zinc metalloprotease may be a member of the astacin-like protease family or the adamalysin/reprolysin-like protease family| M10 family metallopeptidase domain-containing protein is a metalloendopeptidase similar to matrix metalloproteinases that may be endopeptidases that degrade various components of the extracellular matrix
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
221-400
8.99e-32
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.
The actual alignment was detected with superfamily member cd04269:
Pssm-ID: 469599 [Multi-domain] Cd Length: 194 Bit Score: 122.34 E-value: 8.99e-32
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
47-164
1.10e-15
Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.
:
Pssm-ID: 460254 Cd Length: 128 Bit Score: 73.89 E-value: 1.10e-15
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
498-601
6.64e-36
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.
Pssm-ID: 462504 Cd Length: 105 Bit Score: 130.81 E-value: 6.64e-36
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
221-400
8.99e-32
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: 122.34 E-value: 8.99e-32
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
421-495
2.41e-31
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.
Pssm-ID: 214490 Cd Length: 75 Bit Score: 117.02 E-value: 2.41e-31
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
47-164
1.10e-15
Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.
Pssm-ID: 460254 Cd Length: 128 Bit Score: 73.89 E-value: 1.10e-15
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
229-400
1.38e-07
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.
Pssm-ID: 426256 [Multi-domain] Cd Length: 200 Bit Score: 52.69 E-value: 1.38e-07
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
498-601
6.64e-36
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.
Pssm-ID: 462504 Cd Length: 105 Bit Score: 130.81 E-value: 6.64e-36
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
221-400
8.99e-32
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: 122.34 E-value: 8.99e-32
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
421-495
2.41e-31
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.
Pssm-ID: 214490 Cd Length: 75 Bit Score: 117.02 E-value: 2.41e-31
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
47-164
1.10e-15
Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.
Pssm-ID: 460254 Cd Length: 128 Bit Score: 73.89 E-value: 1.10e-15
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
229-400
1.38e-07
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.
Pssm-ID: 426256 [Multi-domain] Cd Length: 200 Bit Score: 52.69 E-value: 1.38e-07
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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