The domain within your query sequence starts at position 478 and ends at position 711; the E-value for the Tryp_SPc domain shown below is 5.03e-5.

WARNING!
Some of the required catalytic sites were not detected in this domain. It is probably inactive! Check the literature (PubMed 95010055 ) for details.

Catalytic residues
PositionAmino acidPresent?
DomainProtein
46523HYes
96573DYes
N/AN/ASNo
VWEHKKGNDYHKQPWQAKISVTRPLKGHETCMGAVVSEYFVLTAAHCFMVDDQKHSIKVS
VGGQRRDLEIEEVLFHPKYNINGKKAEGIPEFYDYDVALVKLKNKLKYGQTLRPICLPCT
EGTTRALRLPQTATCKQHKEQLLPVKDVKALFVSEQGKSLTRKEVYIKNGDKPVVREMLQ
RPKAMRRSKMPLRWSLHGSSAQEGWIPMLTPTHAKEIPGALSLFTREAASFKLV

Tryp_SPc

Trypsin-like serine protease
Tryp_SPc
SMART accession number:SM00020
Description: Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.
Interpro abstract (IPR001254):

This entry represents the active-site-containing domain found in the trypsin family members. The catalytic activity of the serine proteases from the trypsin family is provided by a charge relay system involving an aspartic acid residue hydrogen-bonded to a histidine, which itself is hydrogen-bonded to a serine. The sequences in the vicinity of the active site serine and histidine residues are well conserved in this family of proteases [(PUBMED:3136396)]. A partial list of proteases known to belong to the trypsin family is shown below.

  • Acrosin.
  • Blood coagulation factors VII, IX, X, XI and XII, thrombin, plasminogen, and protein C.
  • Cathepsin G.
  • Chymotrypsins.
  • Complement components C1r, C1s, C2, and complement factors B, D and I.
  • Complement-activating component of RA-reactive factor.
  • Cytotoxic cell proteases (granzymes A to H).
  • Duodenase I.
  • Elastases 1, 2, 3A, 3B (protease E), leukocyte (medullasin).
  • Enterokinase (EC 3.4.21.9) (enteropeptidase).
  • Hepatocyte growth factor activator.
  • Hepsin.
  • Glandular (tissue) kallikreins (including EGF-binding protein types A, B, and C, NGF-gamma chain, gamma-renin, prostate specific antigen (PSA) and tonin).
  • Plasma kallikrein.
  • Mast cell proteases (MCP) 1 (chymase) to 8.
  • Myeloblastin (proteinase 3) (Wegener's autoantigen).
  • Plasminogen activators (urokinase-type, and tissue-type).
  • Trypsins I, II, III, and IV.
  • Tryptases.

All the above proteins belong to family S1 in the classification of peptidases [(PUBMED:7845208)] and originate from eukaryotic species. It should be noted that bacterial proteases that belong to family S2A are similar enough in the regions of the active site residues that they can be picked up by the same patterns. These proteases are listed below.

  • Achromobacter lyticus protease I.
  • Lysobacter alpha-lytic protease.
  • Streptogrisin A and B (Streptomyces proteases A and B).
  • Streptomyces griseus glutamyl endopeptidase II.
  • Streptomyces fradiae proteases 1 and 2.
GO process:proteolysis (GO:0006508)
GO function:serine-type endopeptidase activity (GO:0004252)
Family alignment:
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There are 111555 Tryp_SPc domains in 106560 proteins in SMART's nrdb database.

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