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CATH Superfamily 3.40.630.10

Zn peptidases

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 named:

"
Zn peptidases
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 34847: Zinc carboxypeptidase A 1

There are 12 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
Carboxypeptidase T. [EC: 3.4.17.18]
Releases a C-terminal residue, which may be hydrophobic or positively charged.
  • Belongs to peptidase family M14.
 60 A0A0C1NGT7 A0A0C1NGT7 A0A0D6VLL8 A0A0D6VLL8 A0A0H5CE94 A0A0H5CE94 A0A0H5CG35 A0A0H5CG35 A0A0H5CTN6 A0A0H5CTN6
(50 more...)
Metallocarboxypeptidase D. [EC: 3.4.17.22]
Releases C-terminal Arg and Lys from polypeptides.
  • Activated by cobalt.
  • Inhibited by guanidinoethylmercaptosuccinic acid.
  • Belongs to peptidase family M14.
 60 A0A0B2Q6Y8 A0A0B2Q6Y8 A0A0B2SNJ4 A0A0B2SNJ4 A0A0D2LBV4 A0A0D2LBV4 A0A151SYX5 A0A151SYX5 B0VJI3 B0VJI3
(50 more...)
Carboxypeptidase A. [EC: 3.4.17.1]
Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.
  • Isolated from cattle, pig and dogfish pancreas, and other sources including mast cells and skeletal muscle.
  • Belongs to peptidase family M14.
  • Formerly EC 3.4.2.1 and EC 3.4.12.2.
 42 B0DMB9 B0DMB9 B5LXD6 B5LXD6 C5PGK8 C5PGK8 E3TGR3 E3TGR3 O61532 O61532
(32 more...)
Carboxypeptidase B. [EC: 3.4.17.2]
Preferential release of a C-terminal lysine or arginine amino acid.
  • Isolated from cattle, pig and dogfish pancreas, and other sources, including skin fibroblasts and adrenal medulla.
  • Belongs to peptidase family M14.
  • Formerly EC 3.4.2.2 and EC 3.4.12.3.
 40 A0A084GG21 A0A084GG21 B1PZ69 B1PZ69 B7P4Y5 B7P4Y5 B7QLQ3 B7QLQ3 E0V9S1 E0V9S1
(30 more...)
Carboxypeptidase E. [EC: 3.4.17.10]
Release of C-terminal arginine or lysine residues from polypeptides.
  • Activated by Co(2+).
  • Inhibited by 1,10-phenanthroline and other chelating agents.
  • pH optimum 5.6.
  • Located in storage granules of secretory cells, and active in processing of protein hormones and bioactive peptides.
  • Distinct from EC 3.4.17.2 and EC 3.4.17.3.
  • Belongs to peptidase family M14.
 22 A0A061IN84 A0A061IN84 A5A6K7 A5A6K7 E0W2S8 E0W2S8 O17754 O17754 P04836 P04836
(12 more...)
Lysine carboxypeptidase. [EC: 3.4.17.3]
Release of a C-terminal basic amino acid, preferentially lysine.
  • Inactivates bradykinin and anaphylatoxins in blood plasma.
  • Belongs to peptidase family M14.
  • Formerly EC 3.4.12.7.
 14 A0A061IBQ0 A0A061IBQ0 A0A061IE87 A0A061IE87 G3HZA5 G3HZA5 P15169 P15169 Q2KJ83 Q2KJ83
(4 more...)
Carboxypeptidase U. [EC: 3.4.17.20]
Release of C-terminal Arg and Lys from a polypeptide.
  • Pro-carboxypeptidase U in plasma is activated by thrombin or plasmin during clotting to form the unstable carboxypeptidase U.
  • Activity similar to that of the more stable lysine carboxypeptidase, except no preference is shown for Lys over Arg.
  • Belongs to peptidase family M14.
 10 L8IGL2 L8IGL2 Q2KIG3 Q2KIG3 Q96IY4 Q96IY4 Q9EQV9 Q9EQV9 Q9JHH6 Q9JHH6
Carboxypeptidase M. [EC: 3.4.17.12]
Cleavage of C-terminal arginine or lysine residues from polypeptides.
  • A membrane-bound enzyme optimally active at neutral pH.
  • Distinct from EC 3.4.17.3 and EC 3.4.17.10.
  • Belongs to peptidase family M14.
 8 G4M1C3 G4M1C3 P14384 P14384 Q5RFD6 Q5RFD6 Q80V42 Q80V42
Aminopeptidase Y. [EC: 3.4.11.15]
Preferentially, release of N-terminal lysine.
  • Inhibited by Zn(2+) and Mn(2+).
  • Hydrolyzes L-lysyl-4-nitroanilide and, more slowly, L-arginyl-4- nitroanilide.
  • Belongs to peptidase family M28B.
 6 A0A1J0UV18 A0A1J0UV18 F2RLJ9 F2RLJ9 N0CTE6 N0CTE6
Carboxypeptidase A2. [EC: 3.4.17.15]
Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues.
  • Isolated from rat pancreas but not present in cattle pancreas.
  • Belongs to peptidase family M14.
 6 P19222 P19222 P48052 P48052 Q504N0 Q504N0
Elongation factor 4. [EC: 3.6.5.n1]
GTP + H(2)O = GDP + phosphate.
  • The enzyme is required for accurate and efficient protein synthesis under certain stress conditions.
  • May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes.
  • Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly.
  • Binds to ribosomes in a GTP-dependent manner.
 4 A0A0E0DWR2 A0A0E0DWR2 A0A0E0DWR3 A0A0E0DWR3
Protein-serine/threonine phosphatase. [EC: 3.1.3.16]
[a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate.
  • A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48).
  • The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1).
 2 A0A0N4ZRN1 A0A0N4ZRN1
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