Modomics - A Database of RNA Modifications

ID Card:

Full name: tRNA (guanine(37)-N1)-methyltransferase
Synonym: KIAA1393, TRMT5
GI: 145275187
COG: COG2520
UniProt: Q32P41
Alpha Fold Predicted Structure: AF-Q32P41-F1
Enzyme type: methyltransferase
Position of modification - modification: t:37 - m1G
t:37 - o2yW



Protein sequence:

MVLWILWRPFGFSGRFLKLESHSITESKSLIPVAWTSLTQMLLEAPGIFLLGQRKRFSTMPETETHERETELFSPPSDVRGMTKLDRTAFKKTVNIPVLKVRKEIVSKLMRSLKRAALQRPGIRRVIEDPEDKESRLIMLDPYKIFTHDSFEKAELSVLEQLNVSPQISKYNLELTYEHFKSEEILRAVLPEGQDVTSGFSRIGHIAHLNLRDHQLSFKHLIGQVMIDKNPGITSAVNKINNIDNMYRNFQMEVLSGEQNMMTKVRENNYTYEFDFSKVYWNPRLSTEHSRITELLKPGDVLFDVFAGVGPFAIPVAKKNCTVFANDLNPESHKWLLYNCKLNKVDQKVKVFNLDGKDFLQGPVKEELMQLLGLSKERKPSVHVVMNLPAKAIEFLSAFKWLLDGQPCSSEFLPIVHCYSFSKDANPAEDVRQRAGAVLGISLEACSSVHLVRNVAPNKEMLCITFQIPASVLYKNQTRNPENHEDPPLKRQRTAEAFSDEKTQIVSNT

Comments:

The activity was studied using yeast tRNAPhe and E. coli tRNALeu. It was shown to catalyze also I->m1I reaction in position 37 in E.coli tRNAAsp hence it is predicted to participate in the formation of m1I in position 37 of human tRNAAla.




Reaction Substrate SubstrateType Position (Anti)Codon Modified (Anti)Codon Amino Acid Change Transcript Name Transcript Region Cellular Localization References
G:m1G RNA tRNA 37 #AA #AA tRNAPhe#AA anticodon-loop Mitochondrion 15248782   
G:m1G RNA tRNA 37 .AA .AA tRNALeu.AA anticodon-loop Mitochondrion 15248782   

Alpha Fold Predicted Structure:






Clear Selection and Reset Camera

Protein sequence:

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

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-Q32P41-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-Q32P41-F1.cif  
DSSP Secondary Structures   Q32P41.dssp  





Publications:

Title Authors Journal Details PubMed Id DOI
Isolation and characterization of the human tRNA-(N1G37) methyltransferase (TRM5) and comparison to the Escherichia coli TrmD protein. Brule H, Elliott M, Redlak M, Zehner ZE, Holmes WM Biochemistry [details] 15248782 -
Conservation of structure and mechanism by Trm5 enzymes. Christian T, Gamper H, Hou YM... RNA [details] 23887145 -

Links:

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