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InterPro: IPR018114 Peptidase S1/S6, chymotrypsin/Hap, active site
Protein matches
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UniProtKB Matches: 7885 proteins |
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Accession
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IPR018114 Peptidase_S1/S6_AS |
Type
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Active_site |
Signatures
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InterPro Relationships
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Found in
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IPR001254 Peptidase S1/S6, chymotrypsin/Hap
IPR001314 Peptidase S1A, chymotrypsin
IPR001316 Peptidase S1A, streptogrisin
IPR003966 Peptidase S1A, prothrombin/thrombin
IPR008256 Peptidase S1B, glutamyl endopeptidase I
IPR009003 Serine/cysteine peptidase, trypsin-like
IPR011163 Peptidase S1A, enteropeptidase
IPR011358 Peptidase S1A, plasmin
IPR011360 Complement B/C2
IPR012051 Peptidase S1A, prothrombin
IPR012224 Peptidase S1A, coagulation factor VII/IX/X/C/Z
IPR012267 Peptidase S1A, acrosin
IPR014394 Coagulation factor XII/hepatocyte growth factor activator
IPR017051 Suppressor of tumourigenicity 14
IPR017052 Atrial natriuteric peptide-converting enzyme
IPR017118 Matriptase-2
IPR017324 Transmembrane serine protease, TMPRSS9
IPR017326 Polyserase-2
IPR017327 Transmembrane serine protease, TMPRSS13
IPR017329 Serine protease, transmembrane, TMPRSS11A
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GO Term annotation
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Process
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GO:0006508 proteolysis
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Function
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GO:0004252 serine-type endopeptidase activity
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InterPro annotation
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Entry Details in BioMart
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Abstract
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This group of serine proteases belong to the MEROPS peptidase family S1 (chymotrypsin family, clan PA(S))and to peptidase family S6 (Hap serine peptidases). The catalytic activity of the serine proteases from the chymotrypsin 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 [1].
The chymotrypsin family is almost totally confined to animals, although trypsin-like enzymes are found in actinomycetes of the genera Streptomyces and Saccharopolyspora, and in the fungus Fusarium oxysporum [2]. The enzymes are inherently secreted, being synthesised with a signal peptide that
targets them to the secretory pathway. Animal enzymes are either secreted
directly, packaged into vesicles for regulated secretion, or are retained
in leukocyte granules [2].
The Hap family, 'Haemophilus adhesion and penetration', are proteins that play a role in the interaction with human epithelial cells. The serine protease activity is localized at the N-terminal domain, whereas the binding domain is in the C-terminal region.
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Structural links
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Database links
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Example proteins
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O00187 Mannan-binding lectin serine protease 2
P00743 Coagulation factor X
P00756 Kallikrein 1-related peptidase b3
P00775 Trypsin
P04814 Trypsin alpha
More proteins
Example Proteins Key
| InterPro entry accession number/name and structure databases |
Colour code |
| IPR000294 |
Gamma-carboxyglutamic acid-rich (GLA) domain |
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| IPR001881 |
EGF-like calcium-binding |
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| IPR001254 |
Peptidase S1/S6, chymotrypsin/Hap |
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| IPR002383 |
Coagulation factor, Gla domain |
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| IPR000859 |
CUB |
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| IPR006210 |
EGF-like |
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| IPR009003 |
Serine/cysteine peptidase, trypsin-like |
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| IPR016060 |
Complement control module |
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| IPR000152 |
EGF-type aspartate/asparagine hydroxylation site |
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| IPR000742 |
EGF-like, type 3 |
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| IPR018114 |
Peptidase S1/S6, chymotrypsin/Hap, active site |
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| IPR013032 |
EGF-like region, conserved site |
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| IPR000436 |
Sushi/SCR/CCP |
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| IPR012224 |
Peptidase S1A, coagulation factor VII/IX/X/C/Z |
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| IPR001314 |
Peptidase S1A, chymotrypsin |
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| IPR006209 |
EGF |
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| IPR018097 |
EGF-like calcium-binding, conserved site |
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PDB Chain |
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ModBase |
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CATH Domain |
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SWISS-MODEL |
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SCOP Domain |
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Additional Reading
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Getun IV, Brown CK, Tulla-Puche J, Ohlendorf D, Woodward C, Barany G.
Partially folded bovine pancreatic trypsin inhibitor analogues attain fully native structures when co-crystallized with S195A rat trypsin.
J. Mol. Biol. 375 2008 812-23
[PubMed: 18054043]
http://dx.doi.org/10.1016/j.jmb.2007.10.084
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Isaacs RC, Solinsky MG, Cutrona KJ, Newton CL, Naylor-Olsen AM, McMasters DR, Krueger JA, Lewis SD, Lucas BJ, Kuo LC, Yan Y, Lynch JJ, Lyle EA.
Structure-based design of novel groups for use in the P1 position of thrombin inhibitor scaffolds. Part 2: N-acetamidoimidazoles.
Bioorg. Med. Chem. Lett. 18 2008 2062-6
[PubMed: 18291642]
http://dx.doi.org/10.1016/j.bmcl.2008.01.098
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Lima LM, Becker CF, Giesel GM, Marques AF, Cargnelutti MT, de Oliveira Neto M, Monteiro RQ, Verli H, Polikarpov I.
Structural and thermodynamic analysis of thrombin:suramin interaction in solution and crystal phases.
Biochim. Biophys. Acta 1794 2009 873-81
[PubMed: 19332154]
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Nieman MT, Burke F, Warnock M, Zhou Y, Sweigart J, Chen A, Ricketts D, Lucchesi BR, Chen Z, Di Cera E, Hilfinger J, Kim JS, Mosberg HI, Schmaier AH.
Thrombostatin FM compounds: direct thrombin inhibitors - mechanism of action in vitro and in vivo.
J. Thromb. Haemost. 6 2008 837-45
[PubMed: 18315550]
http://dx.doi.org/10.1111/j.1538-7836.2008.02937.x
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Fernandez IS, Standker L, Magert HJ, Forssmann WG, Gimenez-Gallego G, Romero A.
Crystal structure of human epidermal kallikrein 7 (hK7) synthesized directly in its native state in E. coli: insights into the atomic basis of its inhibition by LEKTI domain 6 (LD6).
J. Mol. Biol. 377 2008 1488-97
[PubMed: 18329042]
http://dx.doi.org/10.1016/j.jmb.2008.01.089
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InterPro 23.1
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