Modomics - A Database of RNA Modifications

ID Card:

Full name: S-adenosyl-L-methionine-dependent methyltransferase
Synonym: YBR141C
GI: 330443457
Orf: YBR1118
UniProt: P38278
Alpha Fold Predicted Structure: AF-P38278-F1
Enzyme type: methyltransferase
Position of modification - modification: l:2142(1784) - m1A



Protein sequence:

MHSRKSKSITGKRKQVGSNVTRVIKPQKTRRIIRRFHHLINKRQSICKFLCLKENLDDSNEEKNDKIIRLSIKGNVRLGKYYEDGKSQSFNDAMESQLLRLHSLIKNESKSKDTSDLAVMYTLLGYIMNQINKLGGLETYQIASQNGQLKERGGDTSKLLEKWIRSSFENCPGAVALEIGSLSSGNRISRCALFRNVVRIDLEEHEGVIKQDFMERPLPRNENDKFDLISCSLVLNFVKNHRDRGAMCHRMVKFLKPQGYIFIVLPQACVTHSRYCDKTLLQNLLGSIGLIMLNSHQSNKLYYCLYQLQVVPPQPSSFSKRIKVNDGPGLNNFGITL

Comments:

S-adenosyl-L-methionine-dependant methyltransferase specifically methylates the N1 position of A2142 in the rRNA LSU-25s. It is predicted to be an Ado-Met dependent methyltransferase from the Rossmann fold superfamily. Noteworthy, LSU-25s is in the domain IV helix 65 region of LSU-25s that accounts for most of the surface of LSU-25s. The loss of m1A2142 modification confers anisomycin and peroxide sensitivity to the cells (Sharma et al. 2013 ).




Reaction Substrate SubstrateType Position (Anti)Codon Modified (Anti)Codon Amino Acid Change Transcript Name Transcript Region Cellular Localization References
A:m1A RNA rRNA 2142 LSU-25S Helix 65 cytosol 23558746   

Alpha Fold Predicted Structure:






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Protein sequence:

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

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-P38278-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-P38278-F1.cif  
DSSP Secondary Structures   P38278.dssp  





Publications:

Title Authors Journal Details PubMed Id DOI
Identification of a novel methyltransferase, Bmt2, responsible for the N-1-methyl-adenosine base modification of 25S rRNA in Saccharomyces cerevisiae Sunny Sharma, Peter Watzinger, Peter Kötter, and Karl-Dieter Entian Nucleic Acids Res [details] 23558746 10.1093/nar/gkt195