CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.100 | mRNA Triphosphatase Cet1; Chain A |
|
3.20.100.10 | mRNA triphosphatase Cet1-like |
Domain Context
CATH Clusters
| Superfamily | mRNA triphosphatase Cet1-like |
| Functional Family |
Enzyme Information
| 3.1.3.33 |
Polynucleotide 5'-phosphatase.
based on mapping to UniProt Q5UQX1
A 5'-phosphopolynucleotide + H(2)O = a polynucleotide + phosphate.
-!- Does not act on nucleoside monophosphates. -!- Induced in Escherichia coli by T-even phages.
|
| 2.1.1.56 |
mRNA (guanine-N(7)-)-methyltransferase.
based on mapping to UniProt Q5UQX1
S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
-!- Adds an N(7)-methylguanine cap to mRNA. -!- The nucleoside next to the terminal guanosine may be either guanosine or adenosine.
|
| 2.7.7.50 |
mRNA guanylyltransferase.
based on mapping to UniProt Q5UQX1
GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.
-!- Can modify also synthetic poly(A) and poly(G) to form the structures m(7)G(5')pppAn and m(7)G(5')pppGn.
|
UniProtKB Entries (1)
| Q5UQX1 |
MCE_MIMIV
Acanthamoeba polyphaga mimivirus
Probable mRNA-capping enzyme
|
PDB Structure
| PDB | 2QY2 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Characterization of a trifunctional mimivirus mRNA capping enzyme and crystal structure of the RNA triphosphatase domain.
Structure
|
