Modomics - A Database of RNA Modifications

Full name: tRNA(His) guanylyltransferase
GI: 45270428
Orf: YGR024c
COG: COG4021
UniProt: P53215
Structures: | |
Enzyme type: guanylyltransferase
Position of modification - modification: t:0 - G


tRNAHis guanylyltransferase, adds a guanosine residue to the 5' end of tRNAHis after transcription and RNase P cleavage. Enzymes from Thg1 family exhibit 3'-to-5' polymerase activity. A crystal structure of Mycobacterium tuberculosis and H. sapiens homologues have been solved (3OTB, 3OTD, 3OTE and 3OTC, respectively).

Protein sequence:


Enzymatic activities:

Reaction Substrate Type Position
pN:pG(pN) tRNA (t)   0


Title Authors Journal Details PubMed Id DOI
tRNAHis maturation: an essential yeast protein catalyzes addition of a guanine nucleotide to the 5' end of tRNAHis. Gu W, Jackman JE, Lohan AJ, Gray MW, Phizicky EM Genes Dev [details] 14633974 -
tRNAHis guanylyltransferase (THG1), a unique 3′-5′ nucleotidyl transferase, shares unexpected structural homology with canonical 5′-3′ DNA polymerases. Hyde SJ, Eckenroth BE, Smith BA, Eberley WA, Heintz NH, Jackman JE, Doublié S Proc Natl Acad Sci U S A [details] 21059936 -
Doing it in reverse: 3'-to-5' polymerization by the Thg1 superfamily. Jackman JE, Gott JM, Gray MW RNA [details] 22456265 -


_Wikipedia - Guanylyl transferase_

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