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Conserved domains on  [gi|768021213|ref|XP_011527957|]
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enteropeptidase isoform X1 [Homo sapiens]

Protein Classification

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 ...
 830-1061 1.75e-101

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: 318.45  E-value: 1.75e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  830 IVGGSNAKEGAWPWVVGLYYG-GRLLCGASLVSSDWLVSAAHCVYGRNlePSKWTAILGLHMKSNLTSPQTVpRLIDEIV 908
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSNEGGGQV-IKVKKVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  909 INPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWGTVVYQGTTANILQEADVPLLSNERCQQ 988
Cdd:cd00190    78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021213  989 QMPE-YNITENMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLAGVTSFGYKCALPNRPGVYARVSRFTEWIQS 1061
Cdd:cd00190   158 AYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 392-548 1.74e-50

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: 175.24  E-value: 1.74e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213   392 CNFEDG-FCFWVQDLNDDNEWERIQGstFSPFTGPNFDHTFGNASGFYISTPTGPGGRQERVGLLSLPLDPTLEPACLSF 470
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSG--PSVKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213   471 WYHMYGENVHKLSINI-SNDQNMEKTVFQKEGNYGDNWNYGQVTLNE-TVKFKVAFNA-FKNKILSDIALDDISLTYGIC 547
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVrENGGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGiRGGGSRGGIALDDISLSSGPC 158


                   .
gi 768021213   548 N 548
Cdd:pfam00629  159 P 159
CUB pfam00431
CUB domain;
569-676 8.66e-37

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 134.34  E-value: 8.66e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213   569 CGGpfELWEPNTTFSSTNFPNSYPNLAFCVWILNAQKGKNIQLHFQEFDLE----NINDVVEIRDGEEADSLLLAVYTGP 644
Cdd:pfam00431    1 CGG--VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 768021213   645 GPVKDVFSTTNRMTVLLITNDVLARGGFKANF 676
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
270-376 9.46e-29

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 111.23  E-value: 9.46e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213   270 CDGRFllTGSSGSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYYT-----DILDIYEGVGSSKILRASIW-E 343
Cdd:pfam00431    1 CGGVL--TDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHdecgyDYVEIRDGPSASSPLLGRFCgS 78

                           90       100       110
                   ....*....|....*....|....*....|...
gi 768021213   344 TNPGTIRIFSNQVTATFLIeSDESDYVGFNATY 376
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVS-DASVQKRGFKATY 110
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 53-195 5.97e-21

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: 89.39  E-value: 5.97e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213     53 GQSHEARATFKITSG--VTYNPNLQDKLSVDFKVLAFDLQQMIDEIFLSSNLKNEYKNSRVLQFDknwrqaenevestvs 130
Cdd:smart00200    2 TQSFGVSLSVLSVEGenLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFR--------------- 66

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768021213    131 lyslygswihqkyqkNGSIIVVFDLFFAQWV-SDENVKEELIQGLEANKSSQLVTfhiDLNSVDIL 195
Cdd:smart00200   67 ---------------NGSVVVDLGLLFNEGVtNGQDVEEDLLQVIKQAAYSLKIT---NVNVVDVL 114
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 723-816 2.60e-13

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: 66.98  E-value: 2.60e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213    723 VRFFNGTTNNNGLVRFRIQSIWHTACAENWTTQISNDVCQLLGLGSGNSSKP--IFPTDGGPFVKLNTAPDGHliLTPSQ 800
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsaYFGPGSGPIWLDNVRCSGT--EASLS 78

                            90
                    ....*....|....*.
gi 768021213    801 QCLQDSLIRLQCNHKS 816
Cdd:smart00202   79 DCPHSGWGSHNCSHGE 94
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 688-722 1.71e-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: 62.22  E-value: 1.71e-12
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 768021213  688 CKADHFQCKNGECVPLVNLCDGHLHCEDGSDEADC 722
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 229-263 2.65e-06

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


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 44.89  E-value: 2.65e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 768021213  229 CLPGSSPCTDaLTCIKADLFCDGEVNCPDGSDEDN 263
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 ...
 830-1061 1.75e-101

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: 318.45  E-value: 1.75e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  830 IVGGSNAKEGAWPWVVGLYYG-GRLLCGASLVSSDWLVSAAHCVYGRNlePSKWTAILGLHMKSNLTSPQTVpRLIDEIV 908
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSNEGGGQV-IKVKKVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  909 INPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWGTVVYQGTTANILQEADVPLLSNERCQQ 988
Cdd:cd00190    78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021213  989 QMPE-YNITENMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLAGVTSFGYKCALPNRPGVYARVSRFTEWIQS 1061
Cdd:cd00190   158 AYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 829-1059 9.72e-98

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: 308.45  E-value: 9.72e-98
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213    829 KIVGGSNAKEGAWPWVVGLYY-GGRLLCGASLVSSDWLVSAAHCVYGRNlePSKWTAILGLHMKSNLTSPQTVPrlIDEI 907
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGSD--PSNIRVRLGSHDLSSGEEGQVIK--VSKV 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213    908 VINPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWG-TVVYQGTTANILQEADVPLLSNERC 986
Cdd:smart00020   77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGrTSEGAGSLPDTLQEVNVPIVSNATC 156

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021213    987 QQQMPEYN-ITENMICAGYEEGGIDSCQGDSGGPLMCQeNNRWFLAGVTSFGYKCALPNRPGVYARVSRFTEWI 1059
Cdd:smart00020  157 RRAYSGGGaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
830-1059 1.22e-74

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 245.43  E-value: 1.22e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213   830 IVGGSNAKEGAWPWVVGLYY-GGRLLCGASLVSSDWLVSAAHCVYGRnlepSKWTAILGLH-MKSNLTSPQTVPrlIDEI 907
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGA----SDVKVVLGAHnIVLREGGEQKFD--VEKI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213   908 VINPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWGTvVYQGTTANILQEADVPLLSNERCQ 987
Cdd:pfam00089   75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGN-TKTLGPSDTLQEVTVPVVSRETCR 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768021213   988 QQMPEYnITENMICAGYeeGGIDSCQGDSGGPLMCQENnrwFLAGVTSFGYKCALPNRPGVYARVSRFTEWI 1059
Cdd:pfam00089  154 SAYGGT-VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 822-1061 3.46e-71

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 237.63  E-value: 3.46e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  822 AAQDITPKIVGGSNAKEGAWPWVVGLYYGG---RLLCGASLVSSDWLVSAAHCVYGRNlePSKWTAILGLHmksNLTSPQ 898
Cdd:COG5640    23 PAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG--PSDLRVVIGST---DLSTSG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  899 TVPRLIDEIVINPHYNRRRKDNDIAMMHLEFKVnytDYIQPICLPEENQVFPPGRNCSIAGWG-TVVYQGTTANILQEAD 977
Cdd:COG5640    98 GTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGrTSEGPGSQSGTLRKAD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  978 VPLLSNERCQQqMPEYnITENMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLAGVTSFGY-KCAlPNRPGVYARVSRFT 1056
Cdd:COG5640   175 VPVVSDATCAA-YGGF-DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGgPCA-AGYPGVYTRVSAYR 251


                  ....*
gi 768021213 1057 EWIQS 1061
Cdd:COG5640   252 DWIKS 256
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 392-548 1.74e-50

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: 175.24  E-value: 1.74e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213   392 CNFEDG-FCFWVQDLNDDNEWERIQGstFSPFTGPNFDHTFGNASGFYISTPTGPGGRQERVGLLSLPLDPTLEPACLSF 470
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSG--PSVKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213   471 WYHMYGENVHKLSINI-SNDQNMEKTVFQKEGNYGDNWNYGQVTLNE-TVKFKVAFNA-FKNKILSDIALDDISLTYGIC 547
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVrENGGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGiRGGGSRGGIALDDISLSSGPC 158


                   .
gi 768021213   548 N 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 3.98e-50

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: 174.45  E-value: 3.98e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213    387 YEKINCNFEDG-FCFWVQDLNDDNEWERIQGSTFSpfTGPNFDHTFGNasGFYISTPTGPGGRQERVGLLSLPLDPTLEP 465
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSATGI--PGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213    466 ACLSFWYHMYGENVHKLSINISNDQNME-KTVFQKEGNYGDNWNYGQVTLN-ETVKFKVAFNAFKNK-ILSDIALDDISL 542
Cdd:smart00137   77 HCLTFWYYMYGSGSGTLNVYVRENNGSQdTLLWSRSGTQGGQWLQAEVALSsWPQPFQVVFEGTRGKgHSGYIALDDILL 156


                    ....*
gi 768021213    543 TYGIC 547
Cdd:smart00137  157 SNGPC 161
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 392-547 8.09e-49

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: 170.25  E-value: 8.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  392 CNFEDGFCFWVQDLNDDNEWERIQGSTFSPFTGPnfDHTFGNASGFYISTPTGPGGRQERVGLLSLPLDPTLEPACLSFW 471
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSSHCLSFW 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768021213  472 YHMYGENVHKLSINI-SNDQNMEKTVFQKEGNYGDNWNYGQVTLNETVK-FKVAFNAFKNK-ILSDIALDDISLTYGIC 547
Cdd:cd06263    79 YHMYGSGVGTLNVYVrEEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSgSRGDIALDDISLSPGPC 157
CUB pfam00431
CUB domain;
569-676 8.66e-37

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 134.34  E-value: 8.66e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213   569 CGGpfELWEPNTTFSSTNFPNSYPNLAFCVWILNAQKGKNIQLHFQEFDLE----NINDVVEIRDGEEADSLLLAVYTGP 644
Cdd:pfam00431    1 CGG--VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 768021213   645 GPVKDVFSTTNRMTVLLITNDVLARGGFKANF 676
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
270-376 9.46e-29

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 111.23  E-value: 9.46e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213   270 CDGRFllTGSSGSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYYT-----DILDIYEGVGSSKILRASIW-E 343
Cdd:pfam00431    1 CGGVL--TDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHdecgyDYVEIRDGPSASSPLLGRFCgS 78

                           90       100       110
                   ....*....|....*....|....*....|...
gi 768021213   344 TNPGTIRIFSNQVTATFLIeSDESDYVGFNATY 376
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVS-DASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 569-678 1.27e-27

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: 108.27  E-value: 1.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  569 CGGPFeLWEPNTTFSSTNFPNSYPNLAFCVWILNAQKGKNIQLHFQEFDLEN----INDVVEIRDGEEADSLLLAVYTGP 644
Cdd:cd00041     1 CGGTL-TASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLLGRFCGS 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 768021213  645 GPVKDVFSTTNRMTVLLITNDVLARGGFKANFTT 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 4.71e-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: 100.54  E-value: 4.71e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213    581 TFSSTNFPNSYPNLAFCVWILNAQKGKNIQLHFQEFDLENIN----DVVEIRDGEEADSLLLAVYTGPGPVKDVFST-TN 655
Cdd:smart00042    2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDnceyDYVEIYDGPSASSPLLGRFCGSEAPPPVISSsSN 81

                            90       100
                    ....*....|....*....|.
gi 768021213    656 RMTVLLITNDVLARGGFKANF 676
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 53-195 5.97e-21

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: 89.39  E-value: 5.97e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213     53 GQSHEARATFKITSG--VTYNPNLQDKLSVDFKVLAFDLQQMIDEIFLSSNLKNEYKNSRVLQFDknwrqaenevestvs 130
Cdd:smart00200    2 TQSFGVSLSVLSVEGenLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFR--------------- 66

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768021213    131 lyslygswihqkyqkNGSIIVVFDLFFAQWV-SDENVKEELIQGLEANKSSQLVTfhiDLNSVDIL 195
Cdd:smart00200   67 ---------------NGSVVVDLGLLFNEGVtNGQDVEEDLLQVIKQAAYSLKIT---NVNVVDVL 114
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 270-378 4.05e-16

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: 75.14  E-value: 4.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  270 CDGRFLLTgSSGSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYY-----TDILDIYEGVGSSKILRASIW-E 343
Cdd:cd00041     1 CGGTLTAS-TSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncsYDYLEIYDGPSTSSPLLGRFCgS 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 768021213  344 TNPGTIRIFSNQVTATFLieSDESD-YVGFNATYTA 378
Cdd:cd00041    80 TLPPPIISSGNSLTVRFR--SDSSVtGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 281-376 2.70e-14

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: 69.73  E-value: 2.70e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213    281 GSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYYT-----DILDIYEG--VGSSKILRASIWETNPGTIRIFS 353
Cdd:smart00042    1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSdnceyDYVEIYDGpsASSPLLGRFCGSEAPPPVISSSS 80

                            90       100
                    ....*....|....*....|....
gi 768021213    354 NQVTATFLieSDESD-YVGFNATY 376
Cdd:smart00042   81 NSLTLTFV--SDSSVqKRGFSARY 102
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 723-816 2.60e-13

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: 66.98  E-value: 2.60e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213    723 VRFFNGTTNNNGLVRFRIQSIWHTACAENWTTQISNDVCQLLGLGSGNSSKP--IFPTDGGPFVKLNTAPDGHliLTPSQ 800
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsaYFGPGSGPIWLDNVRCSGT--EASLS 78

                            90
                    ....*....|....*.
gi 768021213    801 QCLQDSLIRLQCNHKS 816
Cdd:smart00202   79 DCPHSGWGSHNCSHGE 94
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 59-117 5.07e-13

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: 66.11  E-value: 5.07e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 768021213    59 RATFKITSgVTYNPNLQDKLSVDFKVLAFDLQQMIDEIFLSSNLKNEYKNSRVLQFDKN 117
Cdd:pfam01390    4 TGSFKITN-LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPD 61
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 688-722 1.71e-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: 62.22  E-value: 1.71e-12
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 768021213  688 CKADHFQCKNGECVPLVNLCDGHLHCEDGSDEADC 722
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 688-719 7.17e-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: 57.64  E-value: 7.17e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 768021213    688 CKADHFQCKNGECVPLVNLCDGHLHCEDGSDE 719
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
687-722 3.80e-10

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 55.72  E-value: 3.80e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 768021213   687 PCKADHFQCKNGECVPLVNLCDGHLHCEDGSDEADC 722
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
 744-818 8.54e-08

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: 51.18  E-value: 8.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213   744 WHTACAENWTTQISNDVCQLLGLGSGNSSKPIFPTDGGP-----FVKLNTAPDGHLI---LTPSQQCLQDSLIRLQCNHk 815
Cdd:pfam15494   16 WLPVCSDDWNPAYGRAACQQLGYLRLTHHKSVNLTDISSnssqsFMKLNSSSLNTDLyeaLQPRDSCSSGSVVSLRCSE- 94


                   ...
gi 768021213   816 sCG 818
Cdd:pfam15494   95 -CG 96
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 229-263 2.65e-06

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 44.89  E-value: 2.65e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 768021213  229 CLPGSSPCTDaLTCIKADLFCDGEVNCPDGSDEDN 263
Cdd:cd00112     1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEEN 34
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 228-261 2.37e-05

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


Pssm-ID: 197566  Cd Length: 33  Bit Score: 42.24  E-value: 2.37e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 768021213    228 ECLPGSSPCTDAlTCIKADLFCDGEVNCPDGSDE 261
Cdd:smart00192    1 TCPPGEFQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
229-263 1.64e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 37.23  E-value: 1.64e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 768021213   229 CLPGSSPCTDAlTCIKADLFCDGEVNCPDGSDEDN 263
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 ...
 830-1061 1.75e-101

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: 318.45  E-value: 1.75e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  830 IVGGSNAKEGAWPWVVGLYYG-GRLLCGASLVSSDWLVSAAHCVYGRNlePSKWTAILGLHMKSNLTSPQTVpRLIDEIV 908
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSNEGGGQV-IKVKKVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  909 INPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWGTVVYQGTTANILQEADVPLLSNERCQQ 988
Cdd:cd00190    78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021213  989 QMPE-YNITENMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLAGVTSFGYKCALPNRPGVYARVSRFTEWIQS 1061
Cdd:cd00190   158 AYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 829-1059 9.72e-98

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: 308.45  E-value: 9.72e-98
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213    829 KIVGGSNAKEGAWPWVVGLYY-GGRLLCGASLVSSDWLVSAAHCVYGRNlePSKWTAILGLHMKSNLTSPQTVPrlIDEI 907
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGSD--PSNIRVRLGSHDLSSGEEGQVIK--VSKV 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213    908 VINPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWG-TVVYQGTTANILQEADVPLLSNERC 986
Cdd:smart00020   77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGrTSEGAGSLPDTLQEVNVPIVSNATC 156

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021213    987 QQQMPEYN-ITENMICAGYEEGGIDSCQGDSGGPLMCQeNNRWFLAGVTSFGYKCALPNRPGVYARVSRFTEWI 1059
Cdd:smart00020  157 RRAYSGGGaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
830-1059 1.22e-74

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 245.43  E-value: 1.22e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213   830 IVGGSNAKEGAWPWVVGLYY-GGRLLCGASLVSSDWLVSAAHCVYGRnlepSKWTAILGLH-MKSNLTSPQTVPrlIDEI 907
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGA----SDVKVVLGAHnIVLREGGEQKFD--VEKI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213   908 VINPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWGTvVYQGTTANILQEADVPLLSNERCQ 987
Cdd:pfam00089   75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGN-TKTLGPSDTLQEVTVPVVSRETCR 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768021213   988 QQMPEYnITENMICAGYeeGGIDSCQGDSGGPLMCQENnrwFLAGVTSFGYKCALPNRPGVYARVSRFTEWI 1059
Cdd:pfam00089  154 SAYGGT-VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 822-1061 3.46e-71

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 237.63  E-value: 3.46e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  822 AAQDITPKIVGGSNAKEGAWPWVVGLYYGG---RLLCGASLVSSDWLVSAAHCVYGRNlePSKWTAILGLHmksNLTSPQ 898
Cdd:COG5640    23 PAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG--PSDLRVVIGST---DLSTSG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  899 TVPRLIDEIVINPHYNRRRKDNDIAMMHLEFKVnytDYIQPICLPEENQVFPPGRNCSIAGWG-TVVYQGTTANILQEAD 977
Cdd:COG5640    98 GTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGrTSEGPGSQSGTLRKAD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  978 VPLLSNERCQQqMPEYnITENMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLAGVTSFGY-KCAlPNRPGVYARVSRFT 1056
Cdd:COG5640   175 VPVVSDATCAA-YGGF-DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGgPCA-AGYPGVYTRVSAYR 251


                  ....*
gi 768021213 1057 EWIQS 1061
Cdd:COG5640   252 DWIKS 256
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 392-548 1.74e-50

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: 175.24  E-value: 1.74e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213   392 CNFEDG-FCFWVQDLNDDNEWERIQGstFSPFTGPNFDHTFGNASGFYISTPTGPGGRQERVGLLSLPLDPTLEPACLSF 470
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSG--PSVKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213   471 WYHMYGENVHKLSINI-SNDQNMEKTVFQKEGNYGDNWNYGQVTLNE-TVKFKVAFNA-FKNKILSDIALDDISLTYGIC 547
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVrENGGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGiRGGGSRGGIALDDISLSSGPC 158


                   .
gi 768021213   548 N 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 3.98e-50

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: 174.45  E-value: 3.98e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213    387 YEKINCNFEDG-FCFWVQDLNDDNEWERIQGSTFSpfTGPNFDHTFGNasGFYISTPTGPGGRQERVGLLSLPLDPTLEP 465
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSATGI--PGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213    466 ACLSFWYHMYGENVHKLSINISNDQNME-KTVFQKEGNYGDNWNYGQVTLN-ETVKFKVAFNAFKNK-ILSDIALDDISL 542
Cdd:smart00137   77 HCLTFWYYMYGSGSGTLNVYVRENNGSQdTLLWSRSGTQGGQWLQAEVALSsWPQPFQVVFEGTRGKgHSGYIALDDILL 156


                    ....*
gi 768021213    543 TYGIC 547
Cdd:smart00137  157 SNGPC 161
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 392-547 8.09e-49

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: 170.25  E-value: 8.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  392 CNFEDGFCFWVQDLNDDNEWERIQGSTFSPFTGPnfDHTFGNASGFYISTPTGPGGRQERVGLLSLPLDPTLEPACLSFW 471
Cdd:cd06263     1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSSHCLSFW 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768021213  472 YHMYGENVHKLSINI-SNDQNMEKTVFQKEGNYGDNWNYGQVTLNETVK-FKVAFNAFKNK-ILSDIALDDISLTYGIC 547
Cdd:cd06263    79 YHMYGSGVGTLNVYVrEEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSgSRGDIALDDISLSPGPC 157
CUB pfam00431
CUB domain;
569-676 8.66e-37

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 134.34  E-value: 8.66e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213   569 CGGpfELWEPNTTFSSTNFPNSYPNLAFCVWILNAQKGKNIQLHFQEFDLE----NINDVVEIRDGEEADSLLLAVYTGP 644
Cdd:pfam00431    1 CGG--VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 768021213   645 GPVKDVFSTTNRMTVLLITNDVLARGGFKANF 676
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB pfam00431
CUB domain;
270-376 9.46e-29

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 111.23  E-value: 9.46e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213   270 CDGRFllTGSSGSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYYT-----DILDIYEGVGSSKILRASIW-E 343
Cdd:pfam00431    1 CGGVL--TDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHdecgyDYVEIRDGPSASSPLLGRFCgS 78

                           90       100       110
                   ....*....|....*....|....*....|...
gi 768021213   344 TNPGTIRIFSNQVTATFLIeSDESDYVGFNATY 376
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVS-DASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 569-678 1.27e-27

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: 108.27  E-value: 1.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  569 CGGPFeLWEPNTTFSSTNFPNSYPNLAFCVWILNAQKGKNIQLHFQEFDLEN----INDVVEIRDGEEADSLLLAVYTGP 644
Cdd:cd00041     1 CGGTL-TASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLLGRFCGS 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 768021213  645 GPVKDVFSTTNRMTVLLITNDVLARGGFKANFTT 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 4.71e-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: 100.54  E-value: 4.71e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213    581 TFSSTNFPNSYPNLAFCVWILNAQKGKNIQLHFQEFDLENIN----DVVEIRDGEEADSLLLAVYTGPGPVKDVFST-TN 655
Cdd:smart00042    2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDnceyDYVEIYDGPSASSPLLGRFCGSEAPPPVISSsSN 81

                            90       100
                    ....*....|....*....|.
gi 768021213    656 RMTVLLITNDVLARGGFKANF 676
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 53-195 5.97e-21

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: 89.39  E-value: 5.97e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213     53 GQSHEARATFKITSG--VTYNPNLQDKLSVDFKVLAFDLQQMIDEIFLSSNLKNEYKNSRVLQFDknwrqaenevestvs 130
Cdd:smart00200    2 TQSFGVSLSVLSVEGenLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFR--------------- 66

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768021213    131 lyslygswihqkyqkNGSIIVVFDLFFAQWV-SDENVKEELIQGLEANKSSQLVTfhiDLNSVDIL 195
Cdd:smart00200   67 ---------------NGSVVVDLGLLFNEGVtNGQDVEEDLLQVIKQAAYSLKIT---NVNVVDVL 114
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 270-378 4.05e-16

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: 75.14  E-value: 4.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  270 CDGRFLLTgSSGSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYY-----TDILDIYEGVGSSKILRASIW-E 343
Cdd:cd00041     1 CGGTLTAS-TSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncsYDYLEIYDGPSTSSPLLGRFCgS 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 768021213  344 TNPGTIRIFSNQVTATFLieSDESD-YVGFNATYTA 378
Cdd:cd00041    80 TLPPPIISSGNSLTVRFR--SDSSVtGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 281-376 2.70e-14

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: 69.73  E-value: 2.70e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213    281 GSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYYT-----DILDIYEG--VGSSKILRASIWETNPGTIRIFS 353
Cdd:smart00042    1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSdnceyDYVEIYDGpsASSPLLGRFCGSEAPPPVISSSS 80

                            90       100
                    ....*....|....*....|....
gi 768021213    354 NQVTATFLieSDESD-YVGFNATY 376
Cdd:smart00042   81 NSLTLTFV--SDSSVqKRGFSARY 102
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 723-816 2.60e-13

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: 66.98  E-value: 2.60e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213    723 VRFFNGTTNNNGLVRFRIQSIWHTACAENWTTQISNDVCQLLGLGSGNSSKP--IFPTDGGPFVKLNTAPDGHliLTPSQ 800
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsaYFGPGSGPIWLDNVRCSGT--EASLS 78

                            90
                    ....*....|....*.
gi 768021213    801 QCLQDSLIRLQCNHKS 816
Cdd:smart00202   79 DCPHSGWGSHNCSHGE 94
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 59-117 5.07e-13

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: 66.11  E-value: 5.07e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 768021213    59 RATFKITSgVTYNPNLQDKLSVDFKVLAFDLQQMIDEIFLSSNLKNEYKNSRVLQFDKN 117
Cdd:pfam01390    4 TGSFKITN-LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPD 61
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 688-722 1.71e-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: 62.22  E-value: 1.71e-12
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 768021213  688 CKADHFQCKNGECVPLVNLCDGHLHCEDGSDEADC 722
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 688-719 7.17e-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: 57.64  E-value: 7.17e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 768021213    688 CKADHFQCKNGECVPLVNLCDGHLHCEDGSDE 719
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
687-722 3.80e-10

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 55.72  E-value: 3.80e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 768021213   687 PCKADHFQCKNGECVPLVNLCDGHLHCEDGSDEADC 722
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
 744-818 8.54e-08

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: 51.18  E-value: 8.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213   744 WHTACAENWTTQISNDVCQLLGLGSGNSSKPIFPTDGGP-----FVKLNTAPDGHLI---LTPSQQCLQDSLIRLQCNHk 815
Cdd:pfam15494   16 WLPVCSDDWNPAYGRAACQQLGYLRLTHHKSVNLTDISSnssqsFMKLNSSSLNTDLyeaLQPRDSCSSGSVVSLRCSE- 94


                   ...
gi 768021213   816 sCG 818
Cdd:pfam15494   95 -CG 96
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 849-1038 2.13e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 52.37  E-value: 2.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  849 YGGRLLCGASLVSSDWLVSAAHCVYGRNLE--PSKWTAILGLHMKSNLTSPQTvprlidEIVINPHY-NRRRKDNDIAMM 925
Cdd:COG3591     8 DGGGGVCTGTLIGPNLVLTAGHCVYDGAGGgwATNIVFVPGYNGGPYGTATAT------RFRVPPGWvASGDAGYDYALL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021213  926 HLEfkvnytdyiQPIclPEENQVFPPGrncsiagWGTVVYQGTTANILQ-EADVPLLSNERCQQQMpeYNITENMIcaGY 1004
Cdd:COG3591    82 RLD---------EPL--GDTTGWLGLA-------FNDAPLAGEPVTIIGyPGDRPKDLSLDCSGRV--TGVQGNRL--SY 139

                         170       180       190
                  ....*....|....*....|....*....|....
gi 768021213 1005 eegGIDSCQGDSGGPLMCQENNRWFLAGVTSFGY 1038
Cdd:COG3591   140 ---DCDTTGGSSGSPVLDDSDGGGRVVGVHSAGG 170
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 229-263 2.65e-06

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 44.89  E-value: 2.65e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 768021213  229 CLPGSSPCTDaLTCIKADLFCDGEVNCPDGSDEDN 263
Cdd:cd00112     1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEEN 34
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 228-261 2.37e-05

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


Pssm-ID: 197566  Cd Length: 33  Bit Score: 42.24  E-value: 2.37e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 768021213    228 ECLPGSSPCTDAlTCIKADLFCDGEVNCPDGSDE 261
Cdd:smart00192    1 TCPPGEFQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 728-769 1.41e-03

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: 38.90  E-value: 1.41e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 768021213   728 GTTNNNGLVRFRIQSIWHTACAENWTTQISNDVCQLLGLGSG 769
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGA 42
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
229-263 1.64e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 37.23  E-value: 1.64e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 768021213   229 CLPGSSPCTDAlTCIKADLFCDGEVNCPDGSDEDN 263
Cdd:pfam00057    3 CSPNEFQCGSG-ECIPRSWVCDGDPDCGDGSDEEN 36
 
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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