CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.70 | Alpha-Beta Plaits |
|
3.30.70.3000 | tRNA(His) guanylyltransferase (Thg1) |
Domain Context
CATH Clusters
| Superfamily | 3.30.70.3000 |
| Functional Family | tRNA(His) guanylyltransferase |
Enzyme Information
| 2.7.7.79 |
tRNA(His) guanylyltransferase.
based on mapping to UniProt Q9NWX6
p-tRNA(His) + ATP + GTP + H(2)O = pG-P-tRNA(His) + AMP + 2 diphosphate.
-!- In eukarya an additional guanosine residue is added post- transcriptionally to the 5'-end of tRNA(His) molecules. -!- The addition occurs opposite a universally conserved adenosine(73) and is thus the result of a non-templated 3'-5' addition reaction. -!- The additional guanosine residue is an important determinant for aminoacylation by EC 6.1.1.21. -!- The enzyme requires a divalent cation for activity. -!- ATP activation is not required when the substrate contains a 5'-triphosphate (ppp-tRNA(His)).
|
UniProtKB Entries (1)
| Q9NWX6 |
THG1_HUMAN
Homo sapiens
Probable tRNA(His) guanylyltransferase
|
PDB Structure
| PDB | 3OTE |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
tRNAHis guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases.
Proc.Natl.Acad.Sci.USA
|
