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Conserved domains on  [gi|165932352|ref|NP_444490|]
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serine protease 29 precursor [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

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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 ...
31-274 8.17e-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: 281.47  E-value: 8.17e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352  31 IVGGHSAPQGKWPWQVSLRIYRyywafWVHNCGGSIIHPQWVLTAAHCIRerDADPSVFRIRVGEAYLY---GGKELLSV 107
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTG-----GRHFCGGSLISPRWVLTAAHCVY--SSAPSNYTVRLGSHDLSsneGGGQVIKV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352 108 SRVIIHPDFVHAGLGSDVALLQLAVSVQSFPNVKPVKLPSESLEVTKKDVCWVTGWGavSTHRSLPPPYRLQQVQVKIID 187
Cdd:cd00190   74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG--RTSEGGPLPDVLQEVNVPIVS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352 188 NSLCEEMYhnatrhrnRGQKLILKDMLCAGNQ--GQDSCYGDSGGPLVCNVTGSWTLVGVVSWGYGCALRDFPGVYARVQ 265
Cdd:cd00190  152 NAECKRAY--------SYGGTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVS 223

                 ....*....
gi 165932352 266 SFLPWITQQ 274
Cdd:cd00190  224 SYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
31-274 8.17e-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: 281.47  E-value: 8.17e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352  31 IVGGHSAPQGKWPWQVSLRIYRyywafWVHNCGGSIIHPQWVLTAAHCIRerDADPSVFRIRVGEAYLY---GGKELLSV 107
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTG-----GRHFCGGSLISPRWVLTAAHCVY--SSAPSNYTVRLGSHDLSsneGGGQVIKV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352 108 SRVIIHPDFVHAGLGSDVALLQLAVSVQSFPNVKPVKLPSESLEVTKKDVCWVTGWGavSTHRSLPPPYRLQQVQVKIID 187
Cdd:cd00190   74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG--RTSEGGPLPDVLQEVNVPIVS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352 188 NSLCEEMYhnatrhrnRGQKLILKDMLCAGNQ--GQDSCYGDSGGPLVCNVTGSWTLVGVVSWGYGCALRDFPGVYARVQ 265
Cdd:cd00190  152 NAECKRAY--------SYGGTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVS 223

                 ....*....
gi 165932352 266 SFLPWITQQ 274
Cdd:cd00190  224 SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
31-271 4.30e-91

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: 269.16  E-value: 4.30e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352    31 IVGGHSAPQGKWPWQVSLRIYRyywafWVHNCGGSIIHPQWVLTAAHCIRerDADPSVFRIRVGEAYL--YGGKELLSVS 108
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGG-----GRHFCGGSLISPRWVLTAAHCVR--GSDPSNIRVRLGSHDLssGEEGQVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352   109 RVIIHPDFVHAGLGSDVALLQLAVSVQSFPNVKPVKLPSESLEVTKKDVCWVTGWGAVSThRSLPPPYRLQQVQVKIIDN 188
Cdd:smart00020  75 KVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSE-GAGSLPDTLQEVNVPIVSN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352   189 SLCEEMYhnatrhrnRGQKLILKDMLCAGNQ--GQDSCYGDSGGPLVCNVtGSWTLVGVVSWGYGCALRDFPGVYARVQS 266
Cdd:smart00020 154 ATCRRAY--------SGGGAITDNMLCAGGLegGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSS 224

                   ....*
gi 165932352   267 FLPWI 271
Cdd:smart00020 225 YLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
5-279 9.86e-77

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 234.16  E-value: 9.86e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352   5 LCLTLFFLGCSIAGTPAPGPEGvlmGIVGGHSAPQGKWPWQVSLRIYRYYWAfwvHNCGGSIIHPQWVLTAAHCIRerDA 84
Cdd:COG5640    8 AALAAAALALALAAAPAADAAP---AIVGGTPATVGEYPWMVALQSSNGPSG---QFCGGTLIAPRWVLTAAHCVD--GD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352  85 DPSVFRIRVGEAYLYG-GKELLSVSRVIIHPDFVHAGLGSDVALLQLAVSVqsfPNVKPVKLPSESLEVTKKDVCWVTGW 163
Cdd:COG5640   80 GPSDLRVVIGSTDLSTsGGTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGW 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352 164 GAVSTHRSLPPPYrLQQVQVKIIDNSLCeemyhnatrhrNRGQKLILKDMLCAGNQ--GQDSCYGDSGGPLVCNVTGSWT 241
Cdd:COG5640  157 GRTSEGPGSQSGT-LRKADVPVVSDATC-----------AAYGGFDGGTMLCAGYPegGKDACQGDSGGPLVVKDGGGWV 224
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 165932352 242 LVGVVSWGYGCALRDFPGVYARVQSFLPWITQQMQRFS 279
Cdd:COG5640  225 LVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 262
Trypsin pfam00089
Trypsin;
31-271 5.48e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 217.70  E-value: 5.48e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352   31 IVGGHSAPQGKWPWQVSLRIYRYYwafwvHNCGGSIIHPQWVLTAAHCIRERDAdpsvFRIRVGEAYLY---GGKELLSV 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK-----HFCGGSLISENWVLTAAHCVSGASD----VKVVLGAHNIVlreGGEQKFDV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352  108 SRVIIHPDFVHAGLGSDVALLQLAVSVQSFPNVKPVKLPSESLEVTKKDVCWVTGWGAVSTHRslpPPYRLQQVQVKIID 187
Cdd:pfam00089  72 EKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPVVS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352  188 NSLCeemyhnatrhRNRGQKLILKDMLCAGNQGQDSCYGDSGGPLVCNVTgswTLVGVVSWGYGCALRDFPGVYARVQSF 267
Cdd:pfam00089 149 RETC----------RSAYGGTVTDTMICAGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSY 215

                  ....
gi 165932352  268 LPWI 271
Cdd:pfam00089 216 LDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
31-274 8.17e-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: 281.47  E-value: 8.17e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352  31 IVGGHSAPQGKWPWQVSLRIYRyywafWVHNCGGSIIHPQWVLTAAHCIRerDADPSVFRIRVGEAYLY---GGKELLSV 107
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTG-----GRHFCGGSLISPRWVLTAAHCVY--SSAPSNYTVRLGSHDLSsneGGGQVIKV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352 108 SRVIIHPDFVHAGLGSDVALLQLAVSVQSFPNVKPVKLPSESLEVTKKDVCWVTGWGavSTHRSLPPPYRLQQVQVKIID 187
Cdd:cd00190   74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG--RTSEGGPLPDVLQEVNVPIVS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352 188 NSLCEEMYhnatrhrnRGQKLILKDMLCAGNQ--GQDSCYGDSGGPLVCNVTGSWTLVGVVSWGYGCALRDFPGVYARVQ 265
Cdd:cd00190  152 NAECKRAY--------SYGGTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVS 223

                 ....*....
gi 165932352 266 SFLPWITQQ 274
Cdd:cd00190  224 SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
31-271 4.30e-91

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: 269.16  E-value: 4.30e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352    31 IVGGHSAPQGKWPWQVSLRIYRyywafWVHNCGGSIIHPQWVLTAAHCIRerDADPSVFRIRVGEAYL--YGGKELLSVS 108
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGG-----GRHFCGGSLISPRWVLTAAHCVR--GSDPSNIRVRLGSHDLssGEEGQVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352   109 RVIIHPDFVHAGLGSDVALLQLAVSVQSFPNVKPVKLPSESLEVTKKDVCWVTGWGAVSThRSLPPPYRLQQVQVKIIDN 188
Cdd:smart00020  75 KVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSE-GAGSLPDTLQEVNVPIVSN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352   189 SLCEEMYhnatrhrnRGQKLILKDMLCAGNQ--GQDSCYGDSGGPLVCNVtGSWTLVGVVSWGYGCALRDFPGVYARVQS 266
Cdd:smart00020 154 ATCRRAY--------SGGGAITDNMLCAGGLegGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSS 224

                   ....*
gi 165932352   267 FLPWI 271
Cdd:smart00020 225 YLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
5-279 9.86e-77

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 234.16  E-value: 9.86e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352   5 LCLTLFFLGCSIAGTPAPGPEGvlmGIVGGHSAPQGKWPWQVSLRIYRYYWAfwvHNCGGSIIHPQWVLTAAHCIRerDA 84
Cdd:COG5640    8 AALAAAALALALAAAPAADAAP---AIVGGTPATVGEYPWMVALQSSNGPSG---QFCGGTLIAPRWVLTAAHCVD--GD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352  85 DPSVFRIRVGEAYLYG-GKELLSVSRVIIHPDFVHAGLGSDVALLQLAVSVqsfPNVKPVKLPSESLEVTKKDVCWVTGW 163
Cdd:COG5640   80 GPSDLRVVIGSTDLSTsGGTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGW 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352 164 GAVSTHRSLPPPYrLQQVQVKIIDNSLCeemyhnatrhrNRGQKLILKDMLCAGNQ--GQDSCYGDSGGPLVCNVTGSWT 241
Cdd:COG5640  157 GRTSEGPGSQSGT-LRKADVPVVSDATC-----------AAYGGFDGGTMLCAGYPegGKDACQGDSGGPLVVKDGGGWV 224
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 165932352 242 LVGVVSWGYGCALRDFPGVYARVQSFLPWITQQMQRFS 279
Cdd:COG5640  225 LVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 262
Trypsin pfam00089
Trypsin;
31-271 5.48e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 217.70  E-value: 5.48e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352   31 IVGGHSAPQGKWPWQVSLRIYRYYwafwvHNCGGSIIHPQWVLTAAHCIRERDAdpsvFRIRVGEAYLY---GGKELLSV 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK-----HFCGGSLISENWVLTAAHCVSGASD----VKVVLGAHNIVlreGGEQKFDV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352  108 SRVIIHPDFVHAGLGSDVALLQLAVSVQSFPNVKPVKLPSESLEVTKKDVCWVTGWGAVSTHRslpPPYRLQQVQVKIID 187
Cdd:pfam00089  72 EKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPVVS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352  188 NSLCeemyhnatrhRNRGQKLILKDMLCAGNQGQDSCYGDSGGPLVCNVTgswTLVGVVSWGYGCALRDFPGVYARVQSF 267
Cdd:pfam00089 149 RETC----------RSAYGGTVTDTMICAGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSY 215

                  ....
gi 165932352  268 LPWI 271
Cdd:pfam00089 216 LDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
62-277 5.23e-12

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 63.16  E-value: 5.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352  62 CGGSIIHPQWVLTAAHCIRERDADPSVFRIRVGEAYLYGGKELLSVSRVIIHPDFVHAGL-GSDVALLQLAVSVQsfPNV 140
Cdd:COG3591   14 CTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGPYGTATATRFRVPPGWVASGDaGYDYALLRLDEPLG--DTT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352 141 KPVKLPSESLEVTKKDVcWVTGWGAvsthrslpppyrlqqvqvkiiDNSLCEEMYHNATRHRNRGQKLIlkdMLCagnqg 220
Cdd:COG3591   92 GWLGLAFNDAPLAGEPV-TIIGYPG---------------------DRPKDLSLDCSGRVTGVQGNRLS---YDC----- 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 165932352 221 qDSCYGDSGGPLVCNVTGSWTLVGVVSWGYGcalrDFPGVYARVQS-FLPWITQQMQR 277
Cdd:COG3591  142 -DTTGGSSGSPVLDDSDGGGRVVGVHSAGGA----DRANTGVRLTSaIVAALRAWASA 194
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
42-162 4.11e-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: 36.37  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932352   42 WPWQVSLRIYRYYWafwvhnCGGSIIHPQWVLTAAHCIRERDADPSVFRIRVGeaylyGGKELLSVS---RVIIHPDFVH 118
Cdd:pfam09342   1 WPWIAKVYLDGNMI------CSGVLIDASWVIVSGSCLRDTNLRHQYISVVLG-----GAKTLKSIEgpyEQIVRVDCRH 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 165932352  119 AGLGSDVALLQLAVSVQSFPNVKPVKLPSESLEVTKKDVCWVTG 162
Cdd:pfam09342  70 DIPESEISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 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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