Modomics - A Database of RNA Modifications

ID Card:

Full name: tRNA-specific adenosine deaminase 3
Synonym: ADAT3
GI: 74026040
Orf: Tb11.01.6930
COG: COG0590
UniProt: Q381Q7
Structures: | |
Alpha Fold Predicted Structure: AF-Q381Q7-F1
Complex: Tad2/3
Enzyme type: deaminase
Position of modification - modification: t:34 - I



Protein sequence:

MEEVVVPEEPPKLVSALATYVQQERLCTMFLSIANKLLPLKPHACHLKRIRRSSATRVATAPMDGFAGGVICDKRDSSVATSTISDGCERNSAALGTPAAENSHILELLLSVGGPVDSSALKELESAADTTVAVHRVWVPDRAPRSSAEEWTKWCQIWPFATPKPRAPTQLSECEMGSIQRIFRTVVMPLAKRLRTDETLGIAAVLVDPSDGYRVLVSSGEEHALKRGNSAACLGYVSNSGCRKSNRVVLDHPVTFVLKEVTRKQCKDREVEGDASYLANGMDMFVSHEPCVMCSMALVHSRVRRVFYCFPNPVHGGLGSTVSIHAIQELNHHFRVFRCDSRWLSDPEGVSSDHDNPYWEDLTVP

Comments:

Tad3 is part of the functional heterodimeric deaminase Tad2/3, where it contributes to catalysis. Tad3 is not simply a structural component of the dimeric enzyme. In T. brucei only one zinc ion out of two play a role in catalysis. Tad2/3 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as other eukaryotic heterodimeric Tad2/3 it also works on other naturally occurring A34-containing tRNA (Alfonzo J. , unpublished data).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 E E V V V P E E P P K L V S A L A T Y V Q Q E R L C T M F L S I A N K L L P L K P H A C H L K R I R R S S A T R V A T A P M D G F A G G V I C D K R D S S V A T S T I S D G C E R N S A A L G T P A A E N S H I L E L L L S V G G P V D S S A L K E L E S A A D T T V A V H R V W V P D R A P R S S A E E W T K W C Q I W P F A T P K P R A P T Q L S E C E M G S I Q R I F R T V V M P L A K R L R T D E T L G I A A V L V D P S D G Y R V L V S S G E E H A L K R G N S A A C L G Y V S N S G C R K S N R V V L D H P V T F V L K E V T R K Q C K D R E V E G D A S Y L A N G M D M F V S H E P C V M C S M A L V H S R V R R V F Y C F P N P V H G G L G S T V S I H A I Q E L N H H F R V F R C D S R W L S D P E G V S S D H D N P Y W E D L T V P

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-Q381Q7-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-Q381Q7-F1.cif  
DSSP Secondary Structures   Q381Q7.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 -
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:

_GeneDB_
_Wikipedia - Deamination_