Modomics - A Database of RNA Modifications

ID Card:

Full name: tRNA-two-thiouridine synthesizing protein A
Synonym: TT_C0106
GI: 46198414
COG: COG0037
UniProt: Q72LF3
Structures: | |
Alpha Fold Predicted Structure: AF-Q72LF3-F1
Enzyme type: sulfurtransferase
Position of modification - modification: t:54 - m5s2U



Protein sequence:

MVCKVCGQKAQVEMRSRGLALCREHYLDWFVKETERAIRRHRMLLPGERVLVAVSGGKDSLALWDVLSRLGYQAVGLHIELGIGEYSKRSLEVTQAFARERGLELLVVDLKEAYGFGVPELARLSGRVACSACGLSKRYIINQVAVEEGFRVVATGHNLDDEAAVLFGNLLNPQEETLSRQGPVLPEKPGLAARVKPFYRFSEREVLSYTLLRGIRYLHEECPNAKGAKSLLYKEALNLVERSMPGAKLRFLDGFLEKIRPRLDVGEEVALRECERCGYPTTGAVCAFCRMWDAVYRRAKKRKLLPEEVSFRPRVKPLRAG

Comments:

TtuA and TtuB (TTC0105), together with TtuC (TTC0979) and cysteine desulfurases (IscS = TTC0087 or SufS = TTC1373) are responsible for m5s2U (s2T) formation in tRNA of hyperthermophilic bacteria. The reaction requires cysteine (as a sulfur source) and ATP. The C-terminal glycine of TtuB is first activated as an acyl-adenylate by TtuC and then thiocarboxylated by cysteine desulfurases. The sulfur atom of thiocarboxylated TtuB is transferred to tRNA by TtuA. TtuB is a thio-carrier protein that exhibits significant sequence similarity with ThiS of the thiamine synthesis pathway. There may exist additional factors required in the last step of m5s2U biosynthesis because sulfur transfer from TtuB-COSH to tRNA in vitro depends on the addition of a cell extract and the efficiency of tRNA thiolation is low. The activity of the TtuA-C proteins was tested in vitro on substrate yeast tRNAPhe having a m5s2U54. TtuC, an ATPase, seems also to be involved in the biosynthesis of molybdenum cofactor and thiamin.





Alpha Fold Predicted Structure:






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Protein sequence:

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

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-Q72LF3-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-Q72LF3-F1.cif  
DSSP Secondary Structures   Q72LF3.dssp  





Publications:

Title Authors Journal Details PubMed Id DOI
Common thiolation mechanism in the biosynthesis of tRNA thiouridine and sulphur-containing cofactors. Shigi N, Sakaguchi Y, Asai S, Suzuki T, Watanabe K EMBO J [details] 19037260 -
Identification of two tRNA thiolation genes required for cell growth at extremely high temperatures. Shigi N, Sakaguchi Y, Suzuki T, Watanabe K J Biol Chem [details] 16547008 -