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Conserved domains on  [gi|1878348173|ref|NP_001372571|]
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transmembrane protease serine 9 isoform 2 [Homo sapiens]

Protein Classification

Tryp_SPc domain-containing protein( domain architecture ID 12184347)

Tryp_SPc domain-containing protein

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 ...
 4-233 1.98e-98

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: 306.14  E-value: 1.98e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173    4 RIVGGMEASPGEFPWQASLR-ENKEHFCGAAIINARWLVSAAHCFNEFqDPTKWVAYVGATYLSGSEASTVRaQVVQIVK 82
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173   83 HPLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATVELLDQALCAS 162
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1878348173  163 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 233
Cdd:smart00020 159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 629-855 2.83e-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: 300.73  E-value: 2.83e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 629 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPKQWAAFLGTPFLSGAE--GQLERVARIYKH 706
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 707 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREGGSMARQLQKAAVRLLSEQTCRRFY 786
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878348173 787 --PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 855
Cdd:cd00190   160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 306-536 6.89e-90

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: 283.78  E-value: 6.89e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 306 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLGLGGSPVKIGLRRVVLHP 384
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 385 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGnATKPELLQKASVGIIDQKTCSVLY 464
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1878348173 465 --NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEaPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWILEI 536
Cdd:cd00190   160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Pneumo_att_G super family cl25814
Pneumovirinae attachment membrane glycoprotein G;
485-635 3.02e-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: 40.80  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 485 CQGDSGGPLACEEAPGVFYLAGIVSWGigcAQVKKPGVYTRITRlkgwileimSSQPLPM--SPPSTTRMLATTSPRTTA 562
Cdd:pfam05539 155 CTLRGKDVSCCKEPKTAVTTSKTTSWP---TEVSHPTYPSQVTP---------QSQPATQghQTATANQRLSSTEPVGTQ 222

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878348173 563 GLTVPGATPSRPTPGAASR----VTGQPANSTLSAVSTTARGQ--TPFPDAPEATTHTQLPDCGLAPAALTRIVGGSAA 635
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 ...
 4-233 1.98e-98

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: 306.14  E-value: 1.98e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173    4 RIVGGMEASPGEFPWQASLR-ENKEHFCGAAIINARWLVSAAHCFNEFqDPTKWVAYVGATYLSGSEASTVRaQVVQIVK 82
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173   83 HPLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATVELLDQALCAS 162
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1878348173  163 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 233
Cdd:smart00020 159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 5-233 7.33e-97

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: 302.27  E-value: 7.33e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173   5 IVGGMEASPGEFPWQASLR-ENKEHFCGAAIINARWLVSAAHCFNEFqDPTKWVAYVGATYLSGSEASTVRAQVVQIVKH 83
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173  84 PLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDfLVKPEVLQKATVELLDQALCASL 163
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878348173 164 YGHS--LTDRMVCAGYLDGKVDSCQGDSGGPLVCEEPsGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 233
Cdd:cd00190   159 YSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 629-855 2.83e-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: 300.73  E-value: 2.83e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 629 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPKQWAAFLGTPFLSGAE--GQLERVARIYKH 706
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 707 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREGGSMARQLQKAAVRLLSEQTCRRFY 786
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878348173 787 --PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 855
Cdd:cd00190   160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 628-855 2.98e-95

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: 298.05  E-value: 2.98e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173  628 RIVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPKQWAAFLG-TPFLSGAEGQLERVARIYKH 706
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGsHDLSSGEEGQVIKVSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173  707 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREG-GSMARQLQKAAVRLLSEQTCRRF 785
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878348173  786 YPVQ--ISSRMLCAGFPQGGVDSCSGDAGGPLACRepSGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 855
Cdd:smart00020 160 YSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 306-536 6.89e-90

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: 283.78  E-value: 6.89e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 306 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLGLGGSPVKIGLRRVVLHP 384
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 385 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGnATKPELLQKASVGIIDQKTCSVLY 464
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1878348173 465 --NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEaPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWILEI 536
Cdd:cd00190   160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 305-533 2.02e-89

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: 282.64  E-value: 2.02e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173  305 RVVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLgLGGSPVKIGLRRVVLH 383
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173  384 PLYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGNATKPELLQKASVGIIDQKTCSVL 463
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878348173  464 Y--NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEapGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWI 533
Cdd:smart00020 160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
5-233 3.84e-76

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 246.97  E-value: 3.84e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173   5 IVGGMEASPGEFPWQASL-RENKEHFCGAAIINARWLVSAAHCFNefqDPTKWVAYVGATYLSGSEASTVRAQVVQIVKH 83
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173  84 PLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDflVKPEVLQKATVELLDQALCASL 163
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 164 YGHSLTDRMVCAGYldGKVDSCQGDSGGPLVCEEPsgrfFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 233
Cdd:pfam00089 156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Trypsin pfam00089
Trypsin;
629-855 1.98e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 234.26  E-value: 1.98e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 629 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvygDPKQWAAFLGTPFLSGAEG--QLERVARIYKH 706
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGgeQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 707 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREGGSmARQLQKAAVRLLSEQTCRRFY 786
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878348173 787 PVQISSRMLCAGFpqGGVDSCSGDAGGPLACREPsgrwVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 855
Cdd:pfam00089 157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 622-859 3.82e-71

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 234.93  E-value: 3.82e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 622 APAALTRIVGGSAAGRGEWPWQVSLWLR--RREHRCGAVLVAERWLLSAAHCFDVYGdPKQWAAFLGTPFLSGAEGQLER 699
Cdd:COG5640    24 AADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGGTVVK 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 700 VARIYKHPFYNLYTLDYDVALLELAGPVRRsrlVRPICLPEPAPRPPDGTRCVITGWGSVREG-GSMARQLQKAAVRLLS 778
Cdd:COG5640   103 VARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 779 EQTCRRfYPVQISSRMLCAGFPQGGVDSCSGDAGGPLAcREPSGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWIGQH 858
Cdd:COG5640   180 DATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKST 257


                  .
gi 1878348173 859 I 859
Cdd:COG5640   258 A 258
Trypsin pfam00089
Trypsin;
306-533 1.45e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 231.95  E-value: 1.45e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 306 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRahLGTASLLGLGGSPVKIGLRRVVLHP 384
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASDVKVV--LGAHNIVLREGGEQKFDVEKIIVHP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 385 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGNatKPELLQKASVGIIDQKTCSVLY 464
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAY 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878348173 465 NFSLTDRMICAGFleGKVDSCQGDSGGPLACEEApgvfYLAGIVSWGIGCAQVKKPGVYTRITRLKGWI 533
Cdd:pfam00089 157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 1-241 1.03e-63

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 214.90  E-value: 1.03e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173   1 MAGRIVGGMEASPGEFPWQASLRENK---EHFCGAAIINARWLVSAAHCFNEFQDPTKWVaYVGATYLSGSEASTVRaqV 77
Cdd:COG5640    27 AAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRV-VIGSTDLSTSGGTVVK--V 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173  78 VQIVKHPLYNADTADFDVAVLELTSPLPFgrhIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATVELLDQ 157
Cdd:COG5640   104 ARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSD 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 158 ALCASlYGHSLTDRMVCAGYLDGKVDSCQGDSGGPLVcEEPSGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWILEAT 237
Cdd:COG5640   181 ATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258


                  ....
gi 1878348173 238 TKAS 241
Cdd:COG5640   259 GGLG 262
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 295-541 7.26e-61

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 207.19  E-value: 7.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 295 GARPAMEKPTRVVGGFGAASGEVPWQVSL---KEGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLGLGGS 371
Cdd:COG5640    20 AAAPAADAAPAIVGGTPATVGEYPWMVALqssNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 372 PVKIglRRVVLHPLYNPGILDFDLAVLELASPLAFNKYIQpvcLPLAIQKFPVGRKCMISGWGNTQEGNATKPELLQKAS 451
Cdd:COG5640   100 VVKV--ARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 452 VGIIDQKTCSVLYNFsLTDRMICAGFLEGKVDSCQGDSGGPLAcEEAPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKG 531
Cdd:COG5640   175 VPVVSDATCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252

                         250
                  ....*....|
gi 1878348173 532 WILEIMSSQP 541
Cdd:COG5640   253 WIKSTAGGLG 262
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
485-635 3.02e-03

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 40.80  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 485 CQGDSGGPLACEEAPGVFYLAGIVSWGigcAQVKKPGVYTRITRlkgwileimSSQPLPM--SPPSTTRMLATTSPRTTA 562
Cdd:pfam05539 155 CTLRGKDVSCCKEPKTAVTTSKTTSWP---TEVSHPTYPSQVTP---------QSQPATQghQTATANQRLSSTEPVGTQ 222

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878348173 563 GLTVPGATPSRPTPGAASR----VTGQPANSTLSAVSTTARGQ--TPFPDAPEATTHTQLPDCGLAPAALTRIVGGSAA 635
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 ...
 4-233 1.98e-98

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: 306.14  E-value: 1.98e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173    4 RIVGGMEASPGEFPWQASLR-ENKEHFCGAAIINARWLVSAAHCFNEFqDPTKWVAYVGATYLSGSEASTVRaQVVQIVK 82
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVI-KVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173   83 HPLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATVELLDQALCAS 162
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1878348173  163 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 233
Cdd:smart00020 159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 5-233 7.33e-97

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: 302.27  E-value: 7.33e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173   5 IVGGMEASPGEFPWQASLR-ENKEHFCGAAIINARWLVSAAHCFNEFqDPTKWVAYVGATYLSGSEASTVRAQVVQIVKH 83
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173  84 PLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDfLVKPEVLQKATVELLDQALCASL 163
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878348173 164 YGHS--LTDRMVCAGYLDGKVDSCQGDSGGPLVCEEPsGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 233
Cdd:cd00190   159 YSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 629-855 2.83e-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: 300.73  E-value: 2.83e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 629 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPKQWAAFLGTPFLSGAE--GQLERVARIYKH 706
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 707 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREGGSMARQLQKAAVRLLSEQTCRRFY 786
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878348173 787 --PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 855
Cdd:cd00190   160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 628-855 2.98e-95

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: 298.05  E-value: 2.98e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173  628 RIVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPKQWAAFLG-TPFLSGAEGQLERVARIYKH 706
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGsHDLSSGEEGQVIKVSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173  707 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREG-GSMARQLQKAAVRLLSEQTCRRF 785
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878348173  786 YPVQ--ISSRMLCAGFPQGGVDSCSGDAGGPLACRepSGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 855
Cdd:smart00020 160 YSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 306-536 6.89e-90

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: 283.78  E-value: 6.89e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 306 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLGLGGSPVKIGLRRVVLHP 384
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 385 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGnATKPELLQKASVGIIDQKTCSVLY 464
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1878348173 465 --NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEaPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWILEI 536
Cdd:cd00190   160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 305-533 2.02e-89

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: 282.64  E-value: 2.02e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173  305 RVVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLgLGGSPVKIGLRRVVLH 383
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173  384 PLYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGNATKPELLQKASVGIIDQKTCSVL 463
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878348173  464 Y--NFSLTDRMICAGFLEGKVDSCQGDSGGPLACEEapGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKGWI 533
Cdd:smart00020 160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
5-233 3.84e-76

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 246.97  E-value: 3.84e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173   5 IVGGMEASPGEFPWQASL-RENKEHFCGAAIINARWLVSAAHCFNefqDPTKWVAYVGATYLSGSEASTVRAQVVQIVKH 83
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173  84 PLYNADTADFDVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISGWGYLKEDflVKPEVLQKATVELLDQALCASL 163
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 164 YGHSLTDRMVCAGYldGKVDSCQGDSGGPLVCEEPsgrfFLAGIVSWGIGCAEARRPGVYARVTRLRDWI 233
Cdd:pfam00089 156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Trypsin pfam00089
Trypsin;
629-855 1.98e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 234.26  E-value: 1.98e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 629 IVGGSAAGRGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvygDPKQWAAFLGTPFLSGAEG--QLERVARIYKH 706
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGgeQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 707 PFYNLYTLDYDVALLELAGPVRRSRLVRPICLPEPAPRPPDGTRCVITGWGSVREGGSmARQLQKAAVRLLSEQTCRRFY 786
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878348173 787 PVQISSRMLCAGFpqGGVDSCSGDAGGPLACREPsgrwVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWI 855
Cdd:pfam00089 157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 622-859 3.82e-71

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 234.93  E-value: 3.82e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 622 APAALTRIVGGSAAGRGEWPWQVSLWLR--RREHRCGAVLVAERWLLSAAHCFDVYGdPKQWAAFLGTPFLSGAEGQLER 699
Cdd:COG5640    24 AADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGGTVVK 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 700 VARIYKHPFYNLYTLDYDVALLELAGPVRRsrlVRPICLPEPAPRPPDGTRCVITGWGSVREG-GSMARQLQKAAVRLLS 778
Cdd:COG5640   103 VARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 779 EQTCRRfYPVQISSRMLCAGFPQGGVDSCSGDAGGPLAcREPSGRWVLTGVTSWGYGCGRPHFPGVYTRVAAVRGWIGQH 858
Cdd:COG5640   180 DATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKST 257


                  .
gi 1878348173 859 I 859
Cdd:COG5640   258 A 258
Trypsin pfam00089
Trypsin;
306-533 1.45e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 231.95  E-value: 1.45e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 306 VVGGFGAASGEVPWQVSLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRahLGTASLLGLGGSPVKIGLRRVVLHP 384
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASDVKVV--LGAHNIVLREGGEQKFDVEKIIVHP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 385 LYNPGILDFDLAVLELASPLAFNKYIQPVCLPLAIQKFPVGRKCMISGWGNTQEGNatKPELLQKASVGIIDQKTCSVLY 464
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAY 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878348173 465 NFSLTDRMICAGFleGKVDSCQGDSGGPLACEEApgvfYLAGIVSWGIGCAQVKKPGVYTRITRLKGWI 533
Cdd:pfam00089 157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 1-241 1.03e-63

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 214.90  E-value: 1.03e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173   1 MAGRIVGGMEASPGEFPWQASLRENK---EHFCGAAIINARWLVSAAHCFNEFQDPTKWVaYVGATYLSGSEASTVRaqV 77
Cdd:COG5640    27 AAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRV-VIGSTDLSTSGGTVVK--V 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173  78 VQIVKHPLYNADTADFDVAVLELTSPLPFgrhIQPVCLPAATHIFPPSKKCLISGWGYLKEDFLVKPEVLQKATVELLDQ 157
Cdd:COG5640   104 ARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSD 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 158 ALCASlYGHSLTDRMVCAGYLDGKVDSCQGDSGGPLVcEEPSGRFFLAGIVSWGIGCAEARRPGVYARVTRLRDWILEAT 237
Cdd:COG5640   181 ATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258


                  ....
gi 1878348173 238 TKAS 241
Cdd:COG5640   259 GGLG 262
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 295-541 7.26e-61

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 207.19  E-value: 7.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 295 GARPAMEKPTRVVGGFGAASGEVPWQVSL---KEGSRHFCGATVVGDRWLLSAAHCFNHTKVEQVRAHLGTASLLGLGGS 371
Cdd:COG5640    20 AAAPAADAAPAIVGGTPATVGEYPWMVALqssNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 372 PVKIglRRVVLHPLYNPGILDFDLAVLELASPLAFNKYIQpvcLPLAIQKFPVGRKCMISGWGNTQEGNATKPELLQKAS 451
Cdd:COG5640   100 VVKV--ARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 452 VGIIDQKTCSVLYNFsLTDRMICAGFLEGKVDSCQGDSGGPLAcEEAPGVFYLAGIVSWGIGCAQVKKPGVYTRITRLKG 531
Cdd:COG5640   175 VPVVSDATCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252

                         250
                  ....*....|
gi 1878348173 532 WILEIMSSQP 541
Cdd:COG5640   253 WIKSTAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 326-511 3.31e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 48.52  E-value: 3.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 326 GSRHFCGATVVGDRWLLSAAHCFNHTK----VEQVRAHLGtasllGLGGSPVKIGLRRVVLHPLY-NPGILDFDLAVLEL 400
Cdd:COG3591     9 GGGGVCTGTLIGPNLVLTAGHCVYDGAgggwATNIVFVPG-----YNGGPYGTATATRFRVPPGWvASGDAGYDYALLRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 401 ASPLAFnkyiQPVCLPLAIQ-KFPVGRKCMISGWGntqegnATKPELLQkasvgiiDQKTCSVLYnfsltdrmICAGFLE 479
Cdd:COG3591    84 DEPLGD----TTGWLGLAFNdAPLAGEPVTIIGYP------GDRPKDLS-------LDCSGRVTG--------VQGNRLS 138

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1878348173 480 GKVDSCQGDSGGPLACEEaPGVFYLAGIVSWG 511
Cdd:COG3591   139 YDCDTTGGSSGSPVLDDS-DGGGRVVGVHSAG 169
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 17-132 4.36e-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: 43.69  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173  17 PWQASLRENKEHFCGAAIINARWLVSAAHCFNEFQDPTKWVAYV---GATYLSgseastVRAQVVQIVKHPLYNaDTADF 93
Cdd:pfam09342   2 PWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVlggAKTLKS------IEGPYEQIVRVDCRH-DIPES 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1878348173  94 DVAVLELTSPLPFGRHIQPVCLPAATHIFPPSKKCLISG 132
Cdd:pfam09342  75 EISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 28-233 5.15e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 45.05  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173  28 HFCGAAIINARWLVSAAHCFNEFQD---PTKWVAYVGATYLSGSEASTVRAQVvqivkHPLYNADT-ADFDVAVLELTSP 103
Cdd:COG3591    12 GVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPGYNGGPYGTATATRFRV-----PPGWVASGdAGYDYALLRLDEP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 104 LPfgrhiqpvclpaathifppskkcliSGWGYLKEDFLVKPEVLQKATVelldqalcaslYGHSLTDRMVCAGYLDGKV- 182
Cdd:COG3591    87 LG-------------------------DTTGWLGLAFNDAPLAGEPVTI-----------IGYPGDRPKDLSLDCSGRVt 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1878348173 183 -----------DSCQGDSGGPLVCEEpSGRFFLAGIVSWGIGCAEARrpGVY---ARVTRLRDWI 233
Cdd:COG3591   131 gvqgnrlsydcDTTGGSSGSPVLDDS-DGGGRVVGVHSAGGADRANT--GVRltsAIVAALRAWA 192
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
485-635 3.02e-03

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 40.80  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878348173 485 CQGDSGGPLACEEAPGVFYLAGIVSWGigcAQVKKPGVYTRITRlkgwileimSSQPLPM--SPPSTTRMLATTSPRTTA 562
Cdd:pfam05539 155 CTLRGKDVSCCKEPKTAVTTSKTTSWP---TEVSHPTYPSQVTP---------QSQPATQghQTATANQRLSSTEPVGTQ 222

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878348173 563 GLTVPGATPSRPTPGAASR----VTGQPANSTLSAVSTTARGQ--TPFPDAPEATTHTQLPDCGLAPAALTRIVGGSAA 635
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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