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Conserved domains on  [gi|6679489|ref|NP_032967|]
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enteropeptidase isoform 1 precursor [Mus musculus]

Protein Classification

CUB domain-containing protein; LDL receptor domain-containing protein( domain architecture ID 12018318)

CUB (complement C1r/C1s, Uegf, Bmp1) domain-containing protein| Low Density Lipoprotein (LDL) receptor class A domain is a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; similar to Bos taurus CD320 antigen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 830-1066 5.90e-97

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 306.51  E-value: 5.90e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   830 IVGGSDAQAGAWPWVVALYhrdRSTDRLLCGASLVSSDWLVSAAHCVYRRNldPTRWTAVLGLHMQSNLTSPQVVRRVvD 909
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQ---YTGGRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSNEGGGQVIKV-K 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   910 QIVINPHYDRRRKVNDIAMMHLEFKVNYTDYIQPICLPEENQIFIPGRTCSIAGWGYDKiNAGSTVDVLKEADVPLISNE 989
Cdd:cd00190   75 KVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTS-EGGPLPDVLQEVNVPIVSNA 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6679489   990 KCQQQLPE-YNITESMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLVGVTSFGVQCALPNHPGVYVRVSQFIEWIHS 1066
Cdd:cd00190  154 ECKRAYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 392-548 1.25e-44

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: 158.68  E-value: 1.25e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     392 CTFDDG-FCFWTQDLDDDNEWERiqVTTFPCYTGPRFDHTYGNGSGFYISTPTEQGWRSERVGLSSLSLDLTSEPVCLHF 470
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWER--VSGPSVKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     471 WYYMCCENVYNLNIHI-SSAETTDKIVFQRKGNYGRNWNYGQVTLNE-TGEFKVVFNAFRNRG-CSTIALDDISLTNGIC 547
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVrENGGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGsRGGIALDDISLSSGPC 158


                   .
gi 6679489     548 S 548
Cdd:pfam00629  159 P 159
CUB pfam00431
CUB domain;
569-676 1.74e-34

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 127.41  E-value: 1.74e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     569 CGGpfELWEPNSTFSSPNFPDKYPNQASCIWNLNAQRGKNIQLHFQEFDLE----NINDVVEVRDGGEFDSLLLAVYTGP 644
Cdd:pfam00431    1 CGG--VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 6679489     645 GPVKDLFSTTNRMTVIFTTNMETRRKGFKANF 676
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 53-154 1.26e-19

Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains.


:

Pssm-ID: 214554  Cd Length: 121  Bit Score: 85.54  E-value: 1.26e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489       53 GKSHEVRGTFKITSG--VTYNPNLQDKHSVDFKVLAFDLQQMIDEIFESSSLKNEYEKSKVFQFEKGSVIVLFDLFFAQW 130
Cdd:smart00200    2 TQSFGVSLSVLSVEGenLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNEG 81

                            90       100
                    ....*....|....*....|....*
gi 6679489      131 V-SDKNVKEELIQGIEANISSQLVT 154
Cdd:smart00200   82 VtNGQDVEEDLLQVIKQAAYSLKIT 106
CUB super family cl00049
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 270-376 1.28e-17

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


The actual alignment was detected with superfamily member pfam00431:

Pssm-ID: 412131 [Multi-domain]  Cd Length: 110  Bit Score: 79.26  E-value: 1.28e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     270 CDGRFllTGDSGVFQADRYPRPDESGVVCRWIIRVNQGLSIRMNFGSF-----IPHYTDVLDIYEGIGPSKILRGSFW-E 343
Cdd:pfam00431    1 CGGVL--TDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFeledhDECGYDYVEIRDGPSASSPLLGRFCgS 78

                           90       100       110
                   ....*....|....*....|....*....|...
gi 6679489     344 TDPGTIRIFSNLVTVTFLIkSDEYDYIGFNATY 376
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVS-DASVQKRGFKATY 110
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 688-722 3.01e-11

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: 58.76  E-value: 3.01e-11
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 6679489   688 CQDDEFQCKDGNCIPLGNLCDSYPHCRDGSDEASC 722
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 723-816 9.30e-10

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


:

Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 56.58  E-value: 9.30e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489      723 VRFLNGTRSNNGLVQFNIHSIWHIACAENWTTQISNEVCHLLGLGSAN--SSMPISSTGGGPFVRVNQAPNGSLiltPSL 800
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVsaSGSAYFGPGSGPIWLDNVRCSGTE---ASL 77

                            90
                    ....*....|....*..
gi 6679489      801 -QCSQDSLILLQCNHKS 816
Cdd:smart00202   78 sDCPHSGWGSHNCSHGE 94
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 228-261 1.58e-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: 1.58e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 6679489      228 ECQPGSRPCAHAwNCVATDLFCDGEVNCPDGSDE 261
Cdd:smart00192    1 TCPPGEFQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 830-1066 5.90e-97

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 306.51  E-value: 5.90e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   830 IVGGSDAQAGAWPWVVALYhrdRSTDRLLCGASLVSSDWLVSAAHCVYRRNldPTRWTAVLGLHMQSNLTSPQVVRRVvD 909
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQ---YTGGRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSNEGGGQVIKV-K 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   910 QIVINPHYDRRRKVNDIAMMHLEFKVNYTDYIQPICLPEENQIFIPGRTCSIAGWGYDKiNAGSTVDVLKEADVPLISNE 989
Cdd:cd00190   75 KVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTS-EGGPLPDVLQEVNVPIVSNA 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6679489   990 KCQQQLPE-YNITESMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLVGVTSFGVQCALPNHPGVYVRVSQFIEWIHS 1066
Cdd:cd00190  154 ECKRAYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 829-1064 9.83e-96

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 303.06  E-value: 9.83e-96
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489      829 KIVGGSDAQAGAWPWVVALYHRDRstdRLLCGASLVSSDWLVSAAHCVYRRnlDPTRWTAVLGLHMQSNLTSPQVVRrvV 908
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGG---RHFCGGSLISPRWVLTAAHCVRGS--DPSNIRVRLGSHDLSSGEEGQVIK--V 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489      909 DQIVINPHYDRRRKVNDIAMMHLEFKVNYTDYIQPICLPEENQIFIPGRTCSIAGWGYDKINAGSTVDVLKEADVPLISN 988
Cdd:smart00020   74 SKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSN 153

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679489      989 EKCQQQLPEYN-ITESMICAGYEEGGIDSCQGDSGGPLMCQeNNRWFLVGVTSFGVQCALPNHPGVYVRVSQFIEWI 1064
Cdd:smart00020  154 ATCRRAYSGGGaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 826-1066 7.09e-72

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 239.55  E-value: 7.09e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   826 VSPKIVGGSDAQAGAWPWVVALYHRDrSTDRLLCGASLVSSDWLVSAAHCVYrrNLDPTRWTAVLGLHmqsNLTSPQVVR 905
Cdd:COG5640   27 AAPAIVGGTPATVGEYPWMVALQSSN-GPSGQFCGGTLIAPRWVLTAAHCVD--GDGPSDLRVVIGST---DLSTSGGTV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   906 RVVDQIVINPHYDRRRKVNDIAMMHLEFKVnytDYIQPICLPEENQIFIPGRTCSIAGWGYDKINAGSTVDVLKEADVPL 985
Cdd:COG5640  101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPV 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   986 ISNEKCQQqlPEYNITESMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLVGVTSFGVQCALPNHPGVYVRVSQFIEWIH 1065
Cdd:COG5640  178 VSDATCAA--YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIK 255


                 .
gi 6679489  1066 S 1066
Cdd:COG5640  256 S 256
Trypsin pfam00089
Trypsin;
830-1064 6.48e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 235.41  E-value: 6.48e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     830 IVGGSDAQAGAWPWVVALYhrdRSTDRLLCGASLVSSDWLVSAAHCVYrrnlDPTRWTAVLGLHmQSNLTSPQVVRRVVD 909
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQ---LSSGKHFCGGSLISENWVLTAAHCVS----GASDVKVVLGAH-NIVLREGGEQKFDVE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     910 QIVINPHYDRRRKVNDIAMMHLEFKVNYTDYIQPICLPEENQIFIPGRTCSIAGWGYDKinAGSTVDVLKEADVPLISNE 989
Cdd:pfam00089   73 KIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTK--TLGPSDTLQEVTVPVVSRE 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6679489     990 KCQQQLPEYnITESMICAGYeeGGIDSCQGDSGGPLMCQENnrwFLVGVTSFGVQCALPNHPGVYVRVSQFIEWI 1064
Cdd:pfam00089  151 TCRSAYGGT-VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 392-548 1.25e-44

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: 158.68  E-value: 1.25e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     392 CTFDDG-FCFWTQDLDDDNEWERiqVTTFPCYTGPRFDHTYGNGSGFYISTPTEQGWRSERVGLSSLSLDLTSEPVCLHF 470
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWER--VSGPSVKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     471 WYYMCCENVYNLNIHI-SSAETTDKIVFQRKGNYGRNWNYGQVTLNE-TGEFKVVFNAFRNRG-CSTIALDDISLTNGIC 547
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVrENGGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGsRGGIALDDISLSSGPC 158


                   .
gi 6679489     548 S 548
Cdd:pfam00629  159 P 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 387-547 1.26e-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: 141.33  E-value: 1.26e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489      387 YEKIDCTFDDG-FCFWTQDLDDDNEWERIQVTTFpcYTGPRFDHTygNGSGFYISTPTEQGWRSERVGLSSLSLDLTSEP 465
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSATG--IPGPNRDHT--TGNGHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489      466 VCLHFWYYMCCENVYNLNIHI-SSAETTDKIVFQRKGNYGRNWNYGQVTLN-ETGEFKVVFNAFRNRG-CSTIALDDISL 542
Cdd:smart00137   77 HCLTFWYYMYGSGSGTLNVYVrENNGSQDTLLWSRSGTQGGQWLQAEVALSsWPQPFQVVFEGTRGKGhSGYIALDDILL 156


                    ....*
gi 6679489      543 TNGIC 547
Cdd:smart00137  157 SNGPC 161
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 392-547 1.42e-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: 132.50  E-value: 1.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   392 CTFDDGFCFWTQDLDDDNEWERIQVTTFPCYTGPrfDHTYGNGSGFYISTPTEQGWRSERVGLSSLSLDLTSEPVCLHFW 471
Cdd:cd06263    1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSSHCLSFW 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6679489   472 YYMCCENVYNLNIHI-SSAETTDKIVFQRKGNYGRNWNYGQVTLNET-GEFKVVFNAFRNRG-CSTIALDDISLTNGIC 547
Cdd:cd06263   79 YHMYGSGVGTLNVYVrEEGGGLGTLLWSASGGQGNQWQEAEVTLSASsKPFQVVFEGVRGSGsRGDIALDDISLSPGPC 157
CUB pfam00431
CUB domain;
569-676 1.74e-34

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 127.41  E-value: 1.74e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     569 CGGpfELWEPNSTFSSPNFPDKYPNQASCIWNLNAQRGKNIQLHFQEFDLE----NINDVVEVRDGGEFDSLLLAVYTGP 644
Cdd:pfam00431    1 CGG--VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 6679489     645 GPVKDLFSTTNRMTVIFTTNMETRRKGFKANF 676
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 569-678 4.37e-29

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 112.12  E-value: 4.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   569 CGGPFeLWEPNSTFSSPNFPDKYPNQASCIWNLNAQRGKNIQLHFQEFDLEN----INDVVEVRDGGEFDSLLLAVYTGP 644
Cdd:cd00041    1 CGGTL-TASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLLGRFCGS 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 6679489   645 GPVKDLFSTTNRMTVIFTTNMETRRKGFKANFTS 678
Cdd:cd00041   80 TLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 581-676 5.69e-25

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 100.16  E-value: 5.69e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489      581 TFSSPNFPDKYPNQASCIWNLNAQRGKNIQLHFQEFDLENIN----DVVEVRDGGEFDSLLLAVYTGPGPVKDLFST-TN 655
Cdd:smart00042    2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDnceyDYVEIYDGPSASSPLLGRFCGSEAPPPVISSsSN 81

                            90       100
                    ....*....|....*....|.
gi 6679489      656 RMTVIFTTNMETRRKGFKANF 676
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 53-154 1.26e-19

Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains.


Pssm-ID: 214554  Cd Length: 121  Bit Score: 85.54  E-value: 1.26e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489       53 GKSHEVRGTFKITSG--VTYNPNLQDKHSVDFKVLAFDLQQMIDEIFESSSLKNEYEKSKVFQFEKGSVIVLFDLFFAQW 130
Cdd:smart00200    2 TQSFGVSLSVLSVEGenLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNEG 81

                            90       100
                    ....*....|....*....|....*
gi 6679489      131 V-SDKNVKEELIQGIEANISSQLVT 154
Cdd:smart00200   82 VtNGQDVEEDLLQVIKQAAYSLKIT 106
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 56-144 2.56e-18

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


Pssm-ID: 460188  Cd Length: 100  Bit Score: 81.13  E-value: 2.56e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489      56 HEVRGTFKITSgVTYNPNLQDKHSVDFKVLAFDLQQMIDEIFESSSLKNEYEKSKVFQFEK--GSVIVLFDLFFAQWVSD 133
Cdd:pfam01390    1 QYYTGSFKITN-LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPdgGSVVVDVVLVFRFPSTE 79

                           90
                   ....*....|..
gi 6679489     134 -KNVKEELIQGI 144
Cdd:pfam01390   80 pALDREKLIEEI 91
CUB pfam00431
CUB domain;
270-376 1.28e-17

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 79.26  E-value: 1.28e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     270 CDGRFllTGDSGVFQADRYPRPDESGVVCRWIIRVNQGLSIRMNFGSF-----IPHYTDVLDIYEGIGPSKILRGSFW-E 343
Cdd:pfam00431    1 CGGVL--TDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFeledhDECGYDYVEIRDGPSASSPLLGRFCgS 78

                           90       100       110
                   ....*....|....*....|....*....|...
gi 6679489     344 TDPGTIRIFSNLVTVTFLIkSDEYDYIGFNATY 376
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVS-DASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 270-378 1.10e-14

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 71.29  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   270 CDGRFLLTgDSGVFQADRYPRPDESGVVCRWIIRVNQGLSIRMNFGSF-----IPHYTDVLDIYEGIGPSKILRGSFW-E 343
Cdd:cd00041    1 CGGTLTAS-TSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFdlessPNCSYDYLEIYDGPSTSSPLLGRFCgS 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 6679489   344 TDPGTIRIFSNLVTVTFliKSDEYD-YIGFNATYST 378
Cdd:cd00041   80 TLPPPIISSGNSLTVRF--RSDSSVtGRGFKATYSA 113
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 688-722 3.01e-11

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: 58.76  E-value: 3.01e-11
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 6679489   688 CQDDEFQCKDGNCIPLGNLCDSYPHCRDGSDEASC 722
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 281-376 1.71e-10

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 58.94  E-value: 1.71e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489      281 GVFQADRYPRPDESGVVCRWIIRVNQGLSIRMNFGSF-----IPHYTDVLDIYEGIGPSKILRGSF--WETDPGTIRIFS 353
Cdd:smart00042    1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFdlessDNCEYDYVEIYDGPSASSPLLGRFcgSEAPPPVISSSS 80

                            90       100
                    ....*....|....*....|....
gi 6679489      354 NLVTVTFliKSDEYD-YIGFNATY 376
Cdd:smart00042   81 NSLTLTF--VSDSSVqKRGFSARY 102
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 688-719 4.66e-10

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: 55.33  E-value: 4.66e-10
                            10        20        30
                    ....*....|....*....|....*....|..
gi 6679489      688 CQDDEFQCKDGNCIPLGNLCDSYPHCRDGSDE 719
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 723-816 9.30e-10

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 56.58  E-value: 9.30e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489      723 VRFLNGTRSNNGLVQFNIHSIWHIACAENWTTQISNEVCHLLGLGSAN--SSMPISSTGGGPFVRVNQAPNGSLiltPSL 800
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVsaSGSAYFGPGSGPIWLDNVRCSGTE---ASL 77

                            90
                    ....*....|....*..
gi 6679489      801 -QCSQDSLILLQCNHKS 816
Cdd:smart00202   78 sDCPHSGWGSHNCSHGE 94
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
687-722 5.91e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 52.25  E-value: 5.91e-09
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 6679489     687 PCQDDEFQCKDGNCIPLGNLCDSYPHCRDGSDEASC 722
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 728-819 1.39e-04

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 41.98  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     728 GTRSNNGLVQFNIHSIWHIACAENWTTQISNEVCHLLGLGSAnSSMPISSTGGGPfvrvnqaPNGSLILTPSLQCSQDSL 807
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGA-VSAPSGCSYFGP-------GSTGPIWLDDVRCSGNET 72

                           90
                   ....*....|..
gi 6679489     808 ILLQCNHKSCGE 819
Cdd:pfam00530   73 SLWQCPHRPWGN 84
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 228-261 1.58e-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: 1.58e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 6679489      228 ECQPGSRPCAHAwNCVATDLFCDGEVNCPDGSDE 261
Cdd:smart00192    1 TCPPGEFQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 229-262 1.68e-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: 1.68e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 6679489   229 CQPGSRPCAHaWNCVATDLFCDGEVNCPDGSDED 262
Cdd:cd00112    1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEE 33
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 830-1066 5.90e-97

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 306.51  E-value: 5.90e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   830 IVGGSDAQAGAWPWVVALYhrdRSTDRLLCGASLVSSDWLVSAAHCVYRRNldPTRWTAVLGLHMQSNLTSPQVVRRVvD 909
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQ---YTGGRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSNEGGGQVIKV-K 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   910 QIVINPHYDRRRKVNDIAMMHLEFKVNYTDYIQPICLPEENQIFIPGRTCSIAGWGYDKiNAGSTVDVLKEADVPLISNE 989
Cdd:cd00190   75 KVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTS-EGGPLPDVLQEVNVPIVSNA 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6679489   990 KCQQQLPE-YNITESMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLVGVTSFGVQCALPNHPGVYVRVSQFIEWIHS 1066
Cdd:cd00190  154 ECKRAYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 829-1064 9.83e-96

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 303.06  E-value: 9.83e-96
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489      829 KIVGGSDAQAGAWPWVVALYHRDRstdRLLCGASLVSSDWLVSAAHCVYRRnlDPTRWTAVLGLHMQSNLTSPQVVRrvV 908
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGG---RHFCGGSLISPRWVLTAAHCVRGS--DPSNIRVRLGSHDLSSGEEGQVIK--V 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489      909 DQIVINPHYDRRRKVNDIAMMHLEFKVNYTDYIQPICLPEENQIFIPGRTCSIAGWGYDKINAGSTVDVLKEADVPLISN 988
Cdd:smart00020   74 SKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSN 153

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679489      989 EKCQQQLPEYN-ITESMICAGYEEGGIDSCQGDSGGPLMCQeNNRWFLVGVTSFGVQCALPNHPGVYVRVSQFIEWI 1064
Cdd:smart00020  154 ATCRRAYSGGGaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 826-1066 7.09e-72

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 239.55  E-value: 7.09e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   826 VSPKIVGGSDAQAGAWPWVVALYHRDrSTDRLLCGASLVSSDWLVSAAHCVYrrNLDPTRWTAVLGLHmqsNLTSPQVVR 905
Cdd:COG5640   27 AAPAIVGGTPATVGEYPWMVALQSSN-GPSGQFCGGTLIAPRWVLTAAHCVD--GDGPSDLRVVIGST---DLSTSGGTV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   906 RVVDQIVINPHYDRRRKVNDIAMMHLEFKVnytDYIQPICLPEENQIFIPGRTCSIAGWGYDKINAGSTVDVLKEADVPL 985
Cdd:COG5640  101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPV 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   986 ISNEKCQQqlPEYNITESMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLVGVTSFGVQCALPNHPGVYVRVSQFIEWIH 1065
Cdd:COG5640  178 VSDATCAA--YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIK 255


                 .
gi 6679489  1066 S 1066
Cdd:COG5640  256 S 256
Trypsin pfam00089
Trypsin;
830-1064 6.48e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 235.41  E-value: 6.48e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     830 IVGGSDAQAGAWPWVVALYhrdRSTDRLLCGASLVSSDWLVSAAHCVYrrnlDPTRWTAVLGLHmQSNLTSPQVVRRVVD 909
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQ---LSSGKHFCGGSLISENWVLTAAHCVS----GASDVKVVLGAH-NIVLREGGEQKFDVE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     910 QIVINPHYDRRRKVNDIAMMHLEFKVNYTDYIQPICLPEENQIFIPGRTCSIAGWGYDKinAGSTVDVLKEADVPLISNE 989
Cdd:pfam00089   73 KIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTK--TLGPSDTLQEVTVPVVSRE 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6679489     990 KCQQQLPEYnITESMICAGYeeGGIDSCQGDSGGPLMCQENnrwFLVGVTSFGVQCALPNHPGVYVRVSQFIEWI 1064
Cdd:pfam00089  151 TCRSAYGGT-VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 392-548 1.25e-44

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: 158.68  E-value: 1.25e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     392 CTFDDG-FCFWTQDLDDDNEWERiqVTTFPCYTGPRFDHTYGNGSGFYISTPTEQGWRSERVGLSSLSLDLTSEPVCLHF 470
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWER--VSGPSVKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     471 WYYMCCENVYNLNIHI-SSAETTDKIVFQRKGNYGRNWNYGQVTLNE-TGEFKVVFNAFRNRG-CSTIALDDISLTNGIC 547
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVrENGGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGGsRGGIALDDISLSSGPC 158


                   .
gi 6679489     548 S 548
Cdd:pfam00629  159 P 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 387-547 1.26e-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: 141.33  E-value: 1.26e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489      387 YEKIDCTFDDG-FCFWTQDLDDDNEWERIQVTTFpcYTGPRFDHTygNGSGFYISTPTEQGWRSERVGLSSLSLDLTSEP 465
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSATG--IPGPNRDHT--TGNGHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489      466 VCLHFWYYMCCENVYNLNIHI-SSAETTDKIVFQRKGNYGRNWNYGQVTLN-ETGEFKVVFNAFRNRG-CSTIALDDISL 542
Cdd:smart00137   77 HCLTFWYYMYGSGSGTLNVYVrENNGSQDTLLWSRSGTQGGQWLQAEVALSsWPQPFQVVFEGTRGKGhSGYIALDDILL 156


                    ....*
gi 6679489      543 TNGIC 547
Cdd:smart00137  157 SNGPC 161
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 392-547 1.42e-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: 132.50  E-value: 1.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   392 CTFDDGFCFWTQDLDDDNEWERIQVTTFPCYTGPrfDHTYGNGSGFYISTPTEQGWRSERVGLSSLSLDLTSEPVCLHFW 471
Cdd:cd06263    1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSSHCLSFW 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6679489   472 YYMCCENVYNLNIHI-SSAETTDKIVFQRKGNYGRNWNYGQVTLNET-GEFKVVFNAFRNRG-CSTIALDDISLTNGIC 547
Cdd:cd06263   79 YHMYGSGVGTLNVYVrEEGGGLGTLLWSASGGQGNQWQEAEVTLSASsKPFQVVFEGVRGSGsRGDIALDDISLSPGPC 157
CUB pfam00431
CUB domain;
569-676 1.74e-34

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 127.41  E-value: 1.74e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     569 CGGpfELWEPNSTFSSPNFPDKYPNQASCIWNLNAQRGKNIQLHFQEFDLE----NINDVVEVRDGGEFDSLLLAVYTGP 644
Cdd:pfam00431    1 CGG--VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 6679489     645 GPVKDLFSTTNRMTVIFTTNMETRRKGFKANF 676
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 569-678 4.37e-29

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 112.12  E-value: 4.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   569 CGGPFeLWEPNSTFSSPNFPDKYPNQASCIWNLNAQRGKNIQLHFQEFDLEN----INDVVEVRDGGEFDSLLLAVYTGP 644
Cdd:cd00041    1 CGGTL-TASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLLGRFCGS 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 6679489   645 GPVKDLFSTTNRMTVIFTTNMETRRKGFKANFTS 678
Cdd:cd00041   80 TLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 581-676 5.69e-25

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 100.16  E-value: 5.69e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489      581 TFSSPNFPDKYPNQASCIWNLNAQRGKNIQLHFQEFDLENIN----DVVEVRDGGEFDSLLLAVYTGPGPVKDLFST-TN 655
Cdd:smart00042    2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDnceyDYVEIYDGPSASSPLLGRFCGSEAPPPVISSsSN 81

                            90       100
                    ....*....|....*....|.
gi 6679489      656 RMTVIFTTNMETRRKGFKANF 676
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 53-154 1.26e-19

Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains.


Pssm-ID: 214554  Cd Length: 121  Bit Score: 85.54  E-value: 1.26e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489       53 GKSHEVRGTFKITSG--VTYNPNLQDKHSVDFKVLAFDLQQMIDEIFESSSLKNEYEKSKVFQFEKGSVIVLFDLFFAQW 130
Cdd:smart00200    2 TQSFGVSLSVLSVEGenLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNEG 81

                            90       100
                    ....*....|....*....|....*
gi 6679489      131 V-SDKNVKEELIQGIEANISSQLVT 154
Cdd:smart00200   82 VtNGQDVEEDLLQVIKQAAYSLKIT 106
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 56-144 2.56e-18

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


Pssm-ID: 460188  Cd Length: 100  Bit Score: 81.13  E-value: 2.56e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489      56 HEVRGTFKITSgVTYNPNLQDKHSVDFKVLAFDLQQMIDEIFESSSLKNEYEKSKVFQFEK--GSVIVLFDLFFAQWVSD 133
Cdd:pfam01390    1 QYYTGSFKITN-LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPdgGSVVVDVVLVFRFPSTE 79

                           90
                   ....*....|..
gi 6679489     134 -KNVKEELIQGI 144
Cdd:pfam01390   80 pALDREKLIEEI 91
CUB pfam00431
CUB domain;
270-376 1.28e-17

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 79.26  E-value: 1.28e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     270 CDGRFllTGDSGVFQADRYPRPDESGVVCRWIIRVNQGLSIRMNFGSF-----IPHYTDVLDIYEGIGPSKILRGSFW-E 343
Cdd:pfam00431    1 CGGVL--TDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFeledhDECGYDYVEIRDGPSASSPLLGRFCgS 78

                           90       100       110
                   ....*....|....*....|....*....|...
gi 6679489     344 TDPGTIRIFSNLVTVTFLIkSDEYDYIGFNATY 376
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVS-DASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 270-378 1.10e-14

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 71.29  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   270 CDGRFLLTgDSGVFQADRYPRPDESGVVCRWIIRVNQGLSIRMNFGSF-----IPHYTDVLDIYEGIGPSKILRGSFW-E 343
Cdd:cd00041    1 CGGTLTAS-TSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFdlessPNCSYDYLEIYDGPSTSSPLLGRFCgS 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 6679489   344 TDPGTIRIFSNLVTVTFliKSDEYD-YIGFNATYST 378
Cdd:cd00041   80 TLPPPIISSGNSLTVRF--RSDSSVtGRGFKATYSA 113
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 688-722 3.01e-11

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: 58.76  E-value: 3.01e-11
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 6679489   688 CQDDEFQCKDGNCIPLGNLCDSYPHCRDGSDEASC 722
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 281-376 1.71e-10

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 58.94  E-value: 1.71e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489      281 GVFQADRYPRPDESGVVCRWIIRVNQGLSIRMNFGSF-----IPHYTDVLDIYEGIGPSKILRGSF--WETDPGTIRIFS 353
Cdd:smart00042    1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFdlessDNCEYDYVEIYDGPSASSPLLGRFcgSEAPPPVISSSS 80

                            90       100
                    ....*....|....*....|....
gi 6679489      354 NLVTVTFliKSDEYD-YIGFNATY 376
Cdd:smart00042   81 NSLTLTF--VSDSSVqKRGFSARY 102
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 688-719 4.66e-10

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: 55.33  E-value: 4.66e-10
                            10        20        30
                    ....*....|....*....|....*....|..
gi 6679489      688 CQDDEFQCKDGNCIPLGNLCDSYPHCRDGSDE 719
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 723-816 9.30e-10

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 56.58  E-value: 9.30e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489      723 VRFLNGTRSNNGLVQFNIHSIWHIACAENWTTQISNEVCHLLGLGSAN--SSMPISSTGGGPFVRVNQAPNGSLiltPSL 800
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVsaSGSAYFGPGSGPIWLDNVRCSGTE---ASL 77

                            90
                    ....*....|....*..
gi 6679489      801 -QCSQDSLILLQCNHKS 816
Cdd:smart00202   78 sDCPHSGWGSHNCSHGE 94
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
687-722 5.91e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 52.25  E-value: 5.91e-09
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 6679489     687 PCQDDEFQCKDGNCIPLGNLCDSYPHCRDGSDEASC 722
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 858-1068 2.21e-08

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 55.45  E-value: 2.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   858 LCGASLVSSDWLVSAAHCVYRRNLD--PTRWTAVLGLHMQSNLTSpQVVRRVVDQIVINPHYDRrrkvNDIAMMHL-EFK 934
Cdd:COG3591   13 VCTGTLIGPNLVLTAGHCVYDGAGGgwATNIVFVPGYNGGPYGTA-TATRFRVPPGWVASGDAG----YDYALLRLdEPL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489   935 VNYTDYIQPIClpeeNQIFIPGRTCSIAGWGYDKINAGStvdvlkeadvplisnekCQQQLPEYNITESMIcaGYeegGI 1014
Cdd:COG3591   88 GDTTGWLGLAF----NDAPLAGEPVTIIGYPGDRPKDLS-----------------LDCSGRVTGVQGNRL--SY---DC 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6679489  1015 DSCQGDSGGPLMCQENNRWFLVGVTSFGVqCALPNHpGVYVRvSQFIEWIHSFL 1068
Cdd:COG3591  142 DTTGGSSGSPVLDDSDGGGRVVGVHSAGG-ADRANT-GVRLT-SAIVAALRAWA 192
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 728-819 1.39e-04

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 41.98  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     728 GTRSNNGLVQFNIHSIWHIACAENWTTQISNEVCHLLGLGSAnSSMPISSTGGGPfvrvnqaPNGSLILTPSLQCSQDSL 807
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGA-VSAPSGCSYFGP-------GSTGPIWLDDVRCSGNET 72

                           90
                   ....*....|..
gi 6679489     808 ILLQCNHKSCGE 819
Cdd:pfam00530   73 SLWQCPHRPWGN 84
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 228-261 1.58e-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: 1.58e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 6679489      228 ECQPGSRPCAHAwNCVATDLFCDGEVNCPDGSDE 261
Cdd:smart00192    1 TCPPGEFQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 229-262 1.68e-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: 1.68e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 6679489   229 CQPGSRPCAHaWNCVATDLFCDGEVNCPDGSDED 262
Cdd:cd00112    1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEE 33
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
 736-819 4.86e-04

Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain family found largely on vertebrate sequences up-stream of the trypsin-like transmembrane serine protease, Spinesin.


Pssm-ID: 464747  Cd Length: 99  Bit Score: 40.39  E-value: 4.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679489     736 VQFNIHSIWHIACAENWTTQISNEVCHLLGLGSA--NSSMPISSTGGGP---FVRVN-QAPNGSL--ILTPSLQCSQDSL 807
Cdd:pfam15494    8 VYSSARPSWLPVCSDDWNPAYGRAACQQLGYLRLthHKSVNLTDISSNSsqsFMKLNsSSLNTDLyeALQPRDSCSSGSV 87

                           90
                   ....*....|..
gi 6679489     808 ILLQCNHksCGE 819
Cdd:pfam15494   88 VSLRCSE--CGL 97
 
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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