low affinity high capacity ammonium permease [Coccidioides immitis]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
ZnMc_pappalysin_like | cd04275 | Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ... |
57-270 | 2.07e-111 | ||||
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved. : Pssm-ID: 239802 [Multi-domain] Cd Length: 225 Bit Score: 320.44 E-value: 2.07e-111
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Name | Accession | Description | Interval | E-value | ||||
ZnMc_pappalysin_like | cd04275 | Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ... |
57-270 | 2.07e-111 | ||||
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved. Pssm-ID: 239802 [Multi-domain] Cd Length: 225 Bit Score: 320.44 E-value: 2.07e-111
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Peptidase_M43 | pfam05572 | Pregnancy-associated plasma protein-A; Pregnancy-associated plasma protein A (PAPP-A) is a ... |
188-265 | 2.34e-14 | ||||
Pregnancy-associated plasma protein-A; Pregnancy-associated plasma protein A (PAPP-A) is a metallo-protease belonging to Merops family M43. It cleaves insulin-like growth factor (IGF) binding protein-4 (IGFBP-4), causing a dramatic reduction in its affinity for IGF-I and -II. Through this mechanism, PAPP-A is a regulator of IGF bioactivity in several systems, including the human ovary and the cardiovascular system. Pssm-ID: 368506 Cd Length: 152 Bit Score: 68.79 E-value: 2.34e-14
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Name | Accession | Description | Interval | E-value | ||||
ZnMc_pappalysin_like | cd04275 | Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ... |
57-270 | 2.07e-111 | ||||
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved. Pssm-ID: 239802 [Multi-domain] Cd Length: 225 Bit Score: 320.44 E-value: 2.07e-111
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Peptidase_M43 | pfam05572 | Pregnancy-associated plasma protein-A; Pregnancy-associated plasma protein A (PAPP-A) is a ... |
188-265 | 2.34e-14 | ||||
Pregnancy-associated plasma protein-A; Pregnancy-associated plasma protein A (PAPP-A) is a metallo-protease belonging to Merops family M43. It cleaves insulin-like growth factor (IGF) binding protein-4 (IGFBP-4), causing a dramatic reduction in its affinity for IGF-I and -II. Through this mechanism, PAPP-A is a regulator of IGF bioactivity in several systems, including the human ovary and the cardiovascular system. Pssm-ID: 368506 Cd Length: 152 Bit Score: 68.79 E-value: 2.34e-14
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ZnMc_ADAM_like | cd04267 | Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
65-201 | 1.03e-07 | ||||
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: 50.88 E-value: 1.03e-07
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Reprolysin_5 | pfam13688 | Metallo-peptidase family M12; |
88-257 | 1.86e-06 | ||||
Metallo-peptidase family M12; Pssm-ID: 372673 Cd Length: 191 Bit Score: 47.41 E-value: 1.86e-06
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ZnMc | cd00203 | Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
64-267 | 1.16e-04 | ||||
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: 41.74 E-value: 1.16e-04
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ZnMc_serralysin_like | cd04277 | Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ... |
132-206 | 1.20e-04 | ||||
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: 42.02 E-value: 1.20e-04
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ZnMc_MMP_like_1 | cd04279 | Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ... |
133-203 | 2.35e-04 | ||||
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: 40.52 E-value: 2.35e-04
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Reprolysin_3 | pfam13582 | Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
97-202 | 7.54e-04 | ||||
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B. Pssm-ID: 463926 [Multi-domain] Cd Length: 122 Bit Score: 38.51 E-value: 7.54e-04
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Blast search parameters | ||||
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