CATH Superfamily 3.10.170.10
The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was: waiting to be named.
FunFam 614: Peptidase, M4 (Thermolysin) family
There are 5 EC terms in this cluster
Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.
Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
EC Term | Annotations | Evidence |
---|---|---|
Bacillolysin.
[EC: 3.4.24.28]
Similar, but not identical, to that of thermolysin.
|
224 |
A0A023P0D4
A0A075R1Q7
A0A076VXZ2
A0A076W2D8
A0A077MZ73
A0A077N2F7
A0A077NNV3
A0A077NUS5
A0A077PDE2
A0A077PTS8 (214 more...) |
Aureolysin.
[EC: 3.4.24.29]
Cleavage of insulin B chain with specificity similar to that of thermolysin, preferring hydrophobic P1' residues. Activates the glutamyl endopeptidase (EC 3.4.21.19) of Staphylococcus aureus.
|
90 |
A0A068E656
A0A077UVZ8
A0A0A8X0L7
A0A0A8X622
A0A0B5S5G9
A0A0D6T2B8
A0A0E0VTT6
A0A0E1AKF2
A0A0E1VMC1
A0A0E1XAY9 (80 more...) |
Thermolysin.
[EC: 3.4.24.27]
Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe.
|
35 |
A0A0D8BHM5
A0A0D8BQ54
A0A0E0TFP6
A0A0G3Y3S3
A0A0K0Q2H9
A0A150MB51
A0A160FCU7
A0A1C3D4Z7
A0A1C3T2W9
A0A1C6WCB0 (25 more...) |
Pseudolysin.
[EC: 3.4.24.26]
Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1'. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects.
|
18 |
A0A0C5VQV5
A0A0E1ATG1
A0A0H3R469
A0A0P1D8B7
A0A157TCV8
A0A1D5BXM1
A0A1E9CFL3
A0A1F0IBL7
A0A1G5LLJ7
A0A1J0IQ62 (8 more...) |
Vibriolysin.
[EC: 3.4.24.25]
Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1'. Phe at P1' is the most favored residue, which distinguished this enzyme from thermolysin.
|
3 | A0A0C5VQV5 Q9R9S7 V9ZRP7 |