 |
|
| HAMAP annotation rule: MF_00351 |
| Accession |
MF_00351 |
| Dates |
1-JUN-2001 (Created) 20-NOV-2009 (Last updated, Version 13) |
| Names |
RNA_methyltransf_FlpA |
| Protein name |
| RecName: |
Full=Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase; EC=2.1.1.-; |
|
FUNCTION: Involved in pre-rRNA and tRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in rRNA and tRNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA (By similarity).
SUBUNIT: Interacts with nop5. Component of box C/D small ribonucleoprotein (sRNP) particles that contain rpl7ae, flpA and nop5, plus a guide RNA (By similarity).
SIMILARITY: Belongs to the methyltransferase superfamily. Fibrillarin family.
GO:0003723; Molecular function: RNA binding.
GO:0008168; Molecular function: methyltransferase activity.
GO:0006364; Biological process: rRNA processing.
GO:0008033; Biological process: tRNA processing.
| From: FLPA_ARCFU (O28192) |
| Key |
|
From |
|
To |
|
Description |
|
Condition |
|
FTGroup |
| REGION |
|
70 |
|
71 |
|
S-adenosyl-L-methionine binding (By similarity) |
|
T-T |
|
|
| REGION |
|
88 |
|
89 |
|
S-adenosyl-L-methionine binding (By similarity) |
|
E-x |
|
|
| REGION |
|
113 |
|
114 |
|
S-adenosyl-L-methionine binding (By similarity) |
|
D-A |
|
|
| BINDING |
|
42 |
|
42 |
|
S-adenosyl-L-methionine (By similarity) |
|
K |
|
|
| BINDING |
|
133 |
|
133 |
|
S-adenosyl-L-methionine (By similarity) |
|
D |
|
|
| Size range: |
200-235 amino acids |
| Related UniRules: |
None |
| Template: |
O28192 (FLPA_ARCFU); P58032 (FLPA_SULSO); Q58108 (FLPA_METJA); Q8U4M2 (FLPA_PYRFU): [Recover all] |
| Scope: |
Archaea |
| Fusion: |
Nter: None; Cter: None |
| Duplicate: |
None |
| Plasmid encoded: |
None |
| Comments: |
The "x" in the condition of the second S-adenosyl-L-methionine-binding region most often is a large and hydrophobic residue (pi-stacking interaction). |
View rule in raw text format (no links)