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Conserved domains on  [gi|27806097|ref|NP_776864|]
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enteropeptidase precursor [Bos taurus]

Protein Classification

MAM and Tryp_SPc domain-containing protein( domain architecture ID 12193321)

protein containing domains SEA, MAM, CUB, and Tryp_SPc

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 ...
 801-1032 2.26e-99

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: 312.29  E-value: 2.26e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  801 IVGGSDSREGAWPWVVALYFDD-QQVCGASLVSRDWLVSAAHCVYGRNmePSKWKAVLGLHMASNLTSPQiETRLIDQIV 879
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSNEGGG-QVIKVKKVI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  880 INPHYNKRRKNNDIAMMHLEMKVNYTDYIQPICLPEENQVFPPGRICSIAGWGALIYQGSTADVLQEADVPLLSNEKCQQ 959
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27806097  960 QMPE-YNITENMVCAGYEAGGVDSCQGDSGGPLMCQENNRWLLAGVTSFGYQCALPNRPGVYARVPRFTEWIQS 1032
Cdd:cd00190  158 AYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 358-518 8.64e-52

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 179.08  E-value: 8.64e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     358 YEKINCNFEDG-FCFWIQDLNDDNEWERTQGSTFPpsTGPTFDHTFGNesGFYISTPTGPGGRRERVGLLTLPLDPTPEQ 436
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSATGI--PGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     437 ACLSFWYYMYGENVYKLSINISSDQNME-KTIFQKEGNYGQNWNYGQVTLN-ETVEFKVSFYGFKNQ-ILSDIALDDISL 513
Cdd:smart00137   77 HCLTFWYYMYGSGSGTLNVYVRENNGSQdTLLWSRSGTQGGQWLQAEVALSsWPQPFQVVFEGTRGKgHSGYIALDDILL 156


                    ....*
gi 27806097     514 TYGIC 518
Cdd:smart00137  157 SNGPC 161
CUB pfam00431
CUB domain;
540-647 2.00e-34

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 127.41  E-value: 2.00e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097    540 CGGphDLWEPNTTFTSINFPNSYPNQAFCIWNLNAQKGKNIQLHFQEFDLE----NIADVVEIRDGEGDDSLFLAVYTGP 615
Cdd:pfam00431    1 CGG--VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 27806097    616 GPVNDVFSTTNRMTVLFITDNMLAKQGFKANF 647
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 69-154 1.32e-22

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: 94.02  E-value: 1.32e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097      69 TYNPHLQDKLSVDFKVLAFDIQQMIDDIFQSSNLKNEYKNSRVLQFENGSIIVIFDLLFDQWV-SDKNVKEELIQGIEAN 147
Cdd:smart00200   20 QYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNEGVtNGQDVEEDLLQVIKQA 99


                    ....*..
gi 27806097     148 KSSQLVT 154
Cdd:smart00200  100 AYSLKIT 106
CUB super family cl00049
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 240-347 1.51e-22

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: 93.51  E-value: 1.51e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097    240 CDGRFllTGSSGSFEALHYPKPSNNtSAVCRWIIRVNQGLSIQLNFDYFNTYYA-----DVLNIYEGMGSSKILRASLW- 313
Cdd:pfam00431    1 CGGVL--TDSSGSISSPNYPNPYPP-NKDCVWLIRAPPGFRVKLTFQDFELEDHdecgyDYVEIRDGPSASSPLLGRFCg 77

                           90       100       110
                   ....*....|....*....|....*....|....
gi 27806097    314 SNNPGIIRIFSNQVTATFLIqSDESDYIGFKVTY 347
Cdd:pfam00431   78 SGIPEDIVSSSNQMTIKFVS-DASVQKRGFKATY 110
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 694-784 6.32e-15

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: 71.60  E-value: 6.32e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     694 VRLFNGTTDSSGLVQFRIQSIWHVACAENWTTQISDDVCQLLGLGTGNSSVP--TFSTGGGPYVNLNTAPNG---SLILT 768
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsaYFGPGSGPIWLDNVRCSGteaSLSDC 80

                            90       100
                    ....*....|....*....|.
gi 27806097     769 PSQQ-----CLEDSLILLQCN 784
Cdd:smart00202   81 PHSGwgshnCSHGEDAGVVCS 101
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 659-693 4.01e-12

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: 61.45  E-value: 4.01e-12
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 27806097  659 CKEDNFQCKDGECIPLVNLCDGFPHCKDGSDEAHC 693
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 199-233 2.20e-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: 47.97  E-value: 2.20e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 27806097  199 CPPDSRLCADaLKCIAIDLFCDGELNCPDGSDEDN 233
Cdd:cd00112    1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEEN 34
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 801-1032 2.26e-99

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: 312.29  E-value: 2.26e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  801 IVGGSDSREGAWPWVVALYFDD-QQVCGASLVSRDWLVSAAHCVYGRNmePSKWKAVLGLHMASNLTSPQiETRLIDQIV 879
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSNEGGG-QVIKVKKVI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  880 INPHYNKRRKNNDIAMMHLEMKVNYTDYIQPICLPEENQVFPPGRICSIAGWGALIYQGSTADVLQEADVPLLSNEKCQQ 959
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27806097  960 QMPE-YNITENMVCAGYEAGGVDSCQGDSGGPLMCQENNRWLLAGVTSFGYQCALPNRPGVYARVPRFTEWIQS 1032
Cdd:cd00190  158 AYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 800-1030 1.18e-94

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: 299.59  E-value: 1.18e-94
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     800 KIVGGSDSREGAWPWVVALYFDD-QQVCGASLVSRDWLVSAAHCVYGRNmePSKWKAVLGLHMASNLTSPQieTRLIDQI 878
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSD--PSNIRVRLGSHDLSSGEEGQ--VIKVSKV 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     879 VINPHYNKRRKNNDIAMMHLEMKVNYTDYIQPICLPEENQVFPPGRICSIAGWGALIY-QGSTADVLQEADVPLLSNEKC 957
Cdd:smart00020   77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATC 156

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27806097     958 QQQMPEYN-ITENMVCAGYEAGGVDSCQGDSGGPLMCQeNNRWLLAGVTSFGYQCALPNRPGVYARVPRFTEWI 1030
Cdd:smart00020  157 RRAYSGGGaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
801-1030 1.90e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 239.27  E-value: 1.90e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097    801 IVGGSDSREGAWPWVVALYF-DDQQVCGASLVSRDWLVSAAHCVYGRnmepSKWKAVLGLHmASNLTSPQIETRLIDQIV 879
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGA----SDVKVVLGAH-NIVLREGGEQKFDVEKII 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097    880 INPHYNKRRKNNDIAMMHLEMKVNYTDYIQPICLPEENQVFPPGRICSIAGWGaLIYQGSTADVLQEADVPLLSNEKCQQ 959
Cdd:pfam00089   76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG-NTKTLGPSDTLQEVTVPVVSRETCRS 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27806097    960 QMPEYnITENMVCAGYeaGGVDSCQGDSGGPLMCQENnrwLLAGVTSFGYQCALPNRPGVYARVPRFTEWI 1030
Cdd:pfam00089  155 AYGGT-VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 794-1032 8.88e-72

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 239.17  E-value: 8.88e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  794 TQEVSPKIVGGSDSREGAWPWVVALYFDD---QQVCGASLVSRDWLVSAAHCVYGRNmePSKWKAVLGLHmasNLTSPQI 870
Cdd:COG5640   24 AADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG--PSDLRVVIGST---DLSTSGG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  871 ETRLIDQIVINPHYNKRRKNNDIAMMHLEMKVnytDYIQPICLPEENQVFPPGRICSIAGWGALI-YQGSTADVLQEADV 949
Cdd:COG5640   99 TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSeGPGSQSGTLRKADV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  950 PLLSNEKCQQqMPEYnITENMVCAGYEAGGVDSCQGDSGGPLMCQENNRWLLAGVTSFGYQCALPNRPGVYARVPRFTEW 1029
Cdd:COG5640  176 PVVSDATCAA-YGGF-DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253


                 ...
gi 27806097 1030 IQS 1032
Cdd:COG5640  254 IKS 256
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 358-518 8.64e-52

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 179.08  E-value: 8.64e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     358 YEKINCNFEDG-FCFWIQDLNDDNEWERTQGSTFPpsTGPTFDHTFGNesGFYISTPTGPGGRRERVGLLTLPLDPTPEQ 436
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSATGI--PGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     437 ACLSFWYYMYGENVYKLSINISSDQNME-KTIFQKEGNYGQNWNYGQVTLN-ETVEFKVSFYGFKNQ-ILSDIALDDISL 513
Cdd:smart00137   77 HCLTFWYYMYGSGSGTLNVYVRENNGSQdTLLWSRSGTQGGQWLQAEVALSsWPQPFQVVFEGTRGKgHSGYIALDDILL 156


                    ....*
gi 27806097     514 TYGIC 518
Cdd:smart00137  157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 363-519 1.70e-49

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: 172.16  E-value: 1.70e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097    363 CNFEDG-FCFWIQDLNDDNEWERTQGstFPPSTGPTFDHTFGNESGFYISTPTGPGGRRERVGLLTLPLDPTPEQACLSF 441
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSG--PSVKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097    442 WYYMYGENVYKLSINISSDQNM-EKTIFQKEGNYGQNWNYGQVTLNE-TVEFKVSFYGFKNQ-ILSDIALDDISLTYGIC 518
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVRENGGTlDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGgSRGGIALDDISLSSGPC 158


                   .
gi 27806097    519 N 519
Cdd:pfam00629  159 P 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 363-518 1.37e-44

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 158.31  E-value: 1.37e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  363 CNFEDGFCFWIQDLNDDNEWERTQGSTFPPSTGPtfDHTFGNESGFYISTPTGPGGRRERVGLLTLPLDPTPEQACLSFW 442
Cdd:cd06263    1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSSHCLSFW 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27806097  443 YYMYGENVYKLSINISSDQN-MEKTIFQKEGNYGQNWNYGQVTLNETV-EFKVSFYGFKNQ-ILSDIALDDISLTYGIC 518
Cdd:cd06263   79 YHMYGSGVGTLNVYVREEGGgLGTLLWSASGGQGNQWQEAEVTLSASSkPFQVVFEGVRGSgSRGDIALDDISLSPGPC 157
CUB pfam00431
CUB domain;
540-647 2.00e-34

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 127.41  E-value: 2.00e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097    540 CGGphDLWEPNTTFTSINFPNSYPNQAFCIWNLNAQKGKNIQLHFQEFDLE----NIADVVEIRDGEGDDSLFLAVYTGP 615
Cdd:pfam00431    1 CGG--VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 27806097    616 GPVNDVFSTTNRMTVLFITDNMLAKQGFKANF 647
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 540-649 2.91e-28

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: 109.81  E-value: 2.91e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  540 CGGpHDLWEPNTTFTSINFPNSYPNQAFCIWNLNAQKGKNIQLHFQEFDLEN----IADVVEIRDGEGDDSLFLAVYTGP 615
Cdd:cd00041    1 CGG-TLTASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLLGRFCGS 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 27806097  616 GPVNDVFSTTNRMTVLFITDNMLAKQGFKANFTT 649
Cdd:cd00041   80 TLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 552-647 1.06e-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: 102.08  E-value: 1.06e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     552 TFTSINFPNSYPNQAFCIWNLNAQKGKNIQLHFQEFDLEN----IADVVEIRDGEGDDSLFLAVYTGPGPVNDVFST-TN 626
Cdd:smart00042    2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESsdncEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSsSN 81

                            90       100
                    ....*....|....*....|.
gi 27806097     627 RMTVLFITDNMLAKQGFKANF 647
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 69-154 1.32e-22

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: 94.02  E-value: 1.32e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097      69 TYNPHLQDKLSVDFKVLAFDIQQMIDDIFQSSNLKNEYKNSRVLQFENGSIIVIFDLLFDQWV-SDKNVKEELIQGIEAN 147
Cdd:smart00200   20 QYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNEGVtNGQDVEEDLLQVIKQA 99


                    ....*..
gi 27806097     148 KSSQLVT 154
Cdd:smart00200  100 AYSLKIT 106
CUB pfam00431
CUB domain;
240-347 1.51e-22

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 93.51  E-value: 1.51e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097    240 CDGRFllTGSSGSFEALHYPKPSNNtSAVCRWIIRVNQGLSIQLNFDYFNTYYA-----DVLNIYEGMGSSKILRASLW- 313
Cdd:pfam00431    1 CGGVL--TDSSGSISSPNYPNPYPP-NKDCVWLIRAPPGFRVKLTFQDFELEDHdecgyDYVEIRDGPSASSPLLGRFCg 77

                           90       100       110
                   ....*....|....*....|....*....|....
gi 27806097    314 SNNPGIIRIFSNQVTATFLIqSDESDYIGFKVTY 347
Cdd:pfam00431   78 SGIPEDIVSSSNQMTIKFVS-DASVQKRGFKATY 110
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 59-151 2.98e-15

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: 72.27  E-value: 2.98e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     59 RGTLKIISgATYNPHLQDKLSVDFKVLAFDIQQMIDDIFQSSNLKNEYKNSRVLQF--ENGSIIVIFDLLFDQWVSD-KN 135
Cdd:pfam01390    4 TGSFKITN-LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLrpDGGSVVVDVVLVFRFPSTEpAL 82

                           90
                   ....*....|....*...
gi 27806097    136 VKEELIQGI--EANKSSQ 151
Cdd:pfam01390   83 DREKLIEEIlrQTLNNTT 100
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 240-349 3.71e-15

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: 72.45  E-value: 3.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  240 CDGRFLLTgSSGSFEALHYPKPSNNtSAVCRWIIRVNQGLSIQLNFDYFNTYYA-----DVLNIYEGMGSSKILRASLW- 313
Cdd:cd00041    1 CGGTLTAS-TSGTISSPNYPNNYPN-NLNCVWTIEAPPGYRIRLTFEDFDLESSpncsyDYLEIYDGPSTSSPLLGRFCg 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 27806097  314 SNNPGIIRIFSNQVTATFliQSDESD-YIGFKVTYTA 349
Cdd:cd00041   79 STLPPPIISSGNSLTVRF--RSDSSVtGRGFKATYSA 113
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 694-784 6.32e-15

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: 71.60  E-value: 6.32e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     694 VRLFNGTTDSSGLVQFRIQSIWHVACAENWTTQISDDVCQLLGLGTGNSSVP--TFSTGGGPYVNLNTAPNG---SLILT 768
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsaYFGPGSGPIWLDNVRCSGteaSLSDC 80

                            90       100
                    ....*....|....*....|.
gi 27806097     769 PSQQ-----CLEDSLILLQCN 784
Cdd:smart00202   81 PHSGwgshnCSHGEDAGVVCS 101
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 251-347 4.37e-13

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: 66.26  E-value: 4.37e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     251 GSFEALHYPKPSNNtSAVCRWIIRVNQGLSIQLNFDYFNTYYA-----DVLNIYEGMGSSKIL--RASLWSNNPGIIRIF 323
Cdd:smart00042    1 GTITSPNYPQSYPN-NLDCVWTIRAPPGYRIELQFTDFDLESSdnceyDYVEIYDGPSASSPLlgRFCGSEAPPPVISSS 79

                            90       100
                    ....*....|....*....|....*
gi 27806097     324 SNQVTATFliQSDESD-YIGFKVTY 347
Cdd:smart00042   80 SNSLTLTF--VSDSSVqKRGFSARY 102
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 659-693 4.01e-12

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: 61.45  E-value: 4.01e-12
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 27806097  659 CKEDNFQCKDGECIPLVNLCDGFPHCKDGSDEAHC 693
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 659-690 5.36e-11

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: 58.03  E-value: 5.36e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 27806097     659 CKEDNFQCKDGECIPLVNLCDGFPHCKDGSDE 690
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
658-693 1.36e-10

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 56.87  E-value: 1.36e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 27806097    658 PCKEDNFQCKDGECIPLVNLCDGFPHCKDGSDEAHC 693
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 199-233 2.20e-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: 47.97  E-value: 2.20e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 27806097  199 CPPDSRLCADaLKCIAIDLFCDGELNCPDGSDEDN 233
Cdd:cd00112    1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEEN 34
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 198-231 4.43e-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: 4.43e-06
                            10        20        30
                    ....*....|....*....|....*....|....
gi 27806097     198 ECPPDSRLCADAlKCIAIDLFCDGELNCPDGSDE 231
Cdd:smart00192    1 TCPPGEFQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 699-789 1.01e-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: 42.36  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097    699 GTTDSSGLVQFRIQSIWHVACAENWTTQISDDVCQLLGLGTGNSSVPTFSTGGgpyvnlntAPNGSLILTPSQQC--LED 776
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSAPSGCSYFG--------PGSTGPIWLDDVRCsgNET 72

                           90
                   ....*....|...
gi 27806097    777 SliLLQCNYKSCG 789
Cdd:pfam00530   73 S--LWQCPHRPWG 83
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
199-233 4.80e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 38.38  E-value: 4.80e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 27806097    199 CPPDSRLCADAlKCIAIDLFCDGELNCPDGSDEDN 233
Cdd:pfam00057    3 CSPNEFQCGSG-ECIPRSWVCDGDPDCGDGSDEEN 36
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 801-1032 2.26e-99

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: 312.29  E-value: 2.26e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  801 IVGGSDSREGAWPWVVALYFDD-QQVCGASLVSRDWLVSAAHCVYGRNmePSKWKAVLGLHMASNLTSPQiETRLIDQIV 879
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSNEGGG-QVIKVKKVI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  880 INPHYNKRRKNNDIAMMHLEMKVNYTDYIQPICLPEENQVFPPGRICSIAGWGALIYQGSTADVLQEADVPLLSNEKCQQ 959
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27806097  960 QMPE-YNITENMVCAGYEAGGVDSCQGDSGGPLMCQENNRWLLAGVTSFGYQCALPNRPGVYARVPRFTEWIQS 1032
Cdd:cd00190  158 AYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 800-1030 1.18e-94

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: 299.59  E-value: 1.18e-94
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     800 KIVGGSDSREGAWPWVVALYFDD-QQVCGASLVSRDWLVSAAHCVYGRNmePSKWKAVLGLHMASNLTSPQieTRLIDQI 878
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSD--PSNIRVRLGSHDLSSGEEGQ--VIKVSKV 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     879 VINPHYNKRRKNNDIAMMHLEMKVNYTDYIQPICLPEENQVFPPGRICSIAGWGALIY-QGSTADVLQEADVPLLSNEKC 957
Cdd:smart00020   77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATC 156

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27806097     958 QQQMPEYN-ITENMVCAGYEAGGVDSCQGDSGGPLMCQeNNRWLLAGVTSFGYQCALPNRPGVYARVPRFTEWI 1030
Cdd:smart00020  157 RRAYSGGGaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
801-1030 1.90e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 239.27  E-value: 1.90e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097    801 IVGGSDSREGAWPWVVALYF-DDQQVCGASLVSRDWLVSAAHCVYGRnmepSKWKAVLGLHmASNLTSPQIETRLIDQIV 879
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGA----SDVKVVLGAH-NIVLREGGEQKFDVEKII 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097    880 INPHYNKRRKNNDIAMMHLEMKVNYTDYIQPICLPEENQVFPPGRICSIAGWGaLIYQGSTADVLQEADVPLLSNEKCQQ 959
Cdd:pfam00089   76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG-NTKTLGPSDTLQEVTVPVVSRETCRS 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27806097    960 QMPEYnITENMVCAGYeaGGVDSCQGDSGGPLMCQENnrwLLAGVTSFGYQCALPNRPGVYARVPRFTEWI 1030
Cdd:pfam00089  155 AYGGT-VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 794-1032 8.88e-72

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 239.17  E-value: 8.88e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  794 TQEVSPKIVGGSDSREGAWPWVVALYFDD---QQVCGASLVSRDWLVSAAHCVYGRNmePSKWKAVLGLHmasNLTSPQI 870
Cdd:COG5640   24 AADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG--PSDLRVVIGST---DLSTSGG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  871 ETRLIDQIVINPHYNKRRKNNDIAMMHLEMKVnytDYIQPICLPEENQVFPPGRICSIAGWGALI-YQGSTADVLQEADV 949
Cdd:COG5640   99 TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSeGPGSQSGTLRKADV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  950 PLLSNEKCQQqMPEYnITENMVCAGYEAGGVDSCQGDSGGPLMCQENNRWLLAGVTSFGYQCALPNRPGVYARVPRFTEW 1029
Cdd:COG5640  176 PVVSDATCAA-YGGF-DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253


                 ...
gi 27806097 1030 IQS 1032
Cdd:COG5640  254 IKS 256
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 358-518 8.64e-52

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 179.08  E-value: 8.64e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     358 YEKINCNFEDG-FCFWIQDLNDDNEWERTQGSTFPpsTGPTFDHTFGNesGFYISTPTGPGGRRERVGLLTLPLDPTPEQ 436
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSATGI--PGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     437 ACLSFWYYMYGENVYKLSINISSDQNME-KTIFQKEGNYGQNWNYGQVTLN-ETVEFKVSFYGFKNQ-ILSDIALDDISL 513
Cdd:smart00137   77 HCLTFWYYMYGSGSGTLNVYVRENNGSQdTLLWSRSGTQGGQWLQAEVALSsWPQPFQVVFEGTRGKgHSGYIALDDILL 156


                    ....*
gi 27806097     514 TYGIC 518
Cdd:smart00137  157 SNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 363-519 1.70e-49

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: 172.16  E-value: 1.70e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097    363 CNFEDG-FCFWIQDLNDDNEWERTQGstFPPSTGPTFDHTFGNESGFYISTPTGPGGRRERVGLLTLPLDPTPEQACLSF 441
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSG--PSVKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097    442 WYYMYGENVYKLSINISSDQNM-EKTIFQKEGNYGQNWNYGQVTLNE-TVEFKVSFYGFKNQ-ILSDIALDDISLTYGIC 518
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVRENGGTlDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGIRGGgSRGGIALDDISLSSGPC 158


                   .
gi 27806097    519 N 519
Cdd:pfam00629  159 P 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 363-518 1.37e-44

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 158.31  E-value: 1.37e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  363 CNFEDGFCFWIQDLNDDNEWERTQGSTFPPSTGPtfDHTFGNESGFYISTPTGPGGRRERVGLLTLPLDPTPEQACLSFW 442
Cdd:cd06263    1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSSHCLSFW 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27806097  443 YYMYGENVYKLSINISSDQN-MEKTIFQKEGNYGQNWNYGQVTLNETV-EFKVSFYGFKNQ-ILSDIALDDISLTYGIC 518
Cdd:cd06263   79 YHMYGSGVGTLNVYVREEGGgLGTLLWSASGGQGNQWQEAEVTLSASSkPFQVVFEGVRGSgSRGDIALDDISLSPGPC 157
CUB pfam00431
CUB domain;
540-647 2.00e-34

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 127.41  E-value: 2.00e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097    540 CGGphDLWEPNTTFTSINFPNSYPNQAFCIWNLNAQKGKNIQLHFQEFDLE----NIADVVEIRDGEGDDSLFLAVYTGP 615
Cdd:pfam00431    1 CGG--VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 27806097    616 GPVNDVFSTTNRMTVLFITDNMLAKQGFKANF 647
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 540-649 2.91e-28

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: 109.81  E-value: 2.91e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  540 CGGpHDLWEPNTTFTSINFPNSYPNQAFCIWNLNAQKGKNIQLHFQEFDLEN----IADVVEIRDGEGDDSLFLAVYTGP 615
Cdd:cd00041    1 CGG-TLTASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLLGRFCGS 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 27806097  616 GPVNDVFSTTNRMTVLFITDNMLAKQGFKANFTT 649
Cdd:cd00041   80 TLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 552-647 1.06e-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: 102.08  E-value: 1.06e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     552 TFTSINFPNSYPNQAFCIWNLNAQKGKNIQLHFQEFDLEN----IADVVEIRDGEGDDSLFLAVYTGPGPVNDVFST-TN 626
Cdd:smart00042    2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESsdncEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSsSN 81

                            90       100
                    ....*....|....*....|.
gi 27806097     627 RMTVLFITDNMLAKQGFKANF 647
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 69-154 1.32e-22

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: 94.02  E-value: 1.32e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097      69 TYNPHLQDKLSVDFKVLAFDIQQMIDDIFQSSNLKNEYKNSRVLQFENGSIIVIFDLLFDQWV-SDKNVKEELIQGIEAN 147
Cdd:smart00200   20 QYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNEGVtNGQDVEEDLLQVIKQA 99


                    ....*..
gi 27806097     148 KSSQLVT 154
Cdd:smart00200  100 AYSLKIT 106
CUB pfam00431
CUB domain;
240-347 1.51e-22

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 93.51  E-value: 1.51e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097    240 CDGRFllTGSSGSFEALHYPKPSNNtSAVCRWIIRVNQGLSIQLNFDYFNTYYA-----DVLNIYEGMGSSKILRASLW- 313
Cdd:pfam00431    1 CGGVL--TDSSGSISSPNYPNPYPP-NKDCVWLIRAPPGFRVKLTFQDFELEDHdecgyDYVEIRDGPSASSPLLGRFCg 77

                           90       100       110
                   ....*....|....*....|....*....|....
gi 27806097    314 SNNPGIIRIFSNQVTATFLIqSDESDYIGFKVTY 347
Cdd:pfam00431   78 SGIPEDIVSSSNQMTIKFVS-DASVQKRGFKATY 110
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 59-151 2.98e-15

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: 72.27  E-value: 2.98e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     59 RGTLKIISgATYNPHLQDKLSVDFKVLAFDIQQMIDDIFQSSNLKNEYKNSRVLQF--ENGSIIVIFDLLFDQWVSD-KN 135
Cdd:pfam01390    4 TGSFKITN-LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLrpDGGSVVVDVVLVFRFPSTEpAL 82

                           90
                   ....*....|....*...
gi 27806097    136 VKEELIQGI--EANKSSQ 151
Cdd:pfam01390   83 DREKLIEEIlrQTLNNTT 100
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 240-349 3.71e-15

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: 72.45  E-value: 3.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  240 CDGRFLLTgSSGSFEALHYPKPSNNtSAVCRWIIRVNQGLSIQLNFDYFNTYYA-----DVLNIYEGMGSSKILRASLW- 313
Cdd:cd00041    1 CGGTLTAS-TSGTISSPNYPNNYPN-NLNCVWTIEAPPGYRIRLTFEDFDLESSpncsyDYLEIYDGPSTSSPLLGRFCg 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 27806097  314 SNNPGIIRIFSNQVTATFliQSDESD-YIGFKVTYTA 349
Cdd:cd00041   79 STLPPPIISSGNSLTVRF--RSDSSVtGRGFKATYSA 113
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 694-784 6.32e-15

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: 71.60  E-value: 6.32e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     694 VRLFNGTTDSSGLVQFRIQSIWHVACAENWTTQISDDVCQLLGLGTGNSSVP--TFSTGGGPYVNLNTAPNG---SLILT 768
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsaYFGPGSGPIWLDNVRCSGteaSLSDC 80

                            90       100
                    ....*....|....*....|.
gi 27806097     769 PSQQ-----CLEDSLILLQCN 784
Cdd:smart00202   81 PHSGwgshnCSHGEDAGVVCS 101
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 251-347 4.37e-13

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: 66.26  E-value: 4.37e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097     251 GSFEALHYPKPSNNtSAVCRWIIRVNQGLSIQLNFDYFNTYYA-----DVLNIYEGMGSSKIL--RASLWSNNPGIIRIF 323
Cdd:smart00042    1 GTITSPNYPQSYPN-NLDCVWTIRAPPGYRIELQFTDFDLESSdnceyDYVEIYDGPSASSPLlgRFCGSEAPPPVISSS 79

                            90       100
                    ....*....|....*....|....*
gi 27806097     324 SNQVTATFliQSDESD-YIGFKVTY 347
Cdd:smart00042   80 SNSLTLTF--VSDSSVqKRGFSARY 102
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 659-693 4.01e-12

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: 61.45  E-value: 4.01e-12
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 27806097  659 CKEDNFQCKDGECIPLVNLCDGFPHCKDGSDEAHC 693
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 659-690 5.36e-11

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: 58.03  E-value: 5.36e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 27806097     659 CKEDNFQCKDGECIPLVNLCDGFPHCKDGSDE 690
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
658-693 1.36e-10

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 56.87  E-value: 1.36e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 27806097    658 PCKEDNFQCKDGECIPLVNLCDGFPHCKDGSDEAHC 693
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 815-1009 3.16e-08

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 54.68  E-value: 3.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  815 VVALYFDDQQ-VCGASLVSRDWLVSAAHCVYGRNME--PSKWKAVLGLHMASNLTSPqietrlIDQIVINPHY-NKRRKN 890
Cdd:COG3591    2 VGRLETDGGGgVCTGTLIGPNLVLTAGHCVYDGAGGgwATNIVFVPGYNGGPYGTAT------ATRFRVPPGWvASGDAG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097  891 NDIAMMHLEMKVNYTDYIQPIclpEENQVFPPGRICSIAGWGA----LIYQGSTADVLqeadvpllsnekcqqqmpeyNI 966
Cdd:COG3591   76 YDYALLRLDEPLGDTTGWLGL---AFNDAPLAGEPVTIIGYPGdrpkDLSLDCSGRVT--------------------GV 132

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 27806097  967 TENMVcaGYEAggvDSCQGDSGGPLMCQENNRWLLAGVTSFGY 1009
Cdd:COG3591  133 QGNRL--SYDC---DTTGGSSGSPVLDDSDGGGRVVGVHSAGG 170
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 199-233 2.20e-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: 47.97  E-value: 2.20e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 27806097  199 CPPDSRLCADaLKCIAIDLFCDGELNCPDGSDEDN 233
Cdd:cd00112    1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEEN 34
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 198-231 4.43e-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: 4.43e-06
                            10        20        30
                    ....*....|....*....|....*....|....
gi 27806097     198 ECPPDSRLCADAlKCIAIDLFCDGELNCPDGSDE 231
Cdd:smart00192    1 TCPPGEFQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 699-789 1.01e-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: 42.36  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097    699 GTTDSSGLVQFRIQSIWHVACAENWTTQISDDVCQLLGLGTGNSSVPTFSTGGgpyvnlntAPNGSLILTPSQQC--LED 776
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSAPSGCSYFG--------PGSTGPIWLDDVRCsgNET 72

                           90
                   ....*....|...
gi 27806097    777 SliLLQCNYKSCG 789
Cdd:pfam00530   73 S--LWQCPHRPWG 83
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
199-233 4.80e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 38.38  E-value: 4.80e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 27806097    199 CPPDSRLCADAlKCIAIDLFCDGELNCPDGSDEDN 233
Cdd:pfam00057    3 CSPNEFQCGSG-ECIPRSWVCDGDPDCGDGSDEEN 36
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
 707-789 4.84e-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: 4.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806097    707 VQFRIQSIWHVACAENWTTQISDDVCQLLGLG--TGNSSVPTFSTGGGP---YVNLNT-APNGSL--ILTPSQQCLEDSL 778
Cdd:pfam15494    8 VYSSARPSWLPVCSDDWNPAYGRAACQQLGYLrlTHHKSVNLTDISSNSsqsFMKLNSsSLNTDLyeALQPRDSCSSGSV 87

                           90
                   ....*....|.
gi 27806097    779 ILLQCNykSCG 789
Cdd:pfam15494   88 VSLRCS--ECG 96
 
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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