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Conserved domains on  [gi|1519314416|ref|NP_002763|]
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enteropeptidase precursor [Homo sapiens]

Protein Classification

MAM and Tryp_SPc domain-containing protein (domain architecture ID 12193331)

protein containing domains SEA, MAM, CUB, and Tryp_SPc

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
785-1016 8.78e-102

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  Cd Length: 232  Bit Score: 318.45  E-value: 8.78e-102
                           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 8.47e-52

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: 334181  Cd Length: 160  Bit Score: 178.72  E-value: 8.47e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  347 CNFEDG-FCFWVQDLNDDNEWERIQGSTFSPFTGPNFDHTFgNASGFYISTPTGPGGRQERVGLLSLPLDPTLEPACLSF 425
Cdd:pfam00629    1 CDFEDGnLCGWTQDTSDDFDWSRGSGSTPTVKTGPSGDHTT-NGSGHYMYVDTSSAAPGQTARLLSPLLPPPRSPHCLRF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  426 WYHMYGENVHKLSINI-SNDQNMEKTVFQKEGNYGDNWNYGQVTLNE-TVKFKVAFNA-FKNKILSDIALDDISLTYGIC 502
Cdd:pfam00629   80 WYHMSGSGVGTLNVYLrENGGTLGTLLWSISGNQGPSWQEAEVTLSSfTKPFQVVFEGiRGGGSRGDIALDDISLSSGPC 159

                   .
gi 1519314416  503 N 503
Cdd:pfam00629  160 P 160
CUB pfam00431
CUB domain;
524-631 7.06e-37

CUB domain;


:

Pssm-ID: 278839  Cd Length: 110  Bit Score: 134.34  E-value: 7.06e-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 6.10e-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: 6.10e-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 7.71e-29

CUB domain;


:

Pssm-ID: 278839  Cd Length: 110  Bit Score: 111.23  E-value: 7.71e-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 ucrhin egg peptide speract contains 4 repeats of SR ...
678-771 2.32e-13

Scavenger receptor Cys-rich; The sea ucrhin 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  Cd Length: 101  Bit Score: 66.60  E-value: 2.32e-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 1.99e-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: 1.99e-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 3.02e-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: 3.02e-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 8.78e-102

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  Cd Length: 232  Bit Score: 318.45  E-value: 8.78e-102
                           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 4.85e-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: 4.85e-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 5.69e-75

Trypsin;


Pssm-ID: 333831  Cd Length: 219  Bit Score: 245.81  E-value: 5.69e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  785 IVGGSNAKEGAWPWVVGLYY-GGRLLCGASLVSSDWLVSAAHCVYGRnlepSKWTAILGLH-MKSNLTSPQTVPrlIDEI 862
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGS----SDVQVVLGEHnIVLREGGEQKFD--VEKV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  863 VINPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWGTvVYQGTTANILQEADVPLLSNERCQ 942
Cdd:pfam00089   75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDAGSDLPVGTTCTVSGWGN-TKTLGRPDTLQEVTVPVVSRETCR 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519314416  943 QQMPEYnITENMICAGYeeGGIDSCQGDSGGPLMCQENnrwFLAGVTSFGYKCALPNRPGVYARVSRFTEWI 1014
Cdd:pfam00089  154 SAYGGT-VTDNMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNKPGVYTRVSSYLDWI 219
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
347-503 8.47e-52

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: 334181  Cd Length: 160  Bit Score: 178.72  E-value: 8.47e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  347 CNFEDG-FCFWVQDLNDDNEWERIQGSTFSPFTGPNFDHTFgNASGFYISTPTGPGGRQERVGLLSLPLDPTLEPACLSF 425
Cdd:pfam00629    1 CDFEDGnLCGWTQDTSDDFDWSRGSGSTPTVKTGPSGDHTT-NGSGHYMYVDTSSAAPGQTARLLSPLLPPPRSPHCLRF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  426 WYHMYGENVHKLSINI-SNDQNMEKTVFQKEGNYGDNWNYGQVTLNE-TVKFKVAFNA-FKNKILSDIALDDISLTYGIC 502
Cdd:pfam00629   80 WYHMSGSGVGTLNVYLrENGGTLGTLLWSISGNQGPSWQEAEVTLSSfTKPFQVVFEGiRGGGSRGDIALDDISLSSGPC 159

                   .
gi 1519314416  503 N 503
Cdd:pfam00629  160 P 160
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
342-502 2.84e-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  Cd Length: 161  Bit Score: 174.45  E-value: 2.84e-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 5.70e-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: 5.70e-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 7.06e-37

CUB domain;


Pssm-ID: 278839  Cd Length: 110  Bit Score: 134.34  E-value: 7.06e-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 6.10e-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: 6.10e-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 7.71e-29

CUB domain;


Pssm-ID: 278839  Cd Length: 110  Bit Score: 111.23  E-value: 7.71e-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 1.03e-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  Cd Length: 113  Bit Score: 108.27  E-value: 1.03e-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 3.59e-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  Cd Length: 102  Bit Score: 100.54  E-value: 3.59e-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
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
778-1014 2.85e-23

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 103.42  E-value: 2.85e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  778 AQDITPKIVGGSNAKEGAWPWVVGLYYGGRL-----LCGASLVSSDWLVSAAHCVYGRNlePSKWTAILGLhmkSNLTSP 852
Cdd:COG5640     26 ADEVSSRIIGGSNANAGEYPSLVALVDRISDyvsgtFCGGSKLGGRYVLTAAHCADASS--PISSDVNRVV---VDLNDS 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  853 QTVPRL-IDEIVINPHYNRRRKDNDIAMMHLEfkvnytdyiQPICLPEEN----QVFPPGRNCSIA-------GWGTVVY 920
Cdd:COG5640    101 SQAERGhVRTIYVHEFYSPGNLGNDIAVLELA---------RAASLPRVKitsfDASDTFLNSVTTvspmtngTFGVTTP 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  921 ---QGTTAN--ILQEADVPLLSNERCQQQMPEYNITENM-----ICAGyeEGGIDSCQGDSGGPLMCQENNRWFLAGVTS 990
Cdd:COG5640    172 sdvPRSSPKgtILHEVAVLFVPLSTCAQYKGCANASDGAtgltgFCAG--RPPKDACQGDSGGPIFHKGEEGRVQRGVVS 249
                          250       260
                   ....*....|....*....|....*
gi 1519314416  991 FGY-KCALPNRPGVYARVSRFTEWI 1014
Cdd:COG5640    250 WGDgGCGGTLIPGVYTNVSNYQDWI 274
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
59-158 5.57e-18

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


Pssm-ID: 334519  Cd Length: 106  Bit Score: 79.99  E-value: 5.57e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   59 RATFKITSgVTYNPNLQDKLSVDFKVLAFDLQQMIDEIFLSSNLKNEYKNSRVLQF--ENGSIIVVFDLFFAQWVSD--E 134
Cdd:pfam01390    4 TGNFTITN-LQYTEDLGNPSSQEFKSLERVIENLLDELFQNSSLGSHYIGCRVISLrpGSDGVGVDVVLVFRFPSTEgpA 82
                           90       100
                   ....*....|....*....|....
gi 1519314416  135 NVKEELIQGLEANKSSQLVTFHID 158
Cdd:pfam01390   83 LDREKIYSILSTKLITNLGNLTID 106
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
225-333 3.36e-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  Cd Length: 113  Bit Score: 75.14  E-value: 3.36e-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
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
236-331 2.08e-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  Cd Length: 102  Bit Score: 69.73  E-value: 2.08e-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 ucrhin egg peptide speract contains 4 repeats of SR ...
678-771 2.32e-13

Scavenger receptor Cys-rich; The sea ucrhin 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  Cd Length: 101  Bit Score: 66.60  E-value: 2.32e-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 1.99e-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: 1.99e-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 8.50e-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: 8.50e-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 4.90e-10

Low-density lipoprotein receptor domain class A;


Pssm-ID: 333805  Cd Length: 37  Bit Score: 55.34  E-value: 4.90e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1519314416  642 PCKADHFQCKNGECVPLVNLCDGHLHCEDGSDEADC 677
Cdd:pfam00057    2 TCEPNEFQCGSGECIPRSWVCDGEPDCGDGSDEENC 37
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
699-773 1.46e-06

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: 317845  Cd Length: 99  Bit Score: 47.35  E-value: 1.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  699 WHTACAENWTTQISNDVCQLLGLGSGNSSKPIFPTDGGP-----FVKLN-TAPDGHL--ILTPSQQCLQDSLIRLQCNHk 770
Cdd:pfam15494   16 WLPVCSDGWSPAYGKAACQQLGYLSLTHSKSVNLSDLSGsssteFMKLNsSSLDGTLqeKLQPRDSCSSGSVVSLRCSE- 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 3.02e-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: 3.02e-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 2.60e-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: 2.60e-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 1.56e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 333805  Cd Length: 37  Bit Score: 36.85  E-value: 1.56e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1519314416  184 CLPGSSPCTDAlTCIKADLFCDGEVNCPDGSDEDN 218
Cdd:pfam00057    3 CEPNEFQCGSG-ECIPRSWVCDGEPDCGDGSDEEN 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 8.78e-102

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  Cd Length: 232  Bit Score: 318.45  E-value: 8.78e-102
                           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 4.85e-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: 4.85e-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 5.69e-75

Trypsin;


Pssm-ID: 333831  Cd Length: 219  Bit Score: 245.81  E-value: 5.69e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  785 IVGGSNAKEGAWPWVVGLYY-GGRLLCGASLVSSDWLVSAAHCVYGRnlepSKWTAILGLH-MKSNLTSPQTVPrlIDEI 862
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGS----SDVQVVLGEHnIVLREGGEQKFD--VEKV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  863 VINPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWGTvVYQGTTANILQEADVPLLSNERCQ 942
Cdd:pfam00089   75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDAGSDLPVGTTCTVSGWGN-TKTLGRPDTLQEVTVPVVSRETCR 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519314416  943 QQMPEYnITENMICAGYeeGGIDSCQGDSGGPLMCQENnrwFLAGVTSFGYKCALPNRPGVYARVSRFTEWI 1014
Cdd:pfam00089  154 SAYGGT-VTDNMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNKPGVYTRVSSYLDWI 219
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
347-503 8.47e-52

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: 334181  Cd Length: 160  Bit Score: 178.72  E-value: 8.47e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  347 CNFEDG-FCFWVQDLNDDNEWERIQGSTFSPFTGPNFDHTFgNASGFYISTPTGPGGRQERVGLLSLPLDPTLEPACLSF 425
Cdd:pfam00629    1 CDFEDGnLCGWTQDTSDDFDWSRGSGSTPTVKTGPSGDHTT-NGSGHYMYVDTSSAAPGQTARLLSPLLPPPRSPHCLRF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  426 WYHMYGENVHKLSINI-SNDQNMEKTVFQKEGNYGDNWNYGQVTLNE-TVKFKVAFNA-FKNKILSDIALDDISLTYGIC 502
Cdd:pfam00629   80 WYHMSGSGVGTLNVYLrENGGTLGTLLWSISGNQGPSWQEAEVTLSSfTKPFQVVFEGiRGGGSRGDIALDDISLSSGPC 159

                   .
gi 1519314416  503 N 503
Cdd:pfam00629  160 P 160
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
342-502 2.84e-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  Cd Length: 161  Bit Score: 174.45  E-value: 2.84e-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 5.70e-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: 5.70e-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 7.06e-37

CUB domain;


Pssm-ID: 278839  Cd Length: 110  Bit Score: 134.34  E-value: 7.06e-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 6.10e-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: 6.10e-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 7.71e-29

CUB domain;


Pssm-ID: 278839  Cd Length: 110  Bit Score: 111.23  E-value: 7.71e-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 1.03e-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  Cd Length: 113  Bit Score: 108.27  E-value: 1.03e-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 3.59e-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  Cd Length: 102  Bit Score: 100.54  E-value: 3.59e-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
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
778-1014 2.85e-23

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 103.42  E-value: 2.85e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  778 AQDITPKIVGGSNAKEGAWPWVVGLYYGGRL-----LCGASLVSSDWLVSAAHCVYGRNlePSKWTAILGLhmkSNLTSP 852
Cdd:COG5640     26 ADEVSSRIIGGSNANAGEYPSLVALVDRISDyvsgtFCGGSKLGGRYVLTAAHCADASS--PISSDVNRVV---VDLNDS 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  853 QTVPRL-IDEIVINPHYNRRRKDNDIAMMHLEfkvnytdyiQPICLPEEN----QVFPPGRNCSIA-------GWGTVVY 920
Cdd:COG5640    101 SQAERGhVRTIYVHEFYSPGNLGNDIAVLELA---------RAASLPRVKitsfDASDTFLNSVTTvspmtngTFGVTTP 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  921 ---QGTTAN--ILQEADVPLLSNERCQQQMPEYNITENM-----ICAGyeEGGIDSCQGDSGGPLMCQENNRWFLAGVTS 990
Cdd:COG5640    172 sdvPRSSPKgtILHEVAVLFVPLSTCAQYKGCANASDGAtgltgFCAG--RPPKDACQGDSGGPIFHKGEEGRVQRGVVS 249
                          250       260
                   ....*....|....*....|....*
gi 1519314416  991 FGY-KCALPNRPGVYARVSRFTEWI 1014
Cdd:COG5640    250 WGDgGCGGTLIPGVYTNVSNYQDWI 274
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
59-158 5.57e-18

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


Pssm-ID: 334519  Cd Length: 106  Bit Score: 79.99  E-value: 5.57e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416   59 RATFKITSgVTYNPNLQDKLSVDFKVLAFDLQQMIDEIFLSSNLKNEYKNSRVLQF--ENGSIIVVFDLFFAQWVSD--E 134
Cdd:pfam01390    4 TGNFTITN-LQYTEDLGNPSSQEFKSLERVIENLLDELFQNSSLGSHYIGCRVISLrpGSDGVGVDVVLVFRFPSTEgpA 82
                           90       100
                   ....*....|....*....|....
gi 1519314416  135 NVKEELIQGLEANKSSQLVTFHID 158
Cdd:pfam01390   83 LDREKIYSILSTKLITNLGNLTID 106
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
225-333 3.36e-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  Cd Length: 113  Bit Score: 75.14  E-value: 3.36e-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
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
236-331 2.08e-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  Cd Length: 102  Bit Score: 69.73  E-value: 2.08e-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 ucrhin egg peptide speract contains 4 repeats of SR ...
678-771 2.32e-13

Scavenger receptor Cys-rich; The sea ucrhin 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  Cd Length: 101  Bit Score: 66.60  E-value: 2.32e-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 1.99e-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: 1.99e-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 8.50e-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: 8.50e-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 4.90e-10

Low-density lipoprotein receptor domain class A;


Pssm-ID: 333805  Cd Length: 37  Bit Score: 55.34  E-value: 4.90e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1519314416  642 PCKADHFQCKNGECVPLVNLCDGHLHCEDGSDEADC 677
Cdd:pfam00057    2 TCEPNEFQCGSGECIPRSWVCDGEPDCGDGSDEENC 37
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
796-899 6.27e-07

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 49.08  E-value: 6.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  796 WPWVVGLYYGGRLLCGASLVSSDWLVSAAHCVYGRNLEPSKWTAILGLHmKSNLTspqtvprlideiVINPHYNRRRKD- 874
Cdd:pfam09342    1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVLGGA-KTLKS------------IEGPYEQIVRVDc 67
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1519314416  875 ------NDIAMMHLEFKVNYTDYIQPICLPE 899
Cdd:pfam09342   68 rhdipeSEISLLHLASPASFSNHVLPTFVPE 98
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
699-773 1.46e-06

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: 317845  Cd Length: 99  Bit Score: 47.35  E-value: 1.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  699 WHTACAENWTTQISNDVCQLLGLGSGNSSKPIFPTDGGP-----FVKLN-TAPDGHL--ILTPSQQCLQDSLIRLQCNHk 770
Cdd:pfam15494   16 WLPVCSDGWSPAYGKAACQQLGYLSLTHSKSVNLSDLSGsssteFMKLNsSSLDGTLqeKLQPRDSCSSGSVVSLRCSE- 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 3.02e-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: 3.02e-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 2.60e-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: 2.60e-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 ...
683-773 2.01e-04

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


Pssm-ID: 306915  Cd Length: 97  Bit Score: 41.18  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519314416  683 GTTNNNGLVRFRIQSIWHTACAENWTTQISNDVCQLLGLGSGNSSKPifptdGGPFVKlntaPDGHLILTPSQQCL--QD 760
Cdd:pfam00530    1 GSSPCEGRVEVYYNGQWGTVCDDGWDLEDANVVCRQLGCGGAVSASS-----GCSFFG----PGTGPIWLDDVRCSgnET 71
                           90
                   ....*....|...
gi 1519314416  761 SLirLQCNHKSCG 773
Cdd:pfam00530   72 SL--WQCPHRPWG 82
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
184-218 1.56e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 333805  Cd Length: 37  Bit Score: 36.85  E-value: 1.56e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1519314416  184 CLPGSSPCTDAlTCIKADLFCDGEVNCPDGSDEDN 218
Cdd:pfam00057    3 CEPNEFQCGSG-ECIPRSWVCDGEPDCGDGSDEEN 36
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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