MAM domain-containing protein [Caenorhabditis elegans]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
26-185 | 8.95e-44 | ||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. : Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 150.96 E-value: 8.95e-44
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MAM super family | cl46915 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
280-437 | 6.82e-04 | ||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. The actual alignment was detected with superfamily member cd06263: Pssm-ID: 99706 Cd Length: 157 Bit Score: 40.05 E-value: 6.82e-04
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Name | Accession | Description | Interval | E-value | ||||
MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
26-185 | 8.95e-44 | ||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 150.96 E-value: 8.95e-44
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
86-185 | 4.13e-05 | ||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 43.89 E-value: 4.13e-05
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MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
280-437 | 6.82e-04 | ||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. Pssm-ID: 99706 Cd Length: 157 Bit Score: 40.05 E-value: 6.82e-04
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MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
276-437 | 2.42e-03 | ||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 38.48 E-value: 2.42e-03
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
280-438 | 3.83e-03 | ||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 38.11 E-value: 3.83e-03
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MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
86-185 | 6.04e-03 | ||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. Pssm-ID: 99706 Cd Length: 157 Bit Score: 37.36 E-value: 6.04e-03
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Name | Accession | Description | Interval | E-value | ||||
MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
26-185 | 8.95e-44 | ||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 150.96 E-value: 8.95e-44
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
86-185 | 4.13e-05 | ||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 43.89 E-value: 4.13e-05
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MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
280-437 | 6.82e-04 | ||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. Pssm-ID: 99706 Cd Length: 157 Bit Score: 40.05 E-value: 6.82e-04
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MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
276-437 | 2.42e-03 | ||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 38.48 E-value: 2.42e-03
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
280-438 | 3.83e-03 | ||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 38.11 E-value: 3.83e-03
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MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
86-185 | 6.04e-03 | ||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. Pssm-ID: 99706 Cd Length: 157 Bit Score: 37.36 E-value: 6.04e-03
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Blast search parameters | ||||
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