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Conserved domains on  [gi|33469047|ref|NP_777282|]
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MAM domain-containing protein 2 precursor [Mus musculus]

Protein Classification

MAM domain-containing protein( domain architecture ID 11570431)

MAM domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 509-664 1.04e-59

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: 197.60  E-value: 1.04e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047 509 CTFDQDECAFTQEKRNRSSWHRGRGETPTSYTGPKGDHTTGVGYYMYIEASHMVYGQKAHLLSQPLRGVPGKHCLTFFYH 588
Cdd:cd06263   1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSSHCLSFWYH 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33469047 589 MYGAGTGLLSVYLKREEDSEESLLWRRRGEQSISWLRALVEYSC-RRRHQIIFEATRGVSIRSDIAIDDVKLQAGPC 664
Cdd:cd06263  81 MYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGSGSRGDIALDDISLSPGPC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 170-327 7.62e-41

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: 146.35  E-value: 7.62e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047   170 CDFEENHLCGFVNRWNPNVNWFVGGGTAKNThsILPQDHTFRSEHGHYMYVDSVYVKHFQeVAQLISPVTTASMS-GCLS 248
Cdd:pfam00629   1 CDFEDGNLCGWTQDSSDDFDWERVSGPSVKT--GPSSDHTQGTGSGHFMYVDTSSGAPGQ-TARLLSPLLPPSRSpQCLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047   249 FYYQLQQGNDNVFSVYTRDMAG-LYEEIWKVDSPGNAAWNLAEVEFSA-PYPMEVIFEVAFNGPKGGYVALDDISFSPVH 326
Cdd:pfam00629  78 FWYHMSGSGVGTLRVYVRENGGtLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLSSGP 157


                  .
gi 33469047   327 C 327
Cdd:pfam00629 158 C 158
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 342-497 5.37e-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: 138.65  E-value: 5.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047   342 CDFEIG-LCNFYQDKEGPG-WTRVRV-KANMYRAGDHTTGT--GHYLLANTKFtSQPGYIGRLYGPSLPGNM-QYCVRFH 415
Cdd:pfam00629   1 CDFEDGnLCGWTQDSSDDFdWERVSGpSVKTGPSSDHTQGTgsGHFMYVDTSS-GAPGQTARLLSPLLPPSRsPQCLRFW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047   416 YAIFGFLKmsDTLAVYIFEENHVVQEKIWSVLESPRGVWMQAEISFKK-PMPTKVVFMSLcKSFWDCGLVALDDITIQLG 494
Cdd:pfam00629  80 YHMSGSGV--GTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGI-RGGGSRGGIALDDISLSSG 156


                  ...
gi 33469047   495 NCR 497
Cdd:pfam00629 157 PCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 26-167 5.72e-29

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: 112.86  E-value: 5.72e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047  26 CAFEEDTCGFDSVF-AFLPWIL-----------------NEEGHYVYMDTSFARQGEKAVLLSSDLQAEE-WNCLRLVYQ 86
Cdd:cd06263   1 CDFEDGLCGWTQDStDDFDWTRvsgstpspgtppdhthgTGSGHYLYVESSSGREGQKARLLSPLLPPPRsSHCLSFWYH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047  87 ITTppgsvSDPSQLNLYVRFEDESFDRLLWSTKEPS-DSWLIASLDLQNSSKKFKILIEGVLGQGNTASIALFEIKMTAG 165
Cdd:cd06263  81 MYG-----SGVGTLNVYVREEGGGLGTLLWSASGGQgNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLSPG 155


                ..
gi 33469047 166 YC 167
Cdd:cd06263 156 PC 157
 
Name Accession Description Interval E-value
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 509-664 1.04e-59

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: 197.60  E-value: 1.04e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047 509 CTFDQDECAFTQEKRNRSSWHRGRGETPTSYTGPKGDHTTGVGYYMYIEASHMVYGQKAHLLSQPLRGVPGKHCLTFFYH 588
Cdd:cd06263   1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSSHCLSFWYH 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33469047 589 MYGAGTGLLSVYLKREEDSEESLLWRRRGEQSISWLRALVEYSC-RRRHQIIFEATRGVSIRSDIAIDDVKLQAGPC 664
Cdd:cd06263  81 MYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGSGSRGDIALDDISLSPGPC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 509-665 1.76e-53

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: 181.02  E-value: 1.76e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047   509 CTFDQDE-CAFTQEKRNRSSWHRGRGetPTSYTGPKGDHT--TGVGYYMYIEASHMVYGQKAHLLSQPLRGVPGKHCLTF 585
Cdd:pfam00629   1 CDFEDGNlCGWTQDSSDDFDWERVSG--PSVKTGPSSDHTqgTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047   586 FYHMYGAGTGLLSVYLKREEDSEESLLWRRRGEQSISWLRALVEYSCR-RRHQIIFEATRGVSIRSDIAIDDVKLQAGPC 664
Cdd:pfam00629  79 WYHMSGSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSStQPFQVVFEGIRGGGSRGGIALDDISLSSGPC 158


                  .
gi 33469047   665 A 665
Cdd:pfam00629 159 P 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 504-664 2.19e-52

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: 177.92  E-value: 2.19e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047    504 PPPGECTFDQDE-CAFTQEKRNRSSWHRGRGETPtsYTGPKGDHTTGVGYYMYIEASHMVYGQKAHLLSQPLRGVPGKHC 582
Cdd:smart00137   1 TSPGNCDFEEGStCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENRSTHC 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047    583 LTFFYHMYGAGTGLLSVYLKREEDSEESLLWRRRGEQSISWLRALVEYSC-RRRHQIIFEATRGVSIRSDIAIDDVKLQA 661
Cdd:smart00137  79 LTFWYYMYGSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSSwPQPFQVVFEGTRGKGHSGYIALDDILLSN 158


                   ...
gi 33469047    662 GPC 664
Cdd:smart00137 159 GPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 170-327 7.62e-41

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: 146.35  E-value: 7.62e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047   170 CDFEENHLCGFVNRWNPNVNWFVGGGTAKNThsILPQDHTFRSEHGHYMYVDSVYVKHFQeVAQLISPVTTASMS-GCLS 248
Cdd:pfam00629   1 CDFEDGNLCGWTQDSSDDFDWERVSGPSVKT--GPSSDHTQGTGSGHFMYVDTSSGAPGQ-TARLLSPLLPPSRSpQCLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047   249 FYYQLQQGNDNVFSVYTRDMAG-LYEEIWKVDSPGNAAWNLAEVEFSA-PYPMEVIFEVAFNGPKGGYVALDDISFSPVH 326
Cdd:pfam00629  78 FWYHMSGSGVGTLRVYVRENGGtLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLSSGP 157


                  .
gi 33469047   327 C 327
Cdd:pfam00629 158 C 158
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 170-327 1.46e-39

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: 142.90  E-value: 1.46e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047 170 CDFEENhLCGFVNRWNPNVNWFVGGGTAKNTHSilPQDHTFRSEHGHYMYVDSVYVkHFQEVAQLISPVTTAS-MSGCLS 248
Cdd:cd06263   1 CDFEDG-LCGWTQDSTDDFDWTRVSGSTPSPGT--PPDHTHGTGSGHYLYVESSSG-REGQKARLLSPLLPPPrSSHCLS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047 249 FYYQLQQGNDNVFSVYTRDMAG-LYEEIWKVDSPGNAAWNLAEVEFSAP-YPMEVIFEVAFNGPKGGYVALDDISFSPVH 326
Cdd:cd06263  77 FWYHMYGSGVGTLNVYVREEGGgLGTLLWSASGGQGNQWQEAEVTLSASsKPFQVVFEGVRGSGSRGDIALDDISLSPGP 156


                .
gi 33469047 327 C 327
Cdd:cd06263 157 C 157
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 166-327 4.25e-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: 139.02  E-value: 4.25e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047    166 YCIECDFEENHLCGFVNRWNPNVNWFVGGGTAKNTHSilPQDHTFrsEHGHYMYVDSVYVKHfQEVAQLISPVTTASMSG 245
Cdd:smart00137   2 SPGNCDFEEGSTCGWHQDSNDDGHWERVSSATGIPGP--NRDHTT--GNGHFMFFETSSGAE-GQTARLLSPPLYENRST 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047    246 -CLSFYYQLQQGNDNVFSVYTRDMAGLYEE-IWKVDSPGNAAWNLAEVEF-SAPYPMEVIFEVAFNGPKGGYVALDDISF 322
Cdd:smart00137  77 hCLTFWYYMYGSGSGTLNVYVRENNGSQDTlLWSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGKGHSGYIALDDILL 156


                   ....*
gi 33469047    323 SPVHC 327
Cdd:smart00137 157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 342-497 5.37e-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: 138.65  E-value: 5.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047   342 CDFEIG-LCNFYQDKEGPG-WTRVRV-KANMYRAGDHTTGT--GHYLLANTKFtSQPGYIGRLYGPSLPGNM-QYCVRFH 415
Cdd:pfam00629   1 CDFEDGnLCGWTQDSSDDFdWERVSGpSVKTGPSSDHTQGTgsGHFMYVDTSS-GAPGQTARLLSPLLPPSRsPQCLRFW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047   416 YAIFGFLKmsDTLAVYIFEENHVVQEKIWSVLESPRGVWMQAEISFKK-PMPTKVVFMSLcKSFWDCGLVALDDITIQLG 494
Cdd:pfam00629  80 YHMSGSGV--GTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGI-RGGGSRGGIALDDISLSSG 156


                  ...
gi 33469047   495 NCR 497
Cdd:pfam00629 157 PCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 342-496 1.38e-36

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: 134.43  E-value: 1.38e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047 342 CDFEIGLCNFYQDKE-GPGWTRVRVKANM---YRAGDHTTGTGHYLLANTKFtSQPGYIGRLYGPSLPGN-MQYCVRFHY 416
Cdd:cd06263   1 CDFEDGLCGWTQDSTdDFDWTRVSGSTPSpgtPPDHTHGTGSGHYLYVESSS-GREGQKARLLSPLLPPPrSSHCLSFWY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047 417 AIFGFLkmSDTLAVYIFEENHVVQEKIWSVLESPRGVWMQAEISFKKP-MPTKVVFMSLCKSFwDCGLVALDDITIQLGN 495
Cdd:cd06263  80 HMYGSG--VGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASsKPFQVVFEGVRGSG-SRGDIALDDISLSPGP 156


                .
gi 33469047 496 C 496
Cdd:cd06263 157 C 157
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 341-496 5.20e-29

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: 113.21  E-value: 5.20e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047    341 SCDFEIG-LCNFYQD--KEGPgWTRVRVK-ANMYRAGDHTTGTGHYLLANTKFTSqPGYIGRLYGPSLPGNM-QYCVRFH 415
Cdd:smart00137   5 NCDFEEGsTCGWHQDsnDDGH-WERVSSAtGIPGPNRDHTTGNGHFMFFETSSGA-EGQTARLLSPPLYENRsTHCLTFW 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047    416 YAIFGflKMSDTLAVYIFEENHVVQEKIWSVLESPRGVWMQAEISF-KKPMPTKVVFMSLCKSfWDCGLVALDDITIQLG 494
Cdd:smart00137  83 YYMYG--SGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGK-GHSGYIALDDILLSNG 159


                   ..
gi 33469047    495 NC 496
Cdd:smart00137 160 PC 161
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 26-167 5.72e-29

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: 112.86  E-value: 5.72e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047  26 CAFEEDTCGFDSVF-AFLPWIL-----------------NEEGHYVYMDTSFARQGEKAVLLSSDLQAEE-WNCLRLVYQ 86
Cdd:cd06263   1 CDFEDGLCGWTQDStDDFDWTRvsgstpspgtppdhthgTGSGHYLYVESSSGREGQKARLLSPLLPPPRsSHCLSFWYH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047  87 ITTppgsvSDPSQLNLYVRFEDESFDRLLWSTKEPS-DSWLIASLDLQNSSKKFKILIEGVLGQGNTASIALFEIKMTAG 165
Cdd:cd06263  81 MYG-----SGVGTLNVYVREEGGGLGTLLWSASGGQgNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLSPG 155


                ..
gi 33469047 166 YC 167
Cdd:cd06263 156 PC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 47-167 4.29e-22

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: 93.20  E-value: 4.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047    47 NEEGHYVYMDTSFARQGEKAVLLSSDLQAE-EWNCLRLVYQIttppgSVSDPSQLNLYVRFEDESFDRLLWSTK-EPSDS 124
Cdd:pfam00629  41 TGSGHFMYVDTSSGAPGQTARLLSPLLPPSrSPQCLRFWYHM-----SGSGVGTLRVYVRENGGTLDTLLWSISgDQGPS 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 33469047   125 WLIASLDLQNSSKKFKILIEGVLGQGNTASIALFEIKMTAGYC 167
Cdd:pfam00629 116 WKEARVTLSSSTQPFQVVFEGIRGGGSRGGIALDDISLSSGPC 158
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 23-167 4.21e-20

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: 87.78  E-value: 4.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047     23 AGSCAFEED-TCGF--DSVFAFlPWILNE---------------EGHYVYMDTSFARQGEKAVLLSSDLQA-EEWNCLRL 83
Cdd:smart00137   3 PGNCDFEEGsTCGWhqDSNDDG-HWERVSsatgipgpnrdhttgNGHFMFFETSSGAEGQTARLLSPPLYEnRSTHCLTF 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047     84 VYQITTppgsvSDPSQLNLYVRFEDESFDRLLWSTKE-PSDSWLIASLDLQNSSKKFKILIEGVLGQGNTASIALFEIKM 162
Cdd:smart00137  82 WYYMYG-----SGSGTLNVYVRENNGSQDTLLWSRSGtQGGQWLQAEVALSSWPQPFQVVFEGTRGKGHSGYIALDDILL 156


                   ....*
gi 33469047    163 TAGYC 167
Cdd:smart00137 157 SNGPC 161
 
Name Accession Description Interval E-value
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 509-664 1.04e-59

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: 197.60  E-value: 1.04e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047 509 CTFDQDECAFTQEKRNRSSWHRGRGETPTSYTGPKGDHTTGVGYYMYIEASHMVYGQKAHLLSQPLRGVPGKHCLTFFYH 588
Cdd:cd06263   1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSSHCLSFWYH 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33469047 589 MYGAGTGLLSVYLKREEDSEESLLWRRRGEQSISWLRALVEYSC-RRRHQIIFEATRGVSIRSDIAIDDVKLQAGPC 664
Cdd:cd06263  81 MYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGSGSRGDIALDDISLSPGPC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 509-665 1.76e-53

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: 181.02  E-value: 1.76e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047   509 CTFDQDE-CAFTQEKRNRSSWHRGRGetPTSYTGPKGDHT--TGVGYYMYIEASHMVYGQKAHLLSQPLRGVPGKHCLTF 585
Cdd:pfam00629   1 CDFEDGNlCGWTQDSSDDFDWERVSG--PSVKTGPSSDHTqgTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047   586 FYHMYGAGTGLLSVYLKREEDSEESLLWRRRGEQSISWLRALVEYSCR-RRHQIIFEATRGVSIRSDIAIDDVKLQAGPC 664
Cdd:pfam00629  79 WYHMSGSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSStQPFQVVFEGIRGGGSRGGIALDDISLSSGPC 158


                  .
gi 33469047   665 A 665
Cdd:pfam00629 159 P 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 504-664 2.19e-52

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: 177.92  E-value: 2.19e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047    504 PPPGECTFDQDE-CAFTQEKRNRSSWHRGRGETPtsYTGPKGDHTTGVGYYMYIEASHMVYGQKAHLLSQPLRGVPGKHC 582
Cdd:smart00137   1 TSPGNCDFEEGStCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENRSTHC 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047    583 LTFFYHMYGAGTGLLSVYLKREEDSEESLLWRRRGEQSISWLRALVEYSC-RRRHQIIFEATRGVSIRSDIAIDDVKLQA 661
Cdd:smart00137  79 LTFWYYMYGSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSSwPQPFQVVFEGTRGKGHSGYIALDDILLSN 158


                   ...
gi 33469047    662 GPC 664
Cdd:smart00137 159 GPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 170-327 7.62e-41

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: 146.35  E-value: 7.62e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047   170 CDFEENHLCGFVNRWNPNVNWFVGGGTAKNThsILPQDHTFRSEHGHYMYVDSVYVKHFQeVAQLISPVTTASMS-GCLS 248
Cdd:pfam00629   1 CDFEDGNLCGWTQDSSDDFDWERVSGPSVKT--GPSSDHTQGTGSGHFMYVDTSSGAPGQ-TARLLSPLLPPSRSpQCLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047   249 FYYQLQQGNDNVFSVYTRDMAG-LYEEIWKVDSPGNAAWNLAEVEFSA-PYPMEVIFEVAFNGPKGGYVALDDISFSPVH 326
Cdd:pfam00629  78 FWYHMSGSGVGTLRVYVRENGGtLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLSSGP 157


                  .
gi 33469047   327 C 327
Cdd:pfam00629 158 C 158
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 170-327 1.46e-39

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: 142.90  E-value: 1.46e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047 170 CDFEENhLCGFVNRWNPNVNWFVGGGTAKNTHSilPQDHTFRSEHGHYMYVDSVYVkHFQEVAQLISPVTTAS-MSGCLS 248
Cdd:cd06263   1 CDFEDG-LCGWTQDSTDDFDWTRVSGSTPSPGT--PPDHTHGTGSGHYLYVESSSG-REGQKARLLSPLLPPPrSSHCLS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047 249 FYYQLQQGNDNVFSVYTRDMAG-LYEEIWKVDSPGNAAWNLAEVEFSAP-YPMEVIFEVAFNGPKGGYVALDDISFSPVH 326
Cdd:cd06263  77 FWYHMYGSGVGTLNVYVREEGGgLGTLLWSASGGQGNQWQEAEVTLSASsKPFQVVFEGVRGSGSRGDIALDDISLSPGP 156


                .
gi 33469047 327 C 327
Cdd:cd06263 157 C 157
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 166-327 4.25e-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: 139.02  E-value: 4.25e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047    166 YCIECDFEENHLCGFVNRWNPNVNWFVGGGTAKNTHSilPQDHTFrsEHGHYMYVDSVYVKHfQEVAQLISPVTTASMSG 245
Cdd:smart00137   2 SPGNCDFEEGSTCGWHQDSNDDGHWERVSSATGIPGP--NRDHTT--GNGHFMFFETSSGAE-GQTARLLSPPLYENRST 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047    246 -CLSFYYQLQQGNDNVFSVYTRDMAGLYEE-IWKVDSPGNAAWNLAEVEF-SAPYPMEVIFEVAFNGPKGGYVALDDISF 322
Cdd:smart00137  77 hCLTFWYYMYGSGSGTLNVYVRENNGSQDTlLWSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGKGHSGYIALDDILL 156


                   ....*
gi 33469047    323 SPVHC 327
Cdd:smart00137 157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 342-497 5.37e-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: 138.65  E-value: 5.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047   342 CDFEIG-LCNFYQDKEGPG-WTRVRV-KANMYRAGDHTTGT--GHYLLANTKFtSQPGYIGRLYGPSLPGNM-QYCVRFH 415
Cdd:pfam00629   1 CDFEDGnLCGWTQDSSDDFdWERVSGpSVKTGPSSDHTQGTgsGHFMYVDTSS-GAPGQTARLLSPLLPPSRsPQCLRFW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047   416 YAIFGFLKmsDTLAVYIFEENHVVQEKIWSVLESPRGVWMQAEISFKK-PMPTKVVFMSLcKSFWDCGLVALDDITIQLG 494
Cdd:pfam00629  80 YHMSGSGV--GTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGI-RGGGSRGGIALDDISLSSG 156


                  ...
gi 33469047   495 NCR 497
Cdd:pfam00629 157 PCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 342-496 1.38e-36

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: 134.43  E-value: 1.38e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047 342 CDFEIGLCNFYQDKE-GPGWTRVRVKANM---YRAGDHTTGTGHYLLANTKFtSQPGYIGRLYGPSLPGN-MQYCVRFHY 416
Cdd:cd06263   1 CDFEDGLCGWTQDSTdDFDWTRVSGSTPSpgtPPDHTHGTGSGHYLYVESSS-GREGQKARLLSPLLPPPrSSHCLSFWY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047 417 AIFGFLkmSDTLAVYIFEENHVVQEKIWSVLESPRGVWMQAEISFKKP-MPTKVVFMSLCKSFwDCGLVALDDITIQLGN 495
Cdd:cd06263  80 HMYGSG--VGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASsKPFQVVFEGVRGSG-SRGDIALDDISLSPGP 156


                .
gi 33469047 496 C 496
Cdd:cd06263 157 C 157
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 341-496 5.20e-29

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: 113.21  E-value: 5.20e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047    341 SCDFEIG-LCNFYQD--KEGPgWTRVRVK-ANMYRAGDHTTGTGHYLLANTKFTSqPGYIGRLYGPSLPGNM-QYCVRFH 415
Cdd:smart00137   5 NCDFEEGsTCGWHQDsnDDGH-WERVSSAtGIPGPNRDHTTGNGHFMFFETSSGA-EGQTARLLSPPLYENRsTHCLTFW 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047    416 YAIFGflKMSDTLAVYIFEENHVVQEKIWSVLESPRGVWMQAEISF-KKPMPTKVVFMSLCKSfWDCGLVALDDITIQLG 494
Cdd:smart00137  83 YYMYG--SGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGK-GHSGYIALDDILLSNG 159


                   ..
gi 33469047    495 NC 496
Cdd:smart00137 160 PC 161
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 26-167 5.72e-29

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: 112.86  E-value: 5.72e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047  26 CAFEEDTCGFDSVF-AFLPWIL-----------------NEEGHYVYMDTSFARQGEKAVLLSSDLQAEE-WNCLRLVYQ 86
Cdd:cd06263   1 CDFEDGLCGWTQDStDDFDWTRvsgstpspgtppdhthgTGSGHYLYVESSSGREGQKARLLSPLLPPPRsSHCLSFWYH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047  87 ITTppgsvSDPSQLNLYVRFEDESFDRLLWSTKEPS-DSWLIASLDLQNSSKKFKILIEGVLGQGNTASIALFEIKMTAG 165
Cdd:cd06263  81 MYG-----SGVGTLNVYVREEGGGLGTLLWSASGGQgNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLSPG 155


                ..
gi 33469047 166 YC 167
Cdd:cd06263 156 PC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 47-167 4.29e-22

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: 93.20  E-value: 4.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047    47 NEEGHYVYMDTSFARQGEKAVLLSSDLQAE-EWNCLRLVYQIttppgSVSDPSQLNLYVRFEDESFDRLLWSTK-EPSDS 124
Cdd:pfam00629  41 TGSGHFMYVDTSSGAPGQTARLLSPLLPPSrSPQCLRFWYHM-----SGSGVGTLRVYVRENGGTLDTLLWSISgDQGPS 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 33469047   125 WLIASLDLQNSSKKFKILIEGVLGQGNTASIALFEIKMTAGYC 167
Cdd:pfam00629 116 WKEARVTLSSSTQPFQVVFEGIRGGGSRGGIALDDISLSSGPC 158
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 23-167 4.21e-20

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: 87.78  E-value: 4.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047     23 AGSCAFEED-TCGF--DSVFAFlPWILNE---------------EGHYVYMDTSFARQGEKAVLLSSDLQA-EEWNCLRL 83
Cdd:smart00137   3 PGNCDFEEGsTCGWhqDSNDDG-HWERVSsatgipgpnrdhttgNGHFMFFETSSGAEGQTARLLSPPLYEnRSTHCLTF 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469047     84 VYQITTppgsvSDPSQLNLYVRFEDESFDRLLWSTKE-PSDSWLIASLDLQNSSKKFKILIEGVLGQGNTASIALFEIKM 162
Cdd:smart00137  82 WYYMYG-----SGSGTLNVYVRENNGSQDTLLWSRSGtQGGQWLQAEVALSSWPQPFQVVFEGTRGKGHSGYIALDDILL 156


                   ....*
gi 33469047    163 TAGYC 167
Cdd:smart00137 157 SNGPC 161
 
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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