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Conserved domains on  [gi|755556797|ref|XP_011244785|]
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serine protease 30 isoform X1 [Mus musculus]

Protein Classification

serine protease( domain architecture ID 10076129)

serine protease such as human cathepsin G with trypsin- and chymotrypsin-like specificity; also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity

Graphical summary

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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 ...
74-312 2.15e-101

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: 298.42  E-value: 2.15e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797  74 IVGGQDALEGQWPWQVSLWITEDGHICGGSLIHEVWVLTAAHCFRRSlNPSFYHVKVGGLTLSLLEPHSTLVAVRNIFVH 153
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797 154 PTYLwADASSGDIALVQLDTPLRPSQFT-PVCLPAAQTPLTPGTVCWVTGWGATQERD-MASVLQELAVPLLDSEDCEKM 231
Cdd:cd00190   80 PNYN-PSTYDNDIALLKLKRPVTLSDNVrPICLPSSGYNLPAGTTCTVSGWGRTSEGGpLPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797 232 YHTQGsslsgerIIQSDMLCAGYVEGQKDSCQGDSGGPLVCSINSSWTQVGITSWGIGCARPYRPGVYTRVPTYVDWIQR 311
Cdd:cd00190  159 YSYGG-------TITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231

                 .
gi 755556797 312 I 312
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 ...
74-312 2.15e-101

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: 298.42  E-value: 2.15e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797  74 IVGGQDALEGQWPWQVSLWITEDGHICGGSLIHEVWVLTAAHCFRRSlNPSFYHVKVGGLTLSLLEPHSTLVAVRNIFVH 153
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797 154 PTYLwADASSGDIALVQLDTPLRPSQFT-PVCLPAAQTPLTPGTVCWVTGWGATQERD-MASVLQELAVPLLDSEDCEKM 231
Cdd:cd00190   80 PNYN-PSTYDNDIALLKLKRPVTLSDNVrPICLPSSGYNLPAGTTCTVSGWGRTSEGGpLPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797 232 YHTQGsslsgerIIQSDMLCAGYVEGQKDSCQGDSGGPLVCSINSSWTQVGITSWGIGCARPYRPGVYTRVPTYVDWIQR 311
Cdd:cd00190  159 YSYGG-------TITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231

                 .
gi 755556797 312 I 312
Cdd:cd00190  232 T 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
73-309 3.02e-92

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: 274.94  E-value: 3.02e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797    73 KIVGGQDALEGQWPWQVSLWITEDGHICGGSLIHEVWVLTAAHCFRRSlNPSFYHVKVGGLTLSLLEpHSTLVAVRNIFV 152
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGE-EGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797   153 HPTYLwADASSGDIALVQLDTPLRPSQF-TPVCLPAAQTPLTPGTVCWVTGWGATQERDM--ASVLQELAVPLLDSEDCE 229
Cdd:smart00020  79 HPNYN-PSTYDNDIALLKLKEPVTLSDNvRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGslPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797   230 KMYhtqgsslSGERIIQSDMLCAGYVEGQKDSCQGDSGGPLVCSiNSSWTQVGITSWGIGCARPYRPGVYTRVPTYVDWI 309
Cdd:smart00020 158 RAY-------SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
74-309 2.20e-75

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 231.56  E-value: 2.20e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797   74 IVGGQDALEGQWPWQVSLWITEDGHICGGSLIHEVWVLTAAHCFRrslNPSFYHVKVGGLTLSLLEPHSTLVAVRNIFVH 153
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797  154 PTYLwADASSGDIALVQLDTPLRPSQFT-PVCLPAAQTPLTPGTVCWVTGWGATQERDMASVLQELAVPLLDSEDCEKMY 232
Cdd:pfam00089  78 PNYN-PDTLDNDIALLKLESPVTLGDTVrPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755556797  233 HTqgsslsgerIIQSDMLCAGYveGQKDSCQGDSGGPLVCSINsswTQVGITSWGIGCARPYRPGVYTRVPTYVDWI 309
Cdd:pfam00089 157 GG---------TVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
63-316 3.62e-74

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 229.92  E-value: 3.62e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797  63 SVCGHSRDAGKIVGGQDALEGQWPWQVSLWITE--DGHICGGSLIHEVWVLTAAHCFRRSlNPSFYHVKVGGLTLSLLEP 140
Cdd:COG5640   20 AAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpSGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGSTDLSTSGG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797 141 hsTLVAVRNIFVHPTYLWADASsGDIALVQLDTPLrpSQFTPVCLPAAQTPLTPGTVCWVTGWGATQE--RDMASVLQEL 218
Cdd:COG5640   99 --TVVKVARIVVHPDYDPATPG-NDIALLKLATPV--PGVAPAPLATSADAAAPGTPATVAGWGRTSEgpGSQSGTLRKA 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797 219 AVPLLDSEDCEkmyhtqgsslSGERIIQSDMLCAGYVEGQKDSCQGDSGGPLVCSINSSWTQVGITSWGIGCARPYRPGV 298
Cdd:COG5640  174 DVPVVSDATCA----------AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGV 243
                        250
                 ....*....|....*...
gi 755556797 299 YTRVPTYVDWIQRILAEN 316
Cdd:COG5640  244 YTRVSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
74-312 2.15e-101

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: 298.42  E-value: 2.15e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797  74 IVGGQDALEGQWPWQVSLWITEDGHICGGSLIHEVWVLTAAHCFRRSlNPSFYHVKVGGLTLSLLEPHSTLVAVRNIFVH 153
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797 154 PTYLwADASSGDIALVQLDTPLRPSQFT-PVCLPAAQTPLTPGTVCWVTGWGATQERD-MASVLQELAVPLLDSEDCEKM 231
Cdd:cd00190   80 PNYN-PSTYDNDIALLKLKRPVTLSDNVrPICLPSSGYNLPAGTTCTVSGWGRTSEGGpLPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797 232 YHTQGsslsgerIIQSDMLCAGYVEGQKDSCQGDSGGPLVCSINSSWTQVGITSWGIGCARPYRPGVYTRVPTYVDWIQR 311
Cdd:cd00190  159 YSYGG-------TITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231

                 .
gi 755556797 312 I 312
Cdd:cd00190  232 T 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
73-309 3.02e-92

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: 274.94  E-value: 3.02e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797    73 KIVGGQDALEGQWPWQVSLWITEDGHICGGSLIHEVWVLTAAHCFRRSlNPSFYHVKVGGLTLSLLEpHSTLVAVRNIFV 152
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGE-EGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797   153 HPTYLwADASSGDIALVQLDTPLRPSQF-TPVCLPAAQTPLTPGTVCWVTGWGATQERDM--ASVLQELAVPLLDSEDCE 229
Cdd:smart00020  79 HPNYN-PSTYDNDIALLKLKEPVTLSDNvRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGslPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797   230 KMYhtqgsslSGERIIQSDMLCAGYVEGQKDSCQGDSGGPLVCSiNSSWTQVGITSWGIGCARPYRPGVYTRVPTYVDWI 309
Cdd:smart00020 158 RAY-------SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
74-309 2.20e-75

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 231.56  E-value: 2.20e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797   74 IVGGQDALEGQWPWQVSLWITEDGHICGGSLIHEVWVLTAAHCFRrslNPSFYHVKVGGLTLSLLEPHSTLVAVRNIFVH 153
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797  154 PTYLwADASSGDIALVQLDTPLRPSQFT-PVCLPAAQTPLTPGTVCWVTGWGATQERDMASVLQELAVPLLDSEDCEKMY 232
Cdd:pfam00089  78 PNYN-PDTLDNDIALLKLESPVTLGDTVrPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755556797  233 HTqgsslsgerIIQSDMLCAGYveGQKDSCQGDSGGPLVCSINsswTQVGITSWGIGCARPYRPGVYTRVPTYVDWI 309
Cdd:pfam00089 157 GG---------TVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
63-316 3.62e-74

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 229.92  E-value: 3.62e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797  63 SVCGHSRDAGKIVGGQDALEGQWPWQVSLWITE--DGHICGGSLIHEVWVLTAAHCFRRSlNPSFYHVKVGGLTLSLLEP 140
Cdd:COG5640   20 AAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpSGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGSTDLSTSGG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797 141 hsTLVAVRNIFVHPTYLWADASsGDIALVQLDTPLrpSQFTPVCLPAAQTPLTPGTVCWVTGWGATQE--RDMASVLQEL 218
Cdd:COG5640   99 --TVVKVARIVVHPDYDPATPG-NDIALLKLATPV--PGVAPAPLATSADAAAPGTPATVAGWGRTSEgpGSQSGTLRKA 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797 219 AVPLLDSEDCEkmyhtqgsslSGERIIQSDMLCAGYVEGQKDSCQGDSGGPLVCSINSSWTQVGITSWGIGCARPYRPGV 298
Cdd:COG5640  174 DVPVVSDATCA----------AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGV 243
                        250
                 ....*....|....*...
gi 755556797 299 YTRVPTYVDWIQRILAEN 316
Cdd:COG5640  244 YTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
93-287 4.14e-08

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 52.76  E-value: 4.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797  93 ITEDGHICGGSLIHEVWVLTAAHCFRRSLN---PSFYHVKVGgltlSLLEPHSTlVAVRNIFVHPTYLWADASSGDIALV 169
Cdd:COG3591    7 TDGGGGVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPG----YNGGPYGT-ATATRFRVPPGWVASGDAGYDYALL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797 170 QLDTPLRPSqfTPVCLPAAQTPLTPGTVCWVTGWGATQERDMAsvlqelavplldsedcekMYHTQGSSLSGERIIQSDM 249
Cdd:COG3591   82 RLDEPLGDT--TGWLGLAFNDAPLAGEPVTIIGYPGDRPKDLS------------------LDCSGRVTGVQGNRLSYDC 141
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 755556797 250 lcagyvegqkDSCQGDSGGPLVCSINSSWTQVGITSWG 287
Cdd:COG3591  142 ----------DTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
106-283 5.01e-03

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 37.02  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797  106 HEVWVLTAAHCFRRSLNPSFYHVKVGGltlsllePHSTLVAVRNIFVHPTYlwadassgDIALVQLDTPLRPSQFTPVcl 185
Cdd:pfam13365   8 SDGLVLTNAHVVDDAEEAAVELVSVVL-------ADGREYPATVVARDPDL--------DLALLRVSGDGRGLPPLPL-- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755556797  186 pAAQTPLTPGTVCWVTGWGATQERDMAS--VLQELAVPLLDSEDcekmyhtqgsslsgERIIQSDMLCAGyvegqkdscq 263
Cdd:pfam13365  71 -GDSEPLVGGERVYAVGYPLGGEKLSLSegIVSGVDEGRDGGDD--------------GRVIQTDAALSP---------- 125
                         170       180
                  ....*....|....*....|
gi 755556797  264 GDSGGPLVcsiNSSWTQVGI 283
Cdd:pfam13365 126 GSSGGPVF---DADGRVVGI 142
 
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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