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matrilysin preproprotein [Homo sapiens]
matrilysin family metalloendoprotease( domain architecture ID 12021146)
matrilysin family metalloendoprotease may play a role in the degradation and remodeling of the extracellular matrix, such as mammalian matrilysin (matrix metallolproteinase-7 or MMP-7), which degrades casein, type I, III, IV, and V gelatin, as well as fibronectin, and which activates procollagenase
List of domain hits
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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 ... |
103-259 | 7.31e-97 | |||
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: 280.66 E-value: 7.31e-97
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PG_binding_1 | pfam01471 | Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ... |
31-82 | 1.69e-09 | |||
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: 1.69e-09
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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 ... |
103-259 | 7.31e-97 | ||||
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: 280.66 E-value: 7.31e-97
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ZnMc_MMP | cd04278 | Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ... |
103-259 | 1.57e-85 | ||||
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: 252.12 E-value: 1.57e-85
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ZnMc | smart00235 | Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ... |
100-260 | 8.31e-35 | ||||
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: 122.07 E-value: 8.31e-35
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PG_binding_1 | pfam01471 | Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ... |
31-82 | 1.69e-09 | ||||
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: 1.69e-09
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COG5549 | COG5549 | Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ... |
129-258 | 2.51e-08 | ||||
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444292 [Multi-domain] Cd Length: 234 Bit Score: 53.15 E-value: 2.51e-08
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archmetzin | NF033823 | archaemetzincin family Zn-dependent metalloprotease; |
212-233 | 1.08e-04 | ||||
archaemetzincin family Zn-dependent metalloprotease; Pssm-ID: 468195 Cd Length: 170 Bit Score: 41.84 E-value: 1.08e-04
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PRK13267 | PRK13267 | archaemetzincin-like protein; Reviewed |
212-233 | 1.76e-03 | ||||
archaemetzincin-like protein; Reviewed Pssm-ID: 237325 Cd Length: 179 Bit Score: 38.46 E-value: 1.76e-03
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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 ... |
103-259 | 7.31e-97 | ||||
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: 280.66 E-value: 7.31e-97
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ZnMc_MMP | cd04278 | Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ... |
103-259 | 1.57e-85 | ||||
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: 252.12 E-value: 1.57e-85
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ZnMc | smart00235 | Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ... |
100-260 | 8.31e-35 | ||||
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: 122.07 E-value: 8.31e-35
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ZnMc | cd00203 | Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
107-258 | 1.25e-28 | ||||
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: 106.84 E-value: 1.25e-28
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ZnMc_MMP_like | cd04268 | Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ... |
107-258 | 1.03e-17 | ||||
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: 77.92 E-value: 1.03e-17
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ZnMc_MMP_like_1 | cd04279 | Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ... |
129-259 | 1.38e-12 | ||||
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: 64.01 E-value: 1.38e-12
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ZnMc_serralysin_like | cd04277 | Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ... |
127-259 | 9.52e-12 | ||||
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: 62.05 E-value: 9.52e-12
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PG_binding_1 | pfam01471 | Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ... |
31-82 | 1.69e-09 | ||||
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: 1.69e-09
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COG5549 | COG5549 | Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ... |
129-258 | 2.51e-08 | ||||
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444292 [Multi-domain] Cd Length: 234 Bit Score: 53.15 E-value: 2.51e-08
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archmetzin | NF033823 | archaemetzincin family Zn-dependent metalloprotease; |
212-233 | 1.08e-04 | ||||
archaemetzincin family Zn-dependent metalloprotease; Pssm-ID: 468195 Cd Length: 170 Bit Score: 41.84 E-value: 1.08e-04
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Peptidase_M54 | cd11375 | Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ... |
212-235 | 1.80e-04 | ||||
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: 41.13 E-value: 1.80e-04
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COG1913 | COG1913 | Predicted Zn-dependent protease [General function prediction only]; |
212-235 | 3.23e-04 | ||||
Predicted Zn-dependent protease [General function prediction only]; Pssm-ID: 441517 Cd Length: 175 Bit Score: 40.33 E-value: 3.23e-04
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PRK13267 | PRK13267 | archaemetzincin-like protein; Reviewed |
212-233 | 1.76e-03 | ||||
archaemetzincin-like protein; Reviewed Pssm-ID: 237325 Cd Length: 179 Bit Score: 38.46 E-value: 1.76e-03
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ZnMc_ADAM_like | cd04267 | Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
212-259 | 2.27e-03 | ||||
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. Pssm-ID: 239795 Cd Length: 192 Bit Score: 38.17 E-value: 2.27e-03
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ZnMc_MMP_like_3 | cd04327 | Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ... |
129-224 | 4.14e-03 | ||||
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: 37.36 E-value: 4.14e-03
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ZnMc_ADAMTS_like | cd04273 | Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
200-240 | 8.88e-03 | ||||
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix. Pssm-ID: 239801 Cd Length: 207 Bit Score: 36.45 E-value: 8.88e-03
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Blast search parameters | ||||
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