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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_3_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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

There are 19 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 II. [EC: 3.4.14.10]
Release of an N-terminal tripeptide from a polypeptide.
  • A cytosolic enzyme active at neutral pH.
  • Inhibited by diisopropyl fluorophosphate.
  • Belongs to peptidase family S8.
  • Formerly EC 3.4.14.8.
 40 A0A0D9RY25 A0A0E0NIV2 A0A0J5PJ21 A0A178UVT6 A0A229XVA2 A0A2I2YHL1 A0A2K5LBW8 A0A2K5VG99 A0A2K5XM73 A0A2K6D587
(30 more...)
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.
 23 A0A0A0TPQ7 A0A164SYK1 A0A1D8FIM7 A0A1D8NQQ9 C5IKX0 D4G774 D4PBI3 G4EY69 L8AEF2 P00780
(13 more...)
Oryzin. [EC: 3.4.21.63]
Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.
  • Predominant extracellular alkaline endopeptidase of the mold Aspergillus oryzae.
  • Identical or closely related enzymes are produced by A.flavus and A.sojae.
  • Belongs to peptidase family S8.
  • Formerly EC 3.4.4.16, EC 3.4.21.14 and EC 3.4.21.15.
 17 A0A0J5PVB2 A0A172PYV5 A0A229XVZ3 A0A229XZI9 A0A2P2HRF4 A0A364MNR1 A1CIA7 A1CWF3 B0Y473 B0Y708
(7 more...)
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 EC 3.4.14.8.
 12 A0A2R9B3H1 F8W2M8 G2HHK8 O14773 O89023 Q0V8B6 Q55CT0 Q5IS74 Q5RFL1 Q60HH1
(2 more...)
Proprotein convertase 2. [EC: 3.4.21.94]
Release of protein hormones and neuropeptides from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds.
  • A calcium dependent enzyme, maximally active at about pH 5.5.
  • Specificity is broader than that of prohormone convertase 1.
  • Substrates include pro-opiomelanocortin, proenkephalin, prodynorphin, proinsulin and proluteinizing-hormone-releasing hormone.
  • Unlike prohormone convertase 1, does not cleave prorenin or prosomatostatin.
  • Usually processing of prodynorphin occurs at a bond in which P2 is Thr.
  • Present in the regulated secretory pathway of neuroendocrine cells, commonly actin co-operatively with prohormone convertase 1.
  • Belongs to peptidase family S8.
 10 A0A2J8VD76 G3QWE4 G5ECN9 P16519 P21661 P28841 Q03333 Q547J8 Q5REC2 Q9GLR0
Furin. [EC: 3.4.21.75]
Release of mature proteins from their proproteins by cleavage of -Arg- Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors.
  • Activated by calcium.
  • Belongs to peptidase family S8.
 10 A0A024RC70 A0A044RE18 P09958 P23188 P23377 P26016 P29119 P30430 P30432 Q28193
C5a peptidase. [EC: 3.4.21.110]
The primary cleavage site is at 67-His-|-Lys-68 in human C5a with a minor secondary cleavage site at 58-Ala-|-Ser-59.
  • Surface-associated subtilisin-like serine peptidase with very specific substrate specificity.
  • Virulent strains of streptococci, including Streptococcus pyogenes, can evade human detection and phagocytosis by destroying the complement chemotaxin C5a.
  • Cleavage of human C5a by this enzyme reduces the ability of C5a to bind receptors on the surface of polymorphonuclear neutrophil leukocytes (PMNLs) and thereby abolishes its chemotactic properties.
  • Belongs to peptidase family S8A.
 8 A0A0E1EUF2 P0DD34 P0DD35 P15926 P58099 Q1JJR6 Q5X9R0 Q8NZ80
Lactocepin. [EC: 3.4.21.96]
Endopeptidase activity with very broad specificity, although some subsite preference have been noted, e.g. large hydrophobic residues in the P1 and P4 positions, and Pro in the P2 position. Best known for its action on caseins, although it has been shown to hydrolyze hemoglobin and oxidized insulin B-chain.
  • Responsible for the hydrolysis of casein in milk and the provision of peptides essential for cell growth.
  • Specificity differences between lactocepins from different starter strains may be partly responsible for imparating different flavor qualities to cheese.
  • Belongs to peptidase family S8.
 7 A0A165G7Q7 C2FBP6 P15292 P15293 P16271 Q02470 Q49SH0
Proprotein convertase 1. [EC: 3.4.21.93]
Release of protein hormones, neuropeptides and renin from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds.
  • A calcium dependent enzyme, maximally active at about pH 5.5.
  • Substrates include pro-opiomelanocortin, prorenin, proenkephalin, prodynorphin, prosomatostatin and proinsulin.
  • Unlike prohormone convertase 2, does not cleave proluteinizing- hormone-releasing hormone.
  • Usually processing of prodynorphin occurs at a bond in which P2 is Thr.
  • Present in the regulated secretory pathway of neuroendocrine cells, commonly actin co-operatively with prohormone convertase 2.
  • Belongs to peptidase family S8.
 6 P28840 P29120 P63239 P63240 Q32MU0 Q9GLR1
Site-1 protease. [EC: 3.4.21.112]
Processes precursors containing basic and hydrophobic/aliphatic residues at P4 and P2, respectively, with a relatively relaxed acceptance of amino acids at P1 and P3.
  • Cleaves sterol regulatory element-binding proteins (SREBPs) and thereby initiates a process by which the active fragments of the SREBPs translocate to the nucleus and activate genes controlling the synthesis and uptake of cholesterol and unsaturated fatty acids into the bloodstream.
  • The enzyme also processes pro-brain-derived neurotrophic factor and undergoes autocatalytic activation in the endoplasmic reticulum through sequential cleavages.
  • The enzyme can also process the unfolded protein response stress factor ATF6 at an Arg-His-Lys-Lys-|- site, and the envelope glycoprotein of the highly infectious Lassa virus and Crimean Congo hemorrhagic fever virus at Arg-Arg-Lys-Lys-|-.
  • Belongs to peptidase family S8A.
 4 Q14703 Q9WTZ2 Q9WTZ3 Q9Z2A8
Kexin. [EC: 3.4.21.61]
Cleavage of -Lys-Arg-|-Xaa- and -Arg-Arg-|-Xaa- bonds to process yeast alpha-factor pheromone and killer toxin precursors.
  • Calcium activated.
  • Inhibited by p-mercuribenzoate.
  • Belongs to peptidase family S8.
  • Formerly EC 3.4.22.23.
 3 A0A0L8VI93 O13359 P13134
Xanthomonalisin. [EC: 3.4.21.101]
Cleavage of casein.
  • Secreted by the bacterium Xanthomonas sp.
  • Belongs to peptidase family S53.
  • Formerly EC 3.4.23.33.
 1 Q60106
Cucumisin. [EC: 3.4.21.25]
Hydrolysis of proteins with broad specificity.
  • From the sarcocarp of the musk melon (Cucumis melo).
  • Other endopeptidases from plants, which are less well characterized but presumably of serine-type, include euphorbain from Euphorbia cerifera, solanain from horse-nettle Solanum elaeagnifolium, hurain from Hura crepitans and tabernamontanain from Tabernamontana grandiflora.
  • Belongs to peptidase family S8.
 1 Q39547
Cerevisin. [EC: 3.4.21.48]
Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.
  • Contains a Cys residue near the active site His, and is inhibited by mercurials.
  • Proteinase ycaB is a similar enzyme from the yeast Candida albicans.
  • Belongs to peptidase family S8.
  • Formerly EC 3.4.22.9.
 1 P09232
Physarolisin. [EC: 3.4.21.103]
Milk clotting activity. Preferential cleavage of 8-Gly-|-Ser-9 in B chain of insulin most rapidly, followed by 11-Leu-|-Val-12, 19-Cys(SO(3)H)-|-Gly and 24-Phe-|-Phe-25. No action on Ac-Phe-Tyr(I)(2).
  • From the slime mold Physarum polycephalum.
  • Is not inhibited by pepstatin, but is blocked by methyl 2-diazoacetamidohexanoate.
  • Closely similar enzymes are found in Dictyostelium discoideum and P.flavicomum.
  • Belongs to peptidase family S53.
  • Formerly EC 3.4.4.17, EC 3.4.23.6 and EC 3.4.23.27.
 1 Q8MZS4
Thermitase. [EC: 3.4.21.66]
Hydrolysis of proteins, including collagen.
  • From Thermoactinomyces vulgaris containing a single Cys, near the active site His, and inhibited by p-mercuribenzoate.
  • The N-terminal extension of the polypeptide chain relative to subtilisin contributes to calcium-binding and the high thermostability.
  • The amino acid composition and properties of the thermostable enzyme from Streptomyces rectus var. proteolyticus are closely similar.
  • Belongs to peptidase family S8.
  • Formerly EC 3.4.4.16.
 1 P04072
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.
 1 P42790
Peptidase K. [EC: 3.4.21.64]
Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyzes peptide amides.
  • From the mold Tritirachium album Limber.
  • Contains two disulfide bridges and one free Cys near the active site His.
  • Belongs to peptidase family S8.
  • Formerly EC 3.4.4.16 and EC 3.4.21.14.
 1 P06873
Aqualysin 1. [EC: 3.4.21.111]
Exhibits low specificity toward esters of amino acids with small hydrophobic or aromatic residues at the P1 position.
  • This enzyme from the extreme thermophile, Thermus aquaticus, is an alkaline serine peptidase.
  • It has three subsites, S1, S2, and S3, in the substrate binding site.
  • The preferred amino acids at the S1 site are Ala and Phe, at the S2 site are Ala and norleucine and at the S3 site are Phe and Ile.
  • These specificities are similar to those of EC 3.4.21.62 and EC 3.4.21.64.
  • The enzyme displays broad specificity for cleavage of insulin B-chain and hydrolyzes elastin substrates such as succinyl-(Ala)(n)-p- nitroanilide (n = 1,2,3) and some peptide esters.
  • Belongs to peptidase family S8A.
 1 P08594