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Conserved domains on  [gi|1622869768|ref|XP_028690413|]
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apical endosomal glycoprotein isoform X2 [Macaca mulatta]

Protein Classification

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 ...
 677-833 3.15e-45

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: 160.59  E-value: 3.15e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   677 DREVSCNFERD-TCSWYPGHLSDTHWRWVES----RGPDHDHTTGQGHFVLLDpTDPLAWGHSAHLLSRPQVPAAPTECL 751
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSatgiPGPNRDHTTGNGHFMFFE-TSSGAEGQTARLLSPPLYENRSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   752 SFWYYLHGPQIGTLRLAMRREGEE--THLWSRSGTQGNRWHEAWATLSHQPGsraQYQLLFEGLR-DGYHGTMALDDVAV 828
Cdd:smart00137   80 TFWYYMYGSGSGTLNVYVRENNGSqdTLLWSRSGTQGGQWLQAEVALSSWPQ---PFQVVFEGTRgKGHSGYIALDDILL 156


                    ....*
gi 1622869768   829 RPGPC 833
Cdd:smart00137  157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 839-994 1.04e-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: 150.59  E-value: 1.04e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  839 CSFEDSD-CGFS--SGGRGLWRRQANASGHTawGPPTDHTTETAQGHYMVVDTSpdALPRGQTASLTSKEYSPPAQPACL 915
Cdd:pfam00629    1 CDFEDGNlCGWTqdSSDDFDWERVSGPSVKT--GPSSDHTQGTGSGHFMYVDTS--SGAPGQTARLLSPLLPPSRSPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  916 TFWYHGSLHNPGTLRVHLE---KGRKHQVLSLSAHGGLAWRLGSVDVQA-EQAWRVVFEAVAAGVAHSYVALDDLLLQDG 991
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRengGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLSSG 156


                   ...
gi 1622869768  992 PCP 994
Cdd:pfam00629  157 PCP 159
MAM super family cl42956
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 62-219 3.75e-36

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.


The actual alignment was detected with superfamily member smart00137:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 134.39  E-value: 3.75e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768    62 TPFACDFEQDS-CGWRDISTSGYSWLRDRAGAAleGPGPHSDHTLGTdlGWYMAVGTHRGKEASTAALRSPTLREAAPSC 140
Cdd:smart00137    2 SPGNCDFEEGStCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRSTH 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   141 KLRLWYHAASGDVAELRLEVT--HGSETLTLWQSTGPWDPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLAFW 218
Cdd:smart00137   78 CLTFWYYMYGSGSGTLNVYVRenNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRGKGHSGYIALDDILLS 157


                    .
gi 1622869768   219 D 219
Cdd:smart00137  158 N 158
MAM super family cl42956
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 994-1220 1.21e-32

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.


The actual alignment was detected with superfamily member smart00137:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 124.38  E-value: 1.21e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   994 PRPGSCDFESG-LCGWSHLAWPslgGYSWDWGGGATpsRYPQPPVDHTLGTkagtcplepggeatqrphtatwlpaahrv 1072
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSND---DGHWERVSSAT--GIPGPNRDHTTGN----------------------------- 46

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  1073 hapsrggpahsasaralragsahqpginlllfpGHFAFFETGVLGPGgRAAWLRSEPLPAT-PASCLRFWYHMGFPEHfy 1151
Cdd:smart00137   47 ---------------------------------GHFMFFETSSGAEG-QTARLLSPPLYENrSTHCLTFWYYMYGSGS-- 90

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622869768  1152 kGELRVLLRSTQGQLA--VWGTGGHRRHQWLEAQVEV-ASTKEFQVVFEATLGGqPALGPIALDDVEYLAGQ 1220
Cdd:smart00137   91 -GTLNVYVRENNGSQDtlLWSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGK-GHSGYIALDDILLSNGP 160
MAM super family cl47572
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 271-450 6.81e-25

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.


The actual alignment was detected with superfamily member pfam00629:

Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 102.06  E-value: 6.81e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  271 TDFETG-LGPWNRSE----GWSRNHsagGPERPSWPRRDHSRNSAQGSFLV---SVAEPGTPAILSSPAFQASGASNCsv 342
Cdd:pfam00629    1 CDFEDGnLCGWTQDSsddfDWERVS---GPSVKTGPSSDHTQGTGSGHFMYvdtSSGAPGQTARLLSPLLPPSRSPQC-- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  343 rwvgltgppcwlprcrapsqllvpqLIFYHYLHGSEAGCLQLFLQTLGSSAPQapvLLRRRRGELGTAWVRDRVDIQS-A 421
Cdd:pfam00629   76 -------------------------LRFWYHMSGSGVGTLRVYVRENGGTLDT---LLWSISGDQGPSWKEARVTLSSsT 127

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1622869768  422 HPFQILLAGQ--TGPGGVVGLDD-LILSDHCR 450
Cdd:pfam00629  128 QPFQVVFEGIrgGGSRGGIALDDiSLSSGPCP 159
MAM super family cl47572
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 519-669 7.15e-25

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.


The actual alignment was detected with superfamily member pfam00629:

Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 102.06  E-value: 7.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  519 TDFESLEAGGWEDASVGRLQWRRLSA-QESQGSSA-----AAAGHFLSLQRAWGQLSTEARVLTPLLGPSGPSCELHLAY 592
Cdd:pfam00629    1 CDFEDGNLCGWTQDSSDDFDWERVSGpSVKTGPSSdhtqgTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRFWY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  593 YLQSQPRGFLALVVVDNGSR--ELAWQALSSSAGGWKVDKVLLGARRRPFQLEFVGLVdlDGPDQQGAGVDNVTL--RDC 668
Cdd:pfam00629   81 HMSGSGVGTLRVYVRENGGTldTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIR--GGGSRGGIALDDISLssGPC 158


                   .
gi 1622869768  669 S 669
Cdd:pfam00629  159 P 159
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 229-261 3.76e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 50.28  E-value: 3.76e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1622869768  229 CPLGHHHCQNKVCVEPQQLCDGEDNCGDLSDED 261
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 483-516 1.62e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 45.66  E-value: 1.62e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1622869768  483 CKQGHFACGD-LCVPPEQLCDFEEQCAGGEDEQAC 516
Cdd:cd00112      1 CPPNEFRCANgRCIPSSWVCDGEDDCGDGSDEENC 35
 
Name Accession Description Interval E-value
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 677-833 3.15e-45

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: 160.59  E-value: 3.15e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   677 DREVSCNFERD-TCSWYPGHLSDTHWRWVES----RGPDHDHTTGQGHFVLLDpTDPLAWGHSAHLLSRPQVPAAPTECL 751
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSatgiPGPNRDHTTGNGHFMFFE-TSSGAEGQTARLLSPPLYENRSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   752 SFWYYLHGPQIGTLRLAMRREGEE--THLWSRSGTQGNRWHEAWATLSHQPGsraQYQLLFEGLR-DGYHGTMALDDVAV 828
Cdd:smart00137   80 TFWYYMYGSGSGTLNVYVRENNGSqdTLLWSRSGTQGGQWLQAEVALSSWPQ---PFQVVFEGTRgKGHSGYIALDDILL 156


                    ....*
gi 1622869768   829 RPGPC 833
Cdd:smart00137  157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 682-834 7.53e-45

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: 159.45  E-value: 7.53e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  682 CNFERDT-CSWYPGHLSDTHWRWV----ESRGPDHDHT--TGQGHFVLLDPTDPlAWGHSAHLLSRPQVPAAPTECLSFW 754
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVsgpsVKTGPSSDHTqgTGSGHFMYVDTSSG-APGQTARLLSPLLPPSRSPQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  755 YYLHGPQIGTLRLAMRREGEE--THLWSRSGTQGNRWHEAWATLSHQPGsraQYQLLFEGLRD-GYHGTMALDDVAVRPG 831
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTldTLLWSISGDQGPSWKEARVTLSSSTQ---PFQVVFEGIRGgGSRGGIALDDISLSSG 156


                   ...
gi 1622869768  832 PCW 834
Cdd:pfam00629  157 PCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 682-833 4.44e-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: 157.15  E-value: 4.44e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  682 CNFERDTCSWYPGHLSDTHWRWVES------RGPDHDHTTGQGHFVLLDPTDPlAWGHSAHLLSRPQVPAAPTECLSFWY 755
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGstpspgTPPDHTHGTGSGHYLYVESSSG-REGQKARLLSPLLPPPRSSHCLSFWY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  756 YLHGPQIGTLRLAMRREGE--ETHLWSRSGTQGNRWHEAWATLSHqpgSRAQYQLLFEGLRD-GYHGTMALDDVAVRPGP 832
Cdd:cd06263     80 HMYGSGVGTLNVYVREEGGglGTLLWSASGGQGNQWQEAEVTLSA---SSKPFQVVFEGVRGsGSRGDIALDDISLSPGP 156


                   .
gi 1622869768  833 C 833
Cdd:cd06263    157 C 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 839-994 1.04e-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: 150.59  E-value: 1.04e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  839 CSFEDSD-CGFS--SGGRGLWRRQANASGHTawGPPTDHTTETAQGHYMVVDTSpdALPRGQTASLTSKEYSPPAQPACL 915
Cdd:pfam00629    1 CDFEDGNlCGWTqdSSDDFDWERVSGPSVKT--GPSSDHTQGTGSGHFMYVDTS--SGAPGQTARLLSPLLPPSRSPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  916 TFWYHGSLHNPGTLRVHLE---KGRKHQVLSLSAHGGLAWRLGSVDVQA-EQAWRVVFEAVAAGVAHSYVALDDLLLQDG 991
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRengGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLSSG 156


                   ...
gi 1622869768  992 PCP 994
Cdd:pfam00629  157 PCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 839-993 9.54e-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: 141.75  E-value: 9.54e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  839 CSFEDSDCGFS--SGGRGLWRRQANASGHTawGPPTDHTTETAQGHYMVVDTSPDalPRGQTASLTSKEYSPPAQPACLT 916
Cdd:cd06263      1 CDFEDGLCGWTqdSTDDFDWTRVSGSTPSP--GTPPDHTHGTGSGHYLYVESSSG--REGQKARLLSPLLPPPRSSHCLS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  917 FWYHGSLHNPGTLRVHL-EKGRKHQ--VLSLSAHGGLAWRLGSVDVQAEQA-WRVVFEAVAAGVAHSYVALDDLLLQDGP 992
Cdd:cd06263     77 FWYHMYGSGVGTLNVYVrEEGGGLGtlLWSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSGSRGDIALDDISLSPGP 156


                   .
gi 1622869768  993 C 993
Cdd:cd06263    157 C 157
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 62-219 3.75e-36

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: 134.39  E-value: 3.75e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768    62 TPFACDFEQDS-CGWRDISTSGYSWLRDRAGAAleGPGPHSDHTLGTdlGWYMAVGTHRGKEASTAALRSPTLREAAPSC 140
Cdd:smart00137    2 SPGNCDFEEGStCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRSTH 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   141 KLRLWYHAASGDVAELRLEVT--HGSETLTLWQSTGPWDPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLAFW 218
Cdd:smart00137   78 CLTFWYYMYGSGSGTLNVYVRenNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRGKGHSGYIALDDILLS 157


                    .
gi 1622869768   219 D 219
Cdd:smart00137  158 N 158
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 66-219 9.05e-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: 133.27  E-value: 9.05e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   66 CDFEQDSCGWRDISTSGYSWLRDRAGAAleGPGPHSDHTLGTDLGWYMAVGTHRGKEASTAALRSPTLREAA-PSCkLRL 144
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTP--SPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRsSHC-LSF 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622869768  145 WYHAASGDVAELRLEVTHGSETLT--LWQSTGPWDPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLAFWD 219
Cdd:cd06263     78 WYHMYGSGVGTLNVYVREEGGGLGtlLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 66-217 5.35e-34

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: 128.25  E-value: 5.35e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   66 CDFEQDS-CGWRDISTSGYSWLRDRAGAalEGPGPHSDHTLGTDLGWYMAVGTHRGKEASTAALRSPTLREAAPSCKLRL 144
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPS--VKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622869768  145 WYHAASGDVAELRLEVTHGSETL--TLWQSTGPWDPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLAF 217
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGGSRGGIALDDISL 153
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 994-1220 1.21e-32

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: 124.38  E-value: 1.21e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   994 PRPGSCDFESG-LCGWSHLAWPslgGYSWDWGGGATpsRYPQPPVDHTLGTkagtcplepggeatqrphtatwlpaahrv 1072
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSND---DGHWERVSSAT--GIPGPNRDHTTGN----------------------------- 46

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  1073 hapsrggpahsasaralragsahqpginlllfpGHFAFFETGVLGPGgRAAWLRSEPLPAT-PASCLRFWYHMGFPEHfy 1151
Cdd:smart00137   47 ---------------------------------GHFMFFETSSGAEG-QTARLLSPPLYENrSTHCLTFWYYMYGSGS-- 90

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622869768  1152 kGELRVLLRSTQGQLA--VWGTGGHRRHQWLEAQVEV-ASTKEFQVVFEATLGGqPALGPIALDDVEYLAGQ 1220
Cdd:smart00137   91 -GTLNVYVRENNGSQDtlLWSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGK-GHSGYIALDDILLSNGP 160
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 999-1220 3.36e-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: 114.40  E-value: 3.36e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  999 CDFESGLCGWSHLawpSLGGYSWDWGGGATPSryPQPPVDHTLGTKAGtcplepggeatqrphtatwlpaahrvhapsrg 1078
Cdd:cd06263      1 CDFEDGLCGWTQD---STDDFDWTRVSGSTPS--PGTPPDHTHGTGSG-------------------------------- 43

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768 1079 gpahsasaralragsahqpginlllfpgHFAFFETGVlGPGGRAAWLRSEPLPAT-PASCLRFWYHMGFPEHfykGELRV 1157
Cdd:cd06263     44 ----------------------------HYLYVESSS-GREGQKARLLSPLLPPPrSSHCLSFWYHMYGSGV---GTLNV 91

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622869768 1158 LLRSTQGQL--AVWGTGGHRRHQWLEAQVEV-ASTKEFQVVFEATLGGQPAlGPIALDDVEYLAGQ 1220
Cdd:cd06263     92 YVREEGGGLgtLLWSASGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSR-GDIALDDISLSPGP 156
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 999-1222 3.40e-27

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: 108.99  E-value: 3.40e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  999 CDFESG-LCGWSHlawPSLGGYSWDWGGGatPSRYPQPPVDHTLGTKAGtcplepggeatqrphtatwlpaahrvhapsr 1077
Cdd:pfam00629    1 CDFEDGnLCGWTQ---DSSDDFDWERVSG--PSVKTGPSSDHTQGTGSG------------------------------- 44

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768 1078 ggpahsasaralragsahqpginlllfpgHFAFFETgVLGPGGRAAWLRSEPLPATPAS-CLRFWYHMGFPehfYKGELR 1156
Cdd:pfam00629   45 -----------------------------HFMYVDT-SSGAPGQTARLLSPLLPPSRSPqCLRFWYHMSGS---GVGTLR 91

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622869768 1157 VLLRSTQGQL--AVWGTGGHRRHQWLEAQVEV-ASTKEFQVVFEATLGGqPALGPIALDDVEyLAGQRC 1222
Cdd:pfam00629   92 VYVRENGGTLdtLLWSISGDQGPSWKEARVTLsSSTQPFQVVFEGIRGG-GSRGGIALDDIS-LSSGPC 158
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 836-993 2.29e-25

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: 103.58  E-value: 2.29e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   836 PHHCSFED-SDCGF--SSGGRGLWRRQanaSGHTAW-GPPTDHTTETaqGHYMVVDTSPdaLPRGQTASLTSKEYSPPAQ 911
Cdd:smart00137    3 PGNCDFEEgSTCGWhqDSNDDGHWERV---SSATGIpGPNRDHTTGN--GHFMFFETSS--GAEGQTARLLSPPLYENRS 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   912 PACLTFWYHGSLHNPGTLRVHLeKGRKHQ----VLSLSAHGGLAWRLGSVDVQAE-QAWRVVFEAVAAGVAHSYVALDDL 986
Cdd:smart00137   76 THCLTFWYYMYGSGSGTLNVYV-RENNGSqdtlLWSRSGTQGGQWLQAEVALSSWpQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....*..
gi 1622869768   987 LLQDGPC 993
Cdd:smart00137  155 LLSNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 271-450 6.81e-25

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: 102.06  E-value: 6.81e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  271 TDFETG-LGPWNRSE----GWSRNHsagGPERPSWPRRDHSRNSAQGSFLV---SVAEPGTPAILSSPAFQASGASNCsv 342
Cdd:pfam00629    1 CDFEDGnLCGWTQDSsddfDWERVS---GPSVKTGPSSDHTQGTGSGHFMYvdtSSGAPGQTARLLSPLLPPSRSPQC-- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  343 rwvgltgppcwlprcrapsqllvpqLIFYHYLHGSEAGCLQLFLQTLGSSAPQapvLLRRRRGELGTAWVRDRVDIQS-A 421
Cdd:pfam00629   76 -------------------------LRFWYHMSGSGVGTLRVYVRENGGTLDT---LLWSISGDQGPSWKEARVTLSSsT 127

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1622869768  422 HPFQILLAGQ--TGPGGVVGLDD-LILSDHCR 450
Cdd:pfam00629  128 QPFQVVFEGIrgGGSRGGIALDDiSLSSGPCP 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 519-669 7.15e-25

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: 102.06  E-value: 7.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  519 TDFESLEAGGWEDASVGRLQWRRLSA-QESQGSSA-----AAAGHFLSLQRAWGQLSTEARVLTPLLGPSGPSCELHLAY 592
Cdd:pfam00629    1 CDFEDGNLCGWTQDSSDDFDWERVSGpSVKTGPSSdhtqgTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRFWY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  593 YLQSQPRGFLALVVVDNGSR--ELAWQALSSSAGGWKVDKVLLGARRRPFQLEFVGLVdlDGPDQQGAGVDNVTL--RDC 668
Cdd:pfam00629   81 HMSGSGVGTLRVYVRENGGTldTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIR--GGGSRGGIALDDISLssGPC 158


                   .
gi 1622869768  669 S 669
Cdd:pfam00629  159 P 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 249-448 1.34e-21

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: 92.79  E-value: 1.34e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   249 DGEDNCGDlsdEDPLTCGRHTATDFEtglGPWNRSEGWsrnhsaggpERPSWPRRDHSRNSaqGSFL---VSVAEPGTPA 325
Cdd:smart00137    1 TSPGNCDF---EEGSTCGWHQDSNDD---GHWERVSSA---------TGIPGPNRDHTTGN--GHFMffeTSSGAEGQTA 63

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   326 ILSSPAFQASGASNCsvrwvgltgppcwlprcrapsqllvpqLIFYHYLHGSEAGCLQLFLQTLGSSAPQapvLLRRRRG 405
Cdd:smart00137   64 RLLSPPLYENRSTHC---------------------------LTFWYYMYGSGSGTLNVYVRENNGSQDT---LLWSRSG 113

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*.
gi 1622869768   406 ELGTAWVRDRVDIQS-AHPFQILLAGQTGPG--GVVGLDDLILSDH 448
Cdd:smart00137  114 TQGGQWLQAEVALSSwPQPFQVVFEGTRGKGhsGYIALDDILLSNG 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 501-667 1.18e-18

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: 84.35  E-value: 1.18e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  501 CDFEEQcaggedeqACGttdfesleaggWEDASVGRLQWRRLSAQESQ------GSSAAAAGHFLSLQRAWGQLSTEARV 574
Cdd:cd06263      1 CDFEDG--------LCG-----------WTQDSTDDFDWTRVSGSTPSpgtppdHTHGTGSGHYLYVESSSGREGQKARL 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  575 LTPLL-GPSGPSCeLHLAYYLQSQPRGFLALVVVDNGS--RELAWQALSSSAGGWKVDKVLLGARRRPFQLEFVGLVdld 651
Cdd:cd06263     62 LSPLLpPPRSSHC-LSFWYHMYGSGVGTLNVYVREEGGglGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVR--- 137

                          170
                   ....*....|....*..
gi 1622869768  652 GPDQQGA-GVDNVTLRD 667
Cdd:cd06263    138 GSGSRGDiALDDISLSP 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 272-448 4.47e-14

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: 71.25  E-value: 4.47e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  272 DFETGLGPWNRSEG----WSRNHSAGGPERPSwprRDHSRNSAQGSFLV---SVAEPGTPAILSSPAFQASGASNCsvrw 344
Cdd:cd06263      2 DFEDGLCGWTQDSTddfdWTRVSGSTPSPGTP---PDHTHGTGSGHYLYvesSSGREGQKARLLSPLLPPPRSSHC---- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  345 vgltgppcwlprcrapsqllvpqLIFYHYLHGSEAGCLQLFLQTLGSSAPQapvLLRRRRGELGTAWVRDRVDIQSAH-P 423
Cdd:cd06263     75 -----------------------LSFWYHMYGSGVGTLNVYVREEGGGLGT---LLWSASGGQGNQWQEAEVTLSASSkP 128

                          170       180
                   ....*....|....*....|....*..
gi 1622869768  424 FQILLAGQTGPG--GVVGLDDLILSDH 448
Cdd:cd06263    129 FQVVFEGVRGSGsrGDIALDDISLSPG 155
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 229-261 3.76e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 50.28  E-value: 3.76e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1622869768  229 CPLGHHHCQNKVCVEPQQLCDGEDNCGDLSDED 261
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 229-260 7.84e-08

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 49.55  E-value: 7.84e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1622869768   229 CPLGHHHCQNKVCVEPQQLCDGEDNCGDLSDE 260
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 483-516 1.62e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 45.66  E-value: 1.62e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1622869768  483 CKQGHFACGD-LCVPPEQLCDFEEQCAGGEDEQAC 516
Cdd:cd00112      1 CPPNEFRCANgRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 483-513 3.84e-05

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 41.85  E-value: 3.84e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1622869768   483 CKQGHFACGD-LCVPPEQLCDFEEQCAGGEDE 513
Cdd:smart00192    2 CPPGEFQCDNgRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
229-260 4.67e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 38.77  E-value: 4.67e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1622869768  229 CPLGHHHCQNKVCVEPQQLCDGEDNCGDLSDE 260
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDE 34
 
Name Accession Description Interval E-value
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 677-833 3.15e-45

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: 160.59  E-value: 3.15e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   677 DREVSCNFERD-TCSWYPGHLSDTHWRWVES----RGPDHDHTTGQGHFVLLDpTDPLAWGHSAHLLSRPQVPAAPTECL 751
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSatgiPGPNRDHTTGNGHFMFFE-TSSGAEGQTARLLSPPLYENRSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   752 SFWYYLHGPQIGTLRLAMRREGEE--THLWSRSGTQGNRWHEAWATLSHQPGsraQYQLLFEGLR-DGYHGTMALDDVAV 828
Cdd:smart00137   80 TFWYYMYGSGSGTLNVYVRENNGSqdTLLWSRSGTQGGQWLQAEVALSSWPQ---PFQVVFEGTRgKGHSGYIALDDILL 156


                    ....*
gi 1622869768   829 RPGPC 833
Cdd:smart00137  157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 682-834 7.53e-45

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: 159.45  E-value: 7.53e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  682 CNFERDT-CSWYPGHLSDTHWRWV----ESRGPDHDHT--TGQGHFVLLDPTDPlAWGHSAHLLSRPQVPAAPTECLSFW 754
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVsgpsVKTGPSSDHTqgTGSGHFMYVDTSSG-APGQTARLLSPLLPPSRSPQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  755 YYLHGPQIGTLRLAMRREGEE--THLWSRSGTQGNRWHEAWATLSHQPGsraQYQLLFEGLRD-GYHGTMALDDVAVRPG 831
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTldTLLWSISGDQGPSWKEARVTLSSSTQ---PFQVVFEGIRGgGSRGGIALDDISLSSG 156


                   ...
gi 1622869768  832 PCW 834
Cdd:pfam00629  157 PCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 682-833 4.44e-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: 157.15  E-value: 4.44e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  682 CNFERDTCSWYPGHLSDTHWRWVES------RGPDHDHTTGQGHFVLLDPTDPlAWGHSAHLLSRPQVPAAPTECLSFWY 755
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGstpspgTPPDHTHGTGSGHYLYVESSSG-REGQKARLLSPLLPPPRSSHCLSFWY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  756 YLHGPQIGTLRLAMRREGE--ETHLWSRSGTQGNRWHEAWATLSHqpgSRAQYQLLFEGLRD-GYHGTMALDDVAVRPGP 832
Cdd:cd06263     80 HMYGSGVGTLNVYVREEGGglGTLLWSASGGQGNQWQEAEVTLSA---SSKPFQVVFEGVRGsGSRGDIALDDISLSPGP 156


                   .
gi 1622869768  833 C 833
Cdd:cd06263    157 C 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 839-994 1.04e-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: 150.59  E-value: 1.04e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  839 CSFEDSD-CGFS--SGGRGLWRRQANASGHTawGPPTDHTTETAQGHYMVVDTSpdALPRGQTASLTSKEYSPPAQPACL 915
Cdd:pfam00629    1 CDFEDGNlCGWTqdSSDDFDWERVSGPSVKT--GPSSDHTQGTGSGHFMYVDTS--SGAPGQTARLLSPLLPPSRSPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  916 TFWYHGSLHNPGTLRVHLE---KGRKHQVLSLSAHGGLAWRLGSVDVQA-EQAWRVVFEAVAAGVAHSYVALDDLLLQDG 991
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRengGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLSSG 156


                   ...
gi 1622869768  992 PCP 994
Cdd:pfam00629  157 PCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 839-993 9.54e-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: 141.75  E-value: 9.54e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  839 CSFEDSDCGFS--SGGRGLWRRQANASGHTawGPPTDHTTETAQGHYMVVDTSPDalPRGQTASLTSKEYSPPAQPACLT 916
Cdd:cd06263      1 CDFEDGLCGWTqdSTDDFDWTRVSGSTPSP--GTPPDHTHGTGSGHYLYVESSSG--REGQKARLLSPLLPPPRSSHCLS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  917 FWYHGSLHNPGTLRVHL-EKGRKHQ--VLSLSAHGGLAWRLGSVDVQAEQA-WRVVFEAVAAGVAHSYVALDDLLLQDGP 992
Cdd:cd06263     77 FWYHMYGSGVGTLNVYVrEEGGGLGtlLWSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSGSRGDIALDDISLSPGP 156


                   .
gi 1622869768  993 C 993
Cdd:cd06263    157 C 157
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 62-219 3.75e-36

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: 134.39  E-value: 3.75e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768    62 TPFACDFEQDS-CGWRDISTSGYSWLRDRAGAAleGPGPHSDHTLGTdlGWYMAVGTHRGKEASTAALRSPTLREAAPSC 140
Cdd:smart00137    2 SPGNCDFEEGStCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRSTH 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   141 KLRLWYHAASGDVAELRLEVT--HGSETLTLWQSTGPWDPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLAFW 218
Cdd:smart00137   78 CLTFWYYMYGSGSGTLNVYVRenNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRGKGHSGYIALDDILLS 157


                    .
gi 1622869768   219 D 219
Cdd:smart00137  158 N 158
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 66-219 9.05e-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: 133.27  E-value: 9.05e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   66 CDFEQDSCGWRDISTSGYSWLRDRAGAAleGPGPHSDHTLGTDLGWYMAVGTHRGKEASTAALRSPTLREAA-PSCkLRL 144
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTP--SPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRsSHC-LSF 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622869768  145 WYHAASGDVAELRLEVTHGSETLT--LWQSTGPWDPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLAFWD 219
Cdd:cd06263     78 WYHMYGSGVGTLNVYVREEGGGLGtlLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 66-217 5.35e-34

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: 128.25  E-value: 5.35e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   66 CDFEQDS-CGWRDISTSGYSWLRDRAGAalEGPGPHSDHTLGTDLGWYMAVGTHRGKEASTAALRSPTLREAAPSCKLRL 144
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPS--VKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622869768  145 WYHAASGDVAELRLEVTHGSETL--TLWQSTGPWDPGWQELAVTTGRIRGDFRVTFSATRNATHRGAVALDDLAF 217
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGGSRGGIALDDISL 153
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 994-1220 1.21e-32

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: 124.38  E-value: 1.21e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   994 PRPGSCDFESG-LCGWSHLAWPslgGYSWDWGGGATpsRYPQPPVDHTLGTkagtcplepggeatqrphtatwlpaahrv 1072
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSND---DGHWERVSSAT--GIPGPNRDHTTGN----------------------------- 46

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  1073 hapsrggpahsasaralragsahqpginlllfpGHFAFFETGVLGPGgRAAWLRSEPLPAT-PASCLRFWYHMGFPEHfy 1151
Cdd:smart00137   47 ---------------------------------GHFMFFETSSGAEG-QTARLLSPPLYENrSTHCLTFWYYMYGSGS-- 90

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622869768  1152 kGELRVLLRSTQGQLA--VWGTGGHRRHQWLEAQVEV-ASTKEFQVVFEATLGGqPALGPIALDDVEYLAGQ 1220
Cdd:smart00137   91 -GTLNVYVRENNGSQDtlLWSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGK-GHSGYIALDDILLSNGP 160
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 999-1220 3.36e-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: 114.40  E-value: 3.36e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  999 CDFESGLCGWSHLawpSLGGYSWDWGGGATPSryPQPPVDHTLGTKAGtcplepggeatqrphtatwlpaahrvhapsrg 1078
Cdd:cd06263      1 CDFEDGLCGWTQD---STDDFDWTRVSGSTPS--PGTPPDHTHGTGSG-------------------------------- 43

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768 1079 gpahsasaralragsahqpginlllfpgHFAFFETGVlGPGGRAAWLRSEPLPAT-PASCLRFWYHMGFPEHfykGELRV 1157
Cdd:cd06263     44 ----------------------------HYLYVESSS-GREGQKARLLSPLLPPPrSSHCLSFWYHMYGSGV---GTLNV 91

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622869768 1158 LLRSTQGQL--AVWGTGGHRRHQWLEAQVEV-ASTKEFQVVFEATLGGQPAlGPIALDDVEYLAGQ 1220
Cdd:cd06263     92 YVREEGGGLgtLLWSASGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSR-GDIALDDISLSPGP 156
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 999-1222 3.40e-27

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: 108.99  E-value: 3.40e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  999 CDFESG-LCGWSHlawPSLGGYSWDWGGGatPSRYPQPPVDHTLGTKAGtcplepggeatqrphtatwlpaahrvhapsr 1077
Cdd:pfam00629    1 CDFEDGnLCGWTQ---DSSDDFDWERVSG--PSVKTGPSSDHTQGTGSG------------------------------- 44

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768 1078 ggpahsasaralragsahqpginlllfpgHFAFFETgVLGPGGRAAWLRSEPLPATPAS-CLRFWYHMGFPehfYKGELR 1156
Cdd:pfam00629   45 -----------------------------HFMYVDT-SSGAPGQTARLLSPLLPPSRSPqCLRFWYHMSGS---GVGTLR 91

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622869768 1157 VLLRSTQGQL--AVWGTGGHRRHQWLEAQVEV-ASTKEFQVVFEATLGGqPALGPIALDDVEyLAGQRC 1222
Cdd:pfam00629   92 VYVRENGGTLdtLLWSISGDQGPSWKEARVTLsSSTQPFQVVFEGIRGG-GSRGGIALDDIS-LSSGPC 158
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 836-993 2.29e-25

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: 103.58  E-value: 2.29e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   836 PHHCSFED-SDCGF--SSGGRGLWRRQanaSGHTAW-GPPTDHTTETaqGHYMVVDTSPdaLPRGQTASLTSKEYSPPAQ 911
Cdd:smart00137    3 PGNCDFEEgSTCGWhqDSNDDGHWERV---SSATGIpGPNRDHTTGN--GHFMFFETSS--GAEGQTARLLSPPLYENRS 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   912 PACLTFWYHGSLHNPGTLRVHLeKGRKHQ----VLSLSAHGGLAWRLGSVDVQAE-QAWRVVFEAVAAGVAHSYVALDDL 986
Cdd:smart00137   76 THCLTFWYYMYGSGSGTLNVYV-RENNGSqdtlLWSRSGTQGGQWLQAEVALSSWpQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....*..
gi 1622869768   987 LLQDGPC 993
Cdd:smart00137  155 LLSNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 271-450 6.81e-25

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: 102.06  E-value: 6.81e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  271 TDFETG-LGPWNRSE----GWSRNHsagGPERPSWPRRDHSRNSAQGSFLV---SVAEPGTPAILSSPAFQASGASNCsv 342
Cdd:pfam00629    1 CDFEDGnLCGWTQDSsddfDWERVS---GPSVKTGPSSDHTQGTGSGHFMYvdtSSGAPGQTARLLSPLLPPSRSPQC-- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  343 rwvgltgppcwlprcrapsqllvpqLIFYHYLHGSEAGCLQLFLQTLGSSAPQapvLLRRRRGELGTAWVRDRVDIQS-A 421
Cdd:pfam00629   76 -------------------------LRFWYHMSGSGVGTLRVYVRENGGTLDT---LLWSISGDQGPSWKEARVTLSSsT 127

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1622869768  422 HPFQILLAGQ--TGPGGVVGLDD-LILSDHCR 450
Cdd:pfam00629  128 QPFQVVFEGIrgGGSRGGIALDDiSLSSGPCP 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 519-669 7.15e-25

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: 102.06  E-value: 7.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  519 TDFESLEAGGWEDASVGRLQWRRLSA-QESQGSSA-----AAAGHFLSLQRAWGQLSTEARVLTPLLGPSGPSCELHLAY 592
Cdd:pfam00629    1 CDFEDGNLCGWTQDSSDDFDWERVSGpSVKTGPSSdhtqgTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRFWY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  593 YLQSQPRGFLALVVVDNGSR--ELAWQALSSSAGGWKVDKVLLGARRRPFQLEFVGLVdlDGPDQQGAGVDNVTL--RDC 668
Cdd:pfam00629   81 HMSGSGVGTLRVYVRENGGTldTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIR--GGGSRGGIALDDISLssGPC 158


                   .
gi 1622869768  669 S 669
Cdd:pfam00629  159 P 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 249-448 1.34e-21

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: 92.79  E-value: 1.34e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   249 DGEDNCGDlsdEDPLTCGRHTATDFEtglGPWNRSEGWsrnhsaggpERPSWPRRDHSRNSaqGSFL---VSVAEPGTPA 325
Cdd:smart00137    1 TSPGNCDF---EEGSTCGWHQDSNDD---GHWERVSSA---------TGIPGPNRDHTTGN--GHFMffeTSSGAEGQTA 63

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768   326 ILSSPAFQASGASNCsvrwvgltgppcwlprcrapsqllvpqLIFYHYLHGSEAGCLQLFLQTLGSSAPQapvLLRRRRG 405
Cdd:smart00137   64 RLLSPPLYENRSTHC---------------------------LTFWYYMYGSGSGTLNVYVRENNGSQDT---LLWSRSG 113

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*.
gi 1622869768   406 ELGTAWVRDRVDIQS-AHPFQILLAGQTGPG--GVVGLDDLILSDH 448
Cdd:smart00137  114 TQGGQWLQAEVALSSwPQPFQVVFEGTRGKGhsGYIALDDILLSNG 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 501-667 1.18e-18

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: 84.35  E-value: 1.18e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  501 CDFEEQcaggedeqACGttdfesleaggWEDASVGRLQWRRLSAQESQ------GSSAAAAGHFLSLQRAWGQLSTEARV 574
Cdd:cd06263      1 CDFEDG--------LCG-----------WTQDSTDDFDWTRVSGSTPSpgtppdHTHGTGSGHYLYVESSSGREGQKARL 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  575 LTPLL-GPSGPSCeLHLAYYLQSQPRGFLALVVVDNGS--RELAWQALSSSAGGWKVDKVLLGARRRPFQLEFVGLVdld 651
Cdd:cd06263     62 LSPLLpPPRSSHC-LSFWYHMYGSGVGTLNVYVREEGGglGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVR--- 137

                          170
                   ....*....|....*..
gi 1622869768  652 GPDQQGA-GVDNVTLRD 667
Cdd:cd06263    138 GSGSRGDiALDDISLSP 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 272-448 4.47e-14

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: 71.25  E-value: 4.47e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  272 DFETGLGPWNRSEG----WSRNHSAGGPERPSwprRDHSRNSAQGSFLV---SVAEPGTPAILSSPAFQASGASNCsvrw 344
Cdd:cd06263      2 DFEDGLCGWTQDSTddfdWTRVSGSTPSPGTP---PDHTHGTGSGHYLYvesSSGREGQKARLLSPLLPPPRSSHC---- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622869768  345 vgltgppcwlprcrapsqllvpqLIFYHYLHGSEAGCLQLFLQTLGSSAPQapvLLRRRRGELGTAWVRDRVDIQSAH-P 423
Cdd:cd06263     75 -----------------------LSFWYHMYGSGVGTLNVYVREEGGGLGT---LLWSASGGQGNQWQEAEVTLSASSkP 128

                          170       180
                   ....*....|....*....|....*..
gi 1622869768  424 FQILLAGQTGPG--GVVGLDDLILSDH 448
Cdd:cd06263    129 FQVVFEGVRGSGsrGDIALDDISLSPG 155
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 229-261 3.76e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 50.28  E-value: 3.76e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1622869768  229 CPLGHHHCQNKVCVEPQQLCDGEDNCGDLSDED 261
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 229-260 7.84e-08

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 49.55  E-value: 7.84e-08
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1622869768   229 CPLGHHHCQNKVCVEPQQLCDGEDNCGDLSDE 260
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 483-516 1.62e-06

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 45.66  E-value: 1.62e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1622869768  483 CKQGHFACGD-LCVPPEQLCDFEEQCAGGEDEQAC 516
Cdd:cd00112      1 CPPNEFRCANgRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 483-513 3.84e-05

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 41.85  E-value: 3.84e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1622869768   483 CKQGHFACGD-LCVPPEQLCDFEEQCAGGEDE 513
Cdd:smart00192    2 CPPGEFQCDNgRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
229-260 4.67e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 38.77  E-value: 4.67e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1622869768  229 CPLGHHHCQNKVCVEPQQLCDGEDNCGDLSDE 260
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDE 34
 
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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