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Conserved domains on  [gi|755534801|ref|XP_006513907|]
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transmembrane protease serine 9 isoform X3 [Mus musculus]

Protein Classification

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 ...
441-670 3.45e-93

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: 299.59  E-value: 3.45e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801    441 RIVGGVEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEASAVRtRVLRIAK 519
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801    520 HPAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDFLVKPEVLQKATVELLDQSLCSS 599
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755534801    600 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 670
Cdd:smart00020  159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1070-1322 1.06e-87

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: 284.19  E-value: 1.06e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   1070 RIVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiYGDPMQWAAFLGTPFLSSTE-GQLERVARIYRH 1148
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEeGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   1149 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGPAR-PPDGARCVITGWGSLREGGihacvrrspggvgdtphlhlspd 1227
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRTSEGA----------------------- 136
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   1228 ptGSMARQLQKAAVRVLSEQTCRRFYPVQ--ISSRMLCAGFPQGGVDSCSGDAGGPLACRepSGQWVLTGVTSWGYGCGR 1305
Cdd:smart00020  137 --GSLPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCAR 212
                           250
                    ....*....|....*..
gi 755534801   1306 PHFPGVYTRVAAVLGWI 1322
Cdd:smart00020  213 PGKPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
742-970 1.54e-86

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: 281.10  E-value: 1.54e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801    742 RIVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLgVGGSPVKLGLRRVALH 820
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801    821 PRYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKASVGIIEQKMCGAL 900
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755534801    901 Y--NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACEEtpGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 970
Cdd:smart00020  160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
393-428 5.56e-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: 49.90  E-value: 5.56e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 755534801  393 CPGNVFSCQNGQCVSKENpECDDRVDCSDESDEAQC 428
Cdd:cd00112     1 CPPNEFRCANGRCIPSSW-VCDGEDDCGDGSDEENC 35
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
285-365 4.77e-06

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: 46.46  E-value: 4.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   285 IRFTSSLQQENSDFYRLLTHALQTLFVSSFQKTELESSCAGCTVLSYRDGNSTVIVHFRLHFllralQPLSLKQEADILQ 364
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVF-----RFPSTEPALDREK 86

                   .
gi 755534801   365 K 365
Cdd:pfam01390   87 L 87
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
441-670 3.45e-93

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: 299.59  E-value: 3.45e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801    441 RIVGGVEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEASAVRtRVLRIAK 519
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801    520 HPAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDFLVKPEVLQKATVELLDQSLCSS 599
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755534801    600 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 670
Cdd:smart00020  159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
442-670 8.62e-93

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: 298.42  E-value: 8.62e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  442 IVGGVEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEASAVRTRVLRIAKH 520
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  521 PAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDfLVKPEVLQKATVELLDQSLCSSL 600
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755534801  601 YGHS--LTDRMVCAGYLDGKVDSCQGDSGGPLVCEEPsGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 670
Cdd:cd00190   159 YSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1070-1322 1.06e-87

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: 284.19  E-value: 1.06e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   1070 RIVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiYGDPMQWAAFLGTPFLSSTE-GQLERVARIYRH 1148
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEeGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   1149 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGPAR-PPDGARCVITGWGSLREGGihacvrrspggvgdtphlhlspd 1227
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRTSEGA----------------------- 136
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   1228 ptGSMARQLQKAAVRVLSEQTCRRFYPVQ--ISSRMLCAGFPQGGVDSCSGDAGGPLACRepSGQWVLTGVTSWGYGCGR 1305
Cdd:smart00020  137 --GSLPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCAR 212
                           250
                    ....*....|....*..
gi 755534801   1306 PHFPGVYTRVAAVLGWI 1322
Cdd:smart00020  213 PGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1071-1322 1.07e-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: 284.17  E-value: 1.07e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801 1071 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiYGDPMQWAAFLGTPFLSSTE--GQLERVARIYRH 1148
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801 1149 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGP-ARPPDGARCVITGWGSLREGGIHacvrrspggvgdtphlhlspd 1227
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgYNLPAGTTCTVSGWGRTSEGGPL--------------------- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801 1228 ptgsmARQLQKAAVRVLSEQTCRRFY--PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGQWVLTGVTSWGYGCGR 1305
Cdd:cd00190   139 -----PDVLQEVNVPIVSNAECKRAYsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCAR 212
                         250
                  ....*....|....*..
gi 755534801 1306 PHFPGVYTRVAAVLGWI 1322
Cdd:cd00190   213 PNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
742-970 1.54e-86

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: 281.10  E-value: 1.54e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801    742 RIVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLgVGGSPVKLGLRRVALH 820
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801    821 PRYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKASVGIIEQKMCGAL 900
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755534801    901 Y--NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACEEtpGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 970
Cdd:smart00020  160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
743-970 2.25e-86

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: 280.70  E-value: 2.25e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  743 IVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLGVGGSPVKLGLRRVALHP 821
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  822 RYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGnATKPDILQKASVGIIEQKMCGALY 901
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755534801  902 --NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACeETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 970
Cdd:cd00190   160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVC-NDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
442-670 3.91e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 242.73  E-value: 3.91e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   442 IVGGVEAAPGEFPWQVSL-RENHEHFCGATIIGARWLVSAAHCFNefqDPAQWAAQAGSVHLSGSEASAVRTRVLRIAKH 520
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   521 PAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDflVKPEVLQKATVELLDQSLCSSL 600
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   601 YGHSLTDRMVCAGYldGKVDSCQGDSGGPLVCEEPsgrfFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 670
Cdd:pfam00089  156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Trypsin pfam00089
Trypsin;
743-970 1.10e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.10  E-value: 1.10e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   743 IVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKveQVQAHLGTVSLLGVGGSPVKLGLRRVALHP 821
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGAS--DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   822 RYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNatKPDILQKASVGIIEQKMCGALY 901
Cdd:pfam00089   79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755534801   902 NFSLTDRMLCAGFleGRVDSCQGDSGGPLACEETpgvfYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 970
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
433-678 8.72e-68

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 229.15  E-value: 8.72e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  433 QPAWRSAGRIVGGVEAAPGEFPWQVSLREN---HEHFCGATIIGARWLVSAAHCFNEfQDPAQWAAQAGSVHLSGSEAsa 509
Cdd:COG5640    22 APAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGG-- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  510 VRTRVLRIAKHPAYDADTADFDVAVLELARPLPFgryVQPACLPAATHVFPPGKKCLISGWGYLKEDFLVKPEVLQKATV 589
Cdd:COG5640    99 TVVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADV 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  590 ELLDQSLCSSlYGHSLTDRMVCAGYLDGKVDSCQGDSGGPLVcEEPSGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDW 669
Cdd:COG5640   176 PVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                  ....*....
gi 755534801  670 ILEVTSAAD 678
Cdd:COG5640   254 IKSTAGGLG 262
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1061-1326 1.40e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 225.68  E-value: 1.40e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801 1061 GLAPPGALTRIVGGSAASLGEWPWQVSLWLR--RREHRCGAVLVAERWLLSAAHCFDIYGdPMQWAAFLGTPFLSSTEGQ 1138
Cdd:COG5640    21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGGT 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801 1139 LERVARIYRHPFYNIYTLDYDVALLELAGPVRRsrlVRPICLPGPARPPD-GARCVITGWGSLREGGihacvrrspggvg 1217
Cdd:COG5640   100 VVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAApGTPATVAGWGRTSEGP------------- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801 1218 dtphlhlspdptGSMARQLQKAAVRVLSEQTCRRfYPVQISSRMLCAGFPQGGVDSCSGDAGGPLAcREPSGQWVLTGVT 1297
Cdd:COG5640   164 ------------GSQSGTLRKADVPVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVV 229
                         250       260
                  ....*....|....*....|....*....
gi 755534801 1298 SWGYGCGRPHFPGVYTRVAAVLGWIGQNI 1326
Cdd:COG5640   230 SWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
1071-1322 3.52e-66

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 223.09  E-value: 3.52e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  1071 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiygDPMQWAAFLGTPFLSSTEG--QLERVARIYRH 1148
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGgeQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  1149 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGP-ARPPDGARCVITGWGSLREGGIhacvrrspggvgdtphlhlspd 1227
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDAsSDLPVGTTCTVSGWGNTKTLGP---------------------- 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  1228 ptgsmARQLQKAAVRVLSEQTCRRFYPVQISSRMLCAGFpqGGVDSCSGDAGGPLACrepSGQwVLTGVTSWGYGCGRPH 1307
Cdd:pfam00089  136 -----SDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGA--GGKDACQGDSGGPLVC---SDG-ELIGIVSWGYGCASGN 204
                          250
                   ....*....|....*
gi 755534801  1308 FPGVYTRVAAVLGWI 1322
Cdd:pfam00089  205 YPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
732-978 4.31e-61

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 209.89  E-value: 4.31e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  732 GARPAMDKPTRIVGGISAVSGEVPWQASL--KEGPR-HFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLGVGGs 808
Cdd:COG5640    20 AAAPAADAAPAIVGGTPATVGEYPWMVALqsSNGPSgQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGG- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  809 pVKLGLRRVALHPRYNPGILDFDVALLELAQPLvfnKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKAS 888
Cdd:COG5640    99 -TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  889 VGIIEQKMCGALYNFsLTDRMLCAGFLEGRVDSCQGDSGGPLAcEETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKD 968
Cdd:COG5640   175 VPVVSDATCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252
                         250
                  ....*....|
gi 755534801  969 WILKAMSSDP 978
Cdd:COG5640   253 WIKSTAGGLG 262
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
393-428 5.56e-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: 49.90  E-value: 5.56e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 755534801  393 CPGNVFSCQNGQCVSKENpECDDRVDCSDESDEAQC 428
Cdd:cd00112     1 CPPNEFRCANGRCIPSSW-VCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
393-425 6.01e-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: 46.86  E-value: 6.01e-07
                            10        20        30
                    ....*....|....*....|....*....|...
gi 755534801    393 CPGNVFSCQNGQCVSKENpECDDRVDCSDESDE 425
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSW-VCDGVDDCGDGSDE 33
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
285-365 4.77e-06

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: 46.46  E-value: 4.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   285 IRFTSSLQQENSDFYRLLTHALQTLFVSSFQKTELESSCAGCTVLSYRDGNSTVIVHFRLHFllralQPLSLKQEADILQ 364
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVF-----RFPSTEPALDREK 86

                   .
gi 755534801   365 K 365
Cdd:pfam01390   87 L 87
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
393-428 9.19e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 43.78  E-value: 9.19e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 755534801   393 CPGNVFSCQNGQCVSKeNPECDDRVDCSDESDEAQC 428
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 ...
441-670 3.45e-93

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: 299.59  E-value: 3.45e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801    441 RIVGGVEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEASAVRtRVLRIAK 519
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801    520 HPAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDFLVKPEVLQKATVELLDQSLCSS 599
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755534801    600 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 670
Cdd:smart00020  159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
442-670 8.62e-93

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: 298.42  E-value: 8.62e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  442 IVGGVEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEASAVRTRVLRIAKH 520
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  521 PAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDfLVKPEVLQKATVELLDQSLCSSL 600
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755534801  601 YGHS--LTDRMVCAGYLDGKVDSCQGDSGGPLVCEEPsGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 670
Cdd:cd00190   159 YSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1070-1322 1.06e-87

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: 284.19  E-value: 1.06e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   1070 RIVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiYGDPMQWAAFLGTPFLSSTE-GQLERVARIYRH 1148
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEeGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   1149 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGPAR-PPDGARCVITGWGSLREGGihacvrrspggvgdtphlhlspd 1227
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRTSEGA----------------------- 136
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   1228 ptGSMARQLQKAAVRVLSEQTCRRFYPVQ--ISSRMLCAGFPQGGVDSCSGDAGGPLACRepSGQWVLTGVTSWGYGCGR 1305
Cdd:smart00020  137 --GSLPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCAR 212
                           250
                    ....*....|....*..
gi 755534801   1306 PHFPGVYTRVAAVLGWI 1322
Cdd:smart00020  213 PGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1071-1322 1.07e-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: 284.17  E-value: 1.07e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801 1071 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiYGDPMQWAAFLGTPFLSSTE--GQLERVARIYRH 1148
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801 1149 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGP-ARPPDGARCVITGWGSLREGGIHacvrrspggvgdtphlhlspd 1227
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgYNLPAGTTCTVSGWGRTSEGGPL--------------------- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801 1228 ptgsmARQLQKAAVRVLSEQTCRRFY--PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGQWVLTGVTSWGYGCGR 1305
Cdd:cd00190   139 -----PDVLQEVNVPIVSNAECKRAYsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCAR 212
                         250
                  ....*....|....*..
gi 755534801 1306 PHFPGVYTRVAAVLGWI 1322
Cdd:cd00190   213 PNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
742-970 1.54e-86

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: 281.10  E-value: 1.54e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801    742 RIVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLgVGGSPVKLGLRRVALH 820
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801    821 PRYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKASVGIIEQKMCGAL 900
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755534801    901 Y--NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACEEtpGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 970
Cdd:smart00020  160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
743-970 2.25e-86

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: 280.70  E-value: 2.25e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  743 IVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLGVGGSPVKLGLRRVALHP 821
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  822 RYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGnATKPDILQKASVGIIEQKMCGALY 901
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755534801  902 --NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACeETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 970
Cdd:cd00190   160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVC-NDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
442-670 3.91e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 242.73  E-value: 3.91e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   442 IVGGVEAAPGEFPWQVSL-RENHEHFCGATIIGARWLVSAAHCFNefqDPAQWAAQAGSVHLSGSEASAVRTRVLRIAKH 520
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   521 PAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDflVKPEVLQKATVELLDQSLCSSL 600
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   601 YGHSLTDRMVCAGYldGKVDSCQGDSGGPLVCEEPsgrfFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 670
Cdd:pfam00089  156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Trypsin pfam00089
Trypsin;
743-970 1.10e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.10  E-value: 1.10e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   743 IVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKveQVQAHLGTVSLLGVGGSPVKLGLRRVALHP 821
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGAS--DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   822 RYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNatKPDILQKASVGIIEQKMCGALY 901
Cdd:pfam00089   79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755534801   902 NFSLTDRMLCAGFleGRVDSCQGDSGGPLACEETpgvfYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 970
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
433-678 8.72e-68

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 229.15  E-value: 8.72e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  433 QPAWRSAGRIVGGVEAAPGEFPWQVSLREN---HEHFCGATIIGARWLVSAAHCFNEfQDPAQWAAQAGSVHLSGSEAsa 509
Cdd:COG5640    22 APAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGG-- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  510 VRTRVLRIAKHPAYDADTADFDVAVLELARPLPFgryVQPACLPAATHVFPPGKKCLISGWGYLKEDFLVKPEVLQKATV 589
Cdd:COG5640    99 TVVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADV 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  590 ELLDQSLCSSlYGHSLTDRMVCAGYLDGKVDSCQGDSGGPLVcEEPSGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDW 669
Cdd:COG5640   176 PVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                  ....*....
gi 755534801  670 ILEVTSAAD 678
Cdd:COG5640   254 IKSTAGGLG 262
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1061-1326 1.40e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 225.68  E-value: 1.40e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801 1061 GLAPPGALTRIVGGSAASLGEWPWQVSLWLR--RREHRCGAVLVAERWLLSAAHCFDIYGdPMQWAAFLGTPFLSSTEGQ 1138
Cdd:COG5640    21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGGT 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801 1139 LERVARIYRHPFYNIYTLDYDVALLELAGPVRRsrlVRPICLPGPARPPD-GARCVITGWGSLREGGihacvrrspggvg 1217
Cdd:COG5640   100 VVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAApGTPATVAGWGRTSEGP------------- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801 1218 dtphlhlspdptGSMARQLQKAAVRVLSEQTCRRfYPVQISSRMLCAGFPQGGVDSCSGDAGGPLAcREPSGQWVLTGVT 1297
Cdd:COG5640   164 ------------GSQSGTLRKADVPVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVV 229
                         250       260
                  ....*....|....*....|....*....
gi 755534801 1298 SWGYGCGRPHFPGVYTRVAAVLGWIGQNI 1326
Cdd:COG5640   230 SWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
1071-1322 3.52e-66

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 223.09  E-value: 3.52e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  1071 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiygDPMQWAAFLGTPFLSSTEG--QLERVARIYRH 1148
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGgeQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  1149 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGP-ARPPDGARCVITGWGSLREGGIhacvrrspggvgdtphlhlspd 1227
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDAsSDLPVGTTCTVSGWGNTKTLGP---------------------- 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  1228 ptgsmARQLQKAAVRVLSEQTCRRFYPVQISSRMLCAGFpqGGVDSCSGDAGGPLACrepSGQwVLTGVTSWGYGCGRPH 1307
Cdd:pfam00089  136 -----SDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGA--GGKDACQGDSGGPLVC---SDG-ELIGIVSWGYGCASGN 204
                          250
                   ....*....|....*
gi 755534801  1308 FPGVYTRVAAVLGWI 1322
Cdd:pfam00089  205 YPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
732-978 4.31e-61

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 209.89  E-value: 4.31e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  732 GARPAMDKPTRIVGGISAVSGEVPWQASL--KEGPR-HFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLGVGGs 808
Cdd:COG5640    20 AAAPAADAAPAIVGGTPATVGEYPWMVALqsSNGPSgQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGG- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  809 pVKLGLRRVALHPRYNPGILDFDVALLELAQPLvfnKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKAS 888
Cdd:COG5640    99 -TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  889 VGIIEQKMCGALYNFsLTDRMLCAGFLEGRVDSCQGDSGGPLAcEETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKD 968
Cdd:COG5640   175 VPVVSDATCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252
                         250
                  ....*....|
gi 755534801  969 WILKAMSSDP 978
Cdd:COG5640   253 WIKSTAGGLG 262
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
393-428 5.56e-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: 49.90  E-value: 5.56e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 755534801  393 CPGNVFSCQNGQCVSKENpECDDRVDCSDESDEAQC 428
Cdd:cd00112     1 CPPNEFRCANGRCIPSSW-VCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
393-425 6.01e-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: 46.86  E-value: 6.01e-07
                            10        20        30
                    ....*....|....*....|....*....|...
gi 755534801    393 CPGNVFSCQNGQCVSKENpECDDRVDCSDESDE 425
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSW-VCDGVDDCGDGSDE 33
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
763-948 3.83e-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: 3.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  763 GPRHFCGATVVGDRWLLSAAHCFNHTkvEQVQAHLGTVSLLGVGGSP-VKLGLRRVALHPRY-NPGILDFDVALLELAQP 840
Cdd:COG3591     9 GGGGVCTGTLIGPNLVLTAGHCVYDG--AGGGWATNIVFVPGYNGGPyGTATATRFRVPPGWvASGDAGYDYALLRLDEP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  841 LVFnkyiQPVCLPLAI-HKFPVGRKCMISGWGnmqegnATKPDILQKASVGIIeqkmcgalynFSLTDRmlcagFLEGRV 919
Cdd:COG3591    87 LGD----TTGWLGLAFnDAPLAGEPVTIIGYP------GDRPKDLSLDCSGRV----------TGVQGN-----RLSYDC 141
                         170       180
                  ....*....|....*....|....*....
gi 755534801  920 DSCQGDSGGPLaCEETPGVFYLAGIVSWG 948
Cdd:COG3591   142 DTTGGSSGSPV-LDDSDGGGRVVGVHSAG 169
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
465-671 4.71e-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: 4.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  465 HFCGATIIGARWLVSAAHCFNEFQD---PAQWAAQAGSVHLSGSEASAVRTRVlriakHPAYDADT-ADFDVAVLELARP 540
Cdd:COG3591    12 GVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPGYNGGPYGTATATRFRV-----PPGWVASGdAGYDYALLRLDEP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801  541 LPfgrYVQPACLPAATHVFPPGKKCLISGWGylkedflvkpevlqkatvelldqslcsslYGHSLTDRMVCAGYLDG--- 617
Cdd:COG3591    87 LG---DTTGWLGLAFNDAPLAGEPVTIIGYP-----------------------------GDRPKDLSLDCSGRVTGvqg 134
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755534801  618 -----KVDSCQGDSGGPLVCEEpSGRFFLAGIVSWGigcaearRPGVYTRVTRLRDWIL 671
Cdd:COG3591   135 nrlsyDCDTTGGSSGSPVLDDS-DGGGRVVGVHSAG-------GADRANTGVRLTSAIV 185
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
285-365 4.77e-06

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: 46.46  E-value: 4.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534801   285 IRFTSSLQQENSDFYRLLTHALQTLFVSSFQKTELESSCAGCTVLSYRDGNSTVIVHFRLHFllralQPLSLKQEADILQ 364
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVF-----RFPSTEPALDREK 86

                   .
gi 755534801   365 K 365
Cdd:pfam01390   87 L 87
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
393-428 9.19e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 43.78  E-value: 9.19e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 755534801   393 CPGNVFSCQNGQCVSKeNPECDDRVDCSDESDEAQC 428
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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