A6UE14 · RLMN_SINMW
- ProteinDual-specificity RNA methyltransferase RlmN
- GenerlmN
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids413 (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 | 126 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 146 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 150 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 153 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 210-211 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: GE | ||||||
Binding site | 242 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 264-266 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: SLH | ||||||
Binding site | 341 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 384 | 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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Rhizobiaceae > Sinorhizobium/Ensifer group > Sinorhizobium
Accessions
- Primary accessionA6UE14
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000350417 | 1-413 | Dual-specificity RNA methyltransferase RlmN | |||
Sequence: MSMAATETLNRTDIAKAPQVRLAAQPEKPSLIGLLREDMAKLLVEKGVPERQVKMRVSQVWHWLYVRGVSDFNEMSNVSKDMREMLSAHFTIARPEIVEEQVSGDGTRKWLLRFPPRGAGRPVEIETVYIPEEGRGTLCISSQVGCTLTCSFCHTGTQKLVRNLTAEEILAQLLLARDRLGDFPDRDTPQGAIVPAEGRKITNVVMMGMGEPLYNFENVKTALLIASDGDGLSLSKRRITLSTSGIVPEIYRTGEEIGVMLAISLHAVRDDLRDMLVPINKKYPLKELMEACRAYPGLSNARRITFEYVMLKDVNDSLEDAKELVKLLKGIPAKINLIPFNPWPGTNYQCSDWEQIEKFADFINQAGYASPIRTPRGRDILAACGQLKSDSERMRKVDRLAFEAMMIANHGED | ||||||
Disulfide bond | 139↔384 | (transient) | ||||
Sequence: CISSQVGCTLTCSFCHTGTQKLVRNLTAEEILAQLLLARDRLGDFPDRDTPQGAIVPAEGRKITNVVMMGMGEPLYNFENVKTALLIASDGDGLSLSKRRITLSTSGIVPEIYRTGEEIGVMLAISLHAVRDDLRDMLVPINKKYPLKELMEACRAYPGLSNARRITFEYVMLKDVNDSLEDAKELVKLLKGIPAKINLIPFNPWPGTNYQCSDWEQIEKFADFINQAGYASPIRTPRGRDILAAC |
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 132-381 | Radical SAM core | ||||
Sequence: EEGRGTLCISSQVGCTLTCSFCHTGTQKLVRNLTAEEILAQLLLARDRLGDFPDRDTPQGAIVPAEGRKITNVVMMGMGEPLYNFENVKTALLIASDGDGLSLSKRRITLSTSGIVPEIYRTGEEIGVMLAISLHAVRDDLRDMLVPINKKYPLKELMEACRAYPGLSNARRITFEYVMLKDVNDSLEDAKELVKLLKGIPAKINLIPFNPWPGTNYQCSDWEQIEKFADFINQAGYASPIRTPRGRDIL |
Sequence similarities
Belongs to the radical SAM superfamily. RlmN family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length413
- Mass (Da)46,251
- Last updated2007-08-21 v1
- Checksum6561E70B422ED884
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000738 EMBL· GenBank· DDBJ | ABR61894.1 EMBL· GenBank· DDBJ | Genomic DNA |