CATH Domain 3ejfA00

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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)

R1AB_IBVB

Avian infectious bronchitis virus (strain Beaudette)

Replicase polyprotein 1ab

PDB Structure

PDB	3EJF
External Links	PDBSum Proteopedia
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. Piotrowski, Y., Hansen, G., Boomaars-van der Zanden, A.L., Snijder, E.J., Gorbalenya, A.E., Hilgenfeld, R. Protein Sci.