M60 family metallopeptidase similar to enhancin, a peptidase that contains zinc metallopeptidase motif (HEXXHX(8,28)E) and possesses mucinase activity; includes the viral enhancins as well as enhancin-like peptidases from bacterial species
Peptidase M60, enhancin and enhancin-like; This family of peptidases contains a zinc ...
151-420
3.79e-53
Peptidase M60, enhancin and enhancin-like; This family of peptidases contains a zinc metallopeptidase motif (HEXXHX(8,28)E) and possesses mucinase activity. It includes the viral enhancins as well as enhancin-like peptidases from bacterial species. Enhancins are a class of metalloproteases found in some baculoviruses that enhance viral infection by degrading the peritrophic membrane (PM) of the insect midgut. Bacterial enhancins are found to be cytotoxic when compared to viral enhancin, however, suggesting that the bacterial enhancins do not enhance infection in the same way as viral enhancin. Bacterial enhancins may have evolved a distinct biochemical function. These bacterial domains are peptidases targetting host glycoproteins and thus probably play an important role in successful colonization of both vertebrate mucosal surfaces and the invertebrate digestive tract by both mutualistic and pathogenic microbes. This family has been augmented by a merge with the sequences in the Enhancin Pfam family.
The actual alignment was detected with superfamily member pfam13402:
Pssm-ID: 433178 [Multi-domain] Cd Length: 268 Bit Score: 182.19 E-value: 3.79e-53
Peptidase M60, enhancin and enhancin-like; This family of peptidases contains a zinc ...
151-420
3.79e-53
Peptidase M60, enhancin and enhancin-like; This family of peptidases contains a zinc metallopeptidase motif (HEXXHX(8,28)E) and possesses mucinase activity. It includes the viral enhancins as well as enhancin-like peptidases from bacterial species. Enhancins are a class of metalloproteases found in some baculoviruses that enhance viral infection by degrading the peritrophic membrane (PM) of the insect midgut. Bacterial enhancins are found to be cytotoxic when compared to viral enhancin, however, suggesting that the bacterial enhancins do not enhance infection in the same way as viral enhancin. Bacterial enhancins may have evolved a distinct biochemical function. These bacterial domains are peptidases targetting host glycoproteins and thus probably play an important role in successful colonization of both vertebrate mucosal surfaces and the invertebrate digestive tract by both mutualistic and pathogenic microbes. This family has been augmented by a merge with the sequences in the Enhancin Pfam family.
Pssm-ID: 433178 [Multi-domain] Cd Length: 268 Bit Score: 182.19 E-value: 3.79e-53
ImpA family metalloprotease; Members of this family are metalloproteases related to the ImpA ...
79-439
7.79e-09
ImpA family metalloprotease; Members of this family are metalloproteases related to the ImpA from Pseudomonas aeruginosa (PA0572 in strain PAO1), a virulence factor that cleaves CD44 on the surface of human macrophages, inhibiting phagocytosis. Members of this family are distinguished by a strong motif, CGxGCSGNPxD, just a few residues upstream of the familiar metalloprotease motif HExxH (typically HELGH here) and completely lacking in more distant homologs of ImpA.
Pssm-ID: 468474 [Multi-domain] Cd Length: 879 Bit Score: 58.78 E-value: 7.79e-09
Peptidase M60, enhancin and enhancin-like; This family of peptidases contains a zinc ...
151-420
3.79e-53
Peptidase M60, enhancin and enhancin-like; This family of peptidases contains a zinc metallopeptidase motif (HEXXHX(8,28)E) and possesses mucinase activity. It includes the viral enhancins as well as enhancin-like peptidases from bacterial species. Enhancins are a class of metalloproteases found in some baculoviruses that enhance viral infection by degrading the peritrophic membrane (PM) of the insect midgut. Bacterial enhancins are found to be cytotoxic when compared to viral enhancin, however, suggesting that the bacterial enhancins do not enhance infection in the same way as viral enhancin. Bacterial enhancins may have evolved a distinct biochemical function. These bacterial domains are peptidases targetting host glycoproteins and thus probably play an important role in successful colonization of both vertebrate mucosal surfaces and the invertebrate digestive tract by both mutualistic and pathogenic microbes. This family has been augmented by a merge with the sequences in the Enhancin Pfam family.
Pssm-ID: 433178 [Multi-domain] Cd Length: 268 Bit Score: 182.19 E-value: 3.79e-53
ImpA family metalloprotease; Members of this family are metalloproteases related to the ImpA ...
79-439
7.79e-09
ImpA family metalloprotease; Members of this family are metalloproteases related to the ImpA from Pseudomonas aeruginosa (PA0572 in strain PAO1), a virulence factor that cleaves CD44 on the surface of human macrophages, inhibiting phagocytosis. Members of this family are distinguished by a strong motif, CGxGCSGNPxD, just a few residues upstream of the familiar metalloprotease motif HExxH (typically HELGH here) and completely lacking in more distant homologs of ImpA.
Pssm-ID: 468474 [Multi-domain] Cd Length: 879 Bit Score: 58.78 E-value: 7.79e-09
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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