M10 family metallopeptidase similar to serralysin and Pseudomonas aeruginosa alkaline protease, which include an N-terminal peptidase domain and a C-terminal calcium-binding domain
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
29-208
1.15e-41
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.
:
Pssm-ID: 239804 [Multi-domain] Cd Length: 186 Bit Score: 147.95 E-value: 1.15e-41
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ...
209-358
2.27e-19
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain pfam00353.
The actual alignment was detected with superfamily member pfam08548:
Pssm-ID: 451582 [Multi-domain] Cd Length: 222 Bit Score: 87.04 E-value: 2.27e-19
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
29-208
1.15e-41
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.
Pssm-ID: 239804 [Multi-domain] Cd Length: 186 Bit Score: 147.95 E-value: 1.15e-41
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ...
209-358
2.27e-19
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain pfam00353.
Pssm-ID: 430067 [Multi-domain] Cd Length: 222 Bit Score: 87.04 E-value: 2.27e-19
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
68-209
3.68e-07
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.
Pssm-ID: 214576 [Multi-domain] Cd Length: 139 Bit Score: 49.66 E-value: 3.68e-07
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
29-208
1.15e-41
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.
Pssm-ID: 239804 [Multi-domain] Cd Length: 186 Bit Score: 147.95 E-value: 1.15e-41
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ...
209-358
2.27e-19
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain pfam00353.
Pssm-ID: 430067 [Multi-domain] Cd Length: 222 Bit Score: 87.04 E-value: 2.27e-19
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
74-207
1.82e-09
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.
Pssm-ID: 239796 [Multi-domain] Cd Length: 165 Bit Score: 56.74 E-value: 1.82e-09
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
71-207
7.06e-08
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.
Pssm-ID: 238124 [Multi-domain] Cd Length: 167 Bit Score: 52.14 E-value: 7.06e-08
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
68-209
3.68e-07
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.
Pssm-ID: 214576 [Multi-domain] Cd Length: 139 Bit Score: 49.66 E-value: 3.68e-07
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
68-208
3.28e-04
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).
Pssm-ID: 239805 [Multi-domain] Cd Length: 157 Bit Score: 41.42 E-value: 3.28e-04
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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