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Conserved domains on  [gi|2462565139|ref|XP_054176865|]
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transmembrane protease serine 9 isoform X2 [Homo sapiens]

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 ...
225-454 6.44e-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: 6.44e-97
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139   225 RIVGGMEASPGEFPWQASLR-ENKEHFCGAAIINARWLVSAAHCFNEFqDPTKWVAYVGATYLSGSEASTVRaQVVQIVK 303
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139   304 HPLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATVELLDQALCAS 383
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462565139   384 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 454
Cdd:smart00020  159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
850-1076 9.08e-95

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: 300.73  E-value: 9.08e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  850 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPKQWAAFLGTPFLSGAE--GQLERVARIYKH 927
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  928 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREGGSMARQLQKAAVRLLSEQTCRRFY 1007
Cdd:cd00190     80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462565139 1008 --PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 1076
Cdd:cd00190    160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
527-757 1.55e-88

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


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 284.17  E-value: 1.55e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  527 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLGLGGSPVKIGLRRVVLHP 605
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  606 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGnATKPELLQKASVGIIDQKTCSVLY 685
Cdd:cd00190     81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462565139  686 --NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEaPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWILEI 757
Cdd:cd00190    160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
177-212 4.23e-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: 4.23e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2462565139  177 CPGNSFSCGNSQCV--TKVnpeCDDQEDCSDGSDEAHC 212
Cdd:cd00112      1 CPPNEFRCANGRCIpsSWV---CDGEDDCGDGSDEENC 35
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
55-116 9.87e-05

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: 42.22  E-value: 9.87e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462565139   55 IRWTSSLRRETSDYHRTLTPTLEALFVSSFQKTELEASCVGCSVLNYRDGNSSVLVHFQLHF 116
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVF 73
Pneumo_att_G super family cl25814
Pneumovirinae attachment membrane glycoprotein G;
706-856 5.04e-03

Pneumovirinae attachment membrane glycoprotein G;


The actual alignment was detected with superfamily member pfam05539:

Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 40.42  E-value: 5.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  706 CQGDSGGPLACEEAPGVFYLAGIVSWGigcAQVKKPGVYTRITRlkgwileimSSQPLPM--SPPSTTRMLATTSPRTTA 783
Cdd:pfam05539  155 CTLRGKDVSCCKEPKTAVTTSKTTSWP---TEVSHPTYPSQVTP---------QSQPATQghQTATANQRLSSTEPVGTQ 222
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462565139  784 GLTVPGATPSRPTPGAASR----VTGQPANSTLSAVSTTARGQ--TPFPDAPEATTHTQLPDCGLAPAALTRIVGGSAA 856
Cdd:pfam05539  223 GTTTSSNPEPQTEPPPSQRgpsgSPQHPPSTTSQDQSTTGDGQehTQRRKTPPATSNRRSPHSTATPPPTTKRQETGRP 301
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
225-454 6.44e-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: 6.44e-97
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139   225 RIVGGMEASPGEFPWQASLR-ENKEHFCGAAIINARWLVSAAHCFNEFqDPTKWVAYVGATYLSGSEASTVRaQVVQIVK 303
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139   304 HPLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATVELLDQALCAS 383
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462565139   384 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 454
Cdd:smart00020  159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
226-454 2.37e-95

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: 302.66  E-value: 2.37e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  226 IVGGMEASPGEFPWQASLR-ENKEHFCGAAIINARWLVSAAHCFNEFqDPTKWVAYVGATYLSGSEASTVRAQVVQIVKH 304
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  305 PLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDfLVKPEVLQKATVELLDQALCASL 384
Cdd:cd00190     80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRA 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462565139  385 YGHS--LTDRMVCAGYLDGKVDSCQGDSGGPLVCEEPsGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 454
Cdd:cd00190    159 YSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
850-1076 9.08e-95

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: 300.73  E-value: 9.08e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  850 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPKQWAAFLGTPFLSGAE--GQLERVARIYKH 927
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  928 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREGGSMARQLQKAAVRLLSEQTCRRFY 1007
Cdd:cd00190     80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462565139 1008 --PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 1076
Cdd:cd00190    160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
849-1076 7.83e-94

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


Pssm-ID: 214473  Cd Length: 229  Bit Score: 298.44  E-value: 7.83e-94
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139   849 RIVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPKQWAAFLG-TPFLSGAEGQLERVARIYKH 927
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGsHDLSSGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139   928 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREG-GSMARQLQKAAVRLLSEQTCRRF 1006
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462565139  1007 YPVQ--ISSRMLCAGFPQGGVDSCSGDAGGPLACRepSGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 1076
Cdd:smart00020  160 YSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
527-757 1.55e-88

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


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 284.17  E-value: 1.55e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  527 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLGLGGSPVKIGLRRVVLHP 605
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  606 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGnATKPELLQKASVGIIDQKTCSVLY 685
Cdd:cd00190     81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462565139  686 --NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEaPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWILEI 757
Cdd:cd00190    160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
526-754 4.06e-88

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


Pssm-ID: 214473  Cd Length: 229  Bit Score: 283.03  E-value: 4.06e-88
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139   526 RVVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLgLGGSPVKIGLRRVVLH 604
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139   605 PLYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGNATKPELLQKASVGIIDQKTCSVL 684
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462565139   685 Y--NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEapGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWI 754
Cdd:smart00020  160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
226-454 1.70e-75

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 248.13  E-value: 1.70e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  226 IVGGMEASPGEFPWQASL-RENKEHFCGAAIINARWLVSAAHCFNefqDPTKWVAYVGATYLSGSEASTVRAQVVQIVKH 304
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  305 PLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDflVKPEVLQKATVELLDQALCASL 384
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  385 YGHSLTDRMVCAGYldGKVDSCQGDSGGPLVCEEPsgrfFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 454
Cdd:pfam00089  156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
843-1080 1.96e-71

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 238.40  E-value: 1.96e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  843 APAALTRIVGGSAAGRGEWPWQVSLWLR--RREHRCGAVLVAERWLLSAAHCFDVYGdPKQWAAFLGTPFLSGAEGQLER 920
Cdd:COG5640     24 AADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGGTVVK 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  921 VARIYKHPFYNLYTLDYDVALLELAGPVRRsrlVRPICLPEPAPRPPDGTRCVITGWGSVREG-GSMARQLQKAAVRLLS 999
Cdd:COG5640    103 VARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVS 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139 1000 EQTCRRfYPVQISSRMLCAGFPQGGVDSCSGDAGGPLAcREPSGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWIGQH 1079
Cdd:COG5640    180 DATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKST 257

                   .
gi 2462565139 1080 I 1080
Cdd:COG5640    258 A 258
Trypsin pfam00089
Trypsin;
850-1076 6.90e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 235.41  E-value: 6.90e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  850 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvygDPKQWAAFLGTPFLSGAEG--QLERVARIYKH 927
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGgeQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  928 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREGGSmARQLQKAAVRLLSEQTCRRFY 1007
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462565139 1008 PVQISSRMLCAGFpqGGVDSCSGDAGGPLACREPsgrwVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 1076
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Trypsin pfam00089
Trypsin;
527-754 4.32e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.10  E-value: 4.32e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  527 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRahLGTASLLGLGGSPVKIGLRRVVLHP 605
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASDVKVV--LGAHNIVLREGGEQKFDVEKIIVHP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  606 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGNatKPELLQKASVGIIDQKTCSVLY 685
Cdd:pfam00089   79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462565139  686 NFSLTDRMICAGFleGKVDSCQGDSGGPLACEEApgvfYLAGIVSWGIGCAQVKKPGVYTRITRLKGWI 754
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
217-462 1.25e-64

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 219.52  E-value: 1.25e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  217 QPAWRMAGRIVGGMEASPGEFPWQASLRENK---EHFCGAAIINARWLVSAAHCFNEFQDPTKWVaYVGATYLSGSEAST 293
Cdd:COG5640     22 APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRV-VIGSTDLSTSGGTV 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  294 VRaqVVQIVKHPLYNADTADFDVAVLELTSPLPFgrhIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATV 373
Cdd:COG5640    101 VK--VARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADV 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  374 ELLDQALCASlYGHSLTDRMVCAGYLDGKVDSCQGDSGGPLVcEEPSGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDW 453
Cdd:COG5640    176 PVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                   ....*....
gi 2462565139  454 ILEATTKAS 462
Cdd:COG5640    254 IKSTAGGLG 262
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
516-762 2.52e-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: 2.52e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  516 GARPAMEKPTRVVGGFGAASGEVPWQVSL---KEGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLGLGGS 592
Cdd:COG5640     20 AAAPAADAAPAIVGGTPATVGEYPWMVALqssNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGT 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  593 PVKIglRRVVLHPLYNPGILDFDLAVLELASPLAFNKYIQpvcLPLAIQKFPVGRKCMISGWGNTQEGNATKPELLQKAS 672
Cdd:COG5640    100 VVKV--ARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  673 VGIIDQKTCSVLYNFsLTDRMICAGFLEGKVDSCQGDSGGPLAcEEAPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKG 752
Cdd:COG5640    175 VPVVSDATCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252
                          250
                   ....*....|
gi 2462565139  753 WILEIMSSQP 762
Cdd:COG5640    253 WIKSTAGGLG 262
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
177-212 4.23e-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: 4.23e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2462565139  177 CPGNSFSCGNSQCV--TKVnpeCDDQEDCSDGSDEAHC 212
Cdd:cd00112      1 CPPNEFRCANGRCIpsSWV---CDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
176-209 4.28e-07

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


Pssm-ID: 197566  Cd Length: 33  Bit Score: 47.24  E-value: 4.28e-07
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 2462565139   176 RCPGNSFSCGNSQCV--TKVnpeCDDQEDCSDGSDE 209
Cdd:smart00192    1 TCPPGEFQCDNGRCIpsSWV---CDGVDDCGDGSDE 33
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
55-116 9.87e-05

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: 42.22  E-value: 9.87e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462565139   55 IRWTSSLRRETSDYHRTLTPTLEALFVSSFQKTELEASCVGCSVLNYRDGNSSVLVHFQLHF 116
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVF 73
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
706-856 5.04e-03

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 40.42  E-value: 5.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  706 CQGDSGGPLACEEAPGVFYLAGIVSWGigcAQVKKPGVYTRITRlkgwileimSSQPLPM--SPPSTTRMLATTSPRTTA 783
Cdd:pfam05539  155 CTLRGKDVSCCKEPKTAVTTSKTTSWP---TEVSHPTYPSQVTP---------QSQPATQghQTATANQRLSSTEPVGTQ 222
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462565139  784 GLTVPGATPSRPTPGAASR----VTGQPANSTLSAVSTTARGQ--TPFPDAPEATTHTQLPDCGLAPAALTRIVGGSAA 856
Cdd:pfam05539  223 GTTTSSNPEPQTEPPPSQRgpsgSPQHPPSTTSQDQSTTGDGQehTQRRKTPPATSNRRSPHSTATPPPTTKRQETGRP 301
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
225-454 6.44e-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: 6.44e-97
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139   225 RIVGGMEASPGEFPWQASLR-ENKEHFCGAAIINARWLVSAAHCFNEFqDPTKWVAYVGATYLSGSEASTVRaQVVQIVK 303
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139   304 HPLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATVELLDQALCAS 383
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462565139   384 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 454
Cdd:smart00020  159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
226-454 2.37e-95

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: 302.66  E-value: 2.37e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  226 IVGGMEASPGEFPWQASLR-ENKEHFCGAAIINARWLVSAAHCFNEFqDPTKWVAYVGATYLSGSEASTVRAQVVQIVKH 304
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  305 PLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDfLVKPEVLQKATVELLDQALCASL 384
Cdd:cd00190     80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRA 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462565139  385 YGHS--LTDRMVCAGYLDGKVDSCQGDSGGPLVCEEPsGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 454
Cdd:cd00190    159 YSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
850-1076 9.08e-95

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: 300.73  E-value: 9.08e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  850 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPKQWAAFLGTPFLSGAE--GQLERVARIYKH 927
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  928 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREGGSMARQLQKAAVRLLSEQTCRRFY 1007
Cdd:cd00190     80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462565139 1008 --PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 1076
Cdd:cd00190    160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
849-1076 7.83e-94

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


Pssm-ID: 214473  Cd Length: 229  Bit Score: 298.44  E-value: 7.83e-94
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139   849 RIVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPKQWAAFLG-TPFLSGAEGQLERVARIYKH 927
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGsHDLSSGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139   928 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREG-GSMARQLQKAAVRLLSEQTCRRF 1006
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462565139  1007 YPVQ--ISSRMLCAGFPQGGVDSCSGDAGGPLACRepSGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 1076
Cdd:smart00020  160 YSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
527-757 1.55e-88

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


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 284.17  E-value: 1.55e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  527 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLGLGGSPVKIGLRRVVLHP 605
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  606 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGnATKPELLQKASVGIIDQKTCSVLY 685
Cdd:cd00190     81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462565139  686 --NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEaPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWILEI 757
Cdd:cd00190    160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
526-754 4.06e-88

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


Pssm-ID: 214473  Cd Length: 229  Bit Score: 283.03  E-value: 4.06e-88
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139   526 RVVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLgLGGSPVKIGLRRVVLH 604
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139   605 PLYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGNATKPELLQKASVGIIDQKTCSVL 684
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462565139   685 Y--NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEapGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWI 754
Cdd:smart00020  160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
226-454 1.70e-75

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 248.13  E-value: 1.70e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  226 IVGGMEASPGEFPWQASL-RENKEHFCGAAIINARWLVSAAHCFNefqDPTKWVAYVGATYLSGSEASTVRAQVVQIVKH 304
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  305 PLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDflVKPEVLQKATVELLDQALCASL 384
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  385 YGHSLTDRMVCAGYldGKVDSCQGDSGGPLVCEEPsgrfFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 454
Cdd:pfam00089  156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
843-1080 1.96e-71

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 238.40  E-value: 1.96e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  843 APAALTRIVGGSAAGRGEWPWQVSLWLR--RREHRCGAVLVAERWLLSAAHCFDVYGdPKQWAAFLGTPFLSGAEGQLER 920
Cdd:COG5640     24 AADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGGTVVK 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  921 VARIYKHPFYNLYTLDYDVALLELAGPVRRsrlVRPICLPEPAPRPPDGTRCVITGWGSVREG-GSMARQLQKAAVRLLS 999
Cdd:COG5640    103 VARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVS 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139 1000 EQTCRRfYPVQISSRMLCAGFPQGGVDSCSGDAGGPLAcREPSGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWIGQH 1079
Cdd:COG5640    180 DATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKST 257

                   .
gi 2462565139 1080 I 1080
Cdd:COG5640    258 A 258
Trypsin pfam00089
Trypsin;
850-1076 6.90e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 235.41  E-value: 6.90e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  850 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvygDPKQWAAFLGTPFLSGAEG--QLERVARIYKH 927
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGgeQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  928 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREGGSmARQLQKAAVRLLSEQTCRRFY 1007
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462565139 1008 PVQISSRMLCAGFpqGGVDSCSGDAGGPLACREPsgrwVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 1076
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Trypsin pfam00089
Trypsin;
527-754 4.32e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.10  E-value: 4.32e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  527 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRahLGTASLLGLGGSPVKIGLRRVVLHP 605
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASDVKVV--LGAHNIVLREGGEQKFDVEKIIVHP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  606 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGNatKPELLQKASVGIIDQKTCSVLY 685
Cdd:pfam00089   79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462565139  686 NFSLTDRMICAGFleGKVDSCQGDSGGPLACEEApgvfYLAGIVSWGIGCAQVKKPGVYTRITRLKGWI 754
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
217-462 1.25e-64

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 219.52  E-value: 1.25e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  217 QPAWRMAGRIVGGMEASPGEFPWQASLRENK---EHFCGAAIINARWLVSAAHCFNEFQDPTKWVaYVGATYLSGSEAST 293
Cdd:COG5640     22 APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRV-VIGSTDLSTSGGTV 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  294 VRaqVVQIVKHPLYNADTADFDVAVLELTSPLPFgrhIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATV 373
Cdd:COG5640    101 VK--VARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADV 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  374 ELLDQALCASlYGHSLTDRMVCAGYLDGKVDSCQGDSGGPLVcEEPSGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDW 453
Cdd:COG5640    176 PVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                   ....*....
gi 2462565139  454 ILEATTKAS 462
Cdd:COG5640    254 IKSTAGGLG 262
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
516-762 2.52e-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: 2.52e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  516 GARPAMEKPTRVVGGFGAASGEVPWQVSL---KEGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLGLGGS 592
Cdd:COG5640     20 AAAPAADAAPAIVGGTPATVGEYPWMVALqssNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGT 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  593 PVKIglRRVVLHPLYNPGILDFDLAVLELASPLAFNKYIQpvcLPLAIQKFPVGRKCMISGWGNTQEGNATKPELLQKAS 672
Cdd:COG5640    100 VVKV--ARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  673 VGIIDQKTCSVLYNFsLTDRMICAGFLEGKVDSCQGDSGGPLAcEEAPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKG 752
Cdd:COG5640    175 VPVVSDATCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252
                          250
                   ....*....|
gi 2462565139  753 WILEIMSSQP 762
Cdd:COG5640    253 WIKSTAGGLG 262
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
177-212 4.23e-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: 4.23e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2462565139  177 CPGNSFSCGNSQCV--TKVnpeCDDQEDCSDGSDEAHC 212
Cdd:cd00112      1 CPPNEFRCANGRCIpsSWV---CDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
176-209 4.28e-07

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


Pssm-ID: 197566  Cd Length: 33  Bit Score: 47.24  E-value: 4.28e-07
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 2462565139   176 RCPGNSFSCGNSQCV--TKVnpeCDDQEDCSDGSDE 209
Cdd:smart00192    1 TCPPGEFQCDNGRCIpsSWV---CDGVDDCGDGSDE 33
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
547-732 2.42e-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: 2.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  547 GSRHFCGATVVGDRWLLSAAHCFNHTK----VEQVRAHLGtasllGLGGSPVKIGLRRVVLHPLY-NPGILDFDLAVLEL 621
Cdd:COG3591      9 GGGGVCTGTLIGPNLVLTAGHCVYDGAgggwATNIVFVPG-----YNGGPYGTATATRFRVPPGWvASGDAGYDYALLRL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  622 ASPLAFnkyiQPVCLPLAIQ-KFPVGRKCMISGWGntqegnATKPELLQkasvgiiDQKTCSVLYnfsltdrmICAGFLE 700
Cdd:COG3591     84 DEPLGD----TTGWLGLAFNdAPLAGEPVTIIGYP------GDRPKDLS-------LDCSGRVTG--------VQGNRLS 138
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2462565139  701 GKVDSCQGDSGGPLACEEaPGVFYLAGIVSWG 732
Cdd:COG3591    139 YDCDTTGGSSGSPVLDDS-DGGGRVVGVHSAG 169
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
249-454 3.78e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 45.82  E-value: 3.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  249 HFCGAAIINARWLVSAAHCFNEFQD---PTKWVAYVGATYLSGSEASTVRAQVvqivkHPLYNADT-ADFDVAVLELTSP 324
Cdd:COG3591     12 GVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPGYNGGPYGTATATRFRV-----PPGWVASGdAGYDYALLRLDEP 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  325 LPfgrhiqpvclpaathifppskkcliSGWGYLKEDFLVKPEVLQKATVelldqalcaslYGHSLTDRMVCAGYLDGKV- 403
Cdd:COG3591     87 LG-------------------------DTTGWLGLAFNDAPLAGEPVTI-----------IGYPGDRPKDLSLDCSGRVt 130
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462565139  404 -----------DSCQGDSGGPLVCEEpSGRFFLAGIVSWGIGCAEARrpGVY---ARVTRLRDWI 454
Cdd:COG3591    131 gvqgnrlsydcDTTGGSSGSPVLDDS-DGGGRVVGVHSAGGADRANT--GVRltsAIVAALRAWA 192
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
238-353 7.09e-05

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


Pssm-ID: 286432  Cd Length: 116  Bit Score: 43.31  E-value: 7.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  238 PWQASLRENKEHFCGAAIINARWLVSAAHCFNEFQDPTKWVAYV---GATYLSgseastVRAQVVQIVKHPLYNaDTADF 314
Cdd:pfam09342    2 PWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVlggAKTLKS------IEGPYEQIVRVDCRH-DIPES 74
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462565139  315 DVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISG 353
Cdd:pfam09342   75 EISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
55-116 9.87e-05

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: 42.22  E-value: 9.87e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462565139   55 IRWTSSLRRETSDYHRTLTPTLEALFVSSFQKTELEASCVGCSVLNYRDGNSSVLVHFQLHF 116
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVF 73
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
706-856 5.04e-03

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 40.42  E-value: 5.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565139  706 CQGDSGGPLACEEAPGVFYLAGIVSWGigcAQVKKPGVYTRITRlkgwileimSSQPLPM--SPPSTTRMLATTSPRTTA 783
Cdd:pfam05539  155 CTLRGKDVSCCKEPKTAVTTSKTTSWP---TEVSHPTYPSQVTP---------QSQPATQghQTATANQRLSSTEPVGTQ 222
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462565139  784 GLTVPGATPSRPTPGAASR----VTGQPANSTLSAVSTTARGQ--TPFPDAPEATTHTQLPDCGLAPAALTRIVGGSAA 856
Cdd:pfam05539  223 GTTTSSNPEPQTEPPPSQRgpsgSPQHPPSTTSQDQSTTGDGQehTQRRKTPPATSNRRSPHSTATPPPTTKRQETGRP 301
 
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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