CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.60 | 4-Layer Sandwich |
|
3.60.10 | Deoxyribonuclease I; Chain A |
|
3.60.10.10 | Endonuclease/exonuclease/phosphatase |
Domain Context
CATH Clusters
| Superfamily | Endonuclease/exonuclease/phosphatase |
| Functional Family | Deoxyribonuclease |
Enzyme Information
| 3.1.21.1 |
Deoxyribonuclease I.
based on mapping to UniProt P00639
Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products.
-!- Preference for double-stranded DNA. -!- Similar enzymes: streptococcal DNase (streptodornase), T4 endonuclease II, T7 endonuclease II, Escherichia coli endonuclease I, 'nicking' nuclease of calf thymus, colicin E2 and E3. -!- Formerly EC 3.1.4.5.
|
UniProtKB Entries (3)
| P68135 |
ACTS_RABIT
Oryctolagus cuniculus
Actin, alpha skeletal muscle
|
| P00639 |
DNAS1_BOVIN
Bos taurus
Deoxyribonuclease-1
|
| P06396 |
GELS_HUMAN
Homo sapiens
Gelsolin
|
PDB Structure
| PDB | 3CJC |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin.
Proc.Natl.Acad.Sci.USA
|
