Full name: tRNA(pseudouridine54-N1)-methyltransferase
Synonym: HVO_1989
GI: 292656118
Orf:
COG: COG1901
UniProt: D4GTL8
Structures: | |
Complex:
Enzyme type: methyltransferase
Position of modification - modification: t:54 - m1Y

Comments:

AdoMet dependent methyltransferase. Pseudouridine in position 55 is important for efficient conversion of Psi54 to m1Psi54. This modification is located in the T-loop and is important for the tertiary structure of the tRNA molecule. Crystal structure of TrmY from M. jannaschii was solved at 1.4 and 1.55A resolution (see the entry for M. jannaschii TrmY).

Protein sequence:

MRQFIVTGHDAPTTPDFSLDDIAGGAGRLDVLCRCVNSAFFLSHDIREDVRVHLVLGDEYTVRFEGSELR RLNPDERSTAALIRKALEKREEAIGHMPAESSPGVSIRRMGFETTLEEAASDATVVELHEDGDPVVQVEP PENPLFVLSDHHDFTDEEAELLAAAADERVRLGPEILHADHSITVAHNYLDTAGYSRY

Enzymatic activities:

Reaction Substrate Type Position
Y:m1Y tRNA (t) all/all/prokaryotic cytosol 54

Publications:

Title Authors Journal Details PubMed Id DOI
The archaeal COG1901/DUF358 SPOUT-methyltransferase members, together with pseudouridine synthase Pus10, catalyze the formation of 1-methylpseudouridine at position 54 of tRNA. Chatterjee K, Blaby IK, Thiaville PC, Majumder M, Grosjean H, Yuan YA, Gupta R, de Crécy-Lagard V RNA [details] 22274953 -
Identification of the enzyme responsible for N1-methylation of pseudouridine 54 in archaeal tRNAs. Wurm JP, Griese M, Bahr U, Held M, Heckel A, Karas M, Soppa J, Wöhnert J RNA [details] 22274954 -

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