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Conserved domains on  [gi|28202035|ref|NP_780649|]
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serine protease 27 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 ...
39-278 4.17e-102

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: 299.19  E-value: 4.17e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035  39 VGGENALEGEWPWQVSIQRN-GIHFCGGSLIAPTWVLTAAHCFSNtSDISIYQVLLGALKLQQPGPHALYVPVKQVKSNP 117
Cdd:cd00190   2 VGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035 118 QYQGMASSADVALVELQGPVTFTNYILPVCLPDPSVIFESGMNCWVTGWGSpsEQDRLPNPRVLQKLAVPIIDTPKCNLL 197
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGR--TSEGGPLPDVLQEVNVPIVSNAECKRA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035 198 YNKDVesdfqlkTIKDDMLCAGFAEGKKDACKGDSGGPLVCLVDQSWVQAGVISWGEGCARRNRPGVYIRVTSHHKWIHQ 277
Cdd:cd00190 159 YSYGG-------TITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231

                .
gi 28202035 278 I 278
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 ...
39-278 4.17e-102

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: 299.19  E-value: 4.17e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035  39 VGGENALEGEWPWQVSIQRN-GIHFCGGSLIAPTWVLTAAHCFSNtSDISIYQVLLGALKLQQPGPHALYVPVKQVKSNP 117
Cdd:cd00190   2 VGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035 118 QYQGMASSADVALVELQGPVTFTNYILPVCLPDPSVIFESGMNCWVTGWGSpsEQDRLPNPRVLQKLAVPIIDTPKCNLL 197
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGR--TSEGGPLPDVLQEVNVPIVSNAECKRA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035 198 YNKDVesdfqlkTIKDDMLCAGFAEGKKDACKGDSGGPLVCLVDQSWVQAGVISWGEGCARRNRPGVYIRVTSHHKWIHQ 277
Cdd:cd00190 159 YSYGG-------TITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231

                .
gi 28202035 278 I 278
Cdd:cd00190 232 T 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
37-275 9.05e-95

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: 280.72  E-value: 9.05e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035     37 RMVGGENALEGEWPWQVSIQRNGI-HFCGGSLIAPTWVLTAAHCFSNtSDISIYQVLLGALKLQQPGpHALYVPVKQVKS 115
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSSGE-EGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035    116 NPQYQGMASSADVALVELQGPVTFTNYILPVCLPDPSVIFESGMNCWVTGWGSPSEqDRLPNPRVLQKLAVPIIDTPKCN 195
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSE-GAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035    196 LLYnkdvesdFQLKTIKDDMLCAGFAEGKKDACKGDSGGPLVCLvDQSWVQAGVISWGEGCARRNRPGVYIRVTSHHKWI 275
Cdd:smart00020 158 RAY-------SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
39-275 7.53e-74

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 226.94  E-value: 7.53e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035    39 VGGENALEGEWPWQVSIQ-RNGIHFCGGSLIAPTWVLTAAHCFSNTSDisiYQVLLGALKLQQPGPHALYVPVKQVKSNP 117
Cdd:pfam00089   2 VGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035   118 QYQGMASSADVALVELQGPVTFTNYILPVCLPDPSVIFESGMNCWVTGWGSPSEQDRlpnPRVLQKLAVPIIDTPKCNLL 197
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRETCRSA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28202035   198 YNkdvesdfqlKTIKDDMLCAGFaeGKKDACKGDSGGPLVCLVDQswvQAGVISWGEGCARRNRPGVYIRVTSHHKWI 275
Cdd:pfam00089 156 YG---------GTVTDTMICAGA--GGKDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
37-282 7.70e-71

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 220.68  E-value: 7.70e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035  37 RMVGGENALEGEWPWQVSIQRNGI---HFCGGSLIAPTWVLTAAHCFSNTSDISIyQVLLGALKLQQPGPHAlyVPVKQV 113
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGSTDLSTSGGTV--VKVARI 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035 114 KSNPQYQGMASSADVALVELQGPVTFTNyilPVCLPDPSVIFESGMNCWVTGWGSPSEQDRLPnPRVLQKLAVPIIDTPK 193
Cdd:COG5640 107 VVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPGSQ-SGTLRKADVPVVSDAT 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035 194 CNLLYNkdvesdfqlkTIKDDMLCAGFAEGKKDACKGDSGGPLVCLVDQSWVQAGVISWGEGCARRNRPGVYIRVTSHHK 273
Cdd:COG5640 183 CAAYGG----------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252

                ....*....
gi 28202035 274 WIHQIIPEL 282
Cdd:COG5640 253 WIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
39-278 4.17e-102

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: 299.19  E-value: 4.17e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035  39 VGGENALEGEWPWQVSIQRN-GIHFCGGSLIAPTWVLTAAHCFSNtSDISIYQVLLGALKLQQPGPHALYVPVKQVKSNP 117
Cdd:cd00190   2 VGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035 118 QYQGMASSADVALVELQGPVTFTNYILPVCLPDPSVIFESGMNCWVTGWGSpsEQDRLPNPRVLQKLAVPIIDTPKCNLL 197
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGR--TSEGGPLPDVLQEVNVPIVSNAECKRA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035 198 YNKDVesdfqlkTIKDDMLCAGFAEGKKDACKGDSGGPLVCLVDQSWVQAGVISWGEGCARRNRPGVYIRVTSHHKWIHQ 277
Cdd:cd00190 159 YSYGG-------TITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231

                .
gi 28202035 278 I 278
Cdd:cd00190 232 T 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
37-275 9.05e-95

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: 280.72  E-value: 9.05e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035     37 RMVGGENALEGEWPWQVSIQRNGI-HFCGGSLIAPTWVLTAAHCFSNtSDISIYQVLLGALKLQQPGpHALYVPVKQVKS 115
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSSGE-EGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035    116 NPQYQGMASSADVALVELQGPVTFTNYILPVCLPDPSVIFESGMNCWVTGWGSPSEqDRLPNPRVLQKLAVPIIDTPKCN 195
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSE-GAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035    196 LLYnkdvesdFQLKTIKDDMLCAGFAEGKKDACKGDSGGPLVCLvDQSWVQAGVISWGEGCARRNRPGVYIRVTSHHKWI 275
Cdd:smart00020 158 RAY-------SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
39-275 7.53e-74

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 226.94  E-value: 7.53e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035    39 VGGENALEGEWPWQVSIQ-RNGIHFCGGSLIAPTWVLTAAHCFSNTSDisiYQVLLGALKLQQPGPHALYVPVKQVKSNP 117
Cdd:pfam00089   2 VGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035   118 QYQGMASSADVALVELQGPVTFTNYILPVCLPDPSVIFESGMNCWVTGWGSPSEQDRlpnPRVLQKLAVPIIDTPKCNLL 197
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRETCRSA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28202035   198 YNkdvesdfqlKTIKDDMLCAGFaeGKKDACKGDSGGPLVCLVDQswvQAGVISWGEGCARRNRPGVYIRVTSHHKWI 275
Cdd:pfam00089 156 YG---------GTVTDTMICAGA--GGKDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
37-282 7.70e-71

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 220.68  E-value: 7.70e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035  37 RMVGGENALEGEWPWQVSIQRNGI---HFCGGSLIAPTWVLTAAHCFSNTSDISIyQVLLGALKLQQPGPHAlyVPVKQV 113
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGSTDLSTSGGTV--VKVARI 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035 114 KSNPQYQGMASSADVALVELQGPVTFTNyilPVCLPDPSVIFESGMNCWVTGWGSPSEQDRLPnPRVLQKLAVPIIDTPK 193
Cdd:COG5640 107 VVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPGSQ-SGTLRKADVPVVSDAT 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035 194 CNLLYNkdvesdfqlkTIKDDMLCAGFAEGKKDACKGDSGGPLVCLVDQSWVQAGVISWGEGCARRNRPGVYIRVTSHHK 273
Cdd:COG5640 183 CAAYGG----------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252

                ....*....
gi 28202035 274 WIHQIIPEL 282
Cdd:COG5640 253 WIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
58-266 7.26e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 60.46  E-value: 7.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035  58 NGIHFCGGSLIAPTWVLTAAHCFSNTSDISIYQ---VLLGalklQQPGPHAlYVPVKQVKSNPQY-QGMASSADVALVEL 133
Cdd:COG3591   9 GGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATnivFVPG----YNGGPYG-TATATRFRVPPGWvASGDAGYDYALLRL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035 134 QGPVTFTNYILPVCLPDPSVifeSGMNCWVTGWGspseQDRLPNPRVlqklavpiidTPKCNLLynkDVESDFQLktikd 213
Cdd:COG3591  84 DEPLGDTTGWLGLAFNDAPL---AGEPVTIIGYP----GDRPKDLSL----------DCSGRVT---GVQGNRLS----- 138
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 28202035 214 dMLCagfaegkkDACKGDSGGPLVCLVDQSWVQAGVISWGeGCARRNRpGVYI 266
Cdd:COG3591 139 -YDC--------DTTGGSSGSPVLDDSDGGGRVVGVHSAG-GADRANT-GVRL 180
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
49-165 4.39e-10

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: 56.40  E-value: 4.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28202035    49 WPWQVSIQRNGIHFCGGSLIAPTWVLTAAHCFSNTSDISIY-QVLLGALK--LQQPGPHALYVPVKQVKSNPQyqgmass 125
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYiSVVLGGAKtlKSIEGPYEQIVRVDCRHDIPE------- 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 28202035   126 ADVALVELQGPVTFTNYILPVCLPDPSVIFESGMNCWVTG 165
Cdd:pfam09342  74 SEISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 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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