Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.
:
Pssm-ID: 238014 [Multi-domain] Cd Length: 143 Bit Score: 181.01 E-value: 6.45e-53
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
644-795
1.19e-44
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: 158.31 E-value: 1.19e-44
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.
:
Pssm-ID: 238014 [Multi-domain] Cd Length: 143 Bit Score: 120.15 E-value: 1.39e-31
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.
Pssm-ID: 238014 [Multi-domain] Cd Length: 143 Bit Score: 181.01 E-value: 6.45e-53
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
644-795
1.19e-44
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: 158.31 E-value: 1.19e-44
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
639-799
1.12e-38
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: 141.33 E-value: 1.12e-38
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
644-795
5.12e-38
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: 139.42 E-value: 5.12e-38
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.
Pssm-ID: 214572 Cd Length: 139 Bit Score: 138.41 E-value: 5.65e-38
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
38-139
1.47e-36
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.
Pssm-ID: 214483 [Multi-domain] Cd Length: 102 Bit Score: 132.90 E-value: 1.47e-36
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.
Pssm-ID: 238014 [Multi-domain] Cd Length: 143 Bit Score: 120.15 E-value: 1.39e-31
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
158-264
3.48e-31
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.
Pssm-ID: 214483 [Multi-domain] Cd Length: 102 Bit Score: 117.49 E-value: 3.48e-31
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.
Pssm-ID: 214572 Cd Length: 139 Bit Score: 86.79 E-value: 6.00e-20
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.
Pssm-ID: 238014 [Multi-domain] Cd Length: 143 Bit Score: 181.01 E-value: 6.45e-53
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
644-795
1.19e-44
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: 158.31 E-value: 1.19e-44
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
639-799
1.12e-38
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: 141.33 E-value: 1.12e-38
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
644-795
5.12e-38
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: 139.42 E-value: 5.12e-38
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.
Pssm-ID: 214572 Cd Length: 139 Bit Score: 138.41 E-value: 5.65e-38
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
38-139
1.47e-36
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.
Pssm-ID: 214483 [Multi-domain] Cd Length: 102 Bit Score: 132.90 E-value: 1.47e-36
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.
Pssm-ID: 238014 [Multi-domain] Cd Length: 143 Bit Score: 120.15 E-value: 1.39e-31
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
158-264
3.48e-31
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.
Pssm-ID: 214483 [Multi-domain] Cd Length: 102 Bit Score: 117.49 E-value: 3.48e-31
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.
Pssm-ID: 214572 Cd Length: 139 Bit Score: 86.79 E-value: 6.00e-20
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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