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Conserved domains on  [gi|1622897949|ref|XP_028695702|]
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transmembrane protease serine 9 isoform X1 [Macaca mulatta]

Protein Classification

LDL receptor domain-containing protein; serine protease( domain architecture ID 12018001)

Low Density Lipoprotein (LDL) receptor class A domain is a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism| trypsin-like serine protease catalyzes the cleavage of specific peptide bonds in protein substrates using an active site serine as the nucleophile; contains C-terminal DNA polymerase III subunits gamma and tau

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
236-465 7.86e-97

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: 306.53  E-value: 7.86e-97
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949   236 RIVGGVEASPGEFPWQASLR-ENKEHFCGATIISARWLVSAAHCFNEFqDPTEWVAYVGTTYLSGSEASTVRaRVAQIIK 314
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949   315 HPLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATVELLDQALCAS 394
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622897949   395 LYG--HSLTDRMLCAGYLDGKVDSCQGDSGGPLVCEEppGRFFLAGIVSWGIGCAEAQRPGVYARVTKLRDWI 465
Cdd:smart00020  159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
863-1089 3.02e-94

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 299.58  E-value: 3.02e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  863 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDlYGDPKQWAAFLGTPFLSGPE--GQLERVARIYKH 940
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  941 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPVPRPPDGARCVITGWGSVREGGSMARQLQKAAVRLLSEQTCRRFY 1020
Cdd:cd00190     80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622897949 1021 --PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 1089
Cdd:cd00190    160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
538-768 9.30e-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: 279.55  E-value: 9.30e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  538 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVWAHLGTASLLGLGGSPVKIGLRRVVLHP 616
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  617 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNMQEGnATKPELLQKASVGIIDQKTCSVLY 696
Cdd:cd00190     81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622897949  697 --NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEaPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWILEI 768
Cdd:cd00190    160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
188-223 5.63e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 49.51  E-value: 5.63e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1622897949  188 CPGNSFSCQNSQCV--TKVnpeCDDQEDCSDGSDEVHC 223
Cdd:cd00112      1 CPPNEFRCANGRCIpsSWV---CDGEDDCGDGSDEENC 35
SEA super family cl02507
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
66-127 1.07e-03

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.


The actual alignment was detected with superfamily member pfam01390:

Pssm-ID: 470595  Cd Length: 100  Bit Score: 39.53  E-value: 1.07e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897949   66 IRWASSLRQEASDYHRTLTPTLEALFVSSFQKTELEASCVGCTVLNYRDGNSSVLVHFRLRF 127
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVF 73
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
236-465 7.86e-97

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: 306.53  E-value: 7.86e-97
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949   236 RIVGGVEASPGEFPWQASLR-ENKEHFCGATIISARWLVSAAHCFNEFqDPTEWVAYVGTTYLSGSEASTVRaRVAQIIK 314
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949   315 HPLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATVELLDQALCAS 394
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622897949   395 LYG--HSLTDRMLCAGYLDGKVDSCQGDSGGPLVCEEppGRFFLAGIVSWGIGCAEAQRPGVYARVTKLRDWI 465
Cdd:smart00020  159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
237-465 5.48e-96

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: 304.58  E-value: 5.48e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  237 IVGGVEASPGEFPWQASLR-ENKEHFCGATIISARWLVSAAHCFNEFqDPTEWVAYVGTTYLSGSEASTVRARVAQIIKH 315
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  316 PLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDfLVKPEVLQKATVELLDQALCASL 395
Cdd:cd00190     80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRA 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897949  396 YGHS--LTDRMLCAGYLDGKVDSCQGDSGGPLVCEEpPGRFFLAGIVSWGIGCAEAQRPGVYARVTKLRDWI 465
Cdd:cd00190    159 YSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
863-1089 3.02e-94

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 299.58  E-value: 3.02e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  863 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDlYGDPKQWAAFLGTPFLSGPE--GQLERVARIYKH 940
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  941 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPVPRPPDGARCVITGWGSVREGGSMARQLQKAAVRLLSEQTCRRFY 1020
Cdd:cd00190     80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622897949 1021 --PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 1089
Cdd:cd00190    160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
862-1089 3.22e-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: 296.90  E-value: 3.22e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949   862 RIVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDlYGDPKQWAAFLG-TPFLSGPEGQLERVARIYKH 940
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGsHDLSSGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949   941 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPVPRPPDGARCVITGWGSVREG-GSMARQLQKAAVRLLSEQTCRRF 1019
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897949  1020 YPVQ--ISSRMLCAGFPQGGVDSCSGDAGGPLACRepSGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 1089
Cdd:smart00020  160 YSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
538-768 9.30e-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: 279.55  E-value: 9.30e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  538 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVWAHLGTASLLGLGGSPVKIGLRRVVLHP 616
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  617 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNMQEGnATKPELLQKASVGIIDQKTCSVLY 696
Cdd:cd00190     81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622897949  697 --NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEaPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWILEI 768
Cdd:cd00190    160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
537-765 3.16e-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: 278.02  E-value: 3.16e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949   537 RVVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVWAHLGTASLLgLGGSPVKIGLRRVVLH 615
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949   616 PLYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNMQEGNATKPELLQKASVGIIDQKTCSVL 695
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897949   696 Y--NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEapGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWI 765
Cdd:smart00020  160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
237-465 6.82e-75

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 246.59  E-value: 6.82e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  237 IVGGVEASPGEFPWQASL-RENKEHFCGATIISARWLVSAAHCFNefqDPTEWVAYVGTTYLSGSEASTVRARVAQIIKH 315
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  316 PLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDflVKPEVLQKATVELLDQALCASL 395
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  396 YGHSLTDRMLCAGYldGKVDSCQGDSGGPLVCEEPpgrfFLAGIVSWGIGCAEAQRPGVYARVTKLRDWI 465
Cdd:pfam00089  156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Trypsin pfam00089
Trypsin;
863-1089 3.49e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.49  E-value: 3.49e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  863 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDlygDPKQWAAFLGTPFLSGPEG--QLERVARIYKH 940
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGgeQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  941 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPVPRPPDGARCVITGWGSVREGGSmARQLQKAAVRLLSEQTCRRFY 1020
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897949 1021 PVQISSRMLCAGFpqGGVDSCSGDAGGPLACREPsgrwVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 1089
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Trypsin pfam00089
Trypsin;
538-765 7.29e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 232.33  E-value: 7.29e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  538 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVWahLGTASLLGLGGSPVKIGLRRVVLHP 616
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASDVKVV--LGAHNIVLREGGEQKFDVEKIIVHP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  617 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNMQEGNatKPELLQKASVGIIDQKTCSVLY 696
Cdd:pfam00089   79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897949  697 NFSLTDRMICAGFleGKVDSCQGDSGGPLACEEApgvfYLAGIVSWGIGCAQVKKPGVYTRITRLKGWI 765
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
856-1093 9.83e-70

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 233.77  E-value: 9.83e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  856 APAALSRIVGGSAAGRGEWPWQVSLWLR--RREHRCGAVLVAERWLLSAAHCFDLYGdPKQWAAFLGTPFLSGPEGQLER 933
Cdd:COG5640     24 AADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGGTVVK 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  934 VARIYKHPFYNLYTLDYDVALLELAGPVRRsrlVRPICLPEPVPRPPDGARCVITGWGSVREG-GSMARQLQKAAVRLLS 1012
Cdd:COG5640    103 VARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVS 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949 1013 EQTCRRfYPVQISSRMLCAGFPQGGVDSCSGDAGGPLAcREPSGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWIGQH 1092
Cdd:COG5640    180 DATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKST 257

                   .
gi 1622897949 1093 I 1093
Cdd:COG5640    258 A 258
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
228-469 6.01e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 223.37  E-value: 6.01e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  228 QPAWRMAGRIVGGVEASPGEFPWQASLRENK---EHFCGATIISARWLVSAAHCFNEfQDPTEWVAYVGTTYLSGSEAst 304
Cdd:COG5640     22 APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGG-- 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  305 VRARVAQIIKHPLYNADTADFDVAVLELTSPLPFgrhIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATV 384
Cdd:COG5640     99 TVVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADV 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  385 ELLDQALCASlYGHSLTDRMLCAGYLDGKVDSCQGDSGGPLVcEEPPGRFFLAGIVSWGIGCAEAQRPGVYARVTKLRDW 464
Cdd:COG5640    176 PVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                   ....*
gi 1622897949  465 ILEAT 469
Cdd:COG5640    254 IKSTA 258
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
527-773 2.00e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 204.88  E-value: 2.00e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  527 GARPAMEKPTRVVGGFGAASGEVPWQVSL---KEGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVWAHLGTASLLGLGGS 603
Cdd:COG5640     20 AAAPAADAAPAIVGGTPATVGEYPWMVALqssNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGT 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  604 PVKIglRRVVLHPLYNPGILDFDLAVLELASPLAFNKYIQpvcLPLAIQKFPVGRKCMISGWGNMQEGNATKPELLQKAS 683
Cdd:COG5640    100 VVKV--ARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  684 VGIIDQKTCSVLYNFsLTDRMICAGFLEGKVDSCQGDSGGPLAcEEAPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKG 763
Cdd:COG5640    175 VPVVSDATCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252
                          250
                   ....*....|
gi 1622897949  764 WILEIMSSQP 773
Cdd:COG5640    253 WIKSTAGGLG 262
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
188-223 5.63e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 49.51  E-value: 5.63e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1622897949  188 CPGNSFSCQNSQCV--TKVnpeCDDQEDCSDGSDEVHC 223
Cdd:cd00112      1 CPPNEFRCANGRCIpsSWV---CDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
188-220 6.66e-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: 46.47  E-value: 6.66e-07
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1622897949   188 CPGNSFSCQNSQCV--TKVnpeCDDQEDCSDGSDE 220
Cdd:smart00192    2 CPPGEFQCDNGRCIpsSWV---CDGVDDCGDGSDE 33
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
66-127 1.07e-03

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: 39.53  E-value: 1.07e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897949   66 IRWASSLRQEASDYHRTLTPTLEALFVSSFQKTELEASCVGCTVLNYRDGNSSVLVHFRLRF 127
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVF 73
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
236-465 7.86e-97

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: 306.53  E-value: 7.86e-97
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949   236 RIVGGVEASPGEFPWQASLR-ENKEHFCGATIISARWLVSAAHCFNEFqDPTEWVAYVGTTYLSGSEASTVRaRVAQIIK 314
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949   315 HPLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATVELLDQALCAS 394
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622897949   395 LYG--HSLTDRMLCAGYLDGKVDSCQGDSGGPLVCEEppGRFFLAGIVSWGIGCAEAQRPGVYARVTKLRDWI 465
Cdd:smart00020  159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
237-465 5.48e-96

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: 304.58  E-value: 5.48e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  237 IVGGVEASPGEFPWQASLR-ENKEHFCGATIISARWLVSAAHCFNEFqDPTEWVAYVGTTYLSGSEASTVRARVAQIIKH 315
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  316 PLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDfLVKPEVLQKATVELLDQALCASL 395
Cdd:cd00190     80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRA 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897949  396 YGHS--LTDRMLCAGYLDGKVDSCQGDSGGPLVCEEpPGRFFLAGIVSWGIGCAEAQRPGVYARVTKLRDWI 465
Cdd:cd00190    159 YSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
863-1089 3.02e-94

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 299.58  E-value: 3.02e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  863 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDlYGDPKQWAAFLGTPFLSGPE--GQLERVARIYKH 940
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  941 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPVPRPPDGARCVITGWGSVREGGSMARQLQKAAVRLLSEQTCRRFY 1020
Cdd:cd00190     80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622897949 1021 --PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 1089
Cdd:cd00190    160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
862-1089 3.22e-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: 296.90  E-value: 3.22e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949   862 RIVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDlYGDPKQWAAFLG-TPFLSGPEGQLERVARIYKH 940
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGsHDLSSGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949   941 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPVPRPPDGARCVITGWGSVREG-GSMARQLQKAAVRLLSEQTCRRF 1019
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897949  1020 YPVQ--ISSRMLCAGFPQGGVDSCSGDAGGPLACRepSGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 1089
Cdd:smart00020  160 YSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
538-768 9.30e-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: 279.55  E-value: 9.30e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  538 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVWAHLGTASLLGLGGSPVKIGLRRVVLHP 616
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  617 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNMQEGnATKPELLQKASVGIIDQKTCSVLY 696
Cdd:cd00190     81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622897949  697 --NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEaPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWILEI 768
Cdd:cd00190    160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
537-765 3.16e-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: 278.02  E-value: 3.16e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949   537 RVVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVWAHLGTASLLgLGGSPVKIGLRRVVLH 615
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949   616 PLYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNMQEGNATKPELLQKASVGIIDQKTCSVL 695
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897949   696 Y--NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEapGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWI 765
Cdd:smart00020  160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
237-465 6.82e-75

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 246.59  E-value: 6.82e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  237 IVGGVEASPGEFPWQASL-RENKEHFCGATIISARWLVSAAHCFNefqDPTEWVAYVGTTYLSGSEASTVRARVAQIIKH 315
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  316 PLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDflVKPEVLQKATVELLDQALCASL 395
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  396 YGHSLTDRMLCAGYldGKVDSCQGDSGGPLVCEEPpgrfFLAGIVSWGIGCAEAQRPGVYARVTKLRDWI 465
Cdd:pfam00089  156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Trypsin pfam00089
Trypsin;
863-1089 3.49e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.49  E-value: 3.49e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  863 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDlygDPKQWAAFLGTPFLSGPEG--QLERVARIYKH 940
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGgeQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  941 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPVPRPPDGARCVITGWGSVREGGSmARQLQKAAVRLLSEQTCRRFY 1020
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897949 1021 PVQISSRMLCAGFpqGGVDSCSGDAGGPLACREPsgrwVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 1089
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Trypsin pfam00089
Trypsin;
538-765 7.29e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 232.33  E-value: 7.29e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  538 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVWahLGTASLLGLGGSPVKIGLRRVVLHP 616
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASDVKVV--LGAHNIVLREGGEQKFDVEKIIVHP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  617 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNMQEGNatKPELLQKASVGIIDQKTCSVLY 696
Cdd:pfam00089   79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897949  697 NFSLTDRMICAGFleGKVDSCQGDSGGPLACEEApgvfYLAGIVSWGIGCAQVKKPGVYTRITRLKGWI 765
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
856-1093 9.83e-70

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 233.77  E-value: 9.83e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  856 APAALSRIVGGSAAGRGEWPWQVSLWLR--RREHRCGAVLVAERWLLSAAHCFDLYGdPKQWAAFLGTPFLSGPEGQLER 933
Cdd:COG5640     24 AADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGGTVVK 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  934 VARIYKHPFYNLYTLDYDVALLELAGPVRRsrlVRPICLPEPVPRPPDGARCVITGWGSVREG-GSMARQLQKAAVRLLS 1012
Cdd:COG5640    103 VARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVS 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949 1013 EQTCRRfYPVQISSRMLCAGFPQGGVDSCSGDAGGPLAcREPSGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWIGQH 1092
Cdd:COG5640    180 DATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKST 257

                   .
gi 1622897949 1093 I 1093
Cdd:COG5640    258 A 258
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
228-469 6.01e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 223.37  E-value: 6.01e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  228 QPAWRMAGRIVGGVEASPGEFPWQASLRENK---EHFCGATIISARWLVSAAHCFNEfQDPTEWVAYVGTTYLSGSEAst 304
Cdd:COG5640     22 APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGG-- 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  305 VRARVAQIIKHPLYNADTADFDVAVLELTSPLPFgrhIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATV 384
Cdd:COG5640     99 TVVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADV 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  385 ELLDQALCASlYGHSLTDRMLCAGYLDGKVDSCQGDSGGPLVcEEPPGRFFLAGIVSWGIGCAEAQRPGVYARVTKLRDW 464
Cdd:COG5640    176 PVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                   ....*
gi 1622897949  465 ILEAT 469
Cdd:COG5640    254 IKSTA 258
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
527-773 2.00e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 204.88  E-value: 2.00e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  527 GARPAMEKPTRVVGGFGAASGEVPWQVSL---KEGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVWAHLGTASLLGLGGS 603
Cdd:COG5640     20 AAAPAADAAPAIVGGTPATVGEYPWMVALqssNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGT 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  604 PVKIglRRVVLHPLYNPGILDFDLAVLELASPLAFNKYIQpvcLPLAIQKFPVGRKCMISGWGNMQEGNATKPELLQKAS 683
Cdd:COG5640    100 VVKV--ARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  684 VGIIDQKTCSVLYNFsLTDRMICAGFLEGKVDSCQGDSGGPLAcEEAPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKG 763
Cdd:COG5640    175 VPVVSDATCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252
                          250
                   ....*....|
gi 1622897949  764 WILEIMSSQP 773
Cdd:COG5640    253 WIKSTAGGLG 262
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
188-223 5.63e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 49.51  E-value: 5.63e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1622897949  188 CPGNSFSCQNSQCV--TKVnpeCDDQEDCSDGSDEVHC 223
Cdd:cd00112      1 CPPNEFRCANGRCIpsSWV---CDGEDDCGDGSDEENC 35
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
558-743 4.44e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 51.60  E-value: 4.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  558 GSRHFCGATVVGDRWLLSAAHCFnHTKVEQVWAHLGTASLLGLGGSPVKIGLRRVVLHPLY-NPGILDFDLAVLELASPL 636
Cdd:COG3591      9 GGGGVCTGTLIGPNLVLTAGHCV-YDGAGGGWATNIVFVPGYNGGPYGTATATRFRVPPGWvASGDAGYDYALLRLDEPL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  637 AFnkyiQPVCLPLAIQ-KFPVGRKCMISGWGnmqegnATKPELLQkasvgiiDQKTCSVLYnfsltdrmICAGFLEGKVD 715
Cdd:COG3591     88 GD----TTGWLGLAFNdAPLAGEPVTIIGYP------GDRPKDLS-------LDCSGRVTG--------VQGNRLSYDCD 142
                          170       180
                   ....*....|....*....|....*...
gi 1622897949  716 SCQGDSGGPLACEEaPGVFYLAGIVSWG 743
Cdd:COG3591    143 TTGGSSGSPVLDDS-DGGGRVVGVHSAG 169
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
188-220 6.66e-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: 46.47  E-value: 6.66e-07
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1622897949   188 CPGNSFSCQNSQCV--TKVnpeCDDQEDCSDGSDE 220
Cdd:smart00192    2 CPPGEFQCDNGRCIpsSWV---CDGVDDCGDGSDE 33
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
260-465 1.48e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 46.98  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  260 HFCGATIISARWLVSAAHCFNEFQD---PTEWVAYVGttyLSGSEASTVRARVAQIikHPLYNADT-ADFDVAVLELTSP 335
Cdd:COG3591     12 GVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPG---YNGGPYGTATATRFRV--PPGWVASGdAGYDYALLRLDEP 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  336 LPfgrhiqpvclpaathifppskkcliSGWGYLKEDFLVKPEVLQKATVelldqalcaslYGHSLTDRMLCAGYLDGKV- 414
Cdd:COG3591     87 LG-------------------------DTTGWLGLAFNDAPLAGEPVTI-----------IGYPGDRPKDLSLDCSGRVt 130
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622897949  415 -----------DSCQGDSGGPLVCEEpPGRFFLAGIVSWGIGCAEAQrpGVY---ARVTKLRDWI 465
Cdd:COG3591    131 gvqgnrlsydcDTTGGSSGSPVLDDS-DGGGRVVGVHSAGGADRANT--GVRltsAIVAALRAWA 192
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
249-364 1.65e-04

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


Pssm-ID: 286432  Cd Length: 116  Bit Score: 42.15  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897949  249 PWQASLRENKEHFCGATIISARWLVSAAHCFNEFQDPTEWVAYV---GTTYLSgseastVRARVAQIIKHPLYNaDTADF 325
Cdd:pfam09342    2 PWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVlggAKTLKS------IEGPYEQIVRVDCRH-DIPES 74
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622897949  326 DVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISG 364
Cdd:pfam09342   75 EISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
66-127 1.07e-03

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: 39.53  E-value: 1.07e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622897949   66 IRWASSLRQEASDYHRTLTPTLEALFVSSFQKTELEASCVGCTVLNYRDGNSSVLVHFRLRF 127
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVF 73
 
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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