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hypothetical protein WH5701_11619 [Synechococcus sp. WH 5701]
ZnMc_MMP_like_1 domain-containing protein( domain architecture ID 10136682)
ZnMc_MMP_like_1 domain-containing protein
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||
ZnMc_MMP_like_1 | cd04279 | Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ... |
9-167 | 1.01e-42 | ||||
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: 139.90 E-value: 1.01e-42
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Name | Accession | Description | Interval | E-value | ||||
ZnMc_MMP_like_1 | cd04279 | Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ... |
9-167 | 1.01e-42 | ||||
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: 139.90 E-value: 1.01e-42
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COG5549 | COG5549 | Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ... |
1-169 | 5.61e-37 | ||||
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444292 [Multi-domain] Cd Length: 234 Bit Score: 127.49 E-value: 5.61e-37
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Peptidase_M10 | pfam00413 | Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ... |
117-166 | 4.43e-06 | ||||
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: 44.53 E-value: 4.43e-06
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ZnMc | smart00235 | Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ... |
119-168 | 4.07e-04 | ||||
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: 38.49 E-value: 4.07e-04
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Name | Accession | Description | Interval | E-value | ||||
ZnMc_MMP_like_1 | cd04279 | Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ... |
9-167 | 1.01e-42 | ||||
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: 139.90 E-value: 1.01e-42
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COG5549 | COG5549 | Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ... |
1-169 | 5.61e-37 | ||||
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444292 [Multi-domain] Cd Length: 234 Bit Score: 127.49 E-value: 5.61e-37
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ZnMc_MMP | cd04278 | Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ... |
117-166 | 3.91e-06 | ||||
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: 44.50 E-value: 3.91e-06
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Peptidase_M10 | pfam00413 | Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ... |
117-166 | 4.43e-06 | ||||
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: 44.53 E-value: 4.43e-06
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ZnMc_MMP_like | cd04268 | Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ... |
96-166 | 2.45e-04 | ||||
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: 39.79 E-value: 2.45e-04
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ZnMc | smart00235 | Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ... |
119-168 | 4.07e-04 | ||||
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: 38.49 E-value: 4.07e-04
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ZnMc_serralysin_like | cd04277 | Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ... |
24-140 | 2.00e-03 | ||||
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: 37.40 E-value: 2.00e-03
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Blast search parameters | ||||
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