Belongs to the radical SAM superfamily. RlmN family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    431
  • Mass (Da)
    47,723
  • Last updated
    2019-11-13 v1
  • Checksum
    38FA6E6A96951CCE
MTSIDSSTLSAAERKALRQEQAAAQRAQQLRISQSRAKAEGRTQVVPTPEGWKQEMGADGRPQLQFAAKRRVSQPPTHLADLTLAERQEKLKELGLPAFRAKQLSVHYFQHYTTDPDKMSDLPKNGREELAEAMFPTLLTEVKRLTTDDGKTIKFLWRLFDGSLVESVLMRYPNRITLCISSQCGCGMNCPFCATGQAGLTRNMSTAEILDQIVQANRVIAEGGLGGQKHPDERVGNIVFMGMGEPLANYKRVMNAVHRMVADAPEGLGMSARGITVSTVGLVPAIRKLADENIPVTFALSLHAPDDELRDELIPVNSRWKVDEALDAAHDYYVKTGRRVSIEYALIKDMNDHEWRAELLAKKLNARGRGWVHVNPIPLNPVPGSIWTRSEPDITSKFVHRLDELGVPTTLRDTRGKEIDGACGQLAADGD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias22-41Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP034412
EMBL· GenBank· DDBJ
QCY48275.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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