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Conserved domains on  [gi|16716569|ref|NP_444473|]
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protease, serine, 1 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 ...
24-242 4.18e-110

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: 316.14  E-value: 4.18e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569  24 IVGGYTCRENSVPYQVSL--NSGYHFCGGSLINDQWVVSAAHC----YKTRIQVRLGEHNINVLEGNEQFIDAAKIIKHP 97
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569  98 NFNRKTLNNDIMLIKLSSPVTLNARVATVALPSS--CAPAGTQCLISGWGNTlSFGVSEPDLLQCLDAPLLPQADCEASY 175
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16716569 176 --PGKITGNMVCAGFLEGGKDSCQGDSGGPVVCN----GELQGIVSWGYGCALPDNPGVYTKVCNYVDWIQDT 242
Cdd:cd00190 160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
24-242 4.18e-110

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: 316.14  E-value: 4.18e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569  24 IVGGYTCRENSVPYQVSL--NSGYHFCGGSLINDQWVVSAAHC----YKTRIQVRLGEHNINVLEGNEQFIDAAKIIKHP 97
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569  98 NFNRKTLNNDIMLIKLSSPVTLNARVATVALPSS--CAPAGTQCLISGWGNTlSFGVSEPDLLQCLDAPLLPQADCEASY 175
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16716569 176 --PGKITGNMVCAGFLEGGKDSCQGDSGGPVVCN----GELQGIVSWGYGCALPDNPGVYTKVCNYVDWIQDT 242
Cdd:cd00190 160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
23-239 1.21e-108

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: 312.30  E-value: 1.21e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569     23 KIVGGYTCRENSVPYQVSL--NSGYHFCGGSLINDQWVVSAAHC----YKTRIQVRLGEHNINVlEGNEQFIDAAKIIKH 96
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqyGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSS-GEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569     97 PNFNRKTLNNDIMLIKLSSPVTLNARVATVALPSS--CAPAGTQCLISGWGNTLSFGVSEPDLLQCLDAPLLPQADCEAS 174
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569    175 YPG--KITGNMVCAGFLEGGKDSCQGDSGGPVVCN---GELQGIVSWGYGCALPDNPGVYTKVCNYVDWI 239
Cdd:smart00020 160 YSGggAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
24-239 1.09e-94

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 276.63  E-value: 1.09e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569    24 IVGGYTCRENSVPYQVSLN--SGYHFCGGSLINDQWVVSAAHCYK--TRIQVRLGEHNINVLEGNEQFIDAAKIIKHPNF 99
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlsSGKHFCGGSLISENWVLTAAHCVSgaSDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569   100 NRKTLNNDIMLIKLSSPVTLNARVATVALPSSCA--PAGTQCLISGWGNTLSFGVsePDLLQCLDAPLLPQADCEASYPG 177
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGNTKTLGP--SDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16716569   178 KITGNMVCAGFleGGKDSCQGDSGGPVVC-NGELQGIVSWGYGCALPDNPGVYTKVCNYVDWI 239
Cdd:pfam00089 159 TVTDTMICAGA--GGKDACQGDSGGPLVCsDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-246 4.81e-73

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 223.37  E-value: 4.81e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569   1 MSALLFLALVGAAVAFPVDDDDKIVGGYTCRENSVPYQVSLNS----GYHFCGGSLINDQWVVSAAHCY----KTRIQVR 72
Cdd:COG5640   8 AALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSsngpSGQFCGGTLIAPRWVLTAAHCVdgdgPSDLRVV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569  73 LGEHNINVLEGneQFIDAAKIIKHPNFNRKTLNNDIMLIKLSSPVTlNARVATVALPSSCAPAGTQCLISGWGNTLSFGV 152
Cdd:COG5640  88 IGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPVP-GVAPAPLATSADAAAPGTPATVAGWGRTSEGPG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569 153 SEPDLLQCLDAPLLPQADCeASYPGKITGNMVCAGFLEGGKDSCQGDSGGPVV----CNGELQGIVSWGYGCALPDNPGV 228
Cdd:COG5640 165 SQSGTLRKADVPVVSDATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGV 243
                       250
                ....*....|....*...
gi 16716569 229 YTKVCNYVDWIQDTIAAN 246
Cdd:COG5640 244 YTRVSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
24-242 4.18e-110

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: 316.14  E-value: 4.18e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569  24 IVGGYTCRENSVPYQVSL--NSGYHFCGGSLINDQWVVSAAHC----YKTRIQVRLGEHNINVLEGNEQFIDAAKIIKHP 97
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569  98 NFNRKTLNNDIMLIKLSSPVTLNARVATVALPSS--CAPAGTQCLISGWGNTlSFGVSEPDLLQCLDAPLLPQADCEASY 175
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16716569 176 --PGKITGNMVCAGFLEGGKDSCQGDSGGPVVCN----GELQGIVSWGYGCALPDNPGVYTKVCNYVDWIQDT 242
Cdd:cd00190 160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
23-239 1.21e-108

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: 312.30  E-value: 1.21e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569     23 KIVGGYTCRENSVPYQVSL--NSGYHFCGGSLINDQWVVSAAHC----YKTRIQVRLGEHNINVlEGNEQFIDAAKIIKH 96
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqyGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSS-GEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569     97 PNFNRKTLNNDIMLIKLSSPVTLNARVATVALPSS--CAPAGTQCLISGWGNTLSFGVSEPDLLQCLDAPLLPQADCEAS 174
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569    175 YPG--KITGNMVCAGFLEGGKDSCQGDSGGPVVCN---GELQGIVSWGYGCALPDNPGVYTKVCNYVDWI 239
Cdd:smart00020 160 YSGggAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
24-239 1.09e-94

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 276.63  E-value: 1.09e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569    24 IVGGYTCRENSVPYQVSLN--SGYHFCGGSLINDQWVVSAAHCYK--TRIQVRLGEHNINVLEGNEQFIDAAKIIKHPNF 99
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlsSGKHFCGGSLISENWVLTAAHCVSgaSDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569   100 NRKTLNNDIMLIKLSSPVTLNARVATVALPSSCA--PAGTQCLISGWGNTLSFGVsePDLLQCLDAPLLPQADCEASYPG 177
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGNTKTLGP--SDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16716569   178 KITGNMVCAGFleGGKDSCQGDSGGPVVC-NGELQGIVSWGYGCALPDNPGVYTKVCNYVDWI 239
Cdd:pfam00089 159 TVTDTMICAGA--GGKDACQGDSGGPLVCsDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-246 4.81e-73

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 223.37  E-value: 4.81e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569   1 MSALLFLALVGAAVAFPVDDDDKIVGGYTCRENSVPYQVSLNS----GYHFCGGSLINDQWVVSAAHCY----KTRIQVR 72
Cdd:COG5640   8 AALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSsngpSGQFCGGTLIAPRWVLTAAHCVdgdgPSDLRVV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569  73 LGEHNINVLEGneQFIDAAKIIKHPNFNRKTLNNDIMLIKLSSPVTlNARVATVALPSSCAPAGTQCLISGWGNTLSFGV 152
Cdd:COG5640  88 IGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPVP-GVAPAPLATSADAAAPGTPATVAGWGRTSEGPG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569 153 SEPDLLQCLDAPLLPQADCeASYPGKITGNMVCAGFLEGGKDSCQGDSGGPVV----CNGELQGIVSWGYGCALPDNPGV 228
Cdd:COG5640 165 SQSGTLRKADVPVVSDATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGV 243
                       250
                ....*....|....*...
gi 16716569 229 YTKVCNYVDWIQDTIAAN 246
Cdd:COG5640 244 YTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
38-229 1.75e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 50.06  E-value: 1.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569  38 QVSLNSGYHFCGGSLINDQWVVSAAHC--------YKTRIQVRLGEHNinvleGNEQFIDAAKIIKHPNFNRKTL-NNDI 108
Cdd:COG3591   4 RLETDGGGGVCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGDaGYDY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16716569 109 MLIKLSSPVTLNARVATVALPSScAPAGTQCLISGWGNtlsfgvsepdllqclDAPLLPQADCEasypGKITGnmVCAGF 188
Cdd:COG3591  79 ALLRLDEPLGDTTGWLGLAFNDA-PLAGEPVTIIGYPG---------------DRPKDLSLDCS----GRVTG--VQGNR 136
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 16716569 189 LEGGKDSCQGDSGGPVV----CNGELQGIVSWGYgcALPDNPGVY 229
Cdd:COG3591 137 LSYDCDTTGGSSGSPVLddsdGGGRVVGVHSAGG--ADRANTGVR 179
 
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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