Protein Summary

CDAT8 from Methanopyrus kandleri

Full name: tRNA-specific cytidine deaminase
Synonym: MK0935
GI: 238537840
Orf:
COG: COG2131
UniProt: Q8TWU6
Structures: | 3G8Q |
Complex:
Enzyme type: deaminase
Position of modification - modification: t:8 - U

Comments:

CDAT8 is responsible for C-to-U editing at position 8 in tRNA. It is composed of three domains: an N-terminal cytidine deaminase domain (CDD), a central ferredoxin-like domain (FLD), and a C-terminal THUMP domain. Works as a dimer. In Methanopyrus kandleri, only four tRNAs (tRNAGln UUG, tRNAPro GGG, tRNAPro UGG, and tRNAThr GGU) possess a U8 (T8 in the tRNA gene), whereas the other 30 tRNA genes encode C8. The highly conserved U8 in tRNAs forms a reverse Hoogsteen tertiary base pair with A14 that stabilizes the sharp kink between the acceptor stem and base A9. The C8 must be modified to U in order to support the tertiary interaction with A14, which is present in all 34 tRNAs.

Protein sequence:

MKVSLAGQTVDVKKILNEIPKRTVTAALLEGGEIVAVEEADDEHAERKLV
RRHDVEGKVVFVTARPCLYCARELAEAGVAGVVYLGRGRGLGPYYLARSG
VEVVEVHPDEPLGYDPVDRLDVLLTFGGNPYLTEEDVAARVYCLLTGRGF
DADIAPAPENLSGRVEIMVTRGDPDEAVELLKEELPVFRIRRFLISGEFD
RDELRERILEDIEPRILDPFAVRARIARAGAFSSSREAEVFIGDVLTSVG
REVNLNDPRTVVTVDVLGPRVSVGVEKR

Enzymatic activities

Reaction Substrate Type Position
C:U tRNA (t) many 8

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 cytidine deaminase edits C to U in transfer RNAs in Archaea. Randau L, Stanley BJ, Kohlway A, Mechta S, Xiong Y, Soll D Science [details] 19407206 -

Links

_Wikipedia_-_Deamination_
_Wikipedia_-_RNA_editing_

Last modification of this entry: 2012-07-03 16:56:32.514437
Edited by a user: magda
Edited content: Changed protein_sequence, if_enzyme, nomenclature, catalytic_domain_fold and comments.