zinc-dependent metalloprotease containing DUF5118, DUF5117 and DUF4953 domains, contains the extended met-zincin motif HExxHxxGxxH/D, with the first two histidines acting as ligands of the catalytic zinc, the glutamate as the general base, a strictly conserved glycine, and a third zinc-binding histidine or aspartate
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
431-737
6.30e-124
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic met-zincin mmotif HExxHxxGxxH, the extended zinc-binding domain of metallopeptidases.
:
Pssm-ID: 435269 Cd Length: 319 Bit Score: 376.59 E-value: 6.30e-124
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
304-523
1.40e-81
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.
:
Pssm-ID: 239803 Cd Length: 197 Bit Score: 260.72 E-value: 1.40e-81
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
431-737
6.30e-124
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic met-zincin mmotif HExxHxxGxxH, the extended zinc-binding domain of metallopeptidases.
Pssm-ID: 435269 Cd Length: 319 Bit Score: 376.59 E-value: 6.30e-124
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
304-523
1.40e-81
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.
Pssm-ID: 239803 Cd Length: 197 Bit Score: 260.72 E-value: 1.40e-81
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
431-456
6.21e-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: 41.04 E-value: 6.21e-04
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
442-456
8.70e-03
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: 37.33 E-value: 8.70e-03
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
431-737
6.30e-124
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic met-zincin mmotif HExxHxxGxxH, the extended zinc-binding domain of metallopeptidases.
Pssm-ID: 435269 Cd Length: 319 Bit Score: 376.59 E-value: 6.30e-124
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
304-523
1.40e-81
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.
Pssm-ID: 239803 Cd Length: 197 Bit Score: 260.72 E-value: 1.40e-81
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
311-522
6.29e-43
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: 153.42 E-value: 6.29e-43
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
311-522
4.19e-06
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: 47.90 E-value: 4.19e-06
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
431-456
6.21e-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: 41.04 E-value: 6.21e-04
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
441-518
2.05e-03
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: 40.09 E-value: 2.05e-03
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
442-456
8.70e-03
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: 37.33 E-value: 8.70e-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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