Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
638-798
1.82e-56
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: 191.40 E-value: 1.82e-56
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: 174.46 E-value: 1.51e-50
C-terminal domain of neuropilin glycoprotein; This domain is found in eukaryotes at the ...
822-900
3.63e-46
C-terminal domain of neuropilin glycoprotein; This domain is found in eukaryotes at the C-terminus of neuropilins. It represents the transmembrane region of these transmembrane glycoproteins, that are predominantly co-receptors for another class of proteins known as semaphorins. The domain is found associated with pfam00754, pfam00431, pfam00629.
:
Pssm-ID: 403259 Cd Length: 82 Bit Score: 159.65 E-value: 3.63e-46
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: 123.62 E-value: 8.80e-33
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
638-798
1.82e-56
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: 191.40 E-value: 1.82e-56
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
643-804
1.98e-56
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: 191.42 E-value: 1.98e-56
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
643-797
3.68e-54
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: 184.89 E-value: 3.68e-54
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: 174.46 E-value: 1.51e-50
C-terminal domain of neuropilin glycoprotein; This domain is found in eukaryotes at the ...
822-900
3.63e-46
C-terminal domain of neuropilin glycoprotein; This domain is found in eukaryotes at the C-terminus of neuropilins. It represents the transmembrane region of these transmembrane glycoproteins, that are predominantly co-receptors for another class of proteins known as semaphorins. The domain is found associated with pfam00754, pfam00431, pfam00629.
Pssm-ID: 403259 Cd Length: 82 Bit Score: 159.65 E-value: 3.63e-46
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: 140.34 E-value: 1.28e-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: 238014 [Multi-domain] Cd Length: 143 Bit Score: 123.62 E-value: 8.80e-33
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
156-262
1.03e-32
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: 122.11 E-value: 1.03e-32
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
37-138
7.54e-32
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: 119.42 E-value: 7.54e-32
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: 89.49 E-value: 6.69e-21
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
638-798
1.82e-56
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: 191.40 E-value: 1.82e-56
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
643-804
1.98e-56
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: 191.42 E-value: 1.98e-56
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
643-797
3.68e-54
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: 184.89 E-value: 3.68e-54
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: 174.46 E-value: 1.51e-50
C-terminal domain of neuropilin glycoprotein; This domain is found in eukaryotes at the ...
822-900
3.63e-46
C-terminal domain of neuropilin glycoprotein; This domain is found in eukaryotes at the C-terminus of neuropilins. It represents the transmembrane region of these transmembrane glycoproteins, that are predominantly co-receptors for another class of proteins known as semaphorins. The domain is found associated with pfam00754, pfam00431, pfam00629.
Pssm-ID: 403259 Cd Length: 82 Bit Score: 159.65 E-value: 3.63e-46
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: 140.34 E-value: 1.28e-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: 238014 [Multi-domain] Cd Length: 143 Bit Score: 123.62 E-value: 8.80e-33
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
156-262
1.03e-32
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: 122.11 E-value: 1.03e-32
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
37-138
7.54e-32
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: 119.42 E-value: 7.54e-32
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: 89.49 E-value: 6.69e-21
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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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
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.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(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.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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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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