zinc-dependent metalloprotease similar to Xanthomonas campestris peptidyl-Asp metalloendopeptidase that specifically cleaves on the N-terminal side of aspartyl, glutamyl and cysteic acid residues
CHU_C Type IX secretion signal domain; This domain was initially identified from proteins from ...
906-997
3.95e-17
CHU_C Type IX secretion signal domain; This domain was initially identified from proteins from C. hutchinsonii giving rise to the CHU name. This domain adopts an immunoglobulin like domain that is foundat the C-terminus of various bacterial cell surface proteins. This domain was shown to be essential for localization of the CHU_3220 protein. It is likely that this domain target the proteins containing it to the type IX secretion system. This domain is cleaved off the protein which is then anchored to the outer membrane.
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Pssm-ID: 404473 [Multi-domain] Cd Length: 85 Bit Score: 77.22 E-value: 3.95e-17
CHU_C Type IX secretion signal domain; This domain was initially identified from proteins from ...
906-997
3.95e-17
CHU_C Type IX secretion signal domain; This domain was initially identified from proteins from C. hutchinsonii giving rise to the CHU name. This domain adopts an immunoglobulin like domain that is foundat the C-terminus of various bacterial cell surface proteins. This domain was shown to be essential for localization of the CHU_3220 protein. It is likely that this domain target the proteins containing it to the type IX secretion system. This domain is cleaved off the protein which is then anchored to the outer membrane.
Pssm-ID: 404473 [Multi-domain] Cd Length: 85 Bit Score: 77.22 E-value: 3.95e-17
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
247-344
1.60e-05
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: 46.64 E-value: 1.60e-05
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
240-341
5.39e-05
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: 44.26 E-value: 5.39e-05
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
170-364
3.66e-29
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.
Pssm-ID: 404471 Cd Length: 203 Bit Score: 115.79 E-value: 3.66e-29
CHU_C Type IX secretion signal domain; This domain was initially identified from proteins from ...
906-997
3.95e-17
CHU_C Type IX secretion signal domain; This domain was initially identified from proteins from C. hutchinsonii giving rise to the CHU name. This domain adopts an immunoglobulin like domain that is foundat the C-terminus of various bacterial cell surface proteins. This domain was shown to be essential for localization of the CHU_3220 protein. It is likely that this domain target the proteins containing it to the type IX secretion system. This domain is cleaved off the protein which is then anchored to the outer membrane.
Pssm-ID: 404473 [Multi-domain] Cd Length: 85 Bit Score: 77.22 E-value: 3.95e-17
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
208-313
5.86e-07
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.
Pssm-ID: 463926 [Multi-domain] Cd Length: 122 Bit Score: 49.29 E-value: 5.86e-07
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
247-344
1.60e-05
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: 46.64 E-value: 1.60e-05
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
242-355
4.54e-05
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: 44.82 E-value: 4.54e-05
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
240-341
5.39e-05
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: 44.26 E-value: 5.39e-05
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
176-309
9.45e-04
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.
Pssm-ID: 239797 [Multi-domain] Cd Length: 194 Bit Score: 41.45 E-value: 9.45e-04
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
298-353
4.45e-03
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: 39.02 E-value: 4.45e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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