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Conserved domains on  [gi|569000469|ref|XP_006524423|]
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tryptase gamma isoform X3 [Mus musculus]

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 ...
41-271 1.49e-91

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: 272.23  E-value: 1.49e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469  41 IVGGHAAPAGTWPWQASLRLHK-VHVCGGSLLSPEWVLTAAHCFSGSVNSSdYQVHLGELTVT---LSPHFSTVKRIIM- 115
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSAPSN-YTVRLGSHDLSsneGGGQVIKVKKVIVh 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469 116 --YtgspGPPGSSGDIALVQLSSPVALSSQVQPVCLPEASADFYPGMQCWVTGWGYTGEGEPLkpPYNLQEAKVSVVDVK 193
Cdd:cd00190   80 pnY----NPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469 194 TCSQAYnsPNGSLIQPDMLCARGPG---DACQDDSGGPLVCQVAGTWQQAGVVSWGEGCGRPDRPGVYARVTAYVNWIHH 270
Cdd:cd00190  154 ECKRAY--SYGGTITDNMLCAGGLEggkDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231

                 .
gi 569000469 271 H 271
Cdd:cd00190  232 T 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
41-271 1.49e-91

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: 272.23  E-value: 1.49e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469  41 IVGGHAAPAGTWPWQASLRLHK-VHVCGGSLLSPEWVLTAAHCFSGSVNSSdYQVHLGELTVT---LSPHFSTVKRIIM- 115
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSAPSN-YTVRLGSHDLSsneGGGQVIKVKKVIVh 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469 116 --YtgspGPPGSSGDIALVQLSSPVALSSQVQPVCLPEASADFYPGMQCWVTGWGYTGEGEPLkpPYNLQEAKVSVVDVK 193
Cdd:cd00190   80 pnY----NPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469 194 TCSQAYnsPNGSLIQPDMLCARGPG---DACQDDSGGPLVCQVAGTWQQAGVVSWGEGCGRPDRPGVYARVTAYVNWIHH 270
Cdd:cd00190  154 ECKRAY--SYGGTITDNMLCAGGLEggkDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231

                 .
gi 569000469 271 H 271
Cdd:cd00190  232 T 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
40-268 5.44e-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: 265.70  E-value: 5.44e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469    40 RIVGGHAAPAGTWPWQASLRLHK-VHVCGGSLLSPEWVLTAAHCFSGSVNSSdYQVHLGELTVTLSPHFST--VKRIIM- 115
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSN-IRVRLGSHDLSSGEEGQVikVSKVIIh 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469   116 --YtgspGPPGSSGDIALVQLSSPVALSSQVQPVCLPEASADFYPGMQCWVTGWGYTGEGEPlKPPYNLQEAKVSVVDVK 193
Cdd:smart00020  80 pnY----NPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569000469   194 TCSQAYnsPNGSLIQPDMLCARGPG---DACQDDSGGPLVCQVaGTWQQAGVVSWGEGCGRPDRPGVYARVTAYVNWI 268
Cdd:smart00020 155 TCRRAY--SGGGAITDNMLCAGGLEggkDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
41-268 1.40e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 215.77  E-value: 1.40e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469   41 IVGGHAAPAGTWPWQASLRL-HKVHVCGGSLLSPEWVLTAAHCFSgsvNSSDYQVHLGELTVTL---SPHFSTVKRIIMY 116
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLregGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469  117 TGSPGPPGSSgDIALVQLSSPVALSSQVQPVCLPEASADFYPGMQCWVTGWGYTGEgepLKPPYNLQEAKVSVVDVKTCS 196
Cdd:pfam00089  78 PNYNPDTLDN-DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKT---LGPSDTLQEVTVPVVSRETCR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000469  197 QAYNSPngslIQPDMLCARGPG-DACQDDSGGPLVCqvaGTWQQAGVVSWGEGCGRPDRPGVYARVTAYVNWI 268
Cdd:pfam00089 154 SAYGGT----VTDTMICAGAGGkDACQGDSGGPLVC---SDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
32-276 8.40e-62

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 197.56  E-value: 8.40e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469  32 PQVSNSGSRIVGGHAAPAGTWPWQASLRL---HKVHVCGGSLLSPEWVLTAAHCFSGSvNSSDYQVHLGELTVTLSPHF- 107
Cdd:COG5640   22 APAADAAPAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGSTDLSTSGGTv 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469 108 STVKRIIMYtGSPGPPGSSGDIALVQLSSPValsSQVQPVCLPEASADFYPGMQCWVTGWGYTGEGEPLKPPYnLQEAKV 187
Cdd:COG5640  101 VKVARIVVH-PDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGT-LRKADV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469 188 SVVDVKTCsQAYNSPNGSliqpDMLCA---RGPGDACQDDSGGPLVCQVAGTWQQAGVVSWGEGCGRPDRPGVYARVTAY 264
Cdd:COG5640  176 PVVSDATC-AAYGGFDGG----TMLCAgypEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAY 250
                        250
                 ....*....|..
gi 569000469 265 VNWIHHHIPEAG 276
Cdd:COG5640  251 RDWIKSTAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
41-271 1.49e-91

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: 272.23  E-value: 1.49e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469  41 IVGGHAAPAGTWPWQASLRLHK-VHVCGGSLLSPEWVLTAAHCFSGSVNSSdYQVHLGELTVT---LSPHFSTVKRIIM- 115
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSAPSN-YTVRLGSHDLSsneGGGQVIKVKKVIVh 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469 116 --YtgspGPPGSSGDIALVQLSSPVALSSQVQPVCLPEASADFYPGMQCWVTGWGYTGEGEPLkpPYNLQEAKVSVVDVK 193
Cdd:cd00190   80 pnY----NPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469 194 TCSQAYnsPNGSLIQPDMLCARGPG---DACQDDSGGPLVCQVAGTWQQAGVVSWGEGCGRPDRPGVYARVTAYVNWIHH 270
Cdd:cd00190  154 ECKRAY--SYGGTITDNMLCAGGLEggkDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231

                 .
gi 569000469 271 H 271
Cdd:cd00190  232 T 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
40-268 5.44e-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: 265.70  E-value: 5.44e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469    40 RIVGGHAAPAGTWPWQASLRLHK-VHVCGGSLLSPEWVLTAAHCFSGSVNSSdYQVHLGELTVTLSPHFST--VKRIIM- 115
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSN-IRVRLGSHDLSSGEEGQVikVSKVIIh 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469   116 --YtgspGPPGSSGDIALVQLSSPVALSSQVQPVCLPEASADFYPGMQCWVTGWGYTGEGEPlKPPYNLQEAKVSVVDVK 193
Cdd:smart00020  80 pnY----NPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569000469   194 TCSQAYnsPNGSLIQPDMLCARGPG---DACQDDSGGPLVCQVaGTWQQAGVVSWGEGCGRPDRPGVYARVTAYVNWI 268
Cdd:smart00020 155 TCRRAY--SGGGAITDNMLCAGGLEggkDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
41-268 1.40e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 215.77  E-value: 1.40e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469   41 IVGGHAAPAGTWPWQASLRL-HKVHVCGGSLLSPEWVLTAAHCFSgsvNSSDYQVHLGELTVTL---SPHFSTVKRIIMY 116
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLregGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469  117 TGSPGPPGSSgDIALVQLSSPVALSSQVQPVCLPEASADFYPGMQCWVTGWGYTGEgepLKPPYNLQEAKVSVVDVKTCS 196
Cdd:pfam00089  78 PNYNPDTLDN-DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKT---LGPSDTLQEVTVPVVSRETCR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000469  197 QAYNSPngslIQPDMLCARGPG-DACQDDSGGPLVCqvaGTWQQAGVVSWGEGCGRPDRPGVYARVTAYVNWI 268
Cdd:pfam00089 154 SAYGGT----VTDTMICAGAGGkDACQGDSGGPLVC---SDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
32-276 8.40e-62

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 197.56  E-value: 8.40e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469  32 PQVSNSGSRIVGGHAAPAGTWPWQASLRL---HKVHVCGGSLLSPEWVLTAAHCFSGSvNSSDYQVHLGELTVTLSPHF- 107
Cdd:COG5640   22 APAADAAPAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGSTDLSTSGGTv 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469 108 STVKRIIMYtGSPGPPGSSGDIALVQLSSPValsSQVQPVCLPEASADFYPGMQCWVTGWGYTGEGEPLKPPYnLQEAKV 187
Cdd:COG5640  101 VKVARIVVH-PDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGT-LRKADV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469 188 SVVDVKTCsQAYNSPNGSliqpDMLCA---RGPGDACQDDSGGPLVCQVAGTWQQAGVVSWGEGCGRPDRPGVYARVTAY 264
Cdd:COG5640  176 PVVSDATC-AAYGGFDGG----TMLCAgypEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAY 250
                        250
                 ....*....|..
gi 569000469 265 VNWIHHHIPEAG 276
Cdd:COG5640  251 RDWIKSTAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
64-246 1.57e-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: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469  64 HVCGGSLLSPEWVLTAAHCfsgsVNSSDYQVHLGELTVTLSPH-----FSTVKRIIMYTGSPGPPGSSGDIALVQLSSPV 138
Cdd:COG3591   12 GVCTGTLIGPNLVLTAGHC----VYDGAGGGWATNIVFVPGYNggpygTATATRFRVPPGWVASGDAGYDYALLRLDEPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469 139 ALSSQVQPVclpEASADFYPGMQCWVTGWgytGEGEPLKPPYnlqeakvsvvdvkTCSQAYNSPNGSLIQpdMLCargpg 218
Cdd:COG3591   88 GDTTGWLGL---AFNDAPLAGEPVTIIGY---PGDRPKDLSL-------------DCSGRVTGVQGNRLS--YDC----- 141
                        170       180
                 ....*....|....*....|....*...
gi 569000469 219 DACQDDSGGPLVCQVAGTWQQAGVVSWG 246
Cdd:COG3591  142 DTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
52-166 2.57e-03

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: 37.14  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000469   52 WPWQASLRLHKVHVCGGSLLSPEWVLTAAHCFSG-SVNSSDYQVHLGELTVTLS---PHfSTVKRIIMYtgspgPPGSSG 127
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDtNLRHQYISVVLGGAKTLKSiegPY-EQIVRVDCR-----HDIPES 74
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 569000469  128 DIALVQLSSPVALSSQVQPVCLPEASADFYPGMQCWVTG 166
Cdd:pfam09342  75 EISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
 
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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