Modomics - A Database of RNA Modifications

ID Card:

Full name: rRNA 2′-O-methyltransferase fibrillarin
Synonym: Fibrillarin, Lot3p
GI: 6320190
Orf: YDL014W
COG: COG1889
UniProt: P15646
Alpha Fold Predicted Structure: AF-P15646-F1
Complex: C/D RNP
Enzyme type: methyltransferase
Position of modification - modification: s:many - Xm
l:many - Xm



Protein sequence:

MSFRPGSRGGSRGGSRGGFGGRGGSRGGARGGSRGGFGGRGGSRGGARGGSRGGFGGRGGSRGGARGGSRGGRGGAAGGARGGAKVVIEPHRHAGVYIARGKEDLLVTKNMAPGESVYGEKRISVEEPSKEDGVPPTKVEYRVWNPFRSKLAAGIMGGLDELFIAPGKKVLYLGAASGTSVSHVSDVVGPEGVVYAVEFSHRPGRELISMAKKRPNIIPIIEDARHPQKYRMLIGMVDCVFADVAQPDQARIIALNSHMFLKDQGGVVISIKANCIDSTVDAETVFAREVQKLREERIKPLEQLTLEPYERDHCIVVGRYMRSGLKK

Comments:

This is a methyltransferase that depends on S-adenosyl-L-methionine, capable of methylating both RNA and proteins. It plays a role in pre-rRNA processing by performing site-specific 2'-hydroxyl methylation on ribose moieties in pre-ribosomal RNA ( Schimmang et al. 1989, Tollervey et al. 1991, Galardi et al. 2002). The specificity of the methylation site is determined by a guide RNA that pairs with the substrate, with the methylation occurring at a characteristic distance from the sequence involved in base pairing ( Schimmang et al. 1989, Tollervey et al. 1991). This enzyme is also involved in the biogenesis of 18S rRNA. Furthermore, it functions as a protein methyltransferase, catalyzing the methylation of histone H2A's 'Gln-105' (H2AQ105me). This modification impairs binding of the FACT complex and is specifically present at the 35S ribosomal DNA locus ( Schimmang et al. 1989, Tollervey et al. 1991). It is the catalytic subunit of a multiprotein C/D RNP complex. Works in S. cerevisiae with 3 other proteins: Nop58p, Nop56p, Snu13p. About 53 positions methylated by C/D RNP complex were found in S. cerevisiae rRNA





Alpha Fold Predicted Structure:






Clear Selection and Reset Camera

Protein sequence:

M S F R P G S R G G S R G G S R G G F G G R G G S R G G A R G G S R G G F G G R G G S R G G A R G G S R G G F G G R G G S R G G A R G G S R G G R G G A A G G A R G G A K V V I E P H R H A G V Y I A R G K E D L L V T K N M A P G E S V Y G E K R I S V E E P S K E D G V P P T K V E Y R V W N P F R S K L A A G I M G G L D E L F I A P G K K V L Y L G A A S G T S V S H V S D V V G P E G V V Y A V E F S H R P G R E L I S M A K K R P N I I P I I E D A R H P Q K Y R M L I G M V D C V F A D V A Q P D Q A R I I A L N S H M F L K D Q G G V V I S I K A N C I D S T V D A E T V F A R E V Q K L R E E R I K P L E Q L T L E P Y E R D H C I V V G R Y M R S G L K K
50100150200250300SequenceHTSN

Secondary Structure Alphabet

  • G: 3-turn helix (310helix)
  • H: α-helix
  • I: 𝝅-helix (5 - turn helix)
  • T: Hydrogen Bonded Turn
  • B: β-sheet
  • S: Bend
  • C: Coil (residues not present in any of the above conformations)
  • N: Not assigned

Download PDB Structures & DSSP Secondary Structures:

Alpha Fold Pdb Files   AF-P15646-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-P15646-F1.cif  
DSSP Secondary Structures   P15646.dssp  





Publications:

Links:

_Wikipedia_
_SGD_
_The yeast snoRNA database_
_PubMed_