Modomics - A Database of RNA Modifications

ID Card:

Full name: tRNA-specific adenosine deaminase 2
Synonym: ADAT2
GI: 72392897
Orf: Tb927.8.4180
COG: COG0590
UniProt: Q57W17
Structures: | |
Alpha Fold Predicted Structure: AF-Q57W17-F1
Complex: Tad2/3
Enzyme type: deaminase
Position of modification - modification: t:34 - I



Protein sequence:

MVQDTGKDTNLKGTAEANESVVYCDVFMQAALKEATCALEEGEVPVGCVLVKADSSTAAQAQAGDDLALQKLIVARGRNATNRKGHALAHAEFVAVEELLRQATAGTSENIGGGGNCGAVSQDLADYVLYVVVEPCIMCAAMLLYNRVRKVYFGCTNPRFGGNGTVLSVHNSYKGCSGEDAALIGYESCGGYRAEEAVVLLQQFYRRENTNAPLGKRKRKDLSVV

Comments:

Tad2 is part of the functional heterodimeric deaminase Tad2/3. At variance with other dimeric ADAT2/3 deaminases, T. brucei Tad2/3 contains only one functional zinc ion, out of the two per dimeric enzyme. The C-terminal end of subunit tbTad2 plays a critical role in tRNA binding, while subunit Tad3 contributes to catalysis - it is not simply a structural component. This tRNA A:I editing enzyme plays a role in both A:I editing in position 34 and C:U editing in position 32 in vivo. In vitro, this A-to-I tRNA deaminase catalyzes also C-to-U deamination of DNA. The A34-to-I34 deamination reaction was tested with T. brucei tRNA-Thr as substrate. However, as other eukaryotic heterodimeric Tad2/3 it also works on other naturally occurring A34-containing tRNA (Alfonzo J. , unpublished data).





Alpha Fold Predicted Structure:






Clear Selection and Reset Camera

Protein sequence:

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

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-Q57W17-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-Q57W17-F1.cif  
DSSP Secondary Structures   Q57W17.dssp  





Publications:

Title Authors Journal Details PubMed Id DOI
A-to-I and C-to-U editing within transfer RNAs. Su AA, Randau L Biochemistry (Mosc) [details] 22022967 -
Determinants of tRNA editing and modification: Avoiding conundrums, affecting function. Paris Z, Fleming IM, Alfonzo JD Semin Cell Dev Biol [details] 22024020 -
A single zinc ion is sufficient for an active Trypanosoma brucei tRNA editing deaminase. Spears JL, Rubio MA, Gaston KW, Wywial E, Strikoudis A, Bujnicki JM, Papavasiliou FN, Alfonzo JD J Biol Chem [details] 21507956 -
The C-terminal end of the Trypanosoma brucei editing deaminase plays a critical role in tRNA binding. Ragone FL, Spears JL, Wohlgamuth-Benedum JM, Kreel N, Papavasiliou FN, Alfonzo JD RNA [details] 21602302 -
An adenosine-to-inosine tRNA-editing enzyme that can perform C-to-U deamination of DNA. Rubio MA, Pastar I, Gaston KW, Ragone FL, Janzen CJ, Cross GA, Papavasiliou FN, Alfonzo JD Proc Natl Acad Sci U S A [details] 17483465 -

Links:

_TriTrypDB_
_GeneDB_
_Wikipedia - Deamination_