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Conserved domains on  [gi|755534797|ref|XP_006513905|]
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transmembrane protease serine 9 isoform X1 [Mus musculus]

Protein Classification

LDLa and Tryp_SPc domain-containing protein( domain architecture ID 12018001)

protein containing domains SEA, LDLa, PHA03247, and Tryp_SPc

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 ...
455-684 3.75e-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: 3.75e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797    455 RIVGGVEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEASAVRtRVLRIAK 533
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797    534 HPAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDFLVKPEVLQKATVELLDQSLCSS 613
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755534797    614 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 684
Cdd:smart00020  159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1085-1336 1.08e-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: 284.55  E-value: 1.08e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797 1085 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiYGDPMQWAAFLGTPFLSSTE--GQLERVARIYRH 1162
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797 1163 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGP-ARPPDGARCVITGWGSLREGGIHacvrrspggvgdtphlhlspd 1241
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgYNLPAGTTCTVSGWGRTSEGGPL--------------------- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797 1242 ptgsmARQLQKAAVRVLSEQTCRRFY--PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGQWVLTGVTSWGYGCGR 1319
Cdd:cd00190   139 -----PDVLQEVNVPIVSNAECKRAYsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCAR 212
                         250
                  ....*....|....*..
gi 755534797 1320 PHFPGVYTRVAAVLGWI 1336
Cdd:cd00190   213 PNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
756-984 1.62e-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: 1.62e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797    756 RIVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLgVGGSPVKLGLRRVALH 834
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797    835 PRYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKASVGIIEQKMCGAL 914
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755534797    915 Y--NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACEEtpGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 984
Cdd:smart00020  160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
407-442 6.31e-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: 6.31e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 755534797  407 CPGNVFSCQNGQCVSKENpECDDRVDCSDESDEAQC 442
Cdd:cd00112     1 CPPNEFRCANGRCIPSSW-VCDGEDDCGDGSDEENC 35
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
285-365 4.82e-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: 4.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   285 IRFTSSLQQENSDFYRLLTHALQTLFVSSFQKTELESSCAGCTVLSYRDGNSTVIVHFRLHFllralQPLSLKQEADILQ 364
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVF-----RFPSTEPALDREK 86

                   .
gi 755534797   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 ...
455-684 3.75e-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: 3.75e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797    455 RIVGGVEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEASAVRtRVLRIAK 533
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797    534 HPAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDFLVKPEVLQKATVELLDQSLCSS 613
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755534797    614 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 684
Cdd:smart00020  159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
456-684 8.82e-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: 8.82e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  456 IVGGVEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEASAVRTRVLRIAKH 534
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  535 PAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDfLVKPEVLQKATVELLDQSLCSSL 614
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755534797  615 YGHS--LTDRMVCAGYLDGKVDSCQGDSGGPLVCEEPsGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 684
Cdd:cd00190   159 YSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1085-1336 1.08e-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: 284.55  E-value: 1.08e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797 1085 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiYGDPMQWAAFLGTPFLSSTE--GQLERVARIYRH 1162
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797 1163 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGP-ARPPDGARCVITGWGSLREGGIHacvrrspggvgdtphlhlspd 1241
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgYNLPAGTTCTVSGWGRTSEGGPL--------------------- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797 1242 ptgsmARQLQKAAVRVLSEQTCRRFY--PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGQWVLTGVTSWGYGCGR 1319
Cdd:cd00190   139 -----PDVLQEVNVPIVSNAECKRAYsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCAR 212
                         250
                  ....*....|....*..
gi 755534797 1320 PHFPGVYTRVAAVLGWI 1336
Cdd:cd00190   213 PNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1084-1336 1.10e-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: 1.10e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   1084 RIVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiYGDPMQWAAFLGTPFLSSTE-GQLERVARIYRH 1162
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEeGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   1163 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGPAR-PPDGARCVITGWGSLREGGihacvrrspggvgdtphlhlspd 1241
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRTSEGA----------------------- 136
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   1242 ptGSMARQLQKAAVRVLSEQTCRRFYPVQ--ISSRMLCAGFPQGGVDSCSGDAGGPLACRepSGQWVLTGVTSWGYGCGR 1319
Cdd:smart00020  137 --GSLPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCAR 212
                           250
                    ....*....|....*..
gi 755534797   1320 PHFPGVYTRVAAVLGWI 1336
Cdd:smart00020  213 PGKPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
756-984 1.62e-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: 1.62e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797    756 RIVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLgVGGSPVKLGLRRVALH 834
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797    835 PRYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKASVGIIEQKMCGAL 914
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755534797    915 Y--NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACEEtpGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 984
Cdd:smart00020  160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
757-984 2.29e-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: 2.29e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  757 IVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLGVGGSPVKLGLRRVALHP 835
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  836 RYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGnATKPDILQKASVGIIEQKMCGALY 915
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755534797  916 --NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACeETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 984
Cdd:cd00190   160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVC-NDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
456-684 3.98e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 242.73  E-value: 3.98e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   456 IVGGVEAAPGEFPWQVSL-RENHEHFCGATIIGARWLVSAAHCFNefqDPAQWAAQAGSVHLSGSEASAVRTRVLRIAKH 534
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   535 PAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDflVKPEVLQKATVELLDQSLCSSL 614
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   615 YGHSLTDRMVCAGYldGKVDSCQGDSGGPLVCEEPsgrfFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 684
Cdd:pfam00089  156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Trypsin pfam00089
Trypsin;
757-984 1.06e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.10  E-value: 1.06e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   757 IVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKveQVQAHLGTVSLLGVGGSPVKLGLRRVALHP 835
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGAS--DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   836 RYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNatKPDILQKASVGIIEQKMCGALY 915
Cdd:pfam00089   79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755534797   916 NFSLTDRMLCAGFleGRVDSCQGDSGGPLACEETpgvfYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 984
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
447-692 7.69e-68

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 229.54  E-value: 7.69e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  447 QPAWRSAGRIVGGVEAAPGEFPWQVSLREN---HEHFCGATIIGARWLVSAAHCFNEfQDPAQWAAQAGSVHLSGSEAsa 523
Cdd:COG5640    22 APAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGG-- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  524 VRTRVLRIAKHPAYDADTADFDVAVLELARPLPFgryVQPACLPAATHVFPPGKKCLISGWGYLKEDFLVKPEVLQKATV 603
Cdd:COG5640    99 TVVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADV 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  604 ELLDQSLCSSlYGHSLTDRMVCAGYLDGKVDSCQGDSGGPLVcEEPSGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDW 683
Cdd:COG5640   176 PVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                  ....*....
gi 755534797  684 ILEVTSAAD 692
Cdd:COG5640   254 IKSTAGGLG 262
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1075-1340 1.27e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 226.07  E-value: 1.27e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797 1075 GLAPPGALTRIVGGSAASLGEWPWQVSLWLR--RREHRCGAVLVAERWLLSAAHCFDIYGdPMQWAAFLGTPFLSSTEGQ 1152
Cdd:COG5640    21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGGT 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797 1153 LERVARIYRHPFYNIYTLDYDVALLELAGPVRRsrlVRPICLPGPARPPD-GARCVITGWGSLREGGihacvrrspggvg 1231
Cdd:COG5640   100 VVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAApGTPATVAGWGRTSEGP------------- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797 1232 dtphlhlspdptGSMARQLQKAAVRVLSEQTCRRfYPVQISSRMLCAGFPQGGVDSCSGDAGGPLAcREPSGQWVLTGVT 1311
Cdd:COG5640   164 ------------GSQSGTLRKADVPVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVV 229
                         250       260
                  ....*....|....*....|....*....
gi 755534797 1312 SWGYGCGRPHFPGVYTRVAAVLGWIGQNI 1340
Cdd:COG5640   230 SWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
1085-1336 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 755534797  1085 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiygDPMQWAAFLGTPFLSSTEG--QLERVARIYRH 1162
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGgeQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  1163 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGP-ARPPDGARCVITGWGSLREGGIhacvrrspggvgdtphlhlspd 1241
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDAsSDLPVGTTCTVSGWGNTKTLGP---------------------- 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  1242 ptgsmARQLQKAAVRVLSEQTCRRFYPVQISSRMLCAGFpqGGVDSCSGDAGGPLACrepSGQwVLTGVTSWGYGCGRPH 1321
Cdd:pfam00089  136 -----SDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGA--GGKDACQGDSGGPLVC---SDG-ELIGIVSWGYGCASGN 204
                          250
                   ....*....|....*
gi 755534797  1322 FPGVYTRVAAVLGWI 1336
Cdd:pfam00089  205 YPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
746-992 3.89e-61

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 210.28  E-value: 3.89e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  746 GARPAMDKPTRIVGGISAVSGEVPWQASL--KEGPR-HFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLGVGGs 822
Cdd:COG5640    20 AAAPAADAAPAIVGGTPATVGEYPWMVALqsSNGPSgQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGG- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  823 pVKLGLRRVALHPRYNPGILDFDVALLELAQPLvfnKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKAS 902
Cdd:COG5640    99 -TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  903 VGIIEQKMCGALYNFsLTDRMLCAGFLEGRVDSCQGDSGGPLAcEETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKD 982
Cdd:COG5640   175 VPVVSDATCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252
                         250
                  ....*....|
gi 755534797  983 WILKAMSSDP 992
Cdd:COG5640   253 WIKSTAGGLG 262
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
407-442 6.31e-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: 6.31e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 755534797  407 CPGNVFSCQNGQCVSKENpECDDRVDCSDESDEAQC 442
Cdd:cd00112     1 CPPNEFRCANGRCIPSSW-VCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
407-439 6.77e-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: 6.77e-07
                            10        20        30
                    ....*....|....*....|....*....|...
gi 755534797    407 CPGNVFSCQNGQCVSKENpECDDRVDCSDESDE 439
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSW-VCDGVDDCGDGSDE 33
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
285-365 4.82e-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: 4.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   285 IRFTSSLQQENSDFYRLLTHALQTLFVSSFQKTELESSCAGCTVLSYRDGNSTVIVHFRLHFllralQPLSLKQEADILQ 364
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVF-----RFPSTEPALDREK 86

                   .
gi 755534797   365 K 365
Cdd:pfam01390   87 L 87
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
407-442 1.00e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 43.39  E-value: 1.00e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 755534797   407 CPGNVFSCQNGQCVSKeNPECDDRVDCSDESDEAQC 442
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 ...
455-684 3.75e-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: 3.75e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797    455 RIVGGVEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEASAVRtRVLRIAK 533
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797    534 HPAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDFLVKPEVLQKATVELLDQSLCSS 613
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755534797    614 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 684
Cdd:smart00020  159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
456-684 8.82e-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: 8.82e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  456 IVGGVEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEASAVRTRVLRIAKH 534
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  535 PAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDfLVKPEVLQKATVELLDQSLCSSL 614
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755534797  615 YGHS--LTDRMVCAGYLDGKVDSCQGDSGGPLVCEEPsGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 684
Cdd:cd00190   159 YSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1085-1336 1.08e-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: 284.55  E-value: 1.08e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797 1085 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiYGDPMQWAAFLGTPFLSSTE--GQLERVARIYRH 1162
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797 1163 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGP-ARPPDGARCVITGWGSLREGGIHacvrrspggvgdtphlhlspd 1241
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgYNLPAGTTCTVSGWGRTSEGGPL--------------------- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797 1242 ptgsmARQLQKAAVRVLSEQTCRRFY--PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGQWVLTGVTSWGYGCGR 1319
Cdd:cd00190   139 -----PDVLQEVNVPIVSNAECKRAYsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCAR 212
                         250
                  ....*....|....*..
gi 755534797 1320 PHFPGVYTRVAAVLGWI 1336
Cdd:cd00190   213 PNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1084-1336 1.10e-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: 1.10e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   1084 RIVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiYGDPMQWAAFLGTPFLSSTE-GQLERVARIYRH 1162
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEeGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   1163 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGPAR-PPDGARCVITGWGSLREGGihacvrrspggvgdtphlhlspd 1241
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRTSEGA----------------------- 136
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   1242 ptGSMARQLQKAAVRVLSEQTCRRFYPVQ--ISSRMLCAGFPQGGVDSCSGDAGGPLACRepSGQWVLTGVTSWGYGCGR 1319
Cdd:smart00020  137 --GSLPDTLQEVNVPIVSNATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCAR 212
                           250
                    ....*....|....*..
gi 755534797   1320 PHFPGVYTRVAAVLGWI 1336
Cdd:smart00020  213 PGKPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
756-984 1.62e-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: 1.62e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797    756 RIVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLgVGGSPVKLGLRRVALH 834
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797    835 PRYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKASVGIIEQKMCGAL 914
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755534797    915 Y--NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACEEtpGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 984
Cdd:smart00020  160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
757-984 2.29e-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: 2.29e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  757 IVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLGVGGSPVKLGLRRVALHP 835
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  836 RYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGnATKPDILQKASVGIIEQKMCGALY 915
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755534797  916 --NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACeETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 984
Cdd:cd00190   160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVC-NDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
456-684 3.98e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 242.73  E-value: 3.98e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   456 IVGGVEAAPGEFPWQVSL-RENHEHFCGATIIGARWLVSAAHCFNefqDPAQWAAQAGSVHLSGSEASAVRTRVLRIAKH 534
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   535 PAYDADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPGKKCLISGWGYLKEDflVKPEVLQKATVELLDQSLCSSL 614
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   615 YGHSLTDRMVCAGYldGKVDSCQGDSGGPLVCEEPsgrfFLAGIVSWGIGCAEARRPGVYTRVTRLRDWI 684
Cdd:pfam00089  156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Trypsin pfam00089
Trypsin;
757-984 1.06e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.10  E-value: 1.06e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   757 IVGGISAVSGEVPWQASLK-EGPRHFCGATVVGDRWLLSAAHCFNHTKveQVQAHLGTVSLLGVGGSPVKLGLRRVALHP 835
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGAS--DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   836 RYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNatKPDILQKASVGIIEQKMCGALY 915
Cdd:pfam00089   79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755534797   916 NFSLTDRMLCAGFleGRVDSCQGDSGGPLACEETpgvfYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 984
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
447-692 7.69e-68

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 229.54  E-value: 7.69e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  447 QPAWRSAGRIVGGVEAAPGEFPWQVSLREN---HEHFCGATIIGARWLVSAAHCFNEfQDPAQWAAQAGSVHLSGSEAsa 523
Cdd:COG5640    22 APAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGG-- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  524 VRTRVLRIAKHPAYDADTADFDVAVLELARPLPFgryVQPACLPAATHVFPPGKKCLISGWGYLKEDFLVKPEVLQKATV 603
Cdd:COG5640    99 TVVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADV 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  604 ELLDQSLCSSlYGHSLTDRMVCAGYLDGKVDSCQGDSGGPLVcEEPSGRFFLAGIVSWGIGCAEARRPGVYTRVTRLRDW 683
Cdd:COG5640   176 PVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                  ....*....
gi 755534797  684 ILEVTSAAD 692
Cdd:COG5640   254 IKSTAGGLG 262
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1075-1340 1.27e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 226.07  E-value: 1.27e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797 1075 GLAPPGALTRIVGGSAASLGEWPWQVSLWLR--RREHRCGAVLVAERWLLSAAHCFDIYGdPMQWAAFLGTPFLSSTEGQ 1152
Cdd:COG5640    21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGGT 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797 1153 LERVARIYRHPFYNIYTLDYDVALLELAGPVRRsrlVRPICLPGPARPPD-GARCVITGWGSLREGGihacvrrspggvg 1231
Cdd:COG5640   100 VVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAApGTPATVAGWGRTSEGP------------- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797 1232 dtphlhlspdptGSMARQLQKAAVRVLSEQTCRRfYPVQISSRMLCAGFPQGGVDSCSGDAGGPLAcREPSGQWVLTGVT 1311
Cdd:COG5640   164 ------------GSQSGTLRKADVPVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVV 229
                         250       260
                  ....*....|....*....|....*....
gi 755534797 1312 SWGYGCGRPHFPGVYTRVAAVLGWIGQNI 1340
Cdd:COG5640   230 SWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
1085-1336 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 755534797  1085 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDiygDPMQWAAFLGTPFLSSTEG--QLERVARIYRH 1162
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGgeQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  1163 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGP-ARPPDGARCVITGWGSLREGGIhacvrrspggvgdtphlhlspd 1241
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDAsSDLPVGTTCTVSGWGNTKTLGP---------------------- 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  1242 ptgsmARQLQKAAVRVLSEQTCRRFYPVQISSRMLCAGFpqGGVDSCSGDAGGPLACrepSGQwVLTGVTSWGYGCGRPH 1321
Cdd:pfam00089  136 -----SDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGA--GGKDACQGDSGGPLVC---SDG-ELIGIVSWGYGCASGN 204
                          250
                   ....*....|....*
gi 755534797  1322 FPGVYTRVAAVLGWI 1336
Cdd:pfam00089  205 YPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
746-992 3.89e-61

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 210.28  E-value: 3.89e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  746 GARPAMDKPTRIVGGISAVSGEVPWQASL--KEGPR-HFCGATVVGDRWLLSAAHCFNHTKVEQVQAHLGTVSLLGVGGs 822
Cdd:COG5640    20 AAAPAADAAPAIVGGTPATVGEYPWMVALqsSNGPSgQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGG- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  823 pVKLGLRRVALHPRYNPGILDFDVALLELAQPLvfnKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKAS 902
Cdd:COG5640    99 -TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  903 VGIIEQKMCGALYNFsLTDRMLCAGFLEGRVDSCQGDSGGPLAcEETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKD 982
Cdd:COG5640   175 VPVVSDATCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252
                         250
                  ....*....|
gi 755534797  983 WILKAMSSDP 992
Cdd:COG5640   253 WIKSTAGGLG 262
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
407-442 6.31e-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: 6.31e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 755534797  407 CPGNVFSCQNGQCVSKENpECDDRVDCSDESDEAQC 442
Cdd:cd00112     1 CPPNEFRCANGRCIPSSW-VCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
407-439 6.77e-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: 6.77e-07
                            10        20        30
                    ....*....|....*....|....*....|...
gi 755534797    407 CPGNVFSCQNGQCVSKENpECDDRVDCSDESDE 439
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSW-VCDGVDDCGDGSDE 33
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
777-962 3.56e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 49.29  E-value: 3.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  777 GPRHFCGATVVGDRWLLSAAHCFNHTkvEQVQAHLGTVSLLGVGGSP-VKLGLRRVALHPRY-NPGILDFDVALLELAQP 854
Cdd:COG3591     9 GGGGVCTGTLIGPNLVLTAGHCVYDG--AGGGWATNIVFVPGYNGGPyGTATATRFRVPPGWvASGDAGYDYALLRLDEP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  855 LVFnkyiQPVCLPLAI-HKFPVGRKCMISGWGnmqegnATKPDILQKASVGIIeqkmcgalynFSLTDRmlcagFLEGRV 933
Cdd:COG3591    87 LGD----TTGWLGLAFnDAPLAGEPVTIIGYP------GDRPKDLSLDCSGRV----------TGVQGN-----RLSYDC 141
                         170       180
                  ....*....|....*....|....*....
gi 755534797  934 DSCQGDSGGPLaCEETPGVFYLAGIVSWG 962
Cdd:COG3591   142 DTTGGSSGSPV-LDDSDGGGRVVGVHSAG 169
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
479-685 4.38e-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: 4.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  479 HFCGATIIGARWLVSAAHCFNEFQD---PAQWAAQAGSVHLSGSEASAVRTRVlriakHPAYDADT-ADFDVAVLELARP 554
Cdd:COG3591    12 GVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPGYNGGPYGTATATRFRV-----PPGWVASGdAGYDYALLRLDEP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797  555 LPfgrYVQPACLPAATHVFPPGKKCLISGWGylkedflvkpevlqkatvelldqslcsslYGHSLTDRMVCAGYLDG--- 631
Cdd:COG3591    87 LG---DTTGWLGLAFNDAPLAGEPVTIIGYP-----------------------------GDRPKDLSLDCSGRVTGvqg 134
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755534797  632 -----KVDSCQGDSGGPLVCEEpSGRFFLAGIVSWGigcaearRPGVYTRVTRLRDWIL 685
Cdd:COG3591   135 nrlsyDCDTTGGSSGSPVLDDS-DGGGRVVGVHSAG-------GADRANTGVRLTSAIV 185
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
285-365 4.82e-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: 4.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534797   285 IRFTSSLQQENSDFYRLLTHALQTLFVSSFQKTELESSCAGCTVLSYRDGNSTVIVHFRLHFllralQPLSLKQEADILQ 364
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVF-----RFPSTEPALDREK 86

                   .
gi 755534797   365 K 365
Cdd:pfam01390   87 L 87
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
407-442 1.00e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 43.39  E-value: 1.00e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 755534797   407 CPGNVFSCQNGQCVSKeNPECDDRVDCSDESDEAQC 442
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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