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Conserved domains on  [gi|19111160|ref|NP_579929|]
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prostasin 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 ...
45-284 8.37e-103

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: 301.50  E-value: 8.37e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160  45 ITGGGSAKPGQWPWQVSITY-DGNHVCGGSLVSNKWVVSAAHCFPREHsREAYEVKLGAHQLDSYSNDTVVHTVAQIITH 123
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160 124 SSYREEGSQGDIALIRLSSPVTFSRYIRPICLPAANASFPNGLHCTVTGWGHVAPSVSLqtPRPLQQLEVPLISRETCSC 203
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160 204 LYNinavpeEPHTIQQDMLCAGYVKGGKDACQGDSGGPLSCPMEGIWYLAGIVSWGDACGAPNRPGVYTLTSTYASWIHH 283
Cdd:cd00190 158 AYS------YGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231

                .
gi 19111160 284 H 284
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 ...
45-284 8.37e-103

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: 301.50  E-value: 8.37e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160  45 ITGGGSAKPGQWPWQVSITY-DGNHVCGGSLVSNKWVVSAAHCFPREHsREAYEVKLGAHQLDSYSNDTVVHTVAQIITH 123
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160 124 SSYREEGSQGDIALIRLSSPVTFSRYIRPICLPAANASFPNGLHCTVTGWGHVAPSVSLqtPRPLQQLEVPLISRETCSC 203
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160 204 LYNinavpeEPHTIQQDMLCAGYVKGGKDACQGDSGGPLSCPMEGIWYLAGIVSWGDACGAPNRPGVYTLTSTYASWIHH 283
Cdd:cd00190 158 AYS------YGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231

                .
gi 19111160 284 H 284
Cdd:cd00190 232 T 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
44-281 1.21e-97

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: 288.42  E-value: 1.21e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160     44 RITGGGSAKPGQWPWQVSITY-DGNHVCGGSLVSNKWVVSAAHCFpREHSREAYEVKLGAHQLdSYSNDTVVHTVAQIIT 122
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDL-SSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160    123 HSSYREEGSQGDIALIRLSSPVTFSRYIRPICLPAANASFPNGLHCTVTGWGHVAPSvSLQTPRPLQQLEVPLISRETCS 202
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEG-AGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19111160    203 CLYninavpEEPHTIQQDMLCAGYVKGGKDACQGDSGGPLSCpMEGIWYLAGIVSWGDACGAPNRPGVYTLTSTYASWI 281
Cdd:smart00020 158 RAY------SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
45-281 2.53e-80

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 243.89  E-value: 2.53e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160    45 ITGGGSAKPGQWPWQVSITYDGN-HVCGGSLVSNKWVVSAAHCFpreHSREAYEVKLGAHQLDSYSNDTVVHTVAQIITH 123
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160   124 SSYREEGSQGDIALIRLSSPVTFSRYIRPICLPAANASFPNGLHCTVTGWGHVApsvSLQTPRPLQQLEVPLISRETCSC 203
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTK---TLGPSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19111160   204 LYninavpeePHTIQQDMLCAGYvkGGKDACQGDSGGPLSCPMEgiwYLAGIVSWGDACGAPNRPGVYTLTSTYASWI 281
Cdd:pfam00089 155 AY--------GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
39-288 7.77e-70

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 218.75  E-value: 7.77e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160  39 AVIQPRITGGGSAKPGQWPWQVSITYDG---NHVCGGSLVSNKWVVSAAHCFPrEHSREAYEVKLGAHQLDSysNDTVVH 115
Cdd:COG5640  25 ADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVD-GDGPSDLRVVIGSTDLST--SGGTVV 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160 116 TVAQIITHSSYREEGSQGDIALIRLSSPVTFSRYIRpicLPAANASFPNGLHCTVTGWGHVAPSVSlQTPRPLQQLEVPL 195
Cdd:COG5640 102 KVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLRKADVPV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160 196 ISRETCSCLYNINAvpeephtiqQDMLCAGYVKGGKDACQGDSGGPLSCPMEGIWYLAGIVSWGDACGAPNRPGVYTLTS 275
Cdd:COG5640 178 VSDATCAAYGGFDG---------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVS 248
                       250
                ....*....|...
gi 19111160 276 TYASWIHHHVAEL 288
Cdd:COG5640 249 AYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
45-284 8.37e-103

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: 301.50  E-value: 8.37e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160  45 ITGGGSAKPGQWPWQVSITY-DGNHVCGGSLVSNKWVVSAAHCFPREHsREAYEVKLGAHQLDSYSNDTVVHTVAQIITH 123
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160 124 SSYREEGSQGDIALIRLSSPVTFSRYIRPICLPAANASFPNGLHCTVTGWGHVAPSVSLqtPRPLQQLEVPLISRETCSC 203
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160 204 LYNinavpeEPHTIQQDMLCAGYVKGGKDACQGDSGGPLSCPMEGIWYLAGIVSWGDACGAPNRPGVYTLTSTYASWIHH 283
Cdd:cd00190 158 AYS------YGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231

                .
gi 19111160 284 H 284
Cdd:cd00190 232 T 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
44-281 1.21e-97

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: 288.42  E-value: 1.21e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160     44 RITGGGSAKPGQWPWQVSITY-DGNHVCGGSLVSNKWVVSAAHCFpREHSREAYEVKLGAHQLdSYSNDTVVHTVAQIIT 122
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDL-SSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160    123 HSSYREEGSQGDIALIRLSSPVTFSRYIRPICLPAANASFPNGLHCTVTGWGHVAPSvSLQTPRPLQQLEVPLISRETCS 202
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEG-AGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19111160    203 CLYninavpEEPHTIQQDMLCAGYVKGGKDACQGDSGGPLSCpMEGIWYLAGIVSWGDACGAPNRPGVYTLTSTYASWI 281
Cdd:smart00020 158 RAY------SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
45-281 2.53e-80

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 243.89  E-value: 2.53e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160    45 ITGGGSAKPGQWPWQVSITYDGN-HVCGGSLVSNKWVVSAAHCFpreHSREAYEVKLGAHQLDSYSNDTVVHTVAQIITH 123
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160   124 SSYREEGSQGDIALIRLSSPVTFSRYIRPICLPAANASFPNGLHCTVTGWGHVApsvSLQTPRPLQQLEVPLISRETCSC 203
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTK---TLGPSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19111160   204 LYninavpeePHTIQQDMLCAGYvkGGKDACQGDSGGPLSCPMEgiwYLAGIVSWGDACGAPNRPGVYTLTSTYASWI 281
Cdd:pfam00089 155 AY--------GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
39-288 7.77e-70

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 218.75  E-value: 7.77e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160  39 AVIQPRITGGGSAKPGQWPWQVSITYDG---NHVCGGSLVSNKWVVSAAHCFPrEHSREAYEVKLGAHQLDSysNDTVVH 115
Cdd:COG5640  25 ADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVD-GDGPSDLRVVIGSTDLST--SGGTVV 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160 116 TVAQIITHSSYREEGSQGDIALIRLSSPVTFSRYIRpicLPAANASFPNGLHCTVTGWGHVAPSVSlQTPRPLQQLEVPL 195
Cdd:COG5640 102 KVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLRKADVPV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160 196 ISRETCSCLYNINAvpeephtiqQDMLCAGYVKGGKDACQGDSGGPLSCPMEGIWYLAGIVSWGDACGAPNRPGVYTLTS 275
Cdd:COG5640 178 VSDATCAAYGGFDG---------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVS 248
                       250
                ....*....|...
gi 19111160 276 TYASWIHHHVAEL 288
Cdd:COG5640 249 AYRDWIKSTAGGL 261
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
56-156 1.23e-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: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111160    56 WPWQVSITYDGNHVCGGSLVSNKWVVSAAHCFPREHSREAY-EVKLGAHQldsySNDTVVHTVAQIITHSSYrEEGSQGD 134
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYiSVVLGGAK----TLKSIEGPYEQIVRVDCR-HDIPESE 75
                          90       100
                  ....*....|....*....|..
gi 19111160   135 IALIRLSSPVTFSRYIRPICLP 156
Cdd:pfam09342  76 ISLLHLASPASFSNHVLPTFVP 97
 
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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