neutrophil collagenase [Canis lupus familiaris]
matrix metalloproteinase( domain architecture ID 12021147)
matrix metalloproteinase is an M10A family metallopeptidase with a C-terminal hemopexin repeat-containing domain, such as stromelysin-1 (matrix metalloproteinase-3), which can degrade fibronectin, laminin, type I, III, IV, and V gelatins, collagens III, IV, X, and IX, as well as cartilage proteoglycans
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
Peptidase_M10 | pfam00413 | Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ... |
118-273 | 2.25e-90 | ||||
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: 271.80 E-value: 2.25e-90
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HX | cd00094 | Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ... |
287-475 | 4.72e-73 | ||||
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat. : Pssm-ID: 238046 [Multi-domain] Cd Length: 194 Bit Score: 228.74 E-value: 4.72e-73
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PG_binding_1 | pfam01471 | Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ... |
42-97 | 2.77e-07 | ||||
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: 426277 [Multi-domain] Cd Length: 57 Bit Score: 47.12 E-value: 2.77e-07
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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 ... |
118-273 | 2.25e-90 | ||||
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: 271.80 E-value: 2.25e-90
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ZnMc_MMP | cd04278 | Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ... |
118-273 | 2.27e-81 | ||||
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: 248.66 E-value: 2.27e-81
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HX | cd00094 | Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ... |
287-475 | 4.72e-73 | ||||
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat. Pssm-ID: 238046 [Multi-domain] Cd Length: 194 Bit Score: 228.74 E-value: 4.72e-73
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ZnMc | smart00235 | Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ... |
115-274 | 5.13e-34 | ||||
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: 124.77 E-value: 5.13e-34
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HX | smart00120 | Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ... |
388-433 | 1.89e-11 | ||||
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). Pssm-ID: 214524 [Multi-domain] Cd Length: 45 Bit Score: 58.79 E-value: 1.89e-11
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Hemopexin | pfam00045 | Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ... |
388-433 | 2.21e-09 | ||||
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs). Pssm-ID: 395000 [Multi-domain] Cd Length: 44 Bit Score: 52.95 E-value: 2.21e-09
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PG_binding_1 | pfam01471 | Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ... |
42-97 | 2.77e-07 | ||||
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: 426277 [Multi-domain] Cd Length: 57 Bit Score: 47.12 E-value: 2.77e-07
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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 ... |
118-273 | 2.25e-90 | ||||
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: 271.80 E-value: 2.25e-90
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ZnMc_MMP | cd04278 | Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ... |
118-273 | 2.27e-81 | ||||
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: 248.66 E-value: 2.27e-81
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HX | cd00094 | Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ... |
287-475 | 4.72e-73 | ||||
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat. Pssm-ID: 238046 [Multi-domain] Cd Length: 194 Bit Score: 228.74 E-value: 4.72e-73
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ZnMc | smart00235 | Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ... |
115-274 | 5.13e-34 | ||||
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: 124.77 E-value: 5.13e-34
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ZnMc_MMP_like_1 | cd04279 | Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ... |
142-273 | 1.15e-16 | ||||
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin. Pssm-ID: 239806 [Multi-domain] Cd Length: 156 Bit Score: 77.11 E-value: 1.15e-16
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ZnMc_serralysin_like | cd04277 | Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ... |
143-273 | 8.67e-16 | ||||
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: 75.53 E-value: 8.67e-16
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ZnMc | cd00203 | Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
138-272 | 1.18e-12 | ||||
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: 66.01 E-value: 1.18e-12
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HX | smart00120 | Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ... |
388-433 | 1.89e-11 | ||||
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). Pssm-ID: 214524 [Multi-domain] Cd Length: 45 Bit Score: 58.79 E-value: 1.89e-11
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ZnMc_MMP_like | cd04268 | Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ... |
143-272 | 1.10e-10 | ||||
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: 60.20 E-value: 1.10e-10
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Hemopexin | pfam00045 | Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ... |
388-433 | 2.21e-09 | ||||
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs). Pssm-ID: 395000 [Multi-domain] Cd Length: 44 Bit Score: 52.95 E-value: 2.21e-09
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PG_binding_1 | pfam01471 | Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ... |
42-97 | 2.77e-07 | ||||
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: 426277 [Multi-domain] Cd Length: 57 Bit Score: 47.12 E-value: 2.77e-07
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Hemopexin | pfam00045 | Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ... |
340-383 | 1.13e-06 | ||||
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs). Pssm-ID: 395000 [Multi-domain] Cd Length: 44 Bit Score: 45.25 E-value: 1.13e-06
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HX | smart00120 | Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ... |
296-337 | 5.40e-06 | ||||
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). Pssm-ID: 214524 [Multi-domain] Cd Length: 45 Bit Score: 43.39 E-value: 5.40e-06
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HX | smart00120 | Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ... |
340-379 | 7.91e-06 | ||||
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). Pssm-ID: 214524 [Multi-domain] Cd Length: 45 Bit Score: 42.61 E-value: 7.91e-06
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Reprolysin_5 | pfam13688 | Metallo-peptidase family M12; |
146-278 | 1.62e-05 | ||||
Metallo-peptidase family M12; Pssm-ID: 372673 Cd Length: 191 Bit Score: 45.49 E-value: 1.62e-05
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ZnMc_MMP_like_3 | cd04327 | Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ... |
136-238 | 2.67e-05 | ||||
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin. Pssm-ID: 239819 [Multi-domain] Cd Length: 198 Bit Score: 45.06 E-value: 2.67e-05
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Hemopexin | pfam00045 | Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ... |
296-337 | 5.53e-04 | ||||
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs). Pssm-ID: 395000 [Multi-domain] Cd Length: 44 Bit Score: 37.55 E-value: 5.53e-04
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ZnMc_salivary_gland_MPs | cd04272 | Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
215-264 | 1.46e-03 | ||||
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods. Pssm-ID: 239800 Cd Length: 220 Bit Score: 40.03 E-value: 1.46e-03
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Peptidase_M54 | cd11375 | Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ... |
218-248 | 1.91e-03 | ||||
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events. Pssm-ID: 213029 Cd Length: 173 Bit Score: 39.20 E-value: 1.91e-03
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ZnMc_MMP_like_2 | cd04276 | Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ... |
168-258 | 2.37e-03 | ||||
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: 39.23 E-value: 2.37e-03
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Blast search parameters | ||||
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