HAMAP rule MF_01012
General rule information
[?]
| Accession | MF_01012 |
| Dates | 19-APR-2002 (Created)
1-JUN-2023 (Last updated, Version 26) |
| Name | 23SrRNA_methyltr_RlmC |
| Scope(s) |
Bacteria Gammaproteobacteria |
| Template(s) | P75817 (RLMC_ECOLI); P55135 (RLMD_ECOLI); [ Recover all ] |
| Triggered by |
HAMAP; MF_01012 (Get profile general information and statistics) |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
| Identifier | RLMC |
| Protein name | RecName: Full=23S rRNA (uracil(747)-C(5))-methyltransferase RlmC; EC=2.1.1.189; AltName: Full=23S rRNA(m5U747)-methyltransferase; |
| Gene name | Name=rlmC; |
Comments
[?]
| FUNCTION | Catalyzes the formation of 5-methyl-uridine at position 747 (m5U747) in 23S rRNA. |
| CATALYTIC ACTIVITY | Reaction=S-adenosyl-L-methionine + uridine(747) in 23S rRNA = 5- methyluridine(747) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42628, Rhea:RHEA-COMP:10154, Rhea:RHEA-COMP:10155, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.189; |
| SIMILARITY | Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. RlmC subfamily. |
Keywords
[?]
| Methyltransferase | |
| rRNA processing | |
| S-adenosyl-L-methionine | |
| Transferase | |
| case <FTGroup:1> | |
| 4Fe-4S | |
| Iron | |
| Iron-sulfur | |
| Metal-binding | |
| end case | |
Gene Ontology
[?]
| GO:0070041; Molecular function:rRNA (uridine-C5-)-methyltransferase activity | |
| case <FTGroup:1> | |
| GO:0005506; Molecular function:iron ion binding | |
| end case | |
| GO:0031167; Biological process:rRNA methylation | |
Cross-references
[?]
| Pfam | PF05958; tRNA_U5-meth_tr; 1; |
| PROSITE | PS51687; SAM_MT_RNA_M5U; 1; |
| PROSITE | PS01230; TRMA_1; 1; |
| PROSITE | PS01231; TRMA_2; 1; |
| NCBIfam | TIGR02085; Meth_trns_rumB; 1; |
Features
[?]
| From: RLMC_ECOLI (P75817) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 334 | 334 | /note="Nucleophile" | C | ||||||||
| BINDING | 3 | 3 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" |
C | 1 | |||||||
| BINDING | 11 | 11 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" |
C | 1 | |||||||
| BINDING | 14 | 14 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" |
C | 1 | |||||||
| BINDING | 87 | 87 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" |
C | 1 | |||||||
| BINDING | 212 | 212 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
Q | ||||||||
| BINDING | 241 | 241 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
F | ||||||||
| BINDING | 262 | 262 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
E | ||||||||
| BINDING | 307 | 307 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
N | ||||||||
Additional information
[?]
| Size range | 375-392 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |