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Conserved domains on  [gi|392920111|ref|NP_001256156|]
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MAM domain-containing protein [Caenorhabditis elegans]

Protein Classification

MAM domain-containing protein( domain architecture ID 12190778)

MAM domain-containing protein

Graphical summary

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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 7.80e-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: 153.65  E-value: 7.80e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920111    26 SSDLNCDFT--TTCRWRNSSDVGGHFETTSLLEADA-QNRIMPIDENNPKPFAFTAGLMGrMMALLVSEVITCQLGGASL 102
Cdd:smart00137   1 TSPGNCDFEegSTCGWHQDSNDDGHWERVSSATGIPgPNRDHTTGNGHFMFFETSSGAEG-QTARLLSPPLYENRSTHCL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920111   103 KYWYYKTGLDS-QLEVCIRQPPGNKDlsqMRCYDGVSTFGKQWIFRAVELPPIAQPFEIVFKTIYSPP-SSVIALDNIVF 180
Cdd:smart00137  80 TFWYYMYGSGSgTLNVYVRENNGSQD---TLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRGKGhSGYIALDDILL 156


                   ....*
gi 392920111   181 EATLC 185
Cdd:smart00137 157 SNGPC 161
 
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 7.80e-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: 153.65  E-value: 7.80e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920111    26 SSDLNCDFT--TTCRWRNSSDVGGHFETTSLLEADA-QNRIMPIDENNPKPFAFTAGLMGrMMALLVSEVITCQLGGASL 102
Cdd:smart00137   1 TSPGNCDFEegSTCGWHQDSNDDGHWERVSSATGIPgPNRDHTTGNGHFMFFETSSGAEG-QTARLLSPPLYENRSTHCL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920111   103 KYWYYKTGLDS-QLEVCIRQPPGNKDlsqMRCYDGVSTFGKQWIFRAVELPPIAQPFEIVFKTIYSPP-SSVIALDNIVF 180
Cdd:smart00137  80 TFWYYMYGSGSgTLNVYVRENNGSQD---TLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRGKGhSGYIALDDILL 156


                   ....*
gi 392920111   181 EATLC 185
Cdd:smart00137 157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 86-186 2.42e-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: 44.66  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920111   86 ALLVSEVITCQLGGASLKYWYYKTGLDS-QLEVCIRQPPGNKDLS-QMRCYDGvstfGKQWIFRAVELPPIAQPFEIVF- 162
Cdd:pfam00629  60 ARLLSPLLPPSRSPQCLRFWYHMSGSGVgTLRVYVRENGGTLDTLlWSISGDQ----GPSWKEARVTLSSSTQPFQVVFe 135

                          90       100
                  ....*....|....*....|....
gi 392920111  163 KTIYSPPSSVIALDNIVFEATLCG 186
Cdd:pfam00629 136 GIRGGGSRGGIALDDISLSSGPCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 86-185 3.48e-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: 38.51  E-value: 3.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920111  86 ALLVSEVITCQLGGASLKYWYYKTGLDS-QLEVCIR--QPPGNKDLSQMRcYDGvstfGKQWIFRAVELPPIAQPFEIVF 162
Cdd:cd06263   59 ARLLSPLLPPPRSSHCLSFWYHMYGSGVgTLNVYVReeGGGLGTLLWSAS-GGQ----GNQWQEAEVTLSASSKPFQVVF 133

                         90       100
                 ....*....|....*....|....
gi 392920111 163 KTIY-SPPSSVIALDNIVFEATLC 185
Cdd:cd06263  134 EGVRgSGSRGDIALDDISLSPGPC 157
 
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 7.80e-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: 153.65  E-value: 7.80e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920111    26 SSDLNCDFT--TTCRWRNSSDVGGHFETTSLLEADA-QNRIMPIDENNPKPFAFTAGLMGrMMALLVSEVITCQLGGASL 102
Cdd:smart00137   1 TSPGNCDFEegSTCGWHQDSNDDGHWERVSSATGIPgPNRDHTTGNGHFMFFETSSGAEG-QTARLLSPPLYENRSTHCL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920111   103 KYWYYKTGLDS-QLEVCIRQPPGNKDlsqMRCYDGVSTFGKQWIFRAVELPPIAQPFEIVFKTIYSPP-SSVIALDNIVF 180
Cdd:smart00137  80 TFWYYMYGSGSgTLNVYVRENNGSQD---TLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRGKGhSGYIALDDILL 156


                   ....*
gi 392920111   181 EATLC 185
Cdd:smart00137 157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 86-186 2.42e-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: 44.66  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920111   86 ALLVSEVITCQLGGASLKYWYYKTGLDS-QLEVCIRQPPGNKDLS-QMRCYDGvstfGKQWIFRAVELPPIAQPFEIVF- 162
Cdd:pfam00629  60 ARLLSPLLPPSRSPQCLRFWYHMSGSGVgTLRVYVRENGGTLDTLlWSISGDQ----GPSWKEARVTLSSSTQPFQVVFe 135

                          90       100
                  ....*....|....*....|....
gi 392920111  163 KTIYSPPSSVIALDNIVFEATLCG 186
Cdd:pfam00629 136 GIRGGGSRGGIALDDISLSSGPCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 86-185 3.48e-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: 38.51  E-value: 3.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920111  86 ALLVSEVITCQLGGASLKYWYYKTGLDS-QLEVCIR--QPPGNKDLSQMRcYDGvstfGKQWIFRAVELPPIAQPFEIVF 162
Cdd:cd06263   59 ARLLSPLLPPPRSSHCLSFWYHMYGSGVgTLNVYVReeGGGLGTLLWSAS-GGQ----GNQWQEAEVTLSASSKPFQVVF 133

                         90       100
                 ....*....|....*....|....
gi 392920111 163 KTIY-SPPSSVIALDNIVFEATLC 185
Cdd:cd06263  134 EGVRgSGSRGDIALDDISLSPGPC 157
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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