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Conserved domains on  [gi|7019563|ref|NP_037402|]
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probable threonine protease PRSS50 precursor [Homo sapiens]

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 ...
118-353 5.35e-65

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: 206.74  E-value: 5.35e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563  118 EAVARRWPWMVSVR-ANGTHICAGTIIASQWVLTVAHCLI-WRDVIYSVRVGSPWIDQMTQTASDVPVLQVIMHSRYRAQ 195
Cdd:cd00190   6 EAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYsSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563  196 RFWswvgqaNDIGLLKLKQELKYSNYVRPICLPGTDYVLKDHSRCTVTGWGLSKADGMWPQfrTIQEKEVIILNNKECDN 275
Cdd:cd00190  86 TYD------NDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7019563  276 FYHNFTkiptlvqIIKSQMMCAEDTHREK-FCYELTGEPLVCSMEGTWYLVGLVSWGAGCQKSEAPPIYLQVSSYQHWI 353
Cdd:cd00190 158 AYSYGG-------TITDNMLCAGGLEGGKdACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
118-353 5.35e-65

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: 206.74  E-value: 5.35e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563  118 EAVARRWPWMVSVR-ANGTHICAGTIIASQWVLTVAHCLI-WRDVIYSVRVGSPWIDQMTQTASDVPVLQVIMHSRYRAQ 195
Cdd:cd00190   6 EAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYsSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563  196 RFWswvgqaNDIGLLKLKQELKYSNYVRPICLPGTDYVLKDHSRCTVTGWGLSKADGMWPQfrTIQEKEVIILNNKECDN 275
Cdd:cd00190  86 TYD------NDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7019563  276 FYHNFTkiptlvqIIKSQMMCAEDTHREK-FCYELTGEPLVCSMEGTWYLVGLVSWGAGCQKSEAPPIYLQVSSYQHWI 353
Cdd:cd00190 158 AYSYGG-------TITDNMLCAGGLEGGKdACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
118-353 6.46e-60

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: 193.66  E-value: 6.46e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563     118 EAVARRWPWMVSVR-ANGTHICAGTIIASQWVLTVAHCLIWRDV-IYSVRVGSPWIDQmTQTASDVPVLQVIMHSRYRAQ 195
Cdd:smart00020   7 EANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPsNIRVRLGSHDLSS-GEEGQVIKVSKVIIHPNYNPS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563     196 RFWswvgqaNDIGLLKLKQELKYSNYVRPICLPGTDYVLKDHSRCTVTGWGLSKaDGMWPQFRTIQEKEVIILNNKECDN 275
Cdd:smart00020  86 TYD------NDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTS-EGAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7019563     276 FYHNFTkiptlvqIIKSQMMCAEDTHREKF-CYELTGEPLVCSmEGTWYLVGLVSWGAGCQKSEAPPIYLQVSSYQHWI 353
Cdd:smart00020 159 AYSGGG-------AITDNMLCAGGLEGGKDaCQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
118-353 1.48e-45

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 156.06  E-value: 1.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563    118 EAVARRWPWMVSV-RANGTHICAGTIIASQWVLTVAHCLIWRDViYSVRVGSPWIDQMTQTASDVPVLQVIMHSRYRAqr 196
Cdd:pfam00089   6 EAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVSGASD-VKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNP-- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563    197 fwswVGQANDIGLLKLKQELKYSNYVRPICLPGTDYVLKDHSRCTVTGWGLSKADGmwpQFRTIQEKEVIILNNKECDNF 276
Cdd:pfam00089  83 ----DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPVVSRETCRSA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7019563    277 YHNftkiptlvqIIKSQMMCAEDTHREKfCYELTGEPLVCSMEgtwYLVGLVSWGAGCQKSEAPPIYLQVSSYQHWI 353
Cdd:pfam00089 156 YGG---------TVTDTMICAGAGGKDA-CQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
118-353 7.26e-33

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 123.61  E-value: 7.26e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563  118 EAVARRWPWMVSV-RANGT--HICAGTIIASQWVLTVAHCLI-WRDVIYSVRVGSpwIDQMTQTASDVPVLQVIMHSRYR 193
Cdd:COG5640  36 PATVGEYPWMVALqSSNGPsgQFCGGTLIAPRWVLTAAHCVDgDGPSDLRVVIGS--TDLSTSGGTVVKVARIVVHPDYD 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563  194 AQRfwswvgQANDIGLLKLKQELkysNYVRPICLPGTDYVLKDHSRCTVTGWGLSKADGMwPQFRTIQEKEVIILNNKEC 273
Cdd:COG5640 114 PAT------PGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLRKADVPVVSDATC 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563  274 DNFyhnftkiptlVQIIKSQMMCAEDTHREK-FCYELTGEPLVCSMEGTWYLVGLVSWGAGCQKSEAPPIYLQVSSYQHW 352
Cdd:COG5640 184 AAY----------GGFDGGTMLCAGYPEGGKdACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                .
gi 7019563  353 I 353
Cdd:COG5640 254 I 254
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
118-353 5.35e-65

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: 206.74  E-value: 5.35e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563  118 EAVARRWPWMVSVR-ANGTHICAGTIIASQWVLTVAHCLI-WRDVIYSVRVGSPWIDQMTQTASDVPVLQVIMHSRYRAQ 195
Cdd:cd00190   6 EAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYsSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563  196 RFWswvgqaNDIGLLKLKQELKYSNYVRPICLPGTDYVLKDHSRCTVTGWGLSKADGMWPQfrTIQEKEVIILNNKECDN 275
Cdd:cd00190  86 TYD------NDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD--VLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7019563  276 FYHNFTkiptlvqIIKSQMMCAEDTHREK-FCYELTGEPLVCSMEGTWYLVGLVSWGAGCQKSEAPPIYLQVSSYQHWI 353
Cdd:cd00190 158 AYSYGG-------TITDNMLCAGGLEGGKdACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
118-353 6.46e-60

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: 193.66  E-value: 6.46e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563     118 EAVARRWPWMVSVR-ANGTHICAGTIIASQWVLTVAHCLIWRDV-IYSVRVGSPWIDQmTQTASDVPVLQVIMHSRYRAQ 195
Cdd:smart00020   7 EANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPsNIRVRLGSHDLSS-GEEGQVIKVSKVIIHPNYNPS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563     196 RFWswvgqaNDIGLLKLKQELKYSNYVRPICLPGTDYVLKDHSRCTVTGWGLSKaDGMWPQFRTIQEKEVIILNNKECDN 275
Cdd:smart00020  86 TYD------NDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTS-EGAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7019563     276 FYHNFTkiptlvqIIKSQMMCAEDTHREKF-CYELTGEPLVCSmEGTWYLVGLVSWGAGCQKSEAPPIYLQVSSYQHWI 353
Cdd:smart00020 159 AYSGGG-------AITDNMLCAGGLEGGKDaCQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
118-353 1.48e-45

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 156.06  E-value: 1.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563    118 EAVARRWPWMVSV-RANGTHICAGTIIASQWVLTVAHCLIWRDViYSVRVGSPWIDQMTQTASDVPVLQVIMHSRYRAqr 196
Cdd:pfam00089   6 EAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVSGASD-VKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNP-- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563    197 fwswVGQANDIGLLKLKQELKYSNYVRPICLPGTDYVLKDHSRCTVTGWGLSKADGmwpQFRTIQEKEVIILNNKECDNF 276
Cdd:pfam00089  83 ----DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPVVSRETCRSA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7019563    277 YHNftkiptlvqIIKSQMMCAEDTHREKfCYELTGEPLVCSMEgtwYLVGLVSWGAGCQKSEAPPIYLQVSSYQHWI 353
Cdd:pfam00089 156 YGG---------TVTDTMICAGAGGKDA-CQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
118-353 7.26e-33

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 123.61  E-value: 7.26e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563  118 EAVARRWPWMVSV-RANGT--HICAGTIIASQWVLTVAHCLI-WRDVIYSVRVGSpwIDQMTQTASDVPVLQVIMHSRYR 193
Cdd:COG5640  36 PATVGEYPWMVALqSSNGPsgQFCGGTLIAPRWVLTAAHCVDgDGPSDLRVVIGS--TDLSTSGGTVVKVARIVVHPDYD 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563  194 AQRfwswvgQANDIGLLKLKQELkysNYVRPICLPGTDYVLKDHSRCTVTGWGLSKADGMwPQFRTIQEKEVIILNNKEC 273
Cdd:COG5640 114 PAT------PGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPG-SQSGTLRKADVPVVSDATC 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563  274 DNFyhnftkiptlVQIIKSQMMCAEDTHREK-FCYELTGEPLVCSMEGTWYLVGLVSWGAGCQKSEAPPIYLQVSSYQHW 352
Cdd:COG5640 184 AAY----------GGFDGGTMLCAGYPEGGKdACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                .
gi 7019563  353 I 353
Cdd:COG5640 254 I 254
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
124-244 1.25e-06

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: 46.77  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019563    124 WPWMVSVRANGTHICAGTIIASQWVLTVAHCLIWRDVIY---SVRVGSpwidQMTQTASDVPVLQVimhsrYRAQRFwSW 200
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHqyiSVVLGG----AKTLKSIEGPYEQI-----VRVDCR-HD 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 7019563    201 VGQANdIGLLKLKQELKYSNYVRPICLPGTDYVLKDHSRCTVTG 244
Cdd:pfam09342  71 IPESE-ISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 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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