Modomics - A Database of RNA Modifications

ID Card:

Full name: rRNA methyltransferase, mitochondrial
Synonym: Pet56
GI: 1346886
Orf: YOR201C
COG: COG0566
UniProt: P25270
Alpha Fold Predicted Structure: AF-P25270-F1
Enzyme type: methyltransferase
Position of modification - modification: l:2270(2251) - Gm



Protein sequence:

MTSLTNAVFKRYLAVTPSAHQALKTRIKKKSSSFDKFFPQQSNSRKKQWETLNEDKASWFKRKYAHVHAREQDRAADPYGKKKAHVEKLKEIKNQAKLNQKSHKSKFQNKDIALKLMNDNPIFEYVYGTNSVYAALLNPSRNCHSRLLYHGTIPSKFLQIVDELKVTTELVDKHRLNLLTNYGVHNNIALETKPLQPVEIAYLGDMDTSSAALSIHELGFNNENIPHELPYGTKTDAKKFPLGLYLDEITDPHNIGAIIRSAYFLGVDFIVMSRRNCSPLTPVVSKTSSGALELLPIFYVDKPLEFFTKSQEMGGWTFITSHLANATSEKYTVGKTISMHDLNGLCNELPVVLVVGNESQGVRTNLKMRSDFFVEIPFGGIEKGNRAPEPIVDSLNVSVATALLIDNILTCK

Comments:

Mrm1 methylates the universally conserved G2270 in the so-called A-loop (hairpin 92) of the peptidyltransferase center (domain V) of 21S mito rRNA, equivalent to conserved Gm2251 in E. coli 23S rRNA and catalyzed by E. coli RlmB. The purified recombinant Mrm1 enzyme works in vitro on transcripts of both mitochondrial 21S rRNA and E. coli 23S rRNA. AdoMet is the donor of methyl group. In cytoplasmic S. cerevisiae rRNA, the analogous conserved Gm position 2618 (2251 E.coli numbering) is catalyzed at by a C/D box RNP (Nop1), guided by snoR67.





Alpha Fold Predicted Structure:






Clear Selection and Reset Camera

Protein sequence:

M T S L T N A V F K R Y L A V T P S A H Q A L K T R I K K K S S S F D K F F P Q Q S N S R K K Q W E T L N E D K A S W F K R K Y A H V H A R E Q D R A A D P Y G K K K A H V E K L K E I K N Q A K L N Q K S H K S K F Q N K D I A L K L M N D N P I F E Y V Y G T N S V Y A A L L N P S R N C H S R L L Y H G T I P S K F L Q I V D E L K V T T E L V D K H R L N L L T N Y G V H N N I A L E T K P L Q P V E I A Y L G D M D T S S A A L S I H E L G F N N E N I P H E L P Y G T K T D A K K F P L G L Y L D E I T D P H N I G A I I R S A Y F L G V D F I V M S R R N C S P L T P V V S K T S S G A L E L L P I F Y V D K P L E F F T K S Q E M G G W T F I T S H L A N A T S E K Y T V G K T I S M H D L N G L C N E L P V V L V V G N E S Q G V R T N L K M R S D F F V E I P F G G I E K G N R A P E P I V D S L N V S V A T A L L I D N I L T C K
50100150200250300350400SequenceGHTBSN

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-P25270-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-P25270-F1.cif  
DSSP Secondary Structures   P25270.dssp  





Publications:

Links:

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