A0A0U5Z1Z2 · A0A0U5Z1Z2_SERMA

  • 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.

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 site119Proton acceptor
Binding site139[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site143[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site146[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site193-194S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site225S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site247-249S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site326S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site369S-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
    • Synonyms
      trmG
      , trmG/rlmN
    • ORF names
      AB868_03997
      , AN695_0204035
      , C3R40_17190
      , D9B62_13335
      , DMW43_13655
      , ERS381498_02943
      , FHU12_0518
      , FOT62_25545
      , HCO56_19715
      , MC70_004190
      , NCTC10211_02473
      , RF091_30185

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • 1058
    • 945174350
    • AH0650_Sm1
    • 2880STDY5683034
    • FDAARGOS_79
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Yersiniaceae > Serratia

Accessions

  • Primary accession
    A0A0U5Z1Z2
  • Secondary accessions
    • A0A3E2EB31
    • A0A656VCY7

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for disulfide bond.

TypeIDPosition(s)Description
Disulfide bond132↔369(transient)

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-23Disordered
Compositional bias7-23Polar residues
Domain125-364Radical SAM core

Sequence similarities

Belongs to the radical SAM superfamily. RlmN family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    398
  • Mass (Da)
    44,463
  • Last updated
    2018-09-12 v1
  • Checksum
    6791FE087F647F48
MLEPITSEHTVSENNSLTTPSVNVEQPAAAKINLLDLNRQQMREFFAEMGEKPFRADQVMKWIYHYCCDDFEQMTDINKVLRGKLQRVAEIRAPEVAEEQRSADGTIKWAIKVGDQQVETVYIPEADRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAKIIGALKVTGQRPITNVVMMGMGEPLLNLNNVVPAMEIMLDDFGFGLSKRRVTLSTSGVVPALDKLGDMIDVALAISLHAPNDTIRDEIVPINRKYNIETFLSAVRRYLEKSNANQGRVTVEYVMLDHINDSTDDAHQLAEVLKDTPCKINLIPWNPFPGAPYGRSSNSRVDRFSKVLMEYGFTTIVRKTRGDDIDAACGQLAGEVIDRTKRTLKKKMAGEPINVRAV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias7-23Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FCGK01000008
EMBL· GenBank· DDBJ
CUZ28295.1
EMBL· GenBank· DDBJ
Genomic DNA
LFJS01000014
EMBL· GenBank· DDBJ
KMU50062.1
EMBL· GenBank· DDBJ
Genomic DNA
JAVIPQ010000542
EMBL· GenBank· DDBJ
MDQ9559767.1
EMBL· GenBank· DDBJ
Genomic DNA
JAATHL010000001
EMBL· GenBank· DDBJ
NMQ39455.1
EMBL· GenBank· DDBJ
Genomic DNA
LJEX02000114
EMBL· GenBank· DDBJ
OCO82163.1
EMBL· GenBank· DDBJ
Genomic DNA
JTBC02000002
EMBL· GenBank· DDBJ
PNO69239.1
EMBL· GenBank· DDBJ
Genomic DNA
PQGI01000013
EMBL· GenBank· DDBJ
POP15263.1
EMBL· GenBank· DDBJ
Genomic DNA
QJPU01000007
EMBL· GenBank· DDBJ
PYA04993.1
EMBL· GenBank· DDBJ
Genomic DNA
RCEJ01000265
EMBL· GenBank· DDBJ
RTG40333.1
EMBL· GenBank· DDBJ
Genomic DNA
UGYK01000002
EMBL· GenBank· DDBJ
SUI49958.1
EMBL· GenBank· DDBJ
Genomic DNA
VFMJ01000001
EMBL· GenBank· DDBJ
TQI83055.1
EMBL· GenBank· DDBJ
Genomic DNA
VOUQ01000070
EMBL· GenBank· DDBJ
TXE22024.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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