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Conserved domains on  [gi|68508970|ref|NP_077078|]
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tryptase beta-2 preproprotein [Homo sapiens]

Protein Classification

serine protease( domain architecture ID 10076129)

trypsin-like serine protease such as human plasminogen, the precursor of the widely distributed protease plasmin, or granzyme B, a human enzyme necessary for target cell lysis in cell-mediated immune responses

CATH:  2.40.10.10
EC:  3.4.21.-
PubMed:  18259688

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
31-268 4.01e-102

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: 297.27  E-value: 4.01e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970  31 IVGGQEAPRSKWPWQVSLRVRDryWMHFCGGSLIHPQWVLTAAHCVGPdvKDLAALRVQLREQHLYYQD---QLLPVSRI 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHDLSSNEgggQVIKVKKV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970 108 IVHPQFYTAQIGADIALLELEEPVNVSSHVHTVTLPPASETFPPGMPCWVTGWGDvdNDERLPPPFPLKQVKVPIMENHI 187
Cdd:cd00190  77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGR--TSEGGPLPDVLQEVNVPIVSNAE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970 188 CDAKYHLGAYtgddvriVRDDMLCAGNTR--RDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLD 265
Cdd:cd00190 155 CKRAYSYGGT-------ITDNMLCAGGLEggKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLD 227

                ...
gi 68508970 266 WIH 268
Cdd:cd00190 228 WIQ 230
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
31-268 4.01e-102

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: 297.27  E-value: 4.01e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970  31 IVGGQEAPRSKWPWQVSLRVRDryWMHFCGGSLIHPQWVLTAAHCVGPdvKDLAALRVQLREQHLYYQD---QLLPVSRI 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHDLSSNEgggQVIKVKKV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970 108 IVHPQFYTAQIGADIALLELEEPVNVSSHVHTVTLPPASETFPPGMPCWVTGWGDvdNDERLPPPFPLKQVKVPIMENHI 187
Cdd:cd00190  77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGR--TSEGGPLPDVLQEVNVPIVSNAE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970 188 CDAKYHLGAYtgddvriVRDDMLCAGNTR--RDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLD 265
Cdd:cd00190 155 CKRAYSYGGT-------ITDNMLCAGGLEggKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLD 227

                ...
gi 68508970 266 WIH 268
Cdd:cd00190 228 WIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
31-267 4.32e-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: 286.88  E-value: 4.32e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970     31 IVGGQEAPRSKWPWQVSLRVRDryWMHFCGGSLIHPQWVLTAAHCVGPDvkDLAALRVQLREQHLYYQD--QLLPVSRII 108
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGG--GRHFCGGSLISPRWVLTAAHCVRGS--DPSNIRVRLGSHDLSSGEegQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970    109 VHPQFYTAQIGADIALLELEEPVNVSSHVHTVTLPPASETFPPGMPCWVTGWGDVdNDERLPPPFPLKQVKVPIMENHIC 188
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRT-SEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970    189 DAKYHlgaytgdDVRIVRDDMLCAGNTR--RDSCQGDSGGPLVCKvNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDW 266
Cdd:smart00020 157 RRAYS-------GGGAITDNMLCAGGLEggKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228

                   .
gi 68508970    267 I 267
Cdd:smart00020 229 I 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
16-267 3.86e-78

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 237.24  E-value: 3.86e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970  16 AYAAPAPGQALQRvgIVGGQEAPRSKWPWQVSLRVRDRYWMHFCGGSLIHPQWVLTAAHCVGPDvkDLAALRVQLREQHL 95
Cdd:COG5640  18 ALAAAPAADAAPA--IVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDGD--GPSDLRVVIGSTDL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970  96 YYQD-QLLPVSRIIVHPQFYTAQIGADIALLELEEPVNVSShvhTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFp 174
Cdd:COG5640  94 STSGgTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGT- 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970 175 LKQVKVPIMENHICdakyhlGAYTGddvrIVRDDMLCAGNTR--RDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPN 252
Cdd:COG5640 170 LRKADVPVVSDATC------AAYGG----FDGGTMLCAGYPEggKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAG 239
                       250
                ....*....|....*
gi 68508970 253 RPGIYTRVTYYLDWI 267
Cdd:COG5640 240 YPGVYTRVSAYRDWI 254
Trypsin pfam00089
Trypsin;
31-267 1.38e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 234.64  E-value: 1.38e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970    31 IVGGQEAPRSKWPWQVSLRVRDRYwmHFCGGSLIHPQWVLTAAHCVgpdvKDLAALRVQLREQHLYYQD---QLLPVSRI 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK--HFCGGSLISENWVLTAAHCV----SGASDVKVVLGAHNIVLREggeQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970   108 IVHPQFYTAQIGADIALLELEEPVNVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDErlpPPFPLKQVKVPIMENHI 187
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970   188 CDAKYHLGaytgddvriVRDDMLCAGNTRRDSCQGDSGGPLVCKVNgtwLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWI 267
Cdd:pfam00089 152 CRSAYGGT---------VTDTMICAGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
31-268 4.01e-102

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: 297.27  E-value: 4.01e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970  31 IVGGQEAPRSKWPWQVSLRVRDryWMHFCGGSLIHPQWVLTAAHCVGPdvKDLAALRVQLREQHLYYQD---QLLPVSRI 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHDLSSNEgggQVIKVKKV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970 108 IVHPQFYTAQIGADIALLELEEPVNVSSHVHTVTLPPASETFPPGMPCWVTGWGDvdNDERLPPPFPLKQVKVPIMENHI 187
Cdd:cd00190  77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGR--TSEGGPLPDVLQEVNVPIVSNAE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970 188 CDAKYHLGAYtgddvriVRDDMLCAGNTR--RDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLD 265
Cdd:cd00190 155 CKRAYSYGGT-------ITDNMLCAGGLEggKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLD 227

                ...
gi 68508970 266 WIH 268
Cdd:cd00190 228 WIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
31-267 4.32e-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: 286.88  E-value: 4.32e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970     31 IVGGQEAPRSKWPWQVSLRVRDryWMHFCGGSLIHPQWVLTAAHCVGPDvkDLAALRVQLREQHLYYQD--QLLPVSRII 108
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGG--GRHFCGGSLISPRWVLTAAHCVRGS--DPSNIRVRLGSHDLSSGEegQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970    109 VHPQFYTAQIGADIALLELEEPVNVSSHVHTVTLPPASETFPPGMPCWVTGWGDVdNDERLPPPFPLKQVKVPIMENHIC 188
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRT-SEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970    189 DAKYHlgaytgdDVRIVRDDMLCAGNTR--RDSCQGDSGGPLVCKvNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDW 266
Cdd:smart00020 157 RRAYS-------GGGAITDNMLCAGGLEggKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228

                   .
gi 68508970    267 I 267
Cdd:smart00020 229 I 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
16-267 3.86e-78

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 237.24  E-value: 3.86e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970  16 AYAAPAPGQALQRvgIVGGQEAPRSKWPWQVSLRVRDRYWMHFCGGSLIHPQWVLTAAHCVGPDvkDLAALRVQLREQHL 95
Cdd:COG5640  18 ALAAAPAADAAPA--IVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDGD--GPSDLRVVIGSTDL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970  96 YYQD-QLLPVSRIIVHPQFYTAQIGADIALLELEEPVNVSShvhTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFp 174
Cdd:COG5640  94 STSGgTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGT- 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970 175 LKQVKVPIMENHICdakyhlGAYTGddvrIVRDDMLCAGNTR--RDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPN 252
Cdd:COG5640 170 LRKADVPVVSDATC------AAYGG----FDGGTMLCAGYPEggKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAG 239
                       250
                ....*....|....*
gi 68508970 253 RPGIYTRVTYYLDWI 267
Cdd:COG5640 240 YPGVYTRVSAYRDWI 254
Trypsin pfam00089
Trypsin;
31-267 1.38e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 234.64  E-value: 1.38e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970    31 IVGGQEAPRSKWPWQVSLRVRDRYwmHFCGGSLIHPQWVLTAAHCVgpdvKDLAALRVQLREQHLYYQD---QLLPVSRI 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK--HFCGGSLISENWVLTAAHCV----SGASDVKVVLGAHNIVLREggeQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970   108 IVHPQFYTAQIGADIALLELEEPVNVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDErlpPPFPLKQVKVPIMENHI 187
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970   188 CDAKYHLGaytgddvriVRDDMLCAGNTRRDSCQGDSGGPLVCKVNgtwLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWI 267
Cdd:pfam00089 152 CRSAYGGT---------VTDTMICAGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
57-245 3.46e-12

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 63.54  E-value: 3.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970  57 HFCGGSLIHPQWVLTAAHCV--GPDVKDLAALRVQLREQHLYYQDQllPVSRIIVHPQFYT-AQIGADIALLELEEPVNV 133
Cdd:COG3591  12 GVCTGTLIGPNLVLTAGHCVydGAGGGWATNIVFVPGYNGGPYGTA--TATRFRVPPGWVAsGDAGYDYALLRLDEPLGD 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970 134 SshvhTVTLPPASETFP-PGMPCWVTGwgdvdnderlpppfplkqvkvpimenHICDAKYHLGAYTGDDVRIVRDDMLCA 212
Cdd:COG3591  90 T----TGWLGLAFNDAPlAGEPVTIIG--------------------------YPGDRPKDLSLDCSGRVTGVQGNRLSY 139
                       170       180       190
                ....*....|....*....|....*....|...
gi 68508970 213 GNtrrDSCQGDSGGPLVCKVNGTWLQAGVVSWG 245
Cdd:COG3591 140 DC---DTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
61-229 8.15e-03

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 35.86  E-value: 8.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970    61 GSLIHPQ-WVLTAAHCVGPDvkdlAALRVQLREQHLyYQDQLLPVSRIIVHPQfytaqigADIALLELEEPVNvsshvht 139
Cdd:pfam13365   3 GFVVSSDgLVLTNAHVVDDA----EEAAVELVSVVL-ADGREYPATVVARDPD-------LDLALLRVSGDGR------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68508970   140 vTLPPA----SETFPPGMPCWVTGwgdvdnderlpppFPLKQVKVPIMENHICDAKYHLGAYTGDdvRIVRDDMLCAGnt 215
Cdd:pfam13365  64 -GLPPLplgdSEPLVGGERVYAVG-------------YPLGGEKLSLSEGIVSGVDEGRDGGDDG--RVIQTDAALSP-- 125
                         170
                  ....*....|....
gi 68508970   216 rrdscqGDSGGPLV 229
Cdd:pfam13365 126 ------GSSGGPVF 133
 
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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