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CATH Superfamily 3.40.50.200

Peptidase S8/S53 domain

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:

"
Peptidase S8/S53 domain
".

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 10215: Tripeptidyl-peptidase I variant

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
Tripeptidyl-peptidase I. [EC: 3.4.14.9]
Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.
  • A lysosomal enzyme that is active at acidic pH.
  • Belongs to peptidase family S53.
  • Formerly included in EC 3.4.14.8.
 42 A0A0B7FM04 A0A0B7FM04 A0A0B7G433 A0A0B7G433 A0A0F4YRQ8 A0A0F4YRQ8 A2QVE4 A2QVE4 A2R746 A2R746
(32 more...)
Tripeptide aminopeptidase. [EC: 3.4.11.4]
Release of the N-terminal residue from a tripeptide.
  • Widely distributed in mammalian tissues.
  • Belongs to peptidase family M9.
  • Formerly EC 3.4.1.3.
 10 A0A0D9N9A2 A0A0D9N9A2 A0A0F4YEG2 A0A0F4YEG2 I8IAS6 I8IAS6 Q2U0Z5 Q2U0Z5 Q876Z9 Q876Z9
Sedolisin. [EC: 3.4.21.100]
Hydrolysis of the B chain of insulin at 13-Glu-|-Ala-14, 15-Leu-|-Tyr-16 and 25-Phe-|-Tyr-26 and angiotensin I at 4-Tyr-|-Ile-5. A good synthetic substrate is Lys-Pro-Ile-Glu-Phe-|-Phe(NO(2))-Arg-Leu.
  • An enzyme secreted by Pseudomonas sp. No. 101.
  • Optimum pH 4.
  • It is distinguished from EC 3.4.21.101 by its insensitivity to EPNP and from EC 3.4.23.31 by this property and by its unrelated amino- acid sequence.
  • Inhibited by tyrostatin, a peptide aldehyde.
  • Belongs to peptidase family S53.
  • Formerly EC 3.4.23.37.
 2 V5ND88 V5ND88
Succinate dehydrogenase (quinone). [EC: 1.3.5.1]
Succinate + a quinone = fumarate + a quinol.
  • The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria.
  • It catalyzes succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II).
  • In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone.
  • Cf. EC 1.3.5.4.
 2 A0A139IBC4 A0A139IBC4
Subtilisin. [EC: 3.4.21.62]
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
  • Subtilisin is a serine endopeptidase that evolved independently of chymotrypsin.
  • It contains no cysteine residues (although these are found in homologous enzymes).
  • Species variants include subtilisin BPN' (also subtilisin B, subtilopeptidase C, nagarse, nagarse proteinase, subtilisin Novo, bacterial proteinase Novo) and subtilisin Carlsberg (subtilisin A, subtilopeptidase A, alcalase Novo).
  • Similar enzymes are produced by various Bacillus subtilis strains and other Bacillus species.
  • Belongs to peptidase family S8.
  • Formerly EC 3.4.4.16 and EC 3.4.21.14.
 2 F9XK29 F9XK29