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Conserved domains on  [gi|1622838155|ref|XP_015005770|]
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transmembrane protease serine 6 [Macaca mulatta]

Protein Classification

neuropilin and tolloid-like protein; serine protease( domain architecture ID 10672499)

neuropilin and tolloid-like protein is a CUB and LDLa (low-density lipoprotein receptor class A) domain-containing protein similar to Homo sapiens neuropilin and tolloid-like protein 1 involved in the development and/or maintenance of neuronal circuitry| trypsin-like serine protease catalyzes the cleavage of specific peptide bonds in protein substrates using an active site serine as the nucleophile; contains C-terminal DNA polymerase III subunits gamma and tau

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 ...
566-798 1.23e-103

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: 1.23e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 566 IVGGAVSSEGEWPWQASLQVR-GRHICGGALIADRWVITAAHCFQEdsmASPALWTVFLGKVWQNSRWPGEVSFKVSRLL 644
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS---SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 645 LHPYHEEDSHDYDVALLQLDHPVVRSAAVRPVCLPARSHFFEPGLHCWITGWGALREGGPTSNALQKVDVQLIPQDLCSE 724
Cdd:cd00190    78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622838155 725 AYRYQ--VTPRMLCAGYRKGKKDACQGDSGGPLVCKaLSGRWFLAGLVSWGLGCGRPNYFGVYTRITGVIGWIQQV 798
Cdd:cd00190   158 AYSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCN-DNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
518-555 3.20e-08

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 49.94  E-value: 3.20e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622838155 518 VPCGTFTFQCEDQSCVKKpNPQCDGRPDCRDGSDEQHC 555
Cdd:pfam00057   1 STCSPNEFQCGSGECIPR-SWVCDGDPDCGDGSDEENC 37
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
480-514 4.01e-08

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 49.55  E-value: 4.01e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1622838155 480 CRAT-FQCQeDSTCISLLKVCDGQPDCLNGSDEERC 514
Cdd:pfam00057   3 CSPNeFQCG-SGECIPRSWVCDGDPDCGDGSDEENC 37
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
324-438 5.22e-07

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: 48.95  E-value: 5.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 324 CEVNLTLDdrldSQGVLSTPYFPSYYSPRTHCSWHLTVPSlDYGLALWFDAYALRRQK---------YDLPCTQGQwtiQ 394
Cdd:cd00041     1 CGGTLTAS----TSGTISSPNYPNNYPNNLNCVWTIEAPP-GYRIRLTFEDFDLESSPncsydyleiYDGPSTSSP---L 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622838155 395 NRRLCGLRILQPYaeripVVATAGITINFTSQISLTGPGVRVHY 438
Cdd:cd00041    73 LGRFCGSTLPPPI-----ISSGNSLTVRFRSDSSVTGRGFKATY 111
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
75-175 8.79e-07

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: 48.00  E-value: 8.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155  75 QVYSGSLRVLNRHFSQDLTRRESSAFRSETAKAQKMLKELIASTRLGTYYNSSSVYSF--GEGPLTCFFWFILQIPehrr 152
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLrpDGGSVVVDVVLVFRFP---- 76
                          90       100
                  ....*....|....*....|...
gi 1622838155 153 PMLSPEVVQALLVEELLSTVNSS 175
Cdd:pfam01390  77 STEPALDREKLIEEILRQTLNNT 99
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
448-478 1.32e-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: 45.28  E-value: 1.32e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622838155 448 PGEFLCSvNGLCVPA---CDGVKDCPNGLDERNC 478
Cdd:cd00112     3 PNEFRCA-NGRCIPSswvCDGEDDCGDGSDEENC 35
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
566-798 1.23e-103

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: 1.23e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 566 IVGGAVSSEGEWPWQASLQVR-GRHICGGALIADRWVITAAHCFQEdsmASPALWTVFLGKVWQNSRWPGEVSFKVSRLL 644
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS---SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 645 LHPYHEEDSHDYDVALLQLDHPVVRSAAVRPVCLPARSHFFEPGLHCWITGWGALREGGPTSNALQKVDVQLIPQDLCSE 724
Cdd:cd00190    78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622838155 725 AYRYQ--VTPRMLCAGYRKGKKDACQGDSGGPLVCKaLSGRWFLAGLVSWGLGCGRPNYFGVYTRITGVIGWIQQV 798
Cdd:cd00190   158 AYSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCN-DNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
565-795 6.56e-96

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


Pssm-ID: 214473  Cd Length: 229  Bit Score: 298.05  E-value: 6.56e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155  565 RIVGGAVSSEGEWPWQASLQVRG-RHICGGALIADRWVITAAHCFQEDSmasPALWTVFLGKVWQNSRWPGEVsFKVSRL 643
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSD---PSNIRVRLGSHDLSSGEEGQV-IKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155  644 LLHPYHEEDSHDYDVALLQLDHPVVRSAAVRPVCLPARSHFFEPGLHCWITGWGALREG-GPTSNALQKVDVQLIPQDLC 722
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622838155  723 SEAYRYQ--VTPRMLCAGYRKGKKDACQGDSGGPLVCKalSGRWFLAGLVSWGLGCGRPNYFGVYTRITGVIGWI 795
Cdd:smart00020 157 RRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
566-795 6.69e-74

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 240.04  E-value: 6.69e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 566 IVGGAVSSEGEWPWQASLQVR-GRHICGGALIADRWVITAAHCFqedsmASPALWTVFLGKVWQNSRWPGEVSFKVSRLL 644
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCV-----SGASDVKVVLGAHNIVLREGGEQKFDVEKII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 645 LHPYHEEDSHDYDVALLQLDHPVVRSAAVRPVCLPARSHFFEPGLHCWITGWGALREGGPtSNALQKVDVQLIPQDLCSE 724
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622838155 725 AYRYQVTPRMLCAGYrkGKKDACQGDSGGPLVCKALsgrwFLAGLVSWGLGCGRPNYFGVYTRITGVIGWI 795
Cdd:pfam00089 155 AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
557-799 7.72e-72

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 236.08  E-value: 7.72e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 557 CGLQGPSSRIVGGAVSSEGEWPWQASLQVRG---RHICGGALIADRWVITAAHCFQEDSMASpalWTVFLGKVWQNSRwP 633
Cdd:COG5640    22 APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVVIGSTDLSTS-G 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 634 GEVSfKVSRLLLHPYHEEDSHDYDVALLQLDHPVvrsAAVRPVCLPARSHFFEPGLHCWITGWGALREG-GPTSNALQKV 712
Cdd:COG5640    98 GTVV-KVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 713 DVQLIPQDLCSeAYRYQVTPRMLCAGYRKGKKDACQGDSGGPLVcKALSGRWFLAGLVSWGLGCGRPNYFGVYTRITGVI 792
Cdd:COG5640   174 DVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYR 251

                  ....*..
gi 1622838155 793 GWIQQVV 799
Cdd:COG5640   252 DWIKSTA 258
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
518-555 3.20e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 49.94  E-value: 3.20e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622838155 518 VPCGTFTFQCEDQSCVKKpNPQCDGRPDCRDGSDEQHC 555
Cdd:pfam00057   1 STCSPNEFQCGSGECIPR-SWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
520-555 3.97e-08

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: 49.51  E-value: 3.97e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1622838155 520 CGTFTFQCEDQSCVKKpNPQCDGRPDCRDGSDEQHC 555
Cdd:cd00112     1 CPPNEFRCANGRCIPS-SWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
480-514 4.01e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 49.55  E-value: 4.01e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1622838155 480 CRAT-FQCQeDSTCISLLKVCDGQPDCLNGSDEERC 514
Cdd:pfam00057   3 CSPNeFQCG-SGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
484-514 4.42e-08

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: 49.51  E-value: 4.42e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1622838155 484 FQCQeDSTCISLLKVCDGQPDCLNGSDEERC 514
Cdd:cd00112     6 FRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
484-511 1.96e-07

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: 47.63  E-value: 1.96e-07
                           10        20
                   ....*....|....*....|....*...
gi 1622838155  484 FQCQeDSTCISLLKVCDGQPDCLNGSDE 511
Cdd:smart00192   7 FQCD-NGRCIPSSWVCDGVDDCGDGSDE 33
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
324-438 5.22e-07

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: 48.95  E-value: 5.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 324 CEVNLTLDdrldSQGVLSTPYFPSYYSPRTHCSWHLTVPSlDYGLALWFDAYALRRQK---------YDLPCTQGQwtiQ 394
Cdd:cd00041     1 CGGTLTAS----TSGTISSPNYPNNYPNNLNCVWTIEAPP-GYRIRLTFEDFDLESSPncsydyleiYDGPSTSSP---L 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622838155 395 NRRLCGLRILQPYaeripVVATAGITINFTSQISLTGPGVRVHY 438
Cdd:cd00041    73 LGRFCGSTLPPPI-----ISSGNSLTVRFRSDSSVTGRGFKATY 111
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
75-175 8.79e-07

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: 48.00  E-value: 8.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155  75 QVYSGSLRVLNRHFSQDLTRRESSAFRSETAKAQKMLKELIASTRLGTYYNSSSVYSF--GEGPLTCFFWFILQIPehrr 152
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLrpDGGSVVVDVVLVFRFP---- 76
                          90       100
                  ....*....|....*....|...
gi 1622838155 153 PMLSPEVVQALLVEELLSTVNSS 175
Cdd:pfam01390  77 STEPALDREKLIEEILRQTLNNT 99
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
448-478 1.32e-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: 45.28  E-value: 1.32e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622838155 448 PGEFLCSvNGLCVPA---CDGVKDCPNGLDERNC 478
Cdd:cd00112     3 PNEFRCA-NGRCIPSswvCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
520-552 2.23e-06

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


Pssm-ID: 197566  Cd Length: 33  Bit Score: 44.55  E-value: 2.23e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1622838155  520 CGTFTFQCEDQSCVKKPNpQCDGRPDCRDGSDE 552
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSW-VCDGVDDCGDGSDE 33
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
338-438 4.28e-05

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: 43.15  E-value: 4.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155  338 GVLSTPYFPSYYSPRTHCSWHLTVPSlDYGLALWFDAYALRRQK---------YDLPCTQGQwtiQNRRLCGLRILQpya 408
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPP-GYRIELQFTDFDLESSDnceydyveiYDGPSASSP---LLGRFCGSEAPP--- 73
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622838155  409 eriPVVATAG--ITINFTSQISLTGPGVRVHY 438
Cdd:smart00042  74 ---PVISSSSnsLTLTFVSDSSVQKRGFSARY 102
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
448-475 9.56e-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: 39.92  E-value: 9.56e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1622838155  448 PGEFLCSvNGLCVPA---CDGVKDCPNGLDE 475
Cdd:smart00192   4 PGEFQCD-NGRCIPSswvCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
448-478 1.90e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 36.46  E-value: 1.90e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622838155 448 PGEFLCSvNGLCVP---ACDGVKDCPNGLDERNC 478
Cdd:pfam00057   5 PNEFQCG-SGECIPrswVCDGDPDCGDGSDEENC 37
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
566-798 1.23e-103

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: 1.23e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 566 IVGGAVSSEGEWPWQASLQVR-GRHICGGALIADRWVITAAHCFQEdsmASPALWTVFLGKVWQNSRWPGEVSFKVSRLL 644
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS---SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 645 LHPYHEEDSHDYDVALLQLDHPVVRSAAVRPVCLPARSHFFEPGLHCWITGWGALREGGPTSNALQKVDVQLIPQDLCSE 724
Cdd:cd00190    78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622838155 725 AYRYQ--VTPRMLCAGYRKGKKDACQGDSGGPLVCKaLSGRWFLAGLVSWGLGCGRPNYFGVYTRITGVIGWIQQV 798
Cdd:cd00190   158 AYSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCN-DNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
565-795 6.56e-96

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


Pssm-ID: 214473  Cd Length: 229  Bit Score: 298.05  E-value: 6.56e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155  565 RIVGGAVSSEGEWPWQASLQVRG-RHICGGALIADRWVITAAHCFQEDSmasPALWTVFLGKVWQNSRWPGEVsFKVSRL 643
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSD---PSNIRVRLGSHDLSSGEEGQV-IKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155  644 LLHPYHEEDSHDYDVALLQLDHPVVRSAAVRPVCLPARSHFFEPGLHCWITGWGALREG-GPTSNALQKVDVQLIPQDLC 722
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622838155  723 SEAYRYQ--VTPRMLCAGYRKGKKDACQGDSGGPLVCKalSGRWFLAGLVSWGLGCGRPNYFGVYTRITGVIGWI 795
Cdd:smart00020 157 RRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
566-795 6.69e-74

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 240.04  E-value: 6.69e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 566 IVGGAVSSEGEWPWQASLQVR-GRHICGGALIADRWVITAAHCFqedsmASPALWTVFLGKVWQNSRWPGEVSFKVSRLL 644
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCV-----SGASDVKVVLGAHNIVLREGGEQKFDVEKII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 645 LHPYHEEDSHDYDVALLQLDHPVVRSAAVRPVCLPARSHFFEPGLHCWITGWGALREGGPtSNALQKVDVQLIPQDLCSE 724
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622838155 725 AYRYQVTPRMLCAGYrkGKKDACQGDSGGPLVCKALsgrwFLAGLVSWGLGCGRPNYFGVYTRITGVIGWI 795
Cdd:pfam00089 155 AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
557-799 7.72e-72

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 236.08  E-value: 7.72e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 557 CGLQGPSSRIVGGAVSSEGEWPWQASLQVRG---RHICGGALIADRWVITAAHCFQEDSMASpalWTVFLGKVWQNSRwP 633
Cdd:COG5640    22 APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSD---LRVVIGSTDLSTS-G 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 634 GEVSfKVSRLLLHPYHEEDSHDYDVALLQLDHPVvrsAAVRPVCLPARSHFFEPGLHCWITGWGALREG-GPTSNALQKV 712
Cdd:COG5640    98 GTVV-KVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 713 DVQLIPQDLCSeAYRYQVTPRMLCAGYRKGKKDACQGDSGGPLVcKALSGRWFLAGLVSWGLGCGRPNYFGVYTRITGVI 792
Cdd:COG5640   174 DVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYR 251

                  ....*..
gi 1622838155 793 GWIQQVV 799
Cdd:COG5640   252 DWIKSTA 258
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
586-797 1.34e-14

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 73.17  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 586 RGRHICGGALIADRWVITAAHCFQEDSMASPALWTVFL-GkvWQNSRWpgeVSFKVSRLLLHP-YHEEDSHDYDVALLQL 663
Cdd:COG3591     9 GGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVpG--YNGGPY---GTATATRFRVPPgWVASGDAGYDYALLRL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 664 DHPVvrsAAVRPVCLPARSHFFEPGLHCWITGWGAlreGGPTSNALQKVD--VQLIPQDLcseayryqvtpRMLCagyrk 741
Cdd:COG3591    84 DEPL---GDTTGWLGLAFNDAPLAGEPVTIIGYPG---DRPKDLSLDCSGrvTGVQGNRL-----------SYDC----- 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622838155 742 gkkDACQGDSGGPLVCKAlSGRWFLAGLVSWGlGCGRPNYfGVYTrITGVIGWIQQ 797
Cdd:COG3591   142 ---DTTGGSSGSPVLDDS-DGGGRVVGVHSAG-GADRANT-GVRL-TSAIVAALRA 190
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
518-555 3.20e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 49.94  E-value: 3.20e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622838155 518 VPCGTFTFQCEDQSCVKKpNPQCDGRPDCRDGSDEQHC 555
Cdd:pfam00057   1 STCSPNEFQCGSGECIPR-SWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
520-555 3.97e-08

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: 49.51  E-value: 3.97e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1622838155 520 CGTFTFQCEDQSCVKKpNPQCDGRPDCRDGSDEQHC 555
Cdd:cd00112     1 CPPNEFRCANGRCIPS-SWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
480-514 4.01e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 49.55  E-value: 4.01e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1622838155 480 CRAT-FQCQeDSTCISLLKVCDGQPDCLNGSDEERC 514
Cdd:pfam00057   3 CSPNeFQCG-SGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
484-514 4.42e-08

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: 49.51  E-value: 4.42e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1622838155 484 FQCQeDSTCISLLKVCDGQPDCLNGSDEERC 514
Cdd:cd00112     6 FRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
484-511 1.96e-07

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: 47.63  E-value: 1.96e-07
                           10        20
                   ....*....|....*....|....*...
gi 1622838155  484 FQCQeDSTCISLLKVCDGQPDCLNGSDE 511
Cdd:smart00192   7 FQCD-NGRCIPSSWVCDGVDDCGDGSDE 33
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
324-438 5.22e-07

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: 48.95  E-value: 5.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 324 CEVNLTLDdrldSQGVLSTPYFPSYYSPRTHCSWHLTVPSlDYGLALWFDAYALRRQK---------YDLPCTQGQwtiQ 394
Cdd:cd00041     1 CGGTLTAS----TSGTISSPNYPNNYPNNLNCVWTIEAPP-GYRIRLTFEDFDLESSPncsydyleiYDGPSTSSP---L 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622838155 395 NRRLCGLRILQPYaeripVVATAGITINFTSQISLTGPGVRVHY 438
Cdd:cd00041    73 LGRFCGSTLPPPI-----ISSGNSLTVRFRSDSSVTGRGFKATY 111
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
75-175 8.79e-07

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: 48.00  E-value: 8.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155  75 QVYSGSLRVLNRHFSQDLTRRESSAFRSETAKAQKMLKELIASTRLGTYYNSSSVYSF--GEGPLTCFFWFILQIPehrr 152
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLrpDGGSVVVDVVLVFRFP---- 76
                          90       100
                  ....*....|....*....|...
gi 1622838155 153 PMLSPEVVQALLVEELLSTVNSS 175
Cdd:pfam01390  77 STEPALDREKLIEEILRQTLNNT 99
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
448-478 1.32e-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: 45.28  E-value: 1.32e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622838155 448 PGEFLCSvNGLCVPA---CDGVKDCPNGLDERNC 478
Cdd:cd00112     3 PNEFRCA-NGRCIPSswvCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
520-552 2.23e-06

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


Pssm-ID: 197566  Cd Length: 33  Bit Score: 44.55  E-value: 2.23e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1622838155  520 CGTFTFQCEDQSCVKKPNpQCDGRPDCRDGSDE 552
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSW-VCDGVDDCGDGSDE 33
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
338-438 4.28e-05

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: 43.15  E-value: 4.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155  338 GVLSTPYFPSYYSPRTHCSWHLTVPSlDYGLALWFDAYALRRQK---------YDLPCTQGQwtiQNRRLCGLRILQpya 408
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPP-GYRIELQFTDFDLESSDnceydyveiYDGPSASSP---LLGRFCGSEAPP--- 73
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622838155  409 eriPVVATAG--ITINFTSQISLTGPGVRVHY 438
Cdd:smart00042  74 ---PVISSSSnsLTLTFVSDSSVQKRGFSARY 102
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
577-691 5.39e-05

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: 43.31  E-value: 5.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622838155 577 WPWQASLQVRGRHICGGALIADRWVITAAHCFQEDSMASPALwTVFLG--KVWQNSRWPGEVSFKVSRLllhpyheEDSH 654
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYI-SVVLGgaKTLKSIEGPYEQIVRVDCR-------HDIP 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622838155 655 DYDVALLQLDHPVVRSAAVRPVCLPARSHFFEPGLHC 691
Cdd:pfam09342  73 ESEISLLHLASPASFSNHVLPTFVPETRNENEKDNEC 109
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
448-475 9.56e-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: 39.92  E-value: 9.56e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1622838155  448 PGEFLCSvNGLCVPA---CDGVKDCPNGLDE 475
Cdd:smart00192   4 PGEFQCD-NGRCIPSswvCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
448-478 1.90e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 36.46  E-value: 1.90e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622838155 448 PGEFLCSvNGLCVP---ACDGVKDCPNGLDERNC 478
Cdd:pfam00057   5 PNEFQCG-SGECIPrswVCDGDPDCGDGSDEENC 37
 
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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