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unnamed protein product [Homo sapiens]
List of domain hits
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Name | Accession | Description | Interval | E-value | ||
Peptidase_M10 super family | cl37987 | Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ... |
103-167 | 3.39e-25 | ||
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. The actual alignment was detected with superfamily member pfam00413: Pssm-ID: 425668 [Multi-domain] Cd Length: 159 Bit Score: 95.38 E-value: 3.39e-25
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PG_binding_1 | pfam01471 | Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ... |
31-82 | 6.63e-10 | ||
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally. : Pssm-ID: 460223 [Multi-domain] Cd Length: 57 Bit Score: 52.52 E-value: 6.63e-10
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Name | Accession | Description | Interval | E-value | ||
Peptidase_M10 | pfam00413 | Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ... |
103-167 | 3.39e-25 | ||
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Pssm-ID: 425668 [Multi-domain] Cd Length: 159 Bit Score: 95.38 E-value: 3.39e-25
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ZnMc_MMP | cd04278 | Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ... |
103-168 | 3.04e-21 | ||
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: 85.33 E-value: 3.04e-21
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PG_binding_1 | pfam01471 | Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ... |
31-82 | 6.63e-10 | ||
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally. Pssm-ID: 460223 [Multi-domain] Cd Length: 57 Bit Score: 52.52 E-value: 6.63e-10
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ZnMc | smart00235 | Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ... |
100-161 | 1.73e-08 | ||
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: 51.20 E-value: 1.73e-08
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Name | Accession | Description | Interval | E-value | ||
Peptidase_M10 | pfam00413 | Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ... |
103-167 | 3.39e-25 | ||
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Pssm-ID: 425668 [Multi-domain] Cd Length: 159 Bit Score: 95.38 E-value: 3.39e-25
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ZnMc_MMP | cd04278 | Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ... |
103-168 | 3.04e-21 | ||
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: 85.33 E-value: 3.04e-21
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PG_binding_1 | pfam01471 | Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ... |
31-82 | 6.63e-10 | ||
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally. Pssm-ID: 460223 [Multi-domain] Cd Length: 57 Bit Score: 52.52 E-value: 6.63e-10
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ZnMc | smart00235 | Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ... |
100-161 | 1.73e-08 | ||
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: 51.20 E-value: 1.73e-08
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ZnMc | cd00203 | Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
107-168 | 2.55e-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: 45.59 E-value: 2.55e-06
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Blast search parameters | ||||
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