A0A059G7V9 · A0A059G7V9_9PROT
- ProteinDual-specificity RNA methyltransferase RlmN
- GenerlmN
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids389 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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
- adenosine2503 in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine2503 in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine
RHEA-COMP:10152 CHEBI:74411 Position: 2503+ 2 RHEA-COMP:10001 + 2 CHEBI:59789 = RHEA-COMP:10282 CHEBI:74497 Position: 2503+ CHEBI:17319 + CHEBI:57844 + 2 RHEA-COMP:10000 + CHEBI:57856
Cofactor
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 110 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 132 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 136 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 139 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 187-188 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: GE | ||||||
Binding site | 219 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 241-243 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: SLH | ||||||
Binding site | 318 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 361 | S-methylcysteine intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | metal ion binding | |
Molecular Function | rRNA (adenine(2503)-C2-)-methyltransferase activity | |
Molecular Function | rRNA binding | |
Molecular Function | tRNA (adenine(37)-C2)-methyltransferase activity | |
Molecular Function | tRNA binding | |
Biological Process | rRNA base methylation | |
Biological Process | tRNA methylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDual-specificity RNA methyltransferase RlmN
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomonadales > Hyphomonadaceae > Hyphomonas
Accessions
- Primary accessionA0A059G7V9
Proteomes
Subcellular Location
PTM/Processing
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Polar residues | ||||
Sequence: MTITLDLSRKPDQPQ | ||||||
Region | 1-21 | Disordered | ||||
Sequence: MTITLDLSRKPDQPQGQRSLA | ||||||
Domain | 118-350 | Radical SAM core | ||||
Sequence: GMDGGALCVSSQVGCTLNCTFCHTGTQALVRNLTAQEITAQVMIARDALNEWPSSIEARNLTNIVFMGMGEPLYNLDNVAAAIDTISDGDGISIGRRRITVSTAGVAPKIPELGERTNAMLAISLHATNDDLRNELVPINRKYDLQMLFEAIRAYPGSGNSRRVTFEYVMLKGINDTQAEARELVRLLKGVPAKINLIPFNPWPGSPYECSDWETIEAFAEIVNRAGYASPIR | ||||||
Region | 368-389 | Disordered | ||||
Sequence: SVKKSAAEKRREALEAAASPEA | ||||||
Compositional bias | 369-389 | Basic and acidic residues | ||||
Sequence: VKKSAAEKRREALEAAASPEA |
Sequence similarities
Belongs to the radical SAM superfamily. RlmN family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length389
- Mass (Da)42,516
- Last updated2014-07-09 v1
- ChecksumFD984BB05934370E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Polar residues | ||||
Sequence: MTITLDLSRKPDQPQ | ||||||
Compositional bias | 369-389 | Basic and acidic residues | ||||
Sequence: VKKSAAEKRREALEAAASPEA |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ARYL01000011 EMBL· GenBank· DDBJ | KDA02814.1 EMBL· GenBank· DDBJ | Genomic DNA |