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Conserved domains on  [gi|748982954|ref|NP_001291304|]
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serine protease 38 precursor [Rattus norvegicus]

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 ...
58-285 9.08e-84

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: 252.58  E-value: 9.08e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954  58 GGELTIDRKWPWQVSIHY-AGFHVCGGSILNAYWVLTAAHCFaREKRLQTFDMYVGITNLEVANKHTQWFEINQVIIHPT 136
Cdd:cd00190    3 GGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954 137 FEMFhPVGGDVALVQSKSAIVFSDYVLPICLPSSNLNLSD-LSCWTTGWGMVSPQGETGKDLLEAQLPLIPKFQCQLLYG 215
Cdd:cd00190   82 YNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAgTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954 216 LTSYLLPEMLCAGDIKNMKNVCEGDSGSPLVCKVNQTWLQIGIVSWGRGCAQPLYPGVFANVSYFLNWIR 285
Cdd:cd00190  161 YGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
58-285 9.08e-84

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: 252.58  E-value: 9.08e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954  58 GGELTIDRKWPWQVSIHY-AGFHVCGGSILNAYWVLTAAHCFaREKRLQTFDMYVGITNLEVANKHTQWFEINQVIIHPT 136
Cdd:cd00190    3 GGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954 137 FEMFhPVGGDVALVQSKSAIVFSDYVLPICLPSSNLNLSD-LSCWTTGWGMVSPQGETGKDLLEAQLPLIPKFQCQLLYG 215
Cdd:cd00190   82 YNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAgTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954 216 LTSYLLPEMLCAGDIKNMKNVCEGDSGSPLVCKVNQTWLQIGIVSWGRGCAQPLYPGVFANVSYFLNWIR 285
Cdd:cd00190  161 YGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
58-284 7.62e-77

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: 234.88  E-value: 7.62e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954    58 GGELTIDRKWPWQVSIHYAGF-HVCGGSILNAYWVLTAAHCFaREKRLQTFDMYVGITNLEVANkHTQWFEINQVIIHPT 136
Cdd:smart00020   4 GGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSGE-EGQVIKVSKVIIHPN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954   137 FEMfHPVGGDVALVQSKSAIVFSDYVLPICLPSSNLNLSDLS-CWTTGWGMVSP-QGETGKDLLEAQLPLIPKFQCQLLY 214
Cdd:smart00020  82 YNP-STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTtCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954   215 GLTSYLLPEMLCAGDIKNMKNVCEGDSGSPLVCKVNqTWLQIGIVSWGRGCAQPLYPGVFANVSYFLNWI 284
Cdd:smart00020 161 SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG-RWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
58-284 3.91e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 189.19  E-value: 3.91e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954   58 GGELTIDRKWPWQVSIHY-AGFHVCGGSILNAYWVLTAAHCFAREKRLQtfdMYVGITNLEVANKHTQWFEINQVIIHPT 136
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVK---VVLGAHNIVLREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954  137 FEMFHpVGGDVALVQSKSAIVFSDYVLPICLPSSNLNLSD-LSCWTTGWGMVSPQGETGKdLLEAQLPLIPKFQCQLLYG 215
Cdd:pfam00089  80 YNPDT-LDNDIALLKLESPVTLGDTVRPICLPDASSDLPVgTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCRSAYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 748982954  216 ltSYLLPEMLCAGDIKnmKNVCEGDSGSPLVCKVNQtwlQIGIVSWGRGCAQPLYPGVFANVSYFLNWI 284
Cdd:pfam00089 158 --GTVTDTMICAGAGG--KDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
45-285 2.86e-50

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 167.52  E-value: 2.86e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954  45 VACGQPALHGKLLGGELTIDRKWPWQVSIHYAG---FHVCGGSILNAYWVLTAAHCFArEKRLQTFDMYVGITNLevANK 121
Cdd:COG5640   20 AAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVD-GDGPSDLRVVIGSTDL--STS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954 122 HTQWFEINQVIIHPTFEMFHPvGGDVALVQSKSAIvfsDYVLPICLPSSNLNLS-DLSCWTTGWGMVSP-QGETGKDLLE 199
Cdd:COG5640   97 GGTVVKVARIVVHPDYDPATP-GNDIALLKLATPV---PGVAPAPLATSADAAApGTPATVAGWGRTSEgPGSQSGTLRK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954 200 AQLPLIPKFQCQllyGLTSYLLPEMLCAGDIKNMKNVCEGDSGSPLVCKVNQTWLQIGIVSWGRGCAQPLYPGVFANVSY 279
Cdd:COG5640  173 ADVPVVSDATCA---AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSA 249

                 ....*.
gi 748982954 280 FLNWIR 285
Cdd:COG5640  250 YRDWIK 255
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
58-285 9.08e-84

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: 252.58  E-value: 9.08e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954  58 GGELTIDRKWPWQVSIHY-AGFHVCGGSILNAYWVLTAAHCFaREKRLQTFDMYVGITNLEVANKHTQWFEINQVIIHPT 136
Cdd:cd00190    3 GGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954 137 FEMFhPVGGDVALVQSKSAIVFSDYVLPICLPSSNLNLSD-LSCWTTGWGMVSPQGETGKDLLEAQLPLIPKFQCQLLYG 215
Cdd:cd00190   82 YNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAgTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954 216 LTSYLLPEMLCAGDIKNMKNVCEGDSGSPLVCKVNQTWLQIGIVSWGRGCAQPLYPGVFANVSYFLNWIR 285
Cdd:cd00190  161 YGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
58-284 7.62e-77

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: 234.88  E-value: 7.62e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954    58 GGELTIDRKWPWQVSIHYAGF-HVCGGSILNAYWVLTAAHCFaREKRLQTFDMYVGITNLEVANkHTQWFEINQVIIHPT 136
Cdd:smart00020   4 GGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSGE-EGQVIKVSKVIIHPN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954   137 FEMfHPVGGDVALVQSKSAIVFSDYVLPICLPSSNLNLSDLS-CWTTGWGMVSP-QGETGKDLLEAQLPLIPKFQCQLLY 214
Cdd:smart00020  82 YNP-STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTtCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954   215 GLTSYLLPEMLCAGDIKNMKNVCEGDSGSPLVCKVNqTWLQIGIVSWGRGCAQPLYPGVFANVSYFLNWI 284
Cdd:smart00020 161 SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG-RWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
58-284 3.91e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 189.19  E-value: 3.91e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954   58 GGELTIDRKWPWQVSIHY-AGFHVCGGSILNAYWVLTAAHCFAREKRLQtfdMYVGITNLEVANKHTQWFEINQVIIHPT 136
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVK---VVLGAHNIVLREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954  137 FEMFHpVGGDVALVQSKSAIVFSDYVLPICLPSSNLNLSD-LSCWTTGWGMVSPQGETGKdLLEAQLPLIPKFQCQLLYG 215
Cdd:pfam00089  80 YNPDT-LDNDIALLKLESPVTLGDTVRPICLPDASSDLPVgTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCRSAYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 748982954  216 ltSYLLPEMLCAGDIKnmKNVCEGDSGSPLVCKVNQtwlQIGIVSWGRGCAQPLYPGVFANVSYFLNWI 284
Cdd:pfam00089 158 --GTVTDTMICAGAGG--KDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
45-285 2.86e-50

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 167.52  E-value: 2.86e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954  45 VACGQPALHGKLLGGELTIDRKWPWQVSIHYAG---FHVCGGSILNAYWVLTAAHCFArEKRLQTFDMYVGITNLevANK 121
Cdd:COG5640   20 AAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVD-GDGPSDLRVVIGSTDL--STS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954 122 HTQWFEINQVIIHPTFEMFHPvGGDVALVQSKSAIvfsDYVLPICLPSSNLNLS-DLSCWTTGWGMVSP-QGETGKDLLE 199
Cdd:COG5640   97 GGTVVKVARIVVHPDYDPATP-GNDIALLKLATPV---PGVAPAPLATSADAAApGTPATVAGWGRTSEgPGSQSGTLRK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954 200 AQLPLIPKFQCQllyGLTSYLLPEMLCAGDIKNMKNVCEGDSGSPLVCKVNQTWLQIGIVSWGRGCAQPLYPGVFANVSY 279
Cdd:COG5640  173 ADVPVVSDATCA---AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSA 249

                 ....*.
gi 748982954 280 FLNWIR 285
Cdd:COG5640  250 YRDWIK 255
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
75-282 1.60e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 45.05  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954  75 YAGFHVCGGSILNAYWVLTAAHCFAREKRLQTFdmyvgiTNLEVA----NKHTQWFEINQVIIHPTFEMFHPVGGDVALV 150
Cdd:COG3591    8 DGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWA------TNIVFVpgynGGPYGTATATRFRVPPGWVASGDAGYDYALL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954 151 QSKSAIvfSDYVLPICLPSSNLNLSDLSCWTTGWgmvsPQGETGKDLLEAQlplipkfqCQLLYGLTSYLLpeMLCagdi 230
Cdd:COG3591   82 RLDEPL--GDTTGWLGLAFNDAPLAGEPVTIIGY----PGDRPKDLSLDCS--------GRVTGVQGNRLS--YDC---- 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 748982954 231 knmkNVCEGDSGSPLVCKVNQTWLQIGIVSWG----RGCAQPLYPGVFANVSYFLN 282
Cdd:COG3591  142 ----DTTGGSSGSPVLDDSDGGGRVVGVHSAGgadrANTGVRLTSAIVAALRAWAS 193
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
67-183 1.85e-04

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: 40.61  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748982954   67 WPWQVSIHYAGFHVCGGSILNAYWVLTAAHCFaREKRLQTFDMYV----GITNLEVANKHTQWFEInqviihptfEMFHP 142
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCL-RDTNLRHQYISVvlggAKTLKSIEGPYEQIVRV---------DCRHD 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 748982954  143 V-GGDVALVQSKSAIVFSDYVLPICLP-SSNLNLSDLSCWTTG 183
Cdd:pfam09342  71 IpESEISLLHLASPASFSNHVLPTFVPeTRNENEKDNECLAVG 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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