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Annotation rule MF_00351
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General rule information [?]

Accession MF_00351
Dates 1-JUN-2001 (Created)
26-SEP-2014 (Last updated, Version 16)
Name RNA_methyltransf_FlpA
Scope Archaea
Templates O28192 (FLPA_ARCFU); P58032 (FLPA_SULSO); Q58108 (FLPA_METJA); Q8U4M2 (FLPA_PYRFU); Q9Y9U3 (FLPA_AERPE): [Recover all]

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
FLPA
Protein name
RecName: Full=Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase;
EC=2.1.1.-;
Gene name
flpA

Comments [?]

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.
Subunit Interacts with nop5. Component of box C/D small ribonucleoprotein (sRNP) particles that contain rpl7ae, FlpA and nop5, plus a guide RNA.
Similarity Belongs to the methyltransferase superfamily. Fibrillarin family.

Keywords [?]


Gene Ontology [?]

GO:0003723; Molecular function: RNA binding.
GO:0008168; Molecular function: methyltransferase activity.
GO:0006364; Biological process: rRNA processing.
GO:0008033; Biological process: tRNA processing.

Cross-references [?]

Pfam PF01269; Fibrillarin; 1;
PRINTS PR00052; FIBRILLARIN; 1;
PROSITE PS00566; FIBRILLARIN; 1;

Features [?]

From: FLPA_AERPE (Q9Y9U3)
Key     From     To       Description   Tag   Condition   FTGroup
REGION     90     91       S-adenosyl-L-methionine binding     [TS]-T  
REGION     109     110       S-adenosyl-L-methionine binding     [ED]-x  
REGION     134     135       S-adenosyl-L-methionine binding     [DN]-[AS]  
REGION     154     157       S-adenosyl-L-methionine binding     D-[IVL]-[SA]-[QT]  

Additional information [?]

Size range 185-245 amino acids
Related rules None
Fusion 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).