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Conserved domains on  [gi|61217504|sp|P69525|]
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RecName: Full=Transmembrane protease serine 9; AltName: Full=Polyserase-I; AltName: Full=Polyserine protease 1; Short=Polyserase-1; Contains: RecName: Full=Serase-1; Contains: RecName: Full=Serase-2; Contains: RecName: Full=Serase-3

Protein Classification

LDL receptor domain-containing protein; serine protease( domain architecture ID 11517117)

Low Density Lipoprotein (LDL) receptor class A domain is a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism| 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 smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
204-433 1.26e-94

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


:

Pssm-ID: 214473  Cd Length: 229  Bit Score: 299.98  E-value: 1.26e-94
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504     204 RIVGGVEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEASAVRtRVLRIAK 282
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504     283 HPAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDFLVKPEVLQKATVELLDQSLCSS 362
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61217504     363 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 433
Cdd:smart00020  159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
834-1059 4.18e-94

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: 298.81  E-value: 4.18e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  834 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiYGDPMQWAAFLGTPFLSSTE--GQLERVARIYRH 911
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  912 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGP-ARPPDGARCVITGWGSLREGGSMARQLQKAAVRVLSEQTCRRFY 990
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 61217504  991 --PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGQWVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWI 1059
Cdd:cd00190  160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
505-733 9.08e-88

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: 281.87  E-value: 9.08e-88
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504     505 RIVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLgVGGSPVKLGLRRVALH 583
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504     584 PRYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKASVGIIEQKMCGAL 663
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 61217504     664 Y--NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACEEtpGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 733
Cdd:smart00020  160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
156-191 3.39e-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: 50.28  E-value: 3.39e-08
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 61217504  156 CPGNVFSCQNGQCVSKENpECDDRVDCSDESDEAQC 191
Cdd:cd00112    1 CPPNEFRCANGRCIPSSW-VCDGEDDCGDGSDEENC 35
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
204-433 1.26e-94

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


Pssm-ID: 214473  Cd Length: 229  Bit Score: 299.98  E-value: 1.26e-94
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504     204 RIVGGVEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEASAVRtRVLRIAK 282
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504     283 HPAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDFLVKPEVLQKATVELLDQSLCSS 362
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61217504     363 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 433
Cdd:smart00020  159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
205-433 2.91e-94

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: 299.19  E-value: 2.91e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  205 IVGGVEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEASAVRTRVLRIAKH 283
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  284 PAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDfLVKPEVLQKATVELLDQSLCSSL 363
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 61217504  364 YGHS--LTDRMVCAGYLDGKVDSCQGDSGGPLVCEEPsGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 433
Cdd:cd00190  159 YSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
834-1059 4.18e-94

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: 298.81  E-value: 4.18e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  834 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiYGDPMQWAAFLGTPFLSSTE--GQLERVARIYRH 911
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  912 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGP-ARPPDGARCVITGWGSLREGGSMARQLQKAAVRVLSEQTCRRFY 990
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 61217504  991 --PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGQWVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWI 1059
Cdd:cd00190  160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
833-1059 3.21e-92

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: 293.82  E-value: 3.21e-92
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504     833 RIVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiYGDPMQWAAFLGTPFLSSTE-GQLERVARIYRH 911
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEeGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504     912 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGPAR-PPDGARCVITGWGSLREG-GSMARQLQKAAVRVLSEQTCRRF 989
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 61217504     990 YPVQ--ISSRMLCAGFPQGGVDSCSGDAGGPLACRepSGQWVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWI 1059
Cdd:smart00020  160 YSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
505-733 9.08e-88

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: 281.87  E-value: 9.08e-88
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504     505 RIVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLgVGGSPVKLGLRRVALH 583
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504     584 PRYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKASVGIIEQKMCGAL 663
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 61217504     664 Y--NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACEEtpGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 733
Cdd:smart00020  160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
506-733 1.46e-87

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: 281.09  E-value: 1.46e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  506 IVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLGVGGSPVKLGLRRVALHP 584
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  585 RYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGnATKPDILQKASVGIIEQKMCGALY 664
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 61217504  665 --NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACeETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 733
Cdd:cd00190  160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVC-NDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
205-433 1.25e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 242.73  E-value: 1.25e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504    205 IVGGVEAAPGEFPWQVSL-RENHEHFCGATIIGARWLVSAAHCFNefqDPAQWAAQAGSVHLSGSEASAVRTRVLRIAKH 283
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504    284 PAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDflVKPEVLQKATVELLDQSLCSSL 363
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504    364 YGHSLTDRMVCAGYldGKVDSCQGDSGGPLVCEEPsgrfFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 433
Cdd:pfam00089  156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Trypsin pfam00089
Trypsin;
834-1059 3.96e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.10  E-value: 3.96e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504    834 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiygDPMQWAAFLGTPFLSSTEG--QLERVARIYRH 911
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGgeQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504    912 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGP-ARPPDGARCVITGWGSLREGGSmARQLQKAAVRVLSEQTCRRFY 990
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDAsSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61217504    991 PVQISSRMLCAGFpqGGVDSCSGDAGGPLACrepSGQwVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWI 1059
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVC---SDG-ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Trypsin pfam00089
Trypsin;
506-733 4.42e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 232.72  E-value: 4.42e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504    506 IVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKveQVQAHLGTVSLLGVGGSPVKLGLRRVALHP 584
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGAS--DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504    585 RYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNatKPDILQKASVGIIEQKMCGALY 664
Cdd:pfam00089   79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61217504    665 NFSLTDRMLCAGFleGRVDSCQGDSGGPLACEETpgvfYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 733
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
824-1063 6.30e-70

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 234.16  E-value: 6.30e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  824 GLAPPGALTRIVGGSAASLGEWPWQVSLWLR--RREHRCGAVLVAERWLLSAAHCFDIYGdPMQWAAFLGTPFLSSTEGQ 901
Cdd:COG5640   21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGGT 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  902 LERVARIYRHPFYNIYTLDYDVALLELAGPVRRsrlVRPICLPGPARPPD-GARCVITGWGSLREG-GSMARQLQKAAVR 979
Cdd:COG5640  100 VVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAApGTPATVAGWGRTSEGpGSQSGTLRKADVP 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  980 VLSEQTCRRfYPVQISSRMLCAGFPQGGVDSCSGDAGGPLAcREPSGQWVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWI 1059
Cdd:COG5640  177 VVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254

                 ....
gi 61217504 1060 GQNI 1063
Cdd:COG5640  255 KSTA 258
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
196-441 6.33e-68

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 228.38  E-value: 6.33e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  196 QPAWRSAGRIVGGVEAAPGEFPWQVSLREN---HEHFCGATIIGARWLVSAAHCFNEfQDPAQWAAQAGSVHLSGSEAsa 272
Cdd:COG5640   22 APAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGG-- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  273 VRTRVLRIAKHPAYDADTADFDVAVLELARPLPFgryVQPACLPAATHVFPPGKKCLISGWGYLKEDFLVKPEVLQKATV 352
Cdd:COG5640   99 TVVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  353 ELLDQSLCSSlYGHSLTDRMVCAGYLDGKVDSCQGDSGGPLVcEEPSGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDW 432
Cdd:COG5640  176 PVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                 ....*....
gi 61217504  433 ILEVTSAAD 441
Cdd:COG5640  254 IKSTAGGLG 262
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
495-741 4.14e-61

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 209.51  E-value: 4.14e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  495 GARPAMDKPTRIVGGISAVSGEVPWQASL--KEGPR-HFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLGVGGs 571
Cdd:COG5640   20 AAAPAADAAPAIVGGTPATVGEYPWMVALqsSNGPSgQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGG- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  572 pVKLGLRRVALHPRYNPGILDFDVALLELAQPLvfnKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKAS 651
Cdd:COG5640   99 -TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  652 VGIIEQKMCGALYNFsLTDRMLCAGFLEGRVDSCQGDSGGPLAcEETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKD 731
Cdd:COG5640  175 VPVVSDATCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252
                        250
                 ....*....|
gi 61217504  732 WILKAMSSDP 741
Cdd:COG5640  253 WIKSTAGGLG 262
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
156-191 3.39e-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: 50.28  E-value: 3.39e-08
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 61217504  156 CPGNVFSCQNGQCVSKENpECDDRVDCSDESDEAQC 191
Cdd:cd00112    1 CPPNEFRCANGRCIPSSW-VCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
156-188 3.86e-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: 47.24  E-value: 3.86e-07
                            10        20        30
                    ....*....|....*....|....*....|...
gi 61217504     156 CPGNVFSCQNGQCVSKENpECDDRVDCSDESDE 188
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSW-VCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
156-191 5.94e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 43.78  E-value: 5.94e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 61217504    156 CPGNVFSCQNGQCVSKeNPECDDRVDCSDESDEAQC 191
Cdd:pfam00057    3 CSPNEFQCGSGECIPR-SWVCDGDPDCGDGSDEENC 37
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
204-433 1.26e-94

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


Pssm-ID: 214473  Cd Length: 229  Bit Score: 299.98  E-value: 1.26e-94
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504     204 RIVGGVEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEASAVRtRVLRIAK 282
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504     283 HPAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDFLVKPEVLQKATVELLDQSLCSS 362
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61217504     363 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 433
Cdd:smart00020  159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
205-433 2.91e-94

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: 299.19  E-value: 2.91e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  205 IVGGVEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEASAVRTRVLRIAKH 283
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  284 PAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDfLVKPEVLQKATVELLDQSLCSSL 363
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 61217504  364 YGHS--LTDRMVCAGYLDGKVDSCQGDSGGPLVCEEPsGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 433
Cdd:cd00190  159 YSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
834-1059 4.18e-94

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: 298.81  E-value: 4.18e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  834 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiYGDPMQWAAFLGTPFLSSTE--GQLERVARIYRH 911
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  912 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGP-ARPPDGARCVITGWGSLREGGSMARQLQKAAVRVLSEQTCRRFY 990
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 61217504  991 --PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGQWVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWI 1059
Cdd:cd00190  160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
833-1059 3.21e-92

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: 293.82  E-value: 3.21e-92
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504     833 RIVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiYGDPMQWAAFLGTPFLSSTE-GQLERVARIYRH 911
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEeGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504     912 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGPAR-PPDGARCVITGWGSLREG-GSMARQLQKAAVRVLSEQTCRRF 989
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 61217504     990 YPVQ--ISSRMLCAGFPQGGVDSCSGDAGGPLACRepSGQWVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWI 1059
Cdd:smart00020  160 YSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
505-733 9.08e-88

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: 281.87  E-value: 9.08e-88
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504     505 RIVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLgVGGSPVKLGLRRVALH 583
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504     584 PRYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKASVGIIEQKMCGAL 663
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 61217504     664 Y--NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACEEtpGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 733
Cdd:smart00020  160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
506-733 1.46e-87

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: 281.09  E-value: 1.46e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  506 IVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLGVGGSPVKLGLRRVALHP 584
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  585 RYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGnATKPDILQKASVGIIEQKMCGALY 664
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 61217504  665 --NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACeETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 733
Cdd:cd00190  160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVC-NDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
205-433 1.25e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 242.73  E-value: 1.25e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504    205 IVGGVEAAPGEFPWQVSL-RENHEHFCGATIIGARWLVSAAHCFNefqDPAQWAAQAGSVHLSGSEASAVRTRVLRIAKH 283
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504    284 PAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDflVKPEVLQKATVELLDQSLCSSL 363
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504    364 YGHSLTDRMVCAGYldGKVDSCQGDSGGPLVCEEPsgrfFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 433
Cdd:pfam00089  156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Trypsin pfam00089
Trypsin;
834-1059 3.96e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.10  E-value: 3.96e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504    834 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiygDPMQWAAFLGTPFLSSTEG--QLERVARIYRH 911
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGgeQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504    912 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGP-ARPPDGARCVITGWGSLREGGSmARQLQKAAVRVLSEQTCRRFY 990
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDAsSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61217504    991 PVQISSRMLCAGFpqGGVDSCSGDAGGPLACrepSGQwVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWI 1059
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVC---SDG-ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Trypsin pfam00089
Trypsin;
506-733 4.42e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 232.72  E-value: 4.42e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504    506 IVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKveQVQAHLGTVSLLGVGGSPVKLGLRRVALHP 584
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGAS--DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504    585 RYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNatKPDILQKASVGIIEQKMCGALY 664
Cdd:pfam00089   79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61217504    665 NFSLTDRMLCAGFleGRVDSCQGDSGGPLACEETpgvfYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 733
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
824-1063 6.30e-70

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 234.16  E-value: 6.30e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  824 GLAPPGALTRIVGGSAASLGEWPWQVSLWLR--RREHRCGAVLVAERWLLSAAHCFDIYGdPMQWAAFLGTPFLSSTEGQ 901
Cdd:COG5640   21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGGT 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  902 LERVARIYRHPFYNIYTLDYDVALLELAGPVRRsrlVRPICLPGPARPPD-GARCVITGWGSLREG-GSMARQLQKAAVR 979
Cdd:COG5640  100 VVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAApGTPATVAGWGRTSEGpGSQSGTLRKADVP 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  980 VLSEQTCRRfYPVQISSRMLCAGFPQGGVDSCSGDAGGPLAcREPSGQWVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWI 1059
Cdd:COG5640  177 VVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254

                 ....
gi 61217504 1060 GQNI 1063
Cdd:COG5640  255 KSTA 258
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
196-441 6.33e-68

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 228.38  E-value: 6.33e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  196 QPAWRSAGRIVGGVEAAPGEFPWQVSLREN---HEHFCGATIIGARWLVSAAHCFNEfQDPAQWAAQAGSVHLSGSEAsa 272
Cdd:COG5640   22 APAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGG-- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  273 VRTRVLRIAKHPAYDADTADFDVAVLELARPLPFgryVQPACLPAATHVFPPGKKCLISGWGYLKEDFLVKPEVLQKATV 352
Cdd:COG5640   99 TVVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  353 ELLDQSLCSSlYGHSLTDRMVCAGYLDGKVDSCQGDSGGPLVcEEPSGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDW 432
Cdd:COG5640  176 PVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                 ....*....
gi 61217504  433 ILEVTSAAD 441
Cdd:COG5640  254 IKSTAGGLG 262
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
495-741 4.14e-61

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 209.51  E-value: 4.14e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  495 GARPAMDKPTRIVGGISAVSGEVPWQASL--KEGPR-HFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLGVGGs 571
Cdd:COG5640   20 AAAPAADAAPAIVGGTPATVGEYPWMVALqsSNGPSgQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGG- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  572 pVKLGLRRVALHPRYNPGILDFDVALLELAQPLvfnKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKAS 651
Cdd:COG5640   99 -TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  652 VGIIEQKMCGALYNFsLTDRMLCAGFLEGRVDSCQGDSGGPLAcEETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKD 731
Cdd:COG5640  175 VPVVSDATCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252
                        250
                 ....*....|
gi 61217504  732 WILKAMSSDP 741
Cdd:COG5640  253 WIKSTAGGLG 262
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
156-191 3.39e-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: 50.28  E-value: 3.39e-08
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 61217504  156 CPGNVFSCQNGQCVSKENpECDDRVDCSDESDEAQC 191
Cdd:cd00112    1 CPPNEFRCANGRCIPSSW-VCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
156-188 3.86e-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: 47.24  E-value: 3.86e-07
                            10        20        30
                    ....*....|....*....|....*....|...
gi 61217504     156 CPGNVFSCQNGQCVSKENpECDDRVDCSDESDE 188
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSW-VCDGVDDCGDGSDE 33
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
526-711 3.49e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 48.90  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  526 GPRHFCGATVVGDRWLLSAAHCFNHTkvEQVQAHLGTVSLLGVGGSP-VKLGLRRVALHPRY-NPGILDFDVALLELAQP 603
Cdd:COG3591    9 GGGGVCTGTLIGPNLVLTAGHCVYDG--AGGGWATNIVFVPGYNGGPyGTATATRFRVPPGWvASGDAGYDYALLRLDEP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  604 LVFnkyiQPVCLPLAI-HKFPVGRKCMISGWGnmqegnATKPDILQKASVGIIeqkmcgalynFSLTDRmlcagFLEGRV 682
Cdd:COG3591   87 LGD----TTGWLGLAFnDAPLAGEPVTIIGYP------GDRPKDLSLDCSGRV----------TGVQGN-----RLSYDC 141
                        170       180
                 ....*....|....*....|....*....
gi 61217504  683 DSCQGDSGGPLaCEETPGVFYLAGIVSWG 711
Cdd:COG3591  142 DTTGGSSGSPV-LDDSDGGGRVVGVHSAG 169
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
228-434 3.98e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 48.52  E-value: 3.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  228 HFCGATIIGARWLVSAAHCFNEFQD---PAQWAAQAGSVHLSGSEASAVRTRVlriakHPAYDADT-ADFDVAVLELARP 303
Cdd:COG3591   12 GVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPGYNGGPYGTATATRFRV-----PPGWVASGdAGYDYALLRLDEP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61217504  304 LPfgrYVQPACLPAATHVFPPGKKCLISGWGylkedflvkpevlqkatvelldqslcsslYGHSLTDRMVCAGYLDG--- 380
Cdd:COG3591   87 LG---DTTGWLGLAFNDAPLAGEPVTIIGYP-----------------------------GDRPKDLSLDCSGRVTGvqg 134
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 61217504  381 -----KVDSCQGDSGGPLVCEEpSGRFFLAGIVSWGigcaearRPGVYTRVTRLRDWIL 434
Cdd:COG3591  135 nrlsyDCDTTGGSSGSPVLDDS-DGGGRVVGVHSAG-------GADRANTGVRLTSAIV 185
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
156-191 5.94e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 43.78  E-value: 5.94e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 61217504    156 CPGNVFSCQNGQCVSKeNPECDDRVDCSDESDEAQC 191
Cdd:pfam00057    3 CSPNEFQCGSGECIPR-SWVCDGDPDCGDGSDEENC 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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