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Conserved domains on  [gi|2250232533|ref|NP_001394890|]
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prostasin precursor [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 ...
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 2250232533  45 ITGGGSAKPGQWPWQVSITY-DGNHVCGGSLVSNKWVVSAAHCFPREHsREAYEVKLGAHQLDSYSNDTVVHTVAQIITH 123
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250232533 124 SSYREEGSQGDIALIRLSSPVTFSRYIRPICLPAANASFPNGLHCTVTGWGHVAPSVSLqtPRPLQQLEVPLISRETCSC 203
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250232533 204 LYNinavpeEPHTIQQDMLCAGYVKGGKDACQGDSGGPLSCPMEGIWYLAGIVSWGDACGAPNRPGVYTLTSTYASWIHH 283
Cdd:cd00190   158 AYS------YGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231

                  .
gi 2250232533 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 2250232533  45 ITGGGSAKPGQWPWQVSITY-DGNHVCGGSLVSNKWVVSAAHCFPREHsREAYEVKLGAHQLDSYSNDTVVHTVAQIITH 123
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250232533 124 SSYREEGSQGDIALIRLSSPVTFSRYIRPICLPAANASFPNGLHCTVTGWGHVAPSVSLqtPRPLQQLEVPLISRETCSC 203
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250232533 204 LYNinavpeEPHTIQQDMLCAGYVKGGKDACQGDSGGPLSCPMEGIWYLAGIVSWGDACGAPNRPGVYTLTSTYASWIHH 283
Cdd:cd00190   158 AYS------YGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231

                  .
gi 2250232533 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 2250232533   44 RITGGGSAKPGQWPWQVSITY-DGNHVCGGSLVSNKWVVSAAHCFpREHSREAYEVKLGAHQLdSYSNDTVVHTVAQIIT 122
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDL-SSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250232533  123 HSSYREEGSQGDIALIRLSSPVTFSRYIRPICLPAANASFPNGLHCTVTGWGHVAPSvSLQTPRPLQQLEVPLISRETCS 202
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEG-AGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2250232533  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 2250232533  45 ITGGGSAKPGQWPWQVSITYDGN-HVCGGSLVSNKWVVSAAHCFpreHSREAYEVKLGAHQLDSYSNDTVVHTVAQIITH 123
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250232533 124 SSYREEGSQGDIALIRLSSPVTFSRYIRPICLPAANASFPNGLHCTVTGWGHVApsvSLQTPRPLQQLEVPLISRETCSC 203
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTK---TLGPSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2250232533 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 2250232533  39 AVIQPRITGGGSAKPGQWPWQVSITYDG---NHVCGGSLVSNKWVVSAAHCFPrEHSREAYEVKLGAHQLDSysNDTVVH 115
Cdd:COG5640    25 ADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVD-GDGPSDLRVVIGSTDLST--SGGTVV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250232533 116 TVAQIITHSSYREEGSQGDIALIRLSSPVTFSRYIRpicLPAANASFPNGLHCTVTGWGHVAPSVSlQTPRPLQQLEVPL 195
Cdd:COG5640   102 KVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLRKADVPV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250232533 196 ISRETCSCLYNINAvpeephtiqQDMLCAGYVKGGKDACQGDSGGPLSCPMEGIWYLAGIVSWGDACGAPNRPGVYTLTS 275
Cdd:COG5640   178 VSDATCAAYGGFDG---------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVS 248
                         250
                  ....*....|...
gi 2250232533 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 2250232533  45 ITGGGSAKPGQWPWQVSITY-DGNHVCGGSLVSNKWVVSAAHCFPREHsREAYEVKLGAHQLDSYSNDTVVHTVAQIITH 123
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250232533 124 SSYREEGSQGDIALIRLSSPVTFSRYIRPICLPAANASFPNGLHCTVTGWGHVAPSVSLqtPRPLQQLEVPLISRETCSC 203
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250232533 204 LYNinavpeEPHTIQQDMLCAGYVKGGKDACQGDSGGPLSCPMEGIWYLAGIVSWGDACGAPNRPGVYTLTSTYASWIHH 283
Cdd:cd00190   158 AYS------YGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231

                  .
gi 2250232533 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 2250232533   44 RITGGGSAKPGQWPWQVSITY-DGNHVCGGSLVSNKWVVSAAHCFpREHSREAYEVKLGAHQLdSYSNDTVVHTVAQIIT 122
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDL-SSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250232533  123 HSSYREEGSQGDIALIRLSSPVTFSRYIRPICLPAANASFPNGLHCTVTGWGHVAPSvSLQTPRPLQQLEVPLISRETCS 202
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEG-AGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2250232533  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 2250232533  45 ITGGGSAKPGQWPWQVSITYDGN-HVCGGSLVSNKWVVSAAHCFpreHSREAYEVKLGAHQLDSYSNDTVVHTVAQIITH 123
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250232533 124 SSYREEGSQGDIALIRLSSPVTFSRYIRPICLPAANASFPNGLHCTVTGWGHVApsvSLQTPRPLQQLEVPLISRETCSC 203
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTK---TLGPSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2250232533 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 2250232533  39 AVIQPRITGGGSAKPGQWPWQVSITYDG---NHVCGGSLVSNKWVVSAAHCFPrEHSREAYEVKLGAHQLDSysNDTVVH 115
Cdd:COG5640    25 ADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVD-GDGPSDLRVVIGSTDLST--SGGTVV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250232533 116 TVAQIITHSSYREEGSQGDIALIRLSSPVTFSRYIRpicLPAANASFPNGLHCTVTGWGHVAPSVSlQTPRPLQQLEVPL 195
Cdd:COG5640   102 KVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLRKADVPV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250232533 196 ISRETCSCLYNINAvpeephtiqQDMLCAGYVKGGKDACQGDSGGPLSCPMEGIWYLAGIVSWGDACGAPNRPGVYTLTS 275
Cdd:COG5640   178 VSDATCAAYGGFDG---------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVS 248
                         250
                  ....*....|...
gi 2250232533 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 2250232533  56 WPWQVSITYDGNHVCGGSLVSNKWVVSAAHCFPREHSREAY-EVKLGAHQldsySNDTVVHTVAQIITHSSYrEEGSQGD 134
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYiSVVLGGAK----TLKSIEGPYEQIVRVDCR-HDIPESE 75
                          90       100
                  ....*....|....*....|..
gi 2250232533 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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