M60 family metallopeptidase [Bacteroides caccae]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| Peptidase_M60 super family | cl24257 | Peptidase M60, enhancin and enhancin-like; This family of peptidases contains a zinc ... |
456-728 | 1.72e-24 | |||||
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: 104.00 E-value: 1.72e-24
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| Peptidase_M60_C | pfam18630 | Peptidase M60 C-terminal domain; This is C-terminal domain (CTD) of M60-peptidases pfam13402. ... |
812-882 | 2.25e-16 | |||||
Peptidase M60 C-terminal domain; This is C-terminal domain (CTD) of M60-peptidases pfam13402. It Can also be found at the C-terminal region of gingipain B (RgpB) from P. gingivalis. It was found to possess a typical Ig-like fold encompassing seven antiparallel beta-strands organized in two beta-sheets, packed into a beta-sandwich structure that can spontaneously dimerize through C-terminal strand swapping. Translocation of gingipains from the periplasm across the OM is dependent on the conserved CTD, which appears to be important for secretion of the proteins and in particular, truncation of the last few C-terminal residues of this domain leads to accumulation of gingipains in the periplasm. Subsequently, the T9SS targeting signal was demonstrated to reside within the last 22 residues at the C-terminus of the CTD. During gingipain translocation across the OM, the CTD is cleaved off by PorU. : Pssm-ID: 408412 Cd Length: 65 Bit Score: 74.02 E-value: 2.25e-16
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| BACON super family | cl15232 | Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain; The ... |
34-116 | 2.94e-06 | |||||
Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain; The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes. The actual alignment was detected with superfamily member cd14948: Pssm-ID: 449511 [Multi-domain] Cd Length: 83 Bit Score: 46.10 E-value: 2.94e-06
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| F5_F8_type_C | pfam00754 | F5/8 type C domain; This domain is also known as the discoidin (DS) domain family. |
136-268 | 8.01e-04 | |||||
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family. : Pssm-ID: 459925 [Multi-domain] Cd Length: 127 Bit Score: 40.12 E-value: 8.01e-04
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| Name | Accession | Description | Interval | E-value | |||||
| Peptidase_M60 | pfam13402 | Peptidase M60, enhancin and enhancin-like; This family of peptidases contains a zinc ... |
456-728 | 1.72e-24 | |||||
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: 104.00 E-value: 1.72e-24
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| Peptidase_M60_C | pfam18630 | Peptidase M60 C-terminal domain; This is C-terminal domain (CTD) of M60-peptidases pfam13402. ... |
812-882 | 2.25e-16 | |||||
Peptidase M60 C-terminal domain; This is C-terminal domain (CTD) of M60-peptidases pfam13402. It Can also be found at the C-terminal region of gingipain B (RgpB) from P. gingivalis. It was found to possess a typical Ig-like fold encompassing seven antiparallel beta-strands organized in two beta-sheets, packed into a beta-sandwich structure that can spontaneously dimerize through C-terminal strand swapping. Translocation of gingipains from the periplasm across the OM is dependent on the conserved CTD, which appears to be important for secretion of the proteins and in particular, truncation of the last few C-terminal residues of this domain leads to accumulation of gingipains in the periplasm. Subsequently, the T9SS targeting signal was demonstrated to reside within the last 22 residues at the C-terminus of the CTD. During gingipain translocation across the OM, the CTD is cleaved off by PorU. Pssm-ID: 408412 Cd Length: 65 Bit Score: 74.02 E-value: 2.25e-16
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| BACON | cd14948 | Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain; The ... |
34-116 | 2.94e-06 | |||||
Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain; The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes. Pssm-ID: 271342 [Multi-domain] Cd Length: 83 Bit Score: 46.10 E-value: 2.94e-06
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| F5_F8_type_C | pfam00754 | F5/8 type C domain; This domain is also known as the discoidin (DS) domain family. |
136-268 | 8.01e-04 | |||||
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family. Pssm-ID: 459925 [Multi-domain] Cd Length: 127 Bit Score: 40.12 E-value: 8.01e-04
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| ImpA_fam_HExGH | NF038322 | ImpA family metalloprotease; Members of this family are metalloproteases related to the ImpA ... |
583-626 | 9.80e-04 | |||||
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: 42.99 E-value: 9.80e-04
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| Name | Accession | Description | Interval | E-value | |||||
| Peptidase_M60 | pfam13402 | Peptidase M60, enhancin and enhancin-like; This family of peptidases contains a zinc ... |
456-728 | 1.72e-24 | |||||
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: 104.00 E-value: 1.72e-24
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| Peptidase_M60_C | pfam18630 | Peptidase M60 C-terminal domain; This is C-terminal domain (CTD) of M60-peptidases pfam13402. ... |
812-882 | 2.25e-16 | |||||
Peptidase M60 C-terminal domain; This is C-terminal domain (CTD) of M60-peptidases pfam13402. It Can also be found at the C-terminal region of gingipain B (RgpB) from P. gingivalis. It was found to possess a typical Ig-like fold encompassing seven antiparallel beta-strands organized in two beta-sheets, packed into a beta-sandwich structure that can spontaneously dimerize through C-terminal strand swapping. Translocation of gingipains from the periplasm across the OM is dependent on the conserved CTD, which appears to be important for secretion of the proteins and in particular, truncation of the last few C-terminal residues of this domain leads to accumulation of gingipains in the periplasm. Subsequently, the T9SS targeting signal was demonstrated to reside within the last 22 residues at the C-terminus of the CTD. During gingipain translocation across the OM, the CTD is cleaved off by PorU. Pssm-ID: 408412 Cd Length: 65 Bit Score: 74.02 E-value: 2.25e-16
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| BACON | cd14948 | Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain; The ... |
34-116 | 2.94e-06 | |||||
Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain; The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes. Pssm-ID: 271342 [Multi-domain] Cd Length: 83 Bit Score: 46.10 E-value: 2.94e-06
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| F5_F8_type_C | pfam00754 | F5/8 type C domain; This domain is also known as the discoidin (DS) domain family. |
136-268 | 8.01e-04 | |||||
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family. Pssm-ID: 459925 [Multi-domain] Cd Length: 127 Bit Score: 40.12 E-value: 8.01e-04
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| ImpA_fam_HExGH | NF038322 | ImpA family metalloprotease; Members of this family are metalloproteases related to the ImpA ... |
583-626 | 9.80e-04 | |||||
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: 42.99 E-value: 9.80e-04
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