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Conserved domains on  [gi|1519314416|ref|NP_002763|]
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enteropeptidase isoform 2 precursor [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 ...
 785-1016 1.03e-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: 1.03e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  785 IVGGSNAKEGAWPWVVGLYYG-GRLLCGASLVSSDWLVSAAHCVYGRNlePSKWTAILGLHMKSNLTSPQTVpRLIDEIV 863
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSNEGGGQV-IKVKKVI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  864 INPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWGTVVYQGTTANILQEADVPLLSNERCQQ 943
Cdd:cd00190     78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519314416  944 QMPE-YNITENMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLAGVTSFGYKCALPNRPGVYARVSRFTEWIQS 1016
Cdd:cd00190    158 AYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 347-503 1.40e-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: 1.40e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  347 CNFEDG-FCFWVQDLNDDNEWERIQGstFSPFTGPNFDHTFGNASGFYISTPTGPGGRQERVGLLSLPLDPTLEPACLSF 425
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSG--PSVKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  426 WYHMYGENVHKLSINI-SNDQNMEKTVFQKEGNYGDNWNYGQVTLNE-TVKFKVAFNA-FKNKILSDIALDDISLTYGIC 502
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVrENGGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGiRGGGSRGGIALDDISLSSGPC 158


                   .
gi 1519314416  503 N 503
Cdd:pfam00629  159 P 159
CUB pfam00431
CUB domain;
524-631 8.27e-37

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 134.34  E-value: 8.27e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  524 CGGpfELWEPNTTFSSTNFPNSYPNLAFCVWILNAQKGKNIQLHFQEFDLE----NINDVVEIRDGEEADSLLLAVYTGP 599
Cdd:pfam00431    1 CGG--VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1519314416  600 GPVKDVFSTTNRMTVLLITNDVLARGGFKANF 631
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 53-172 7.14e-29

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: 111.73  E-value: 7.14e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416    53 GQSHEARATFKITSG--VTYNPNLQDKLSVDFKVLAFDLQQMIDEIFLSSNLKNEYKNSRVLQFENGSIIVVFDLFFAQW 130
Cdd:smart00200    2 TQSFGVSLSVLSVEGenLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNEG 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1519314416   131 V-SDENVKEELIQGLEANKSSQLVTfhiDLNSVDILDKLTTTS 172
Cdd:smart00200   82 VtNGQDVEEDLLQVIKQAAYSLKIT---NVNVVDVLDPDSADS 121
CUB pfam00431
CUB domain;
225-331 9.04e-29

CUB domain;


:

Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 111.23  E-value: 9.04e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  225 CDGRFllTGSSGSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYYT-----DILDIYEGVGSSKILRASIW-E 298
Cdd:pfam00431    1 CGGVL--TDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHdecgyDYVEIRDGPSASSPLLGRFCgS 78

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1519314416  299 TNPGTIRIFSNQVTATFLIeSDESDYVGFNATY 331
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVS-DASVQKRGFKATY 110
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 678-771 2.71e-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: 66.60  E-value: 2.71e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   678 VRFFNGTTNNNGLVRFRIQSIWHTACAENWTTQISNDVCQLLGLGSGNSSKP--IFPTDGGPFVKLNTAPDGHliLTPSQ 755
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsaYFGPGSGPIWLDNVRCSGT--EASLS 78

                            90
                    ....*....|....*.
gi 1519314416   756 QCLQDSLIRLQCNHKS 771
Cdd:smart00202   79 DCPHSGWGSHNCSHGE 94
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 643-677 2.33e-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: 61.84  E-value: 2.33e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1519314416  643 CKADHFQCKNGECVPLVNLCDGHLHCEDGSDEADC 677
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 184-218 3.55e-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: 44.50  E-value: 3.55e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1519314416  184 CLPGSSPCTDaLTCIKADLFCDGEVNCPDGSDEDN 218
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 ...
 785-1016 1.03e-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: 1.03e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  785 IVGGSNAKEGAWPWVVGLYYG-GRLLCGASLVSSDWLVSAAHCVYGRNlePSKWTAILGLHMKSNLTSPQTVpRLIDEIV 863
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSNEGGGQV-IKVKKVI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  864 INPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWGTVVYQGTTANILQEADVPLLSNERCQQ 943
Cdd:cd00190     78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519314416  944 QMPE-YNITENMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLAGVTSFGYKCALPNRPGVYARVSRFTEWIQS 1016
Cdd:cd00190    158 AYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 784-1014 5.68e-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: 5.68e-98
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   784 KIVGGSNAKEGAWPWVVGLYY-GGRLLCGASLVSSDWLVSAAHCVYGRNlePSKWTAILGLHMKSNLTSPQTVPrlIDEI 862
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGSD--PSNIRVRLGSHDLSSGEEGQVIK--VSKV 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   863 VINPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWG-TVVYQGTTANILQEADVPLLSNERC 941
Cdd:smart00020   77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGrTSEGAGSLPDTLQEVNVPIVSNATC 156

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519314416   942 QQQMPEYN-ITENMICAGYEEGGIDSCQGDSGGPLMCQeNNRWFLAGVTSFGYKCALPNRPGVYARVSRFTEWI 1014
Cdd:smart00020  157 RRAYSGGGaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
785-1014 1.09e-74

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 245.04  E-value: 1.09e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  785 IVGGSNAKEGAWPWVVGLYY-GGRLLCGASLVSSDWLVSAAHCVYGRnlepSKWTAILGLH-MKSNLTSPQTVPrlIDEI 862
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGA----SDVKVVLGAHnIVLREGGEQKFD--VEKI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  863 VINPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWGTvVYQGTTANILQEADVPLLSNERCQ 942
Cdd:pfam00089   75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGN-TKTLGPSDTLQEVTVPVVSRETCR 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519314416  943 QQMPEYnITENMICAGYeeGGIDSCQGDSGGPLMCQENnrwFLAGVTSFGYKCALPNRPGVYARVSRFTEWI 1014
Cdd:pfam00089  154 SAYGGT-VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 777-1016 2.45e-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: 2.45e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  777 AAQDITPKIVGGSNAKEGAWPWVVGLYYGG---RLLCGASLVSSDWLVSAAHCVYGRNlePSKWTAILGLHmksNLTSPQ 853
Cdd:COG5640     23 PAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG--PSDLRVVIGST---DLSTSG 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  854 TVPRLIDEIVINPHYNRRRKDNDIAMMHLEFKVnytDYIQPICLPEENQVFPPGRNCSIAGWG-TVVYQGTTANILQEAD 932
Cdd:COG5640     98 GTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGrTSEGPGSQSGTLRKAD 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  933 VPLLSNERCQQqMPEYnITENMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLAGVTSFGY-KCAlPNRPGVYARVSRFT 1011
Cdd:COG5640    175 VPVVSDATCAA-YGGF-DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGgPCA-AGYPGVYTRVSAYR 251


                   ....*
gi 1519314416 1012 EWIQS 1016
Cdd:COG5640    252 DWIKS 256
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 347-503 1.40e-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: 1.40e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  347 CNFEDG-FCFWVQDLNDDNEWERIQGstFSPFTGPNFDHTFGNASGFYISTPTGPGGRQERVGLLSLPLDPTLEPACLSF 425
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSG--PSVKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  426 WYHMYGENVHKLSINI-SNDQNMEKTVFQKEGNYGDNWNYGQVTLNE-TVKFKVAFNA-FKNKILSDIALDDISLTYGIC 502
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVrENGGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGiRGGGSRGGIALDDISLSSGPC 158


                   .
gi 1519314416  503 N 503
Cdd:pfam00629  159 P 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 342-502 3.33e-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: 3.33e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   342 YEKINCNFEDG-FCFWVQDLNDDNEWERIQGSTFSpfTGPNFDHTFGNasGFYISTPTGPGGRQERVGLLSLPLDPTLEP 420
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSATGI--PGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   421 ACLSFWYHMYGENVHKLSINISNDQNME-KTVFQKEGNYGDNWNYGQVTLN-ETVKFKVAFNAFKNK-ILSDIALDDISL 497
Cdd:smart00137   77 HCLTFWYYMYGSGSGTLNVYVRENNGSQdTLLWSRSGTQGGQWLQAEVALSsWPQPFQVVFEGTRGKgHSGYIALDDILL 156


                    ....*
gi 1519314416   498 TYGIC 502
Cdd:smart00137  157 SNGPC 161
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 347-502 6.68e-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: 170.64  E-value: 6.68e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  347 CNFEDGFCFWVQDLNDDNEWERIQGSTFSPFTGPnfDHTFGNASGFYISTPTGPGGRQERVGLLSLPLDPTLEPACLSFW 426
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSSHCLSFW 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519314416  427 YHMYGENVHKLSINI-SNDQNMEKTVFQKEGNYGDNWNYGQVTLNETVK-FKVAFNAFKNK-ILSDIALDDISLTYGIC 502
Cdd:cd06263     79 YHMYGSGVGTLNVYVrEEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSgSRGDIALDDISLSPGPC 157
CUB pfam00431
CUB domain;
524-631 8.27e-37

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 134.34  E-value: 8.27e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  524 CGGpfELWEPNTTFSSTNFPNSYPNLAFCVWILNAQKGKNIQLHFQEFDLE----NINDVVEIRDGEEADSLLLAVYTGP 599
Cdd:pfam00431    1 CGG--VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1519314416  600 GPVKDVFSTTNRMTVLLITNDVLARGGFKANF 631
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 53-172 7.14e-29

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: 111.73  E-value: 7.14e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416    53 GQSHEARATFKITSG--VTYNPNLQDKLSVDFKVLAFDLQQMIDEIFLSSNLKNEYKNSRVLQFENGSIIVVFDLFFAQW 130
Cdd:smart00200    2 TQSFGVSLSVLSVEGenLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNEG 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1519314416   131 V-SDENVKEELIQGLEANKSSQLVTfhiDLNSVDILDKLTTTS 172
Cdd:smart00200   82 VtNGQDVEEDLLQVIKQAAYSLKIT---NVNVVDVLDPDSADS 121
CUB pfam00431
CUB domain;
225-331 9.04e-29

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 111.23  E-value: 9.04e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  225 CDGRFllTGSSGSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYYT-----DILDIYEGVGSSKILRASIW-E 298
Cdd:pfam00431    1 CGGVL--TDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHdecgyDYVEIRDGPSASSPLLGRFCgS 78

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1519314416  299 TNPGTIRIFSNQVTATFLIeSDESDYVGFNATY 331
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVS-DASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 524-633 1.21e-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: 1.21e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  524 CGGPFeLWEPNTTFSSTNFPNSYPNLAFCVWILNAQKGKNIQLHFQEFDLEN----INDVVEIRDGEEADSLLLAVYTGP 599
Cdd:cd00041      1 CGGTL-TASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLLGRFCGS 79

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1519314416  600 GPVKDVFSTTNRMTVLLITNDVLARGGFKANFTT 633
Cdd:cd00041     80 TLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 536-631 4.21e-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: 4.21e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   536 TFSSTNFPNSYPNLAFCVWILNAQKGKNIQLHFQEFDLENIN----DVVEIRDGEEADSLLLAVYTGPGPVKDVFST-TN 610
Cdd:smart00042    2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDnceyDYVEIYDGPSASSPLLGRFCGSEAPPPVISSsSN 81

                            90       100
                    ....*....|....*....|.
gi 1519314416   611 RMTVLLITNDVLARGGFKANF 631
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 225-333 3.94e-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: 3.94e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  225 CDGRFLLTgSSGSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYY-----TDILDIYEGVGSSKILRASIW-E 298
Cdd:cd00041      1 CGGTLTAS-TSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncsYDYLEIYDGPSTSSPLLGRFCgS 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1519314416  299 TNPGTIRIFSNQVTATFLieSDESD-YVGFNATYTA 333
Cdd:cd00041     80 TLPPPIISSGNSLTVRFR--SDSSVtGRGFKATYSA 113
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 59-151 4.79e-16

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: 74.58  E-value: 4.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   59 RATFKITSgVTYNPNLQDKLSVDFKVLAFDLQQMIDEIFLSSNLKNEYKNSRVLQF--ENGSIIVVFDLFFAQWVSD--- 133
Cdd:pfam01390    4 TGSFKITN-LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLrpDGGSVVVDVVLVFRFPSTEpal 82

                           90       100
                   ....*....|....*....|
gi 1519314416  134 --ENVKEELIQglEANKSSQ 151
Cdd:pfam01390   83 drEKLIEEILR--QTLNNTT 100
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 236-331 2.44e-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: 2.44e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   236 GSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYYT-----DILDIYEG--VGSSKILRASIWETNPGTIRIFS 308
Cdd:smart00042    1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSdnceyDYVEIYDGpsASSPLLGRFCGSEAPPPVISSSS 80

                            90       100
                    ....*....|....*....|....
gi 1519314416   309 NQVTATFLieSDESD-YVGFNATY 331
Cdd:smart00042   81 NSLTLTFV--SDSSVqKRGFSARY 102
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 678-771 2.71e-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: 66.60  E-value: 2.71e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   678 VRFFNGTTNNNGLVRFRIQSIWHTACAENWTTQISNDVCQLLGLGSGNSSKP--IFPTDGGPFVKLNTAPDGHliLTPSQ 755
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsaYFGPGSGPIWLDNVRCSGT--EASLS 78

                            90
                    ....*....|....*.
gi 1519314416   756 QCLQDSLIRLQCNHKS 771
Cdd:smart00202   79 DCPHSGWGSHNCSHGE 94
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 643-677 2.33e-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: 61.84  E-value: 2.33e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1519314416  643 CKADHFQCKNGECVPLVNLCDGHLHCEDGSDEADC 677
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 643-674 9.97e-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: 57.26  E-value: 9.97e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1519314416   643 CKADHFQCKNGECVPLVNLCDGHLHCEDGSDE 674
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
642-677 4.56e-10

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 55.33  E-value: 4.56e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1519314416  642 PCKADHFQCKNGECVPLVNLCDGHLHCEDGSDEADC 677
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
 699-773 6.92e-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: 6.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  699 WHTACAENWTTQISNDVCQLLGLGSGNSSKPIFPTDGGP-----FVKLNTAPDGHLI---LTPSQQCLQDSLIRLQCNHk 770
Cdd:pfam15494   16 WLPVCSDDWNPAYGRAACQQLGYLRLTHHKSVNLTDISSnssqsFMKLNSSSLNTDLyeaLQPRDSCSSGSVVSLRCSE- 94


                   ...
gi 1519314416  771 sCG 773
Cdd:pfam15494   95 -CG 96
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 184-218 3.55e-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: 44.50  E-value: 3.55e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1519314416  184 CLPGSSPCTDaLTCIKADLFCDGEVNCPDGSDEDN 218
Cdd:cd00112      1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEEN 34
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 183-216 3.04e-05

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


Pssm-ID: 197566  Cd Length: 33  Bit Score: 41.85  E-value: 3.04e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1519314416   183 ECLPGSSPCTDAlTCIKADLFCDGEVNCPDGSDE 216
Cdd:smart00192    1 TCPPGEFQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
184-218 1.91e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 36.84  E-value: 1.91e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1519314416  184 CLPGSSPCTDAlTCIKADLFCDGEVNCPDGSDEDN 218
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 ...
 785-1016 1.03e-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: 1.03e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  785 IVGGSNAKEGAWPWVVGLYYG-GRLLCGASLVSSDWLVSAAHCVYGRNlePSKWTAILGLHMKSNLTSPQTVpRLIDEIV 863
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSNEGGGQV-IKVKKVI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  864 INPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWGTVVYQGTTANILQEADVPLLSNERCQQ 943
Cdd:cd00190     78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519314416  944 QMPE-YNITENMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLAGVTSFGYKCALPNRPGVYARVSRFTEWIQS 1016
Cdd:cd00190    158 AYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 784-1014 5.68e-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: 5.68e-98
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   784 KIVGGSNAKEGAWPWVVGLYY-GGRLLCGASLVSSDWLVSAAHCVYGRNlePSKWTAILGLHMKSNLTSPQTVPrlIDEI 862
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGSD--PSNIRVRLGSHDLSSGEEGQVIK--VSKV 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   863 VINPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWG-TVVYQGTTANILQEADVPLLSNERC 941
Cdd:smart00020   77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGrTSEGAGSLPDTLQEVNVPIVSNATC 156

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519314416   942 QQQMPEYN-ITENMICAGYEEGGIDSCQGDSGGPLMCQeNNRWFLAGVTSFGYKCALPNRPGVYARVSRFTEWI 1014
Cdd:smart00020  157 RRAYSGGGaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
785-1014 1.09e-74

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 245.04  E-value: 1.09e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  785 IVGGSNAKEGAWPWVVGLYY-GGRLLCGASLVSSDWLVSAAHCVYGRnlepSKWTAILGLH-MKSNLTSPQTVPrlIDEI 862
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGA----SDVKVVLGAHnIVLREGGEQKFD--VEKI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  863 VINPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWGTvVYQGTTANILQEADVPLLSNERCQ 942
Cdd:pfam00089   75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGN-TKTLGPSDTLQEVTVPVVSRETCR 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519314416  943 QQMPEYnITENMICAGYeeGGIDSCQGDSGGPLMCQENnrwFLAGVTSFGYKCALPNRPGVYARVSRFTEWI 1014
Cdd:pfam00089  154 SAYGGT-VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 777-1016 2.45e-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: 2.45e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  777 AAQDITPKIVGGSNAKEGAWPWVVGLYYGG---RLLCGASLVSSDWLVSAAHCVYGRNlePSKWTAILGLHmksNLTSPQ 853
Cdd:COG5640     23 PAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG--PSDLRVVIGST---DLSTSG 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  854 TVPRLIDEIVINPHYNRRRKDNDIAMMHLEFKVnytDYIQPICLPEENQVFPPGRNCSIAGWG-TVVYQGTTANILQEAD 932
Cdd:COG5640     98 GTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGrTSEGPGSQSGTLRKAD 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  933 VPLLSNERCQQqMPEYnITENMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLAGVTSFGY-KCAlPNRPGVYARVSRFT 1011
Cdd:COG5640    175 VPVVSDATCAA-YGGF-DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGgPCA-AGYPGVYTRVSAYR 251


                   ....*
gi 1519314416 1012 EWIQS 1016
Cdd:COG5640    252 DWIKS 256
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 347-503 1.40e-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: 1.40e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  347 CNFEDG-FCFWVQDLNDDNEWERIQGstFSPFTGPNFDHTFGNASGFYISTPTGPGGRQERVGLLSLPLDPTLEPACLSF 425
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSG--PSVKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  426 WYHMYGENVHKLSINI-SNDQNMEKTVFQKEGNYGDNWNYGQVTLNE-TVKFKVAFNA-FKNKILSDIALDDISLTYGIC 502
Cdd:pfam00629   79 WYHMSGSGVGTLRVYVrENGGTLDTLLWSISGDQGPSWKEARVTLSSsTQPFQVVFEGiRGGGSRGGIALDDISLSSGPC 158


                   .
gi 1519314416  503 N 503
Cdd:pfam00629  159 P 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 342-502 3.33e-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: 3.33e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   342 YEKINCNFEDG-FCFWVQDLNDDNEWERIQGSTFSpfTGPNFDHTFGNasGFYISTPTGPGGRQERVGLLSLPLDPTLEP 420
Cdd:smart00137    1 TSPGNCDFEEGsTCGWHQDSNDDGHWERVSSATGI--PGPNRDHTTGN--GHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   421 ACLSFWYHMYGENVHKLSINISNDQNME-KTVFQKEGNYGDNWNYGQVTLN-ETVKFKVAFNAFKNK-ILSDIALDDISL 497
Cdd:smart00137   77 HCLTFWYYMYGSGSGTLNVYVRENNGSQdTLLWSRSGTQGGQWLQAEVALSsWPQPFQVVFEGTRGKgHSGYIALDDILL 156


                    ....*
gi 1519314416   498 TYGIC 502
Cdd:smart00137  157 SNGPC 161
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 347-502 6.68e-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: 170.64  E-value: 6.68e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  347 CNFEDGFCFWVQDLNDDNEWERIQGSTFSPFTGPnfDHTFGNASGFYISTPTGPGGRQERVGLLSLPLDPTLEPACLSFW 426
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPP--DHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSSHCLSFW 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519314416  427 YHMYGENVHKLSINI-SNDQNMEKTVFQKEGNYGDNWNYGQVTLNETVK-FKVAFNAFKNK-ILSDIALDDISLTYGIC 502
Cdd:cd06263     79 YHMYGSGVGTLNVYVrEEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSgSRGDIALDDISLSPGPC 157
CUB pfam00431
CUB domain;
524-631 8.27e-37

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 134.34  E-value: 8.27e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  524 CGGpfELWEPNTTFSSTNFPNSYPNLAFCVWILNAQKGKNIQLHFQEFDLE----NINDVVEIRDGEEADSLLLAVYTGP 599
Cdd:pfam00431    1 CGG--VLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1519314416  600 GPVKDVFSTTNRMTVLLITNDVLARGGFKANF 631
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
 53-172 7.14e-29

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: 111.73  E-value: 7.14e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416    53 GQSHEARATFKITSG--VTYNPNLQDKLSVDFKVLAFDLQQMIDEIFLSSNLKNEYKNSRVLQFENGSIIVVFDLFFAQW 130
Cdd:smart00200    2 TQSFGVSLSVLSVEGenLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNEG 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1519314416   131 V-SDENVKEELIQGLEANKSSQLVTfhiDLNSVDILDKLTTTS 172
Cdd:smart00200   82 VtNGQDVEEDLLQVIKQAAYSLKIT---NVNVVDVLDPDSADS 121
CUB pfam00431
CUB domain;
225-331 9.04e-29

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 111.23  E-value: 9.04e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  225 CDGRFllTGSSGSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYYT-----DILDIYEGVGSSKILRASIW-E 298
Cdd:pfam00431    1 CGGVL--TDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHdecgyDYVEIRDGPSASSPLLGRFCgS 78

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1519314416  299 TNPGTIRIFSNQVTATFLIeSDESDYVGFNATY 331
Cdd:pfam00431   79 GIPEDIVSSSNQMTIKFVS-DASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 524-633 1.21e-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: 1.21e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  524 CGGPFeLWEPNTTFSSTNFPNSYPNLAFCVWILNAQKGKNIQLHFQEFDLEN----INDVVEIRDGEEADSLLLAVYTGP 599
Cdd:cd00041      1 CGGTL-TASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLLGRFCGS 79

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1519314416  600 GPVKDVFSTTNRMTVLLITNDVLARGGFKANFTT 633
Cdd:cd00041     80 TLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 536-631 4.21e-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: 4.21e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   536 TFSSTNFPNSYPNLAFCVWILNAQKGKNIQLHFQEFDLENIN----DVVEIRDGEEADSLLLAVYTGPGPVKDVFST-TN 610
Cdd:smart00042    2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDnceyDYVEIYDGPSASSPLLGRFCGSEAPPPVISSsSN 81

                            90       100
                    ....*....|....*....|.
gi 1519314416   611 RMTVLLITNDVLARGGFKANF 631
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 225-333 3.94e-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: 3.94e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  225 CDGRFLLTgSSGSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYY-----TDILDIYEGVGSSKILRASIW-E 298
Cdd:cd00041      1 CGGTLTAS-TSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncsYDYLEIYDGPSTSSPLLGRFCgS 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1519314416  299 TNPGTIRIFSNQVTATFLieSDESD-YVGFNATYTA 333
Cdd:cd00041     80 TLPPPIISSGNSLTVRFR--SDSSVtGRGFKATYSA 113
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 59-151 4.79e-16

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: 74.58  E-value: 4.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   59 RATFKITSgVTYNPNLQDKLSVDFKVLAFDLQQMIDEIFLSSNLKNEYKNSRVLQF--ENGSIIVVFDLFFAQWVSD--- 133
Cdd:pfam01390    4 TGSFKITN-LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLrpDGGSVVVDVVLVFRFPSTEpal 82

                           90       100
                   ....*....|....*....|
gi 1519314416  134 --ENVKEELIQglEANKSSQ 151
Cdd:pfam01390   83 drEKLIEEILR--QTLNNTT 100
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 236-331 2.44e-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: 2.44e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   236 GSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYYT-----DILDIYEG--VGSSKILRASIWETNPGTIRIFS 308
Cdd:smart00042    1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSdnceyDYVEIYDGpsASSPLLGRFCGSEAPPPVISSSS 80

                            90       100
                    ....*....|....*....|....
gi 1519314416   309 NQVTATFLieSDESD-YVGFNATY 331
Cdd:smart00042   81 NSLTLTFV--SDSSVqKRGFSARY 102
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 678-771 2.71e-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: 66.60  E-value: 2.71e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   678 VRFFNGTTNNNGLVRFRIQSIWHTACAENWTTQISNDVCQLLGLGSGNSSKP--IFPTDGGPFVKLNTAPDGHliLTPSQ 755
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsaYFGPGSGPIWLDNVRCSGT--EASLS 78

                            90
                    ....*....|....*.
gi 1519314416   756 QCLQDSLIRLQCNHKS 771
Cdd:smart00202   79 DCPHSGWGSHNCSHGE 94
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 643-677 2.33e-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: 61.84  E-value: 2.33e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1519314416  643 CKADHFQCKNGECVPLVNLCDGHLHCEDGSDEADC 677
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 643-674 9.97e-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: 57.26  E-value: 9.97e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1519314416   643 CKADHFQCKNGECVPLVNLCDGHLHCEDGSDE 674
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
642-677 4.56e-10

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 55.33  E-value: 4.56e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1519314416  642 PCKADHFQCKNGECVPLVNLCDGHLHCEDGSDEADC 677
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
 699-773 6.92e-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: 6.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  699 WHTACAENWTTQISNDVCQLLGLGSGNSSKPIFPTDGGP-----FVKLNTAPDGHLI---LTPSQQCLQDSLIRLQCNHk 770
Cdd:pfam15494   16 WLPVCSDDWNPAYGRAACQQLGYLRLTHHKSVNLTDISSnssqsFMKLNSSSLNTDLyeaLQPRDSCSSGSVVSLRCSE- 94


                   ...
gi 1519314416  771 sCG 773
Cdd:pfam15494   95 -CG 96
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 804-993 2.12e-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: 2.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  804 YGGRLLCGASLVSSDWLVSAAHCVYGRNLE--PSKWTAILGLHMKSNLTSPQTvprlidEIVINPHY-NRRRKDNDIAMM 880
Cdd:COG3591      8 DGGGGVCTGTLIGPNLVLTAGHCVYDGAGGgwATNIVFVPGYNGGPYGTATAT------RFRVPPGWvASGDAGYDYALL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  881 HLEfkvnytdyiQPIclPEENQVFPPGrncsiagWGTVVYQGTTANILQ-EADVPLLSNERCQQQMpeYNITENMIcaGY 959
Cdd:COG3591     82 RLD---------EPL--GDTTGWLGLA-------FNDAPLAGEPVTIIGyPGDRPKDLSLDCSGRV--TGVQGNRL--SY 139

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1519314416  960 eegGIDSCQGDSGGPLMCQENNRWFLAGVTSFGY 993
Cdd:COG3591    140 ---DCDTTGGSSGSPVLDDSDGGGRVVGVHSAGG 170
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 184-218 3.55e-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: 44.50  E-value: 3.55e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1519314416  184 CLPGSSPCTDaLTCIKADLFCDGEVNCPDGSDEDN 218
Cdd:cd00112      1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEEN 34
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 183-216 3.04e-05

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


Pssm-ID: 197566  Cd Length: 33  Bit Score: 41.85  E-value: 3.04e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1519314416   183 ECLPGSSPCTDAlTCIKADLFCDGEVNCPDGSDE 216
Cdd:smart00192    1 TCPPGEFQCDNG-RCIPSSWVCDGVDDCGDGSDE 33
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 683-724 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 1519314416  683 GTTNNNGLVRFRIQSIWHTACAENWTTQISNDVCQLLGLGSG 724
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGA 42
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
184-218 1.91e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 36.84  E-value: 1.91e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1519314416  184 CLPGSSPCTDAlTCIKADLFCDGEVNCPDGSDEDN 218
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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