CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.220 | Leucine Aminopeptidase, subunit E; domain 1 |
|
3.40.220.10 | Leucine Aminopeptidase, subunit E, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Leucine Aminopeptidase, subunit E, domain 1 |
| Functional Family |
Enzyme Information
| 3.4.22.- |
Cysteine endopeptidases.
based on mapping to UniProt P0C6Y1
|
| 3.1.13.- |
Exoribonucleases producing 5'-phosphomonoesters.
based on mapping to UniProt P0C6Y1
|
| 3.6.4.12 |
DNA helicase.
based on mapping to UniProt P0C6Y1
ATP + H(2)O = ADP + phosphate.
-!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase).
|
| 3.1.-.- |
Acting on ester bonds.
based on mapping to UniProt P0C6Y1
|
| 2.1.1.- |
Methyltransferases.
based on mapping to UniProt P0C6Y1
|
| 2.7.7.48 |
RNA-directed RNA polymerase.
based on mapping to UniProt P0C6Y1
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
-!- Catalyzes RNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- See also EC 2.7.7.6.
|
| 3.6.4.13 |
RNA helicase.
based on mapping to UniProt P0C6Y1
ATP + H(2)O = ADP + phosphate.
-!- RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. -!- Some of them unwind RNA with a 3' to 5' polarity, other show 5' to 3' polarity. -!- Some helicases unwind DNA as well as RNA. -!- May be identical with EC 3.6.4.12 (DNA helicase).
|
UniProtKB Entries (1)
| P0C6Y1 |
R1AB_IBVB
Avian infectious bronchitis virus (strain Beaudette)
Replicase polyprotein 1ab
|
PDB Structure
| PDB | 3EJF |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved property.
Protein Sci.
|
