Modomics - A Database of RNA Modifications

ID Card:

Full name: tRNA:m(4)X modification enzyme TRM13 homolog
UniProt: Q9NUP7
Alpha Fold Predicted Structure: AF-Q9NUP7-F1
Enzyme type: methyltransferase



Protein sequence:

MATSATSPHAPGFPAEGRCGYYVEKKKRFCRMVVAAGKRFCGEHAGAAEEEDARKRILCPLDPKHTVYEDQLAKHLKKCNSREKPKPDFYIQDINAGLRDETEIPEQLVPISSLSEEQLEKLIKKLRKASEGLNSTLKDHIMSHPALHDALNDPKNGDSATKHLKQQASILGNIENLKLLGPRRCFVEFGAGKGKLSHWVDIALKDAEKVHFILVEKVTTRFKVDGKHRKKNSVFERLQIDIQHLCLNKIPVLREEKLPVVGIGKHLCGMATDLALRCLVETYAASFEERNEEPLAKRIKNDKTEKEIYTLAKEGNEKNVPEKWNPVAGIVIALCCHHRCDWRHYVGKEYFRALGLGAVEFHYFQRMSSWATCGMRKTSLETSNSTTKRQDNQNDDSEEHDDGGYRITDDGADCLPGLLSVEEKKKIGHLCKLLIDQGRIQYLQQKGFSPALQYYTDPLVSLENVLLTALPNHSSSPETTA

Comments:

hTrmt13 acts in the cytoplasm to catalyze 2'-O-methylation of tRNAs at position 4, thus regulating translation in a manner depending on its tRNA-modification activity.Specifically, tRNA methylase which 2'-O-methylates cytidine4 in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine4 in tRNA(His). The nucleus-localized hTrmt13 directly binds DNA as a transcriptional co-activator of key epithelial–mesenchymal transition factors, thereby promoting cell migration independent of tRNA-modification activity. These dual functions of hTrmt13 are mutually exclusive, as it can bind either DNA or tRNA through its CHHC zinc finger domain. The hTrmt13 expression is tightly associated with poor prognosis and survival in diverse cancer patients.





Alpha Fold Predicted Structure:






Clear Selection and Reset Camera

Protein sequence:

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

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-Q9NUP7-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-Q9NUP7-F1.cif  
DSSP Secondary Structures   Q9NUP7.dssp  





Publications:

Title Authors Journal Details PubMed Id DOI
A dual role of human tRNA methyltransferase hTrmt13 in regulating translation and transcription Hao Li, 1 , 2 , † Han Dong, 2 , † Beisi Xu, 3 , † Qing‐Ping Xiong, 2 Cai‐Tao Li, 1 , 2 Wen‐Qing Yang, 1 Jing Li, 1 Zhi‐Xuan Huang, 1 , 2 Qi‐Yu Zeng, 2 En‐Duo Wang,corresponding author 1 , 2 and Ru‐Juan Liucorresponding author 1 [details] 34850409 10.15252/embj.2021108544