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Conserved domains on  [gi|881185998|ref|NP_001297384|]
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MAM and LDL-receptor class A domain-containing protein 1 precursor [Mus musculus]

Protein Classification

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 ...
 831-987 1.96e-45

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: 161.78  E-value: 1.96e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  831 CNFENGICNWEQSTKDDFNWTRYQGPTSTMNTGPmkDHTLGTAKGHYLYIETSGPQgFQDKAVLLSPILNATEAKVCtFR 910
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGR-EGQKARLLSPLLPPPRSSHC-LS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881185998  911 LYYHMFGKHIYRLAIYQRIWSNTKGQLLWQIFGDQGNRWIRKDLSI-TSRKPFQILIMASVGDGFTGDIAIDDLSFMD 987
Cdd:cd06263    77 FWYHMYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 1695-1855 5.78e-39

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: 143.27  E-value: 5.78e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  1695 CNFETTSgdwtvECGLTQDPEDDLDWSIGSIiPTEGLSRDSDHTPGSGR-HFLYVNTSLAEEGSTARIItSHFFPASLGI 1773
Cdd:pfam00629    1 CDFEDGN-----LCGWTQDSSDDFDWERVSG-PSVKTGPSSDHTQGTGSgHFMYVDTSSGAPGQTARLL-SPLLPPSRSP 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  1774 CTVRFWFYMVDPHiVGILKVYLIEKSG-LNILMWSMMRNKNTGWTYAHVPLSSNS-PFKVAFEADLGGKEDIFIALDDIT 1851
Cdd:pfam00629   74 QCLRFWYHMSGSG-VGTLRVYVRENGGtLDTLLWSISGDQGPSWKEARVTLSSSTqPFQVVFEGIRGGGSRGGIALDDIS 152


                   ....
gi 881185998  1852 FTPT 1855
Cdd:pfam00629  153 LSSG 156
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 620-781 1.12e-36

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: 136.72  E-value: 1.12e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   620 CDFE-ANSCGWFEASGgDHFDWVWSSQSNLSadleqQAPPRDHTHGTAQGHFMFILKTSNSLFQTAKLQSPTFSQTGPGC 698
Cdd:pfam00629    1 CDFEdGNLCGWTQDSS-DDFDWERVSGPSVK-----TGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQ 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   699 TMSFWFYNYGLSVGAAELQLHLENSRDTTALWRVLYNQGNQWSEATVQLGRLTQPFYLSLEKVSLAVYSGVSAVDDIHF- 777
Cdd:pfam00629   75 CLRFWYHMSGSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGGSRGGIALDDISLs 154


                   ....*
gi 881185998   778 -ENCA 781
Cdd:pfam00629  155 sGPCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 1487-1639 2.67e-34

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: 129.81  E-value: 2.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998 1487 CTFEKGWCGWKNSLAENSDWVLGIGSYKSQRPPKDHTLGNEHGHFMYLEATPvGLHGDKAHFKSAT-WQESSAACtMSFW 1565
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSS-GREGQKARLLSPLlPPPRSSHC-LSFW 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 881185998 1566 YFISAKATGSIQILIKTDKG-LWEVWQQSKPDPGNHWRRATILLGKLRN-FEVIFQGIRTRDLGGGAAIDDIEFNN 1639
Cdd:cd06263    79 YHMYGSGVGTLNVYVREEGGgLGTLLWSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSGSRGDIALDDISLSP 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 1273-1426 1.28e-33

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: 127.88  E-value: 1.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998 1273 CDFEFDLCTWEQDQDEDIDWNLKASNIPATSTEPavDHTLGNSSGHYIILKSFFPQQPvKTGRISSPVIS-KRSKDCkII 1351
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGREG-QKARLLSPLLPpPRSSHC-LS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881185998 1352 FNYHMYGSGIAALLLLQVTVTNHTRVLL-NLTKEQGNFWQRKELSLSS-DEDFRVKFEGRVGEGIRGNIALDDIVLT 1426
Cdd:cd06263    77 FWYHMYGSGVGTLNVYVREEGGGLGTLLwSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGSGSRGDIALDDISLS 153
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 1056-1219 3.21e-32

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: 123.64  E-value: 3.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998 1056 CTFEERkLCKWYQPipanslhDSNTFRWGLGNGISIHHGeenhrPSVDHTKNTTDGWYLYADSSNGKFGDLADIVTPVIS 1135
Cdd:cd06263     1 CDFEDG-LCGWTQD-------STDDFDWTRVSGSTPSPG-----TPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998 1136 LM-GPRCtLVFWTYMNGATVGSLQVLIK--MGNTISKVWAQSGQQGPQWKKAEVFLG-IHSHVEIVFRAKRGVSYIGDVA 1211
Cdd:cd06263    68 PPrSSHC-LSFWYHMYGSGVGTLNVYVReeGGGLGTLLWSASGGQGNQWQEAEVTLSaSSKPFQVVFEGVRGSGSRGDIA 146


                  ....*...
gi 881185998 1212 VDDVSFQN 1219
Cdd:cd06263   147 LDDISLSP 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 443-601 1.67e-23

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: 98.99  E-value: 1.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  443 DFESGFCGWEPFPTEDSHWEVVRGLSNGEHlfLEAGHTVSRNQGSFIYFGPQKSTA--VARLGSPILTKSLTTFtpCqVR 520
Cdd:cd06263     2 DFEDGLCGWTQDSTDDFDWTRVSGSTPSPG--TPPDHTHGTGSGHYLYVESSSGREgqKARLLSPLLPPPRSSH--C-LS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  521 FWYHLS--EHSSLSVFTRTSVDGSLLKQSEVTQFSDSQWSQAKVDLHAKAEestlPFQLVLEATILSSNA-TVAVDDISI 597
Cdd:cd06263    77 FWYHMYgsGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSK----PFQVVFEGVRGSGSRgDIALDDISL 152


                  ....*
gi 881185998  598 S-HEC 601
Cdd:cd06263   153 SpGPC 157
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 73-226 1.94e-21

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: 92.83  E-value: 1.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   73 CNFEDRLCSMTEDQTLQPGWTRRSGII-SNSPPFWDHNGNISAHFLALVSRVDSISS--NLRSRIFLPTNDQQvCQITFY 149
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTpSPGTPPDHTHGTGSGHYLYVESSSGREGQkaRLLSPLLPPPRSSH-CLSFWY 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881185998  150 NFSSNQNGKLIAGLQTLCGDPIEHLWQKTEILQSRWERNVITVQS-SQQFQVIFQAQMLAthGQEEVIAIDDISFSSG 226
Cdd:cd06263    80 HMYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGS--GSRGDIALDDISLSPG 155
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1229-1261 1.40e-09

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: 54.95  E-value: 1.40e-09
                            10        20        30
                    ....*....|....*....|....*....|...
gi 881185998   1229 KCTTDEFMCANKHCIEKDKLCDFVNDCADNSDE 1261
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1449-1483 5.27e-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: 50.67  E-value: 5.27e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 881185998 1449 CPRGYEECQNGRCYSPEQRCNFVDDCGDNSDENEC 1483
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1913-1947 7.29e-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: 7.29e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 881185998 1913 CSDTEFQCFESQCIPSLLLCDGVADCQFNEDESSC 1947
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1653-1685 1.92e-07

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: 48.74  E-value: 1.92e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 881185998 1653 ETDFLCQDKKCIASHLVCDYKPDCSDTSDEAHC 1685
Cdd:cd00112     3 PNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1869-1904 8.52e-07

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: 47.20  E-value: 8.52e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 881185998 1869 CEEGQFACIYaLQCVSASEKCDGQEDCIDGSDEMNC 1904
Cdd:cd00112     1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1016-1051 1.25e-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: 46.82  E-value: 1.25e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 881185998 1016 CTDDQFVCRsNGHCVGNIQKCDFRYDCIDKSDESSC 1051
Cdd:cd00112     1 CPPNEFRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
MAM super family cl47572
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 236-384 2.08e-05

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


The actual alignment was detected with superfamily member pfam00629:

Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 46.59  E-value: 2.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   236 CGF-DLDTCGLaTEASAGRTSWmctKVREIPSLDSVPWQD-QRGHDEGSFVWMRAGHA---SVSRLVESSAYLNSSVcHC 310
Cdd:pfam00629    1 CDFeDGNLCGW-TQDSSDDFDW---ERVSGPSVKTGPSSDhTQGTGSGHFMYVDTSSGapgQTARLLSPLLPPSRSP-QC 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   311 mdgncrLQFNYTMENS---ILRV--RLYNDKEEKKTWTFNTSTYSTWMKADVLIPEDLKAFKVVLEGTVLS-QKSFIGID 384
Cdd:pfam00629   76 ------LRFWYHMSGSgvgTLRVyvRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGgSRGGIALD 149
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 792-825 1.24e-04

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: 41.04  E-value: 1.24e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 881185998  792 PDHFWCRQTKaCIGRHQLCDLVDDCGDYTDETGC 825
Cdd:cd00112     3 PNEFRCANGR-CIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 38-67 3.13e-04

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: 39.88  E-value: 3.13e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 881185998   38 FQCSNGVSLPSDYVCDFTDHCGDNSEEQQC 67
Cdd:cd00112     6 FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1991-2021 3.33e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


:

Pssm-ID: 394967  Cd Length: 31  Bit Score: 36.98  E-value: 3.33e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 881185998  1991 CPIHYCRNGGTCVIENIGPTCRCVQGWTGNR 2021
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
 
Name Accession Description Interval E-value
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 831-987 1.96e-45

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: 161.78  E-value: 1.96e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  831 CNFENGICNWEQSTKDDFNWTRYQGPTSTMNTGPmkDHTLGTAKGHYLYIETSGPQgFQDKAVLLSPILNATEAKVCtFR 910
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGR-EGQKARLLSPLLPPPRSSHC-LS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881185998  911 LYYHMFGKHIYRLAIYQRIWSNTKGQLLWQIFGDQGNRWIRKDLSI-TSRKPFQILIMASVGDGFTGDIAIDDLSFMD 987
Cdd:cd06263    77 FWYHMYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 831-988 5.61e-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: 160.22  E-value: 5.61e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   831 CNFENG-ICNWEQSTKDDFNWTRYQGPTStmNTGPMKDHTLGTAKGHYLYIETSGPQGFQdKAVLLSPILNATEAKVCtF 909
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSGPSV--KTGPSSDHTQGTGSGHFMYVDTSSGAPGQ-TARLLSPLLPPSRSPQC-L 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   910 RLYYHMFGKHIYRLAIYQRIWSNTKGQLLWQIFGDQGNRWIRKDLSITSR-KPFQILIMASVGDGFTGDIAIDDLSFM-- 986
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSStQPFQVVFEGIRGGGSRGGIALDDISLSsg 156


                   ..
gi 881185998   987 DC 988
Cdd:pfam00629  157 PC 158
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 1695-1855 5.78e-39

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: 143.27  E-value: 5.78e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  1695 CNFETTSgdwtvECGLTQDPEDDLDWSIGSIiPTEGLSRDSDHTPGSGR-HFLYVNTSLAEEGSTARIItSHFFPASLGI 1773
Cdd:pfam00629    1 CDFEDGN-----LCGWTQDSSDDFDWERVSG-PSVKTGPSSDHTQGTGSgHFMYVDTSSGAPGQTARLL-SPLLPPSRSP 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  1774 CTVRFWFYMVDPHiVGILKVYLIEKSG-LNILMWSMMRNKNTGWTYAHVPLSSNS-PFKVAFEADLGGKEDIFIALDDIT 1851
Cdd:pfam00629   74 QCLRFWYHMSGSG-VGTLRVYVRENGGtLDTLLWSISGDQGPSWKEARVTLSSSTqPFQVVFEGIRGGGSRGGIALDDIS 152


                   ....
gi 881185998  1852 FTPT 1855
Cdd:pfam00629  153 LSSG 156
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 826-987 3.66e-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: 140.94  E-value: 3.66e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998    826 APGLQCNFE-NGICNWEQSTKDDFNWTRYQGptSTMNTGPMKDHTLGTakGHYLYIETSGPqGFQDKAVLLSPILNATEA 904
Cdd:smart00137    1 TSPGNCDFEeGSTCGWHQDSNDDGHWERVSS--ATGIPGPNRDHTTGN--GHFMFFETSSG-AEGQTARLLSPPLYENRS 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998    905 KVCtFRLYYHMFGKHIYRLAIYQRIWSNTKGQLLWQIFGDQGNRWIRKDLSI-TSRKPFQILIMASVGDGFTGDIAIDDL 983
Cdd:smart00137   76 THC-LTFWYYMYGSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....
gi 881185998    984 SFMD 987
Cdd:smart00137  155 LLSN 158
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 620-781 1.12e-36

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: 136.72  E-value: 1.12e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   620 CDFE-ANSCGWFEASGgDHFDWVWSSQSNLSadleqQAPPRDHTHGTAQGHFMFILKTSNSLFQTAKLQSPTFSQTGPGC 698
Cdd:pfam00629    1 CDFEdGNLCGWTQDSS-DDFDWERVSGPSVK-----TGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQ 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   699 TMSFWFYNYGLSVGAAELQLHLENSRDTTALWRVLYNQGNQWSEATVQLGRLTQPFYLSLEKVSLAVYSGVSAVDDIHF- 777
Cdd:pfam00629   75 CLRFWYHMSGSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGGSRGGIALDDISLs 154


                   ....*
gi 881185998   778 -ENCA 781
Cdd:pfam00629  155 sGPCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 620-779 1.33e-35

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: 133.66  E-value: 1.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  620 CDFEANSCGWFEASGgDHFDWVWSSQSNLSADleqqaPPRDHTHGTAQGHFMFILKTSNSLFQTAKLQSPTFSQT-GPGC 698
Cdd:cd06263     1 CDFEDGLCGWTQDST-DDFDWTRVSGSTPSPG-----TPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHC 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  699 tMSFWFYNYGLSVGAAELQLHLENSRDTTALWRVLYNQGNQWSEATVQLGRLTQPFYLSLEKVSLAVYSGVSAVDDIHFE 778
Cdd:cd06263    75 -LSFWYHMYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLS 153


                  .
gi 881185998  779 N 779
Cdd:cd06263   154 P 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 1487-1639 2.67e-34

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: 129.81  E-value: 2.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998 1487 CTFEKGWCGWKNSLAENSDWVLGIGSYKSQRPPKDHTLGNEHGHFMYLEATPvGLHGDKAHFKSAT-WQESSAACtMSFW 1565
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSS-GREGQKARLLSPLlPPPRSSHC-LSFW 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 881185998 1566 YFISAKATGSIQILIKTDKG-LWEVWQQSKPDPGNHWRRATILLGKLRN-FEVIFQGIRTRDLGGGAAIDDIEFNN 1639
Cdd:cd06263    79 YHMYGSGVGTLNVYVREEGGgLGTLLWSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSGSRGDIALDDISLSP 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 1273-1426 1.28e-33

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: 127.88  E-value: 1.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998 1273 CDFEFDLCTWEQDQDEDIDWNLKASNIPATSTEPavDHTLGNSSGHYIILKSFFPQQPvKTGRISSPVIS-KRSKDCkII 1351
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGREG-QKARLLSPLLPpPRSSHC-LS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881185998 1352 FNYHMYGSGIAALLLLQVTVTNHTRVLL-NLTKEQGNFWQRKELSLSS-DEDFRVKFEGRVGEGIRGNIALDDIVLT 1426
Cdd:cd06263    77 FWYHMYGSGVGTLNVYVREEGGGLGTLLwSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGSGSRGDIALDDISLS 153
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 1056-1219 3.21e-32

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: 123.64  E-value: 3.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998 1056 CTFEERkLCKWYQPipanslhDSNTFRWGLGNGISIHHGeenhrPSVDHTKNTTDGWYLYADSSNGKFGDLADIVTPVIS 1135
Cdd:cd06263     1 CDFEDG-LCGWTQD-------STDDFDWTRVSGSTPSPG-----TPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998 1136 LM-GPRCtLVFWTYMNGATVGSLQVLIK--MGNTISKVWAQSGQQGPQWKKAEVFLG-IHSHVEIVFRAKRGVSYIGDVA 1211
Cdd:cd06263    68 PPrSSHC-LSFWYHMYGSGVGTLNVYVReeGGGLGTLLWSASGGQGNQWQEAEVTLSaSSKPFQVVFEGVRGSGSRGDIA 146


                  ....*...
gi 881185998 1212 VDDVSFQN 1219
Cdd:cd06263   147 LDDISLSP 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 1695-1855 3.51e-32

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: 123.64  E-value: 3.51e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998 1695 CNFETTSgdwtveCGLTQDPEDDLDWSIG-SIIPTEGLSRDSDHTPGSGrHFLYVNTSLAEEGSTARIITSHFFPASLGI 1773
Cdd:cd06263     1 CDFEDGL------CGWTQDSTDDFDWTRVsGSTPSPGTPPDHTHGTGSG-HYLYVESSSGREGQKARLLSPLLPPPRSSH 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998 1774 CtVRFWFYMVDPHiVGILKVYLIEKSG-LNILMWSMMRNKNTGWTYAHVPLSSNS-PFKVAFEADLGGKEDIFIALDDIT 1851
Cdd:cd06263    74 C-LSFWYHMYGSG-VGTLNVYVREEGGgLGTLLWSASGGQGNQWQEAEVTLSASSkPFQVVFEGVRGSGSRGDIALDDIS 151


                  ....
gi 881185998 1852 FTPT 1855
Cdd:cd06263   152 LSPG 155
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 1487-1641 2.71e-30

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: 118.23  E-value: 2.71e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  1487 CTFEKGW-CGWKNSLAENSDWVLGIGSYKSQRPPKDHTLGNEHGHFMYLEATpVGLHGDKAHFKSATWQESSAACTMSFW 1565
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPSVKTGPSSDHTQGTGSGHFMYVDTS-SGAPGQTARLLSPLLPPSRSPQCLRFW 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881185998  1566 YFISAKATGSIQILIKTDKGLWE--VWQQSKpDPGNHWRRATILLGKLRN-FEVIFQGIRTRDLGGGAAIDDIEFNNCT 1641
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTLDtlLWSISG-DQGPSWKEARVTLSSSTQpFQVVFEGIRGGGSRGGIALDDISLSSGP 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 1056-1219 2.56e-29

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: 115.54  E-value: 2.56e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  1056 CTFEERKLCKWYQPIPANslhdsntFRWGLGNGISIHHGeenhrPSVDHTKNTTDGWYLYADSSNGKFGDLADIVTPVIS 1135
Cdd:pfam00629    1 CDFEDGNLCGWTQDSSDD-------FDWERVSGPSVKTG-----PSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLP 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  1136 LMGPRCTLVFWTYMNGATVGSLQVLIKM--GNTISKVWAQSGQQGPQWKKAEVFLGIHSHV-EIVFRAKRGVSYIGDVAV 1212
Cdd:pfam00629   69 PSRSPQCLRFWYHMSGSGVGTLRVYVREngGTLDTLLWSISGDQGPSWKEARVTLSSSTQPfQVVFEGIRGGGSRGGIAL 148


                   ....*..
gi 881185998  1213 DDVSFQN 1219
Cdd:pfam00629  149 DDISLSS 155
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 1273-1426 6.30e-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: 108.60  E-value: 6.30e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  1273 CDFEFD-LCTWEQDQDEDIDWNLKASNIPATStePAVDHTLGNSSGHYIILKSFFPQqPVKTGRISSPVISKRSKDCKII 1351
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSGPSVKTG--PSSDHTQGTGSGHFMYVDTSSGA-PGQTARLLSPLLPPSRSPQCLR 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881185998  1352 FNYHMYGSGIAAL-LLLQVTVTNHTRVLLNLTKEQGNFWQRKELSLSS-DEDFRVKFEGRVGEGIRGNIALDDIVLT 1426
Cdd:pfam00629   78 FWYHMSGSGVGTLrVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLS 154
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 1056-1219 3.67e-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: 3.67e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   1056 CTFEERKLCKWYQpipanslhDSNT-FRWGLGNGisihhGEENHRPSVDHTKNttDGWYLYADSSNGKFGDLADIVTPVI 1134
Cdd:smart00137    6 CDFEEGSTCGWHQ--------DSNDdGHWERVSS-----ATGIPGPNRDHTTG--NGHFMFFETSSGAEGQTARLLSPPL 70

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   1135 SLMGPRCTLVFWTYMNGATVGSLQVLIK--MGNTISKVWAQSGQQGPQWKKAEVFLGIHSH-VEIVFRAKRGVSYIGDVA 1211
Cdd:smart00137   71 YENRSTHCLTFWYYMYGSGSGTLNVYVRenNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQpFQVVFEGTRGKGHSGYIA 150


                    ....*...
gi 881185998   1212 VDDVSFQN 1219
Cdd:smart00137  151 LDDILLSN 158
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 1268-1426 7.58e-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: 102.81  E-value: 7.58e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   1268 TSSGRCDFEFD-LCTWEQDQDEDIDWnlKASNIPATSTEPAVDHTLGNssGHYIILKSFFPQQPVKTGRISSPVISKRSK 1346
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHW--ERVSSATGIPGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   1347 DCkIIFNYHMYGSGIAAL-LLLQVTVTNHTRVLLNLTKEQGNFWQRKELSLSS-DEDFRVKFEGRVGEGIRGNIALDDIV 1424
Cdd:smart00137   77 HC-LTFWYYMYGSGSGTLnVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSSwPQPFQVVFEGTRGKGHSGYIALDDIL 155


                    ..
gi 881185998   1425 LT 1426
Cdd:smart00137  156 LS 157
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 1485-1639 4.19e-24

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: 100.88  E-value: 4.19e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   1485 GSCTFEKGW-CGWKNSLAENSDWVLGIGSYKSQRPPKDHTLGNehGHFMYLEATPvGLHGDKAHFKSATWQESSAACTMS 1563
Cdd:smart00137    4 GNCDFEEGStCGWHQDSNDDGHWERVSSATGIPGPNRDHTTGN--GHFMFFETSS-GAEGQTARLLSPPLYENRSTHCLT 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   1564 FWYFISAKATGSIQILIKTDKG-----LWEVwqqsKPDPGNHWRRATILLGKLRN-FEVIFQGIRTRDLGGGAAIDDIEF 1637
Cdd:smart00137   81 FWYYMYGSGSGTLNVYVRENNGsqdtlLWSR----SGTQGGQWLQAEVALSSWPQpFQVVFEGTRGKGHSGYIALDDILL 156


                    ..
gi 881185998   1638 NN 1639
Cdd:smart00137  157 SN 158
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 618-779 4.99e-24

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: 100.50  E-value: 4.99e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998    618 ADCDFE-ANSCGWfEASGGDHFDWVWSSQSNLSAdleqqAPPRDHTHGTaqGHFMFILKTSNSLFQTAKLQSPTFSQTGP 696
Cdd:smart00137    4 GNCDFEeGSTCGW-HQDSNDDGHWERVSSATGIP-----GPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRS 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998    697 GCTMSFWFYNYGLSVGAaeLQLHL-ENSRD-TTALWRVLYNQGNQWSEATVQLGRLTQPFYLSLEKVSLAVYSGVSAVDD 774
Cdd:smart00137   76 THCLTFWYYMYGSGSGT--LNVYVrENNGSqDTLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRGKGHSGYIALDD 153


                    ....*
gi 881185998    775 IHFEN 779
Cdd:smart00137  154 ILLSN 158
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 443-601 1.67e-23

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: 98.99  E-value: 1.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  443 DFESGFCGWEPFPTEDSHWEVVRGLSNGEHlfLEAGHTVSRNQGSFIYFGPQKSTA--VARLGSPILTKSLTTFtpCqVR 520
Cdd:cd06263     2 DFEDGLCGWTQDSTDDFDWTRVSGSTPSPG--TPPDHTHGTGSGHYLYVESSSGREgqKARLLSPLLPPPRSSH--C-LS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  521 FWYHLS--EHSSLSVFTRTSVDGSLLKQSEVTQFSDSQWSQAKVDLHAKAEestlPFQLVLEATILSSNA-TVAVDDISI 597
Cdd:cd06263    77 FWYHMYgsGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSK----PFQVVFEGVRGSGSRgDIALDDISL 152


                  ....*
gi 881185998  598 S-HEC 601
Cdd:cd06263   153 SpGPC 157
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 1690-1855 5.48e-23

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: 97.41  E-value: 5.48e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   1690 STAGSCNFEttsgdWTVECGLTQDPEDDLDWSIGSIIPTEGLSRdSDHTPGSGrHFLYVNTSLAEEGSTARIItSHFFPA 1769
Cdd:smart00137    1 TSPGNCDFE-----EGSTCGWHQDSNDDGHWERVSSATGIPGPN-RDHTTGNG-HFMFFETSSGAEGQTARLL-SPPLYE 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   1770 SLGICTVRFWFYMVDPHiVGILKVYLIEKSGLNI-LMWSMMRNKNTGWTYAHVPLSSNS-PFKVAFEADLGGKEDIFIAL 1847
Cdd:smart00137   73 NRSTHCLTFWYYMYGSG-SGTLNVYVRENNGSQDtLLWSRSGTQGGQWLQAEVALSSWPqPFQVVFEGTRGKGHSGYIAL 151


                    ....*...
gi 881185998   1848 DDITFTPT 1855
Cdd:smart00137  152 DDILLSNG 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 443-600 2.43e-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: 95.51  E-value: 2.43e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   443 DFESG-FCGWEPFPTEDSHWEVVRGLSngEHLFLEAGHTVSRNQGSFIYFGPQKSTA--VARLGSPILTKSLTtfTPCqV 519
Cdd:pfam00629    2 DFEDGnLCGWTQDSSDDFDWERVSGPS--VKTGPSSDHTQGTGSGHFMYVDTSSGAPgqTARLLSPLLPPSRS--PQC-L 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   520 RFWYHLSEHS--SLSVFTRTSVDGSLLKQSEVTQFSDSQWSQAKVDLHAKAEestlPFQLVLEATILSSNA-TVAVDDIS 596
Cdd:pfam00629   77 RFWYHMSGSGvgTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQ----PFQVVFEGIRGGGSRgGIALDDIS 152


                   ....
gi 881185998   597 ISHE 600
Cdd:pfam00629  153 LSSG 156
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 73-226 1.94e-21

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: 92.83  E-value: 1.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   73 CNFEDRLCSMTEDQTLQPGWTRRSGII-SNSPPFWDHNGNISAHFLALVSRVDSISS--NLRSRIFLPTNDQQvCQITFY 149
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTpSPGTPPDHTHGTGSGHYLYVESSSGREGQkaRLLSPLLPPPRSSH-CLSFWY 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881185998  150 NFSSNQNGKLIAGLQTLCGDPIEHLWQKTEILQSRWERNVITVQS-SQQFQVIFQAQMLAthGQEEVIAIDDISFSSG 226
Cdd:cd06263    80 HMYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGS--GSRGDIALDDISLSPG 155
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 443-599 1.26e-18

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: 85.09  E-value: 1.26e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998    443 DFESG-FCGWEPFPTEDSHWEVVRGLSNGEHLFLeaGHTvsRNQGSFIYFGPQ--KSTAVARLGSPILTKSLTTftpCQV 519
Cdd:smart00137    7 DFEEGsTCGWHQDSNDDGHWERVSSATGIPGPNR--DHT--TGNGHFMFFETSsgAEGQTARLLSPPLYENRST---HCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998    520 RFWYHL--SEHSSLSVFTR---TSVDGSLLKQSEVTQfsdSQWSQAKVDLHAKAEestlPFQLVLEATILSSNA-TVAVD 593
Cdd:smart00137   80 TFWYYMygSGSGTLNVYVRennGSQDTLLWSRSGTQG---GQWLQAEVALSSWPQ----PFQVVFEGTRGKGHSgYIALD 152


                    ....*.
gi 881185998    594 DISISH 599
Cdd:smart00137  153 DILLSN 158
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 73-226 8.39e-18

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: 82.41  E-value: 8.39e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998    73 CNFED-RLCSMTEDQTLQPGWTRRSGIISNSPPFWDHNGNISA-HFLalvsRVDSISSN------LRSRIFlPTNDQQVC 144
Cdd:pfam00629    1 CDFEDgNLCGWTQDSSDDFDWERVSGPSVKTGPSSDHTQGTGSgHFM----YVDTSSGApgqtarLLSPLL-PPSRSPQC 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   145 qITFYNFSSNQN-GKLIAGLQTLCGDPIEHLWQKTEILQSRWERNVITVQSSQQ-FQVIFQAqmLATHGQEEVIAIDDIS 222
Cdd:pfam00629   76 -LRFWYHMSGSGvGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQpFQVVFEG--IRGGGSRGGIALDDIS 152


                   ....
gi 881185998   223 FSSG 226
Cdd:pfam00629  153 LSSG 156
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 73-226 1.39e-10

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: 61.98  E-value: 1.39e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998     73 CNFED-RLCSMTEDQTLQPGWTRRSGIISNSPPFWDH-NGNISAHFLALVSRVDSISSNLRSRIFLPTNDQQVCQITFYN 150
Cdd:smart00137    6 CDFEEgSTCGWHQDSNDDGHWERVSSATGIPGPNRDHtTGNGHFMFFETSSGAEGQTARLLSPPLYENRSTHCLTFWYYM 85

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881185998    151 FSSNQnGKLIAGLQTLCGDPIEHLWQKTEILQSRWERNVITVQSSQQ-FQVIFQAQMLAthGQEEVIAIDDISFSSG 226
Cdd:smart00137   86 YGSGS-GTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQpFQVVFEGTRGK--GHSGYIALDDILLSNG 159
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1229-1261 1.40e-09

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: 54.95  E-value: 1.40e-09
                            10        20        30
                    ....*....|....*....|....*....|...
gi 881185998   1229 KCTTDEFMCANKHCIEKDKLCDFVNDCADNSDE 1261
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1230-1261 2.72e-09

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: 54.13  E-value: 2.72e-09
                          10        20        30
                  ....*....|....*....|....*....|..
gi 881185998 1230 CTTDEFMCANKHCIEKDKLCDFVNDCADNSDE 1261
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDE 32
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1449-1483 5.27e-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: 50.67  E-value: 5.27e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 881185998 1449 CPRGYEECQNGRCYSPEQRCNFVDDCGDNSDENEC 1483
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1913-1947 7.29e-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: 7.29e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 881185998 1913 CSDTEFQCFESQCIPSLLLCDGVADCQFNEDESSC 1947
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1653-1685 1.92e-07

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: 48.74  E-value: 1.92e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 881185998 1653 ETDFLCQDKKCIASHLVCDYKPDCSDTSDEAHC 1685
Cdd:cd00112     3 PNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1913-1944 3.82e-07

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: 48.01  E-value: 3.82e-07
                            10        20        30
                    ....*....|....*....|....*....|..
gi 881185998   1913 CSDTEFQCFESQCIPSLLLCDGVADCQFNEDE 1944
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1869-1904 8.52e-07

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: 47.20  E-value: 8.52e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 881185998 1869 CEEGQFACIYaLQCVSASEKCDGQEDCIDGSDEMNC 1904
Cdd:cd00112     1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1016-1051 1.25e-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: 46.82  E-value: 1.25e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 881185998 1016 CTDDQFVCRsNGHCVGNIQKCDFRYDCIDKSDESSC 1051
Cdd:cd00112     1 CPPNEFRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1449-1480 2.21e-06

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: 45.70  E-value: 2.21e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 881185998   1449 CPRGYEECQNGRCYSPEQRCNFVDDCGDNSDE 1480
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1650-1682 7.97e-06

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: 44.16  E-value: 7.97e-06
                            10        20        30
                    ....*....|....*....|....*....|...
gi 881185998   1650 CSEETDFLCQDKKCIASHLVCDYKPDCSDTSDE 1682
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1912-1947 9.81e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 44.16  E-value: 9.81e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 881185998  1912 PCSDTEFQCFESQCIPSLLLCDGVADCQFNEDESSC 1947
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 236-384 2.08e-05

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 46.59  E-value: 2.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   236 CGF-DLDTCGLaTEASAGRTSWmctKVREIPSLDSVPWQD-QRGHDEGSFVWMRAGHA---SVSRLVESSAYLNSSVcHC 310
Cdd:pfam00629    1 CDFeDGNLCGW-TQDSSDDFDW---ERVSGPSVKTGPSSDhTQGTGSGHFMYVDTSSGapgQTARLLSPLLPPSRSP-QC 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   311 mdgncrLQFNYTMENS---ILRV--RLYNDKEEKKTWTFNTSTYSTWMKADVLIPEDLKAFKVVLEGTVLS-QKSFIGID 384
Cdd:pfam00629   76 ------LRFWYHMSGSgvgTLRVyvRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGgSRGGIALD 149
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1652-1685 2.49e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 43.01  E-value: 2.49e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 881185998  1652 EETDFLCQDKKCIASHLVCDYKPDCSDTSDEAHC 1685
Cdd:pfam00057    4 SPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 236-384 3.83e-05

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: 45.83  E-value: 3.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  236 CGFDLDTCGLaTEASAGRTSWmcTKVREIPSLDSVPWQDQRGHDEGSFVWMRA---GHASVSRLVESSAYLNSSVcHCmd 312
Cdd:cd06263     1 CDFEDGLCGW-TQDSTDDFDW--TRVSGSTPSPGTPPDHTHGTGSGHYLYVESssgREGQKARLLSPLLPPPRSS-HC-- 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881185998  313 gncrLQFNYTM---ENSILRVRLYNDKEEKKT--WTFNTSTYSTWMKADVLIPEDLKAFKVVLEGTVLS-QKSFIGID 384
Cdd:cd06263    75 ----LSFWYHMygsGVGTLNVYVREEGGGLGTllWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSgSRGDIALD 148
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1016-1048 6.07e-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: 6.07e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 881185998   1016 CTDDQFVCRsNGHCVGNIQKCDFRYDCIDKSDE 1048
Cdd:smart00192    2 CPPGEFQCD-NGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1869-1904 7.78e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 41.47  E-value: 7.78e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 881185998  1869 CEEGQFACiYALQCVSASEKCDGQEDCIDGSDEMNC 1904
Cdd:pfam00057    3 CSPNEFQC-GSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 792-825 1.24e-04

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: 41.04  E-value: 1.24e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 881185998  792 PDHFWCRQTKaCIGRHQLCDLVDDCGDYTDETGC 825
Cdd:cd00112     3 PNEFRCANGR-CIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1869-1901 2.52e-04

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: 39.92  E-value: 2.52e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 881185998   1869 CEEGQFACIYAlQCVSASEKCDGQEDCIDGSDE 1901
Cdd:smart00192    2 CPPGEFQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 38-67 3.13e-04

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: 39.88  E-value: 3.13e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 881185998   38 FQCSNGVSLPSDYVCDFTDHCGDNSEEQQC 67
Cdd:cd00112     6 FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1228-1261 6.13e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 39.15  E-value: 6.13e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 881185998  1228 RKCTTDEFMCANKHCIEKDKLCDFVNDCADNSDE 1261
Cdd:pfam00057    1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDE 34
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 36-64 1.39e-03

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: 38.00  E-value: 1.39e-03
                            10        20
                    ....*....|....*....|....*....
gi 881185998     36 QAFQCSNGVSLPSDYVCDFTDHCGDNSEE 64
Cdd:smart00192    5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1991-2021 3.33e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 36.98  E-value: 3.33e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 881185998  1991 CPIHYCRNGGTCVIENIGPTCRCVQGWTGNR 2021
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
38-67 4.18e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 36.84  E-value: 4.18e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 881185998    38 FQCSNGVSLPSDYVCDFTDHCGDNSEEQQC 67
Cdd:pfam00057    8 FQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
 
Name Accession Description Interval E-value
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 831-987 1.96e-45

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: 161.78  E-value: 1.96e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  831 CNFENGICNWEQSTKDDFNWTRYQGPTSTMNTGPmkDHTLGTAKGHYLYIETSGPQgFQDKAVLLSPILNATEAKVCtFR 910
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGR-EGQKARLLSPLLPPPRSSHC-LS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881185998  911 LYYHMFGKHIYRLAIYQRIWSNTKGQLLWQIFGDQGNRWIRKDLSI-TSRKPFQILIMASVGDGFTGDIAIDDLSFMD 987
Cdd:cd06263    77 FWYHMYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 831-988 5.61e-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: 160.22  E-value: 5.61e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   831 CNFENG-ICNWEQSTKDDFNWTRYQGPTStmNTGPMKDHTLGTAKGHYLYIETSGPQGFQdKAVLLSPILNATEAKVCtF 909
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSGPSV--KTGPSSDHTQGTGSGHFMYVDTSSGAPGQ-TARLLSPLLPPSRSPQC-L 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   910 RLYYHMFGKHIYRLAIYQRIWSNTKGQLLWQIFGDQGNRWIRKDLSITSR-KPFQILIMASVGDGFTGDIAIDDLSFM-- 986
Cdd:pfam00629   77 RFWYHMSGSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSStQPFQVVFEGIRGGGSRGGIALDDISLSsg 156


                   ..
gi 881185998   987 DC 988
Cdd:pfam00629  157 PC 158
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 1695-1855 5.78e-39

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: 143.27  E-value: 5.78e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  1695 CNFETTSgdwtvECGLTQDPEDDLDWSIGSIiPTEGLSRDSDHTPGSGR-HFLYVNTSLAEEGSTARIItSHFFPASLGI 1773
Cdd:pfam00629    1 CDFEDGN-----LCGWTQDSSDDFDWERVSG-PSVKTGPSSDHTQGTGSgHFMYVDTSSGAPGQTARLL-SPLLPPSRSP 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  1774 CTVRFWFYMVDPHiVGILKVYLIEKSG-LNILMWSMMRNKNTGWTYAHVPLSSNS-PFKVAFEADLGGKEDIFIALDDIT 1851
Cdd:pfam00629   74 QCLRFWYHMSGSG-VGTLRVYVRENGGtLDTLLWSISGDQGPSWKEARVTLSSSTqPFQVVFEGIRGGGSRGGIALDDIS 152


                   ....
gi 881185998  1852 FTPT 1855
Cdd:pfam00629  153 LSSG 156
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 826-987 3.66e-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: 140.94  E-value: 3.66e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998    826 APGLQCNFE-NGICNWEQSTKDDFNWTRYQGptSTMNTGPMKDHTLGTakGHYLYIETSGPqGFQDKAVLLSPILNATEA 904
Cdd:smart00137    1 TSPGNCDFEeGSTCGWHQDSNDDGHWERVSS--ATGIPGPNRDHTTGN--GHFMFFETSSG-AEGQTARLLSPPLYENRS 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998    905 KVCtFRLYYHMFGKHIYRLAIYQRIWSNTKGQLLWQIFGDQGNRWIRKDLSI-TSRKPFQILIMASVGDGFTGDIAIDDL 983
Cdd:smart00137   76 THC-LTFWYYMYGSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....
gi 881185998    984 SFMD 987
Cdd:smart00137  155 LLSN 158
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 620-781 1.12e-36

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: 136.72  E-value: 1.12e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   620 CDFE-ANSCGWFEASGgDHFDWVWSSQSNLSadleqQAPPRDHTHGTAQGHFMFILKTSNSLFQTAKLQSPTFSQTGPGC 698
Cdd:pfam00629    1 CDFEdGNLCGWTQDSS-DDFDWERVSGPSVK-----TGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQ 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   699 TMSFWFYNYGLSVGAAELQLHLENSRDTTALWRVLYNQGNQWSEATVQLGRLTQPFYLSLEKVSLAVYSGVSAVDDIHF- 777
Cdd:pfam00629   75 CLRFWYHMSGSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGGSRGGIALDDISLs 154


                   ....*
gi 881185998   778 -ENCA 781
Cdd:pfam00629  155 sGPCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 620-779 1.33e-35

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: 133.66  E-value: 1.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  620 CDFEANSCGWFEASGgDHFDWVWSSQSNLSADleqqaPPRDHTHGTAQGHFMFILKTSNSLFQTAKLQSPTFSQT-GPGC 698
Cdd:cd06263     1 CDFEDGLCGWTQDST-DDFDWTRVSGSTPSPG-----TPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHC 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  699 tMSFWFYNYGLSVGAAELQLHLENSRDTTALWRVLYNQGNQWSEATVQLGRLTQPFYLSLEKVSLAVYSGVSAVDDIHFE 778
Cdd:cd06263    75 -LSFWYHMYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSGSRGDIALDDISLS 153


                  .
gi 881185998  779 N 779
Cdd:cd06263   154 P 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 1487-1639 2.67e-34

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: 129.81  E-value: 2.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998 1487 CTFEKGWCGWKNSLAENSDWVLGIGSYKSQRPPKDHTLGNEHGHFMYLEATPvGLHGDKAHFKSAT-WQESSAACtMSFW 1565
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSS-GREGQKARLLSPLlPPPRSSHC-LSFW 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 881185998 1566 YFISAKATGSIQILIKTDKG-LWEVWQQSKPDPGNHWRRATILLGKLRN-FEVIFQGIRTRDLGGGAAIDDIEFNN 1639
Cdd:cd06263    79 YHMYGSGVGTLNVYVREEGGgLGTLLWSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSGSRGDIALDDISLSP 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 1273-1426 1.28e-33

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: 127.88  E-value: 1.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998 1273 CDFEFDLCTWEQDQDEDIDWNLKASNIPATSTEPavDHTLGNSSGHYIILKSFFPQQPvKTGRISSPVIS-KRSKDCkII 1351
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGREG-QKARLLSPLLPpPRSSHC-LS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881185998 1352 FNYHMYGSGIAALLLLQVTVTNHTRVLL-NLTKEQGNFWQRKELSLSS-DEDFRVKFEGRVGEGIRGNIALDDIVLT 1426
Cdd:cd06263    77 FWYHMYGSGVGTLNVYVREEGGGLGTLLwSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGSGSRGDIALDDISLS 153
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 1056-1219 3.21e-32

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: 123.64  E-value: 3.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998 1056 CTFEERkLCKWYQPipanslhDSNTFRWGLGNGISIHHGeenhrPSVDHTKNTTDGWYLYADSSNGKFGDLADIVTPVIS 1135
Cdd:cd06263     1 CDFEDG-LCGWTQD-------STDDFDWTRVSGSTPSPG-----TPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998 1136 LM-GPRCtLVFWTYMNGATVGSLQVLIK--MGNTISKVWAQSGQQGPQWKKAEVFLG-IHSHVEIVFRAKRGVSYIGDVA 1211
Cdd:cd06263    68 PPrSSHC-LSFWYHMYGSGVGTLNVYVReeGGGLGTLLWSASGGQGNQWQEAEVTLSaSSKPFQVVFEGVRGSGSRGDIA 146


                  ....*...
gi 881185998 1212 VDDVSFQN 1219
Cdd:cd06263   147 LDDISLSP 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 1695-1855 3.51e-32

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: 123.64  E-value: 3.51e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998 1695 CNFETTSgdwtveCGLTQDPEDDLDWSIG-SIIPTEGLSRDSDHTPGSGrHFLYVNTSLAEEGSTARIITSHFFPASLGI 1773
Cdd:cd06263     1 CDFEDGL------CGWTQDSTDDFDWTRVsGSTPSPGTPPDHTHGTGSG-HYLYVESSSGREGQKARLLSPLLPPPRSSH 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998 1774 CtVRFWFYMVDPHiVGILKVYLIEKSG-LNILMWSMMRNKNTGWTYAHVPLSSNS-PFKVAFEADLGGKEDIFIALDDIT 1851
Cdd:cd06263    74 C-LSFWYHMYGSG-VGTLNVYVREEGGgLGTLLWSASGGQGNQWQEAEVTLSASSkPFQVVFEGVRGSGSRGDIALDDIS 151


                  ....
gi 881185998 1852 FTPT 1855
Cdd:cd06263   152 LSPG 155
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 1487-1641 2.71e-30

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: 118.23  E-value: 2.71e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  1487 CTFEKGW-CGWKNSLAENSDWVLGIGSYKSQRPPKDHTLGNEHGHFMYLEATpVGLHGDKAHFKSATWQESSAACTMSFW 1565
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPSVKTGPSSDHTQGTGSGHFMYVDTS-SGAPGQTARLLSPLLPPSRSPQCLRFW 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881185998  1566 YFISAKATGSIQILIKTDKGLWE--VWQQSKpDPGNHWRRATILLGKLRN-FEVIFQGIRTRDLGGGAAIDDIEFNNCT 1641
Cdd:pfam00629   80 YHMSGSGVGTLRVYVRENGGTLDtlLWSISG-DQGPSWKEARVTLSSSTQpFQVVFEGIRGGGSRGGIALDDISLSSGP 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 1056-1219 2.56e-29

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: 115.54  E-value: 2.56e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  1056 CTFEERKLCKWYQPIPANslhdsntFRWGLGNGISIHHGeenhrPSVDHTKNTTDGWYLYADSSNGKFGDLADIVTPVIS 1135
Cdd:pfam00629    1 CDFEDGNLCGWTQDSSDD-------FDWERVSGPSVKTG-----PSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLP 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  1136 LMGPRCTLVFWTYMNGATVGSLQVLIKM--GNTISKVWAQSGQQGPQWKKAEVFLGIHSHV-EIVFRAKRGVSYIGDVAV 1212
Cdd:pfam00629   69 PSRSPQCLRFWYHMSGSGVGTLRVYVREngGTLDTLLWSISGDQGPSWKEARVTLSSSTQPfQVVFEGIRGGGSRGGIAL 148


                   ....*..
gi 881185998  1213 DDVSFQN 1219
Cdd:pfam00629  149 DDISLSS 155
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 1273-1426 6.30e-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: 108.60  E-value: 6.30e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  1273 CDFEFD-LCTWEQDQDEDIDWNLKASNIPATStePAVDHTLGNSSGHYIILKSFFPQqPVKTGRISSPVISKRSKDCKII 1351
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSGPSVKTG--PSSDHTQGTGSGHFMYVDTSSGA-PGQTARLLSPLLPPSRSPQCLR 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881185998  1352 FNYHMYGSGIAAL-LLLQVTVTNHTRVLLNLTKEQGNFWQRKELSLSS-DEDFRVKFEGRVGEGIRGNIALDDIVLT 1426
Cdd:pfam00629   78 FWYHMSGSGVGTLrVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLS 154
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 1056-1219 3.67e-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: 3.67e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   1056 CTFEERKLCKWYQpipanslhDSNT-FRWGLGNGisihhGEENHRPSVDHTKNttDGWYLYADSSNGKFGDLADIVTPVI 1134
Cdd:smart00137    6 CDFEEGSTCGWHQ--------DSNDdGHWERVSS-----ATGIPGPNRDHTTG--NGHFMFFETSSGAEGQTARLLSPPL 70

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   1135 SLMGPRCTLVFWTYMNGATVGSLQVLIK--MGNTISKVWAQSGQQGPQWKKAEVFLGIHSH-VEIVFRAKRGVSYIGDVA 1211
Cdd:smart00137   71 YENRSTHCLTFWYYMYGSGSGTLNVYVRenNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQpFQVVFEGTRGKGHSGYIA 150


                    ....*...
gi 881185998   1212 VDDVSFQN 1219
Cdd:smart00137  151 LDDILLSN 158
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 1268-1426 7.58e-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: 102.81  E-value: 7.58e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   1268 TSSGRCDFEFD-LCTWEQDQDEDIDWnlKASNIPATSTEPAVDHTLGNssGHYIILKSFFPQQPVKTGRISSPVISKRSK 1346
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHW--ERVSSATGIPGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   1347 DCkIIFNYHMYGSGIAAL-LLLQVTVTNHTRVLLNLTKEQGNFWQRKELSLSS-DEDFRVKFEGRVGEGIRGNIALDDIV 1424
Cdd:smart00137   77 HC-LTFWYYMYGSGSGTLnVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSSwPQPFQVVFEGTRGKGHSGYIALDDIL 155


                    ..
gi 881185998   1425 LT 1426
Cdd:smart00137  156 LS 157
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 1485-1639 4.19e-24

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: 100.88  E-value: 4.19e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   1485 GSCTFEKGW-CGWKNSLAENSDWVLGIGSYKSQRPPKDHTLGNehGHFMYLEATPvGLHGDKAHFKSATWQESSAACTMS 1563
Cdd:smart00137    4 GNCDFEEGStCGWHQDSNDDGHWERVSSATGIPGPNRDHTTGN--GHFMFFETSS-GAEGQTARLLSPPLYENRSTHCLT 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   1564 FWYFISAKATGSIQILIKTDKG-----LWEVwqqsKPDPGNHWRRATILLGKLRN-FEVIFQGIRTRDLGGGAAIDDIEF 1637
Cdd:smart00137   81 FWYYMYGSGSGTLNVYVRENNGsqdtlLWSR----SGTQGGQWLQAEVALSSWPQpFQVVFEGTRGKGHSGYIALDDILL 156


                    ..
gi 881185998   1638 NN 1639
Cdd:smart00137  157 SN 158
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 618-779 4.99e-24

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: 100.50  E-value: 4.99e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998    618 ADCDFE-ANSCGWfEASGGDHFDWVWSSQSNLSAdleqqAPPRDHTHGTaqGHFMFILKTSNSLFQTAKLQSPTFSQTGP 696
Cdd:smart00137    4 GNCDFEeGSTCGW-HQDSNDDGHWERVSSATGIP-----GPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRS 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998    697 GCTMSFWFYNYGLSVGAaeLQLHL-ENSRD-TTALWRVLYNQGNQWSEATVQLGRLTQPFYLSLEKVSLAVYSGVSAVDD 774
Cdd:smart00137   76 THCLTFWYYMYGSGSGT--LNVYVrENNGSqDTLLWSRSGTQGGQWLQAEVALSSWPQPFQVVFEGTRGKGHSGYIALDD 153


                    ....*
gi 881185998    775 IHFEN 779
Cdd:smart00137  154 ILLSN 158
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 443-601 1.67e-23

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: 98.99  E-value: 1.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  443 DFESGFCGWEPFPTEDSHWEVVRGLSNGEHlfLEAGHTVSRNQGSFIYFGPQKSTA--VARLGSPILTKSLTTFtpCqVR 520
Cdd:cd06263     2 DFEDGLCGWTQDSTDDFDWTRVSGSTPSPG--TPPDHTHGTGSGHYLYVESSSGREgqKARLLSPLLPPPRSSH--C-LS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  521 FWYHLS--EHSSLSVFTRTSVDGSLLKQSEVTQFSDSQWSQAKVDLHAKAEestlPFQLVLEATILSSNA-TVAVDDISI 597
Cdd:cd06263    77 FWYHMYgsGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSK----PFQVVFEGVRGSGSRgDIALDDISL 152


                  ....*
gi 881185998  598 S-HEC 601
Cdd:cd06263   153 SpGPC 157
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 1690-1855 5.48e-23

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: 97.41  E-value: 5.48e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   1690 STAGSCNFEttsgdWTVECGLTQDPEDDLDWSIGSIIPTEGLSRdSDHTPGSGrHFLYVNTSLAEEGSTARIItSHFFPA 1769
Cdd:smart00137    1 TSPGNCDFE-----EGSTCGWHQDSNDDGHWERVSSATGIPGPN-RDHTTGNG-HFMFFETSSGAEGQTARLL-SPPLYE 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   1770 SLGICTVRFWFYMVDPHiVGILKVYLIEKSGLNI-LMWSMMRNKNTGWTYAHVPLSSNS-PFKVAFEADLGGKEDIFIAL 1847
Cdd:smart00137   73 NRSTHCLTFWYYMYGSG-SGTLNVYVRENNGSQDtLLWSRSGTQGGQWLQAEVALSSWPqPFQVVFEGTRGKGHSGYIAL 151


                    ....*...
gi 881185998   1848 DDITFTPT 1855
Cdd:smart00137  152 DDILLSNG 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 443-600 2.43e-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: 95.51  E-value: 2.43e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   443 DFESG-FCGWEPFPTEDSHWEVVRGLSngEHLFLEAGHTVSRNQGSFIYFGPQKSTA--VARLGSPILTKSLTtfTPCqV 519
Cdd:pfam00629    2 DFEDGnLCGWTQDSSDDFDWERVSGPS--VKTGPSSDHTQGTGSGHFMYVDTSSGAPgqTARLLSPLLPPSRS--PQC-L 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   520 RFWYHLSEHS--SLSVFTRTSVDGSLLKQSEVTQFSDSQWSQAKVDLHAKAEestlPFQLVLEATILSSNA-TVAVDDIS 596
Cdd:pfam00629   77 RFWYHMSGSGvgTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQ----PFQVVFEGIRGGGSRgGIALDDIS 152


                   ....
gi 881185998   597 ISHE 600
Cdd:pfam00629  153 LSSG 156
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 73-226 1.94e-21

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: 92.83  E-value: 1.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   73 CNFEDRLCSMTEDQTLQPGWTRRSGII-SNSPPFWDHNGNISAHFLALVSRVDSISS--NLRSRIFLPTNDQQvCQITFY 149
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTpSPGTPPDHTHGTGSGHYLYVESSSGREGQkaRLLSPLLPPPRSSH-CLSFWY 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881185998  150 NFSSNQNGKLIAGLQTLCGDPIEHLWQKTEILQSRWERNVITVQS-SQQFQVIFQAQMLAthGQEEVIAIDDISFSSG 226
Cdd:cd06263    80 HMYGSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSAsSKPFQVVFEGVRGS--GSRGDIALDDISLSPG 155
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 443-599 1.26e-18

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: 85.09  E-value: 1.26e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998    443 DFESG-FCGWEPFPTEDSHWEVVRGLSNGEHLFLeaGHTvsRNQGSFIYFGPQ--KSTAVARLGSPILTKSLTTftpCQV 519
Cdd:smart00137    7 DFEEGsTCGWHQDSNDDGHWERVSSATGIPGPNR--DHT--TGNGHFMFFETSsgAEGQTARLLSPPLYENRST---HCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998    520 RFWYHL--SEHSSLSVFTR---TSVDGSLLKQSEVTQfsdSQWSQAKVDLHAKAEestlPFQLVLEATILSSNA-TVAVD 593
Cdd:smart00137   80 TFWYYMygSGSGTLNVYVRennGSQDTLLWSRSGTQG---GQWLQAEVALSSWPQ----PFQVVFEGTRGKGHSgYIALD 152


                    ....*.
gi 881185998    594 DISISH 599
Cdd:smart00137  153 DILLSN 158
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 73-226 8.39e-18

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: 82.41  E-value: 8.39e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998    73 CNFED-RLCSMTEDQTLQPGWTRRSGIISNSPPFWDHNGNISA-HFLalvsRVDSISSN------LRSRIFlPTNDQQVC 144
Cdd:pfam00629    1 CDFEDgNLCGWTQDSSDDFDWERVSGPSVKTGPSSDHTQGTGSgHFM----YVDTSSGApgqtarLLSPLL-PPSRSPQC 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   145 qITFYNFSSNQN-GKLIAGLQTLCGDPIEHLWQKTEILQSRWERNVITVQSSQQ-FQVIFQAqmLATHGQEEVIAIDDIS 222
Cdd:pfam00629   76 -LRFWYHMSGSGvGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQpFQVVFEG--IRGGGSRGGIALDDIS 152


                   ....
gi 881185998   223 FSSG 226
Cdd:pfam00629  153 LSSG 156
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 73-226 1.39e-10

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: 61.98  E-value: 1.39e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998     73 CNFED-RLCSMTEDQTLQPGWTRRSGIISNSPPFWDH-NGNISAHFLALVSRVDSISSNLRSRIFLPTNDQQVCQITFYN 150
Cdd:smart00137    6 CDFEEgSTCGWHQDSNDDGHWERVSSATGIPGPNRDHtTGNGHFMFFETSSGAEGQTARLLSPPLYENRSTHCLTFWYYM 85

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881185998    151 FSSNQnGKLIAGLQTLCGDPIEHLWQKTEILQSRWERNVITVQSSQQ-FQVIFQAQMLAthGQEEVIAIDDISFSSG 226
Cdd:smart00137   86 YGSGS-GTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSSWPQpFQVVFEGTRGK--GHSGYIALDDILLSNG 159
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1229-1261 1.40e-09

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: 54.95  E-value: 1.40e-09
                            10        20        30
                    ....*....|....*....|....*....|...
gi 881185998   1229 KCTTDEFMCANKHCIEKDKLCDFVNDCADNSDE 1261
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1230-1261 2.72e-09

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: 54.13  E-value: 2.72e-09
                          10        20        30
                  ....*....|....*....|....*....|..
gi 881185998 1230 CTTDEFMCANKHCIEKDKLCDFVNDCADNSDE 1261
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDE 32
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1449-1483 5.27e-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: 50.67  E-value: 5.27e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 881185998 1449 CPRGYEECQNGRCYSPEQRCNFVDDCGDNSDENEC 1483
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1913-1947 7.29e-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: 7.29e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 881185998 1913 CSDTEFQCFESQCIPSLLLCDGVADCQFNEDESSC 1947
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1653-1685 1.92e-07

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: 48.74  E-value: 1.92e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 881185998 1653 ETDFLCQDKKCIASHLVCDYKPDCSDTSDEAHC 1685
Cdd:cd00112     3 PNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1913-1944 3.82e-07

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: 48.01  E-value: 3.82e-07
                            10        20        30
                    ....*....|....*....|....*....|..
gi 881185998   1913 CSDTEFQCFESQCIPSLLLCDGVADCQFNEDE 1944
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1869-1904 8.52e-07

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: 47.20  E-value: 8.52e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 881185998 1869 CEEGQFACIYaLQCVSASEKCDGQEDCIDGSDEMNC 1904
Cdd:cd00112     1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1016-1051 1.25e-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: 46.82  E-value: 1.25e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 881185998 1016 CTDDQFVCRsNGHCVGNIQKCDFRYDCIDKSDESSC 1051
Cdd:cd00112     1 CPPNEFRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1449-1480 2.21e-06

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: 45.70  E-value: 2.21e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 881185998   1449 CPRGYEECQNGRCYSPEQRCNFVDDCGDNSDE 1480
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1650-1682 7.97e-06

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: 44.16  E-value: 7.97e-06
                            10        20        30
                    ....*....|....*....|....*....|...
gi 881185998   1650 CSEETDFLCQDKKCIASHLVCDYKPDCSDTSDE 1682
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1912-1947 9.81e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 44.16  E-value: 9.81e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 881185998  1912 PCSDTEFQCFESQCIPSLLLCDGVADCQFNEDESSC 1947
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 236-384 2.08e-05

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 46.59  E-value: 2.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   236 CGF-DLDTCGLaTEASAGRTSWmctKVREIPSLDSVPWQD-QRGHDEGSFVWMRAGHA---SVSRLVESSAYLNSSVcHC 310
Cdd:pfam00629    1 CDFeDGNLCGW-TQDSSDDFDW---ERVSGPSVKTGPSSDhTQGTGSGHFMYVDTSSGapgQTARLLSPLLPPSRSP-QC 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998   311 mdgncrLQFNYTMENS---ILRV--RLYNDKEEKKTWTFNTSTYSTWMKADVLIPEDLKAFKVVLEGTVLS-QKSFIGID 384
Cdd:pfam00629   76 ------LRFWYHMSGSgvgTLRVyvRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQPFQVVFEGIRGGgSRGGIALD 149
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1652-1685 2.49e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 43.01  E-value: 2.49e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 881185998  1652 EETDFLCQDKKCIASHLVCDYKPDCSDTSDEAHC 1685
Cdd:pfam00057    4 SPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 236-384 3.83e-05

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: 45.83  E-value: 3.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881185998  236 CGFDLDTCGLaTEASAGRTSWmcTKVREIPSLDSVPWQDQRGHDEGSFVWMRA---GHASVSRLVESSAYLNSSVcHCmd 312
Cdd:cd06263     1 CDFEDGLCGW-TQDSTDDFDW--TRVSGSTPSPGTPPDHTHGTGSGHYLYVESssgREGQKARLLSPLLPPPRSS-HC-- 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881185998  313 gncrLQFNYTM---ENSILRVRLYNDKEEKKT--WTFNTSTYSTWMKADVLIPEDLKAFKVVLEGTVLS-QKSFIGID 384
Cdd:cd06263    75 ----LSFWYHMygsGVGTLNVYVREEGGGLGTllWSASGGQGNQWQEAEVTLSASSKPFQVVFEGVRGSgSRGDIALD 148
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1016-1048 6.07e-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: 6.07e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 881185998   1016 CTDDQFVCRsNGHCVGNIQKCDFRYDCIDKSDE 1048
Cdd:smart00192    2 CPPGEFQCD-NGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1869-1904 7.78e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 41.47  E-value: 7.78e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 881185998  1869 CEEGQFACiYALQCVSASEKCDGQEDCIDGSDEMNC 1904
Cdd:pfam00057    3 CSPNEFQC-GSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 792-825 1.24e-04

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: 41.04  E-value: 1.24e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 881185998  792 PDHFWCRQTKaCIGRHQLCDLVDDCGDYTDETGC 825
Cdd:cd00112     3 PNEFRCANGR-CIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1869-1901 2.52e-04

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: 39.92  E-value: 2.52e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 881185998   1869 CEEGQFACIYAlQCVSASEKCDGQEDCIDGSDE 1901
Cdd:smart00192    2 CPPGEFQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 38-67 3.13e-04

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: 39.88  E-value: 3.13e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 881185998   38 FQCSNGVSLPSDYVCDFTDHCGDNSEEQQC 67
Cdd:cd00112     6 FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1228-1261 6.13e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 39.15  E-value: 6.13e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 881185998  1228 RKCTTDEFMCANKHCIEKDKLCDFVNDCADNSDE 1261
Cdd:pfam00057    1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDE 34
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 36-64 1.39e-03

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: 38.00  E-value: 1.39e-03
                            10        20
                    ....*....|....*....|....*....
gi 881185998     36 QAFQCSNGVSLPSDYVCDFTDHCGDNSEE 64
Cdd:smart00192    5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1991-2021 3.33e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 36.98  E-value: 3.33e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 881185998  1991 CPIHYCRNGGTCVIENIGPTCRCVQGWTGNR 2021
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
38-67 4.18e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 36.84  E-value: 4.18e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 881185998    38 FQCSNGVSLPSDYVCDFTDHCGDNSEEQQC 67
Cdd:pfam00057    8 FQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
 
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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