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Conserved domains on  [gi|111607469|ref|NP_001036175|]
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serine protease 57 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 ...
40-264 1.12e-77

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: 235.63  E-value: 1.12e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469  40 IVGGHEVTPHSRPYMASVSFE-GHHYCGGFLIHTHWVVSAAHCFSDRDPSMGLVVLGAHALLAPEPTQQTFSIAAAVSHP 118
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469 119 DFQPATQANDICLLRLNGSAVLGPAVRLLRLPRRNAKPPaAGTRCHVSGWGFVSDFEEPPPGLMEVEVRILDLSVCNSSW 198
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLP-AGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111607469 199 Q--GQLNPAMLCThSGDRRRRGFCSADSGGPLVCGRR----AHGLVSFsGLWCGDPKTPDVYTQVSAFVTWI 264
Cdd:cd00190  160 SygGTITDNMLCA-GGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSW-GSGCARPNYPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
40-264 1.12e-77

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: 235.63  E-value: 1.12e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469  40 IVGGHEVTPHSRPYMASVSFE-GHHYCGGFLIHTHWVVSAAHCFSDRDPSMGLVVLGAHALLAPEPTQQTFSIAAAVSHP 118
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469 119 DFQPATQANDICLLRLNGSAVLGPAVRLLRLPRRNAKPPaAGTRCHVSGWGFVSDFEEPPPGLMEVEVRILDLSVCNSSW 198
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLP-AGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111607469 199 Q--GQLNPAMLCThSGDRRRRGFCSADSGGPLVCGRR----AHGLVSFsGLWCGDPKTPDVYTQVSAFVTWI 264
Cdd:cd00190  160 SygGTITDNMLCA-GGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSW-GSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
40-264 1.32e-73

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: 224.86  E-value: 1.32e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469    40 IVGGHEVTPHSRPYMASVSFEG-HHYCGGFLIHTHWVVSAAHCFSDRDPSMGLVVLGAHALLAPEPtQQTFSIAAAVSHP 118
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469   119 DFQPATQANDICLLRLNGSAVLGPAVRLLRLPRRNAkPPAAGTRCHVSGWGFVSDFEEPPP-GLMEVEVRILDLSVCNSS 197
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNY-NVPAGTTCTVSGWGRTSEGAGSLPdTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111607469   198 WQGQ--LNPAMLCThSGDRRRRGFCSADSGGPLVCGRR---AHGLVSFsGLWCGDPKTPDVYTQVSAFVTWI 264
Cdd:smart00020 160 YSGGgaITDNMLCA-GGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSW-GSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
40-264 6.19e-64

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 199.98  E-value: 6.19e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469   40 IVGGHEVTPHSRPYMASVSFE-GHHYCGGFLIHTHWVVSAAHCFSDRdpSMGLVVLGAHALLAPEPTQQTFSIAAAVSHP 118
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469  119 DFQPATQANDICLLRLNGSAVLGPAVRLLRLPRRNAKPPaAGTRCHVSGWGFVSDFEEPPPgLMEVEVRILDLSVCNSSW 198
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLP-VGTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 111607469  199 QGQLNPAMLCTHSGDrrrRGFCSADSGGPLVC-GRRAHGLVSFsGLWCGDPKTPDVYTQVSAFVTWI 264
Cdd:pfam00089 157 GGTVTDTMICAGAGG---KDACQGDSGGPLVCsDGELIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
18-272 1.38e-48

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 162.13  E-value: 1.38e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469  18 LVLTTAAALTQLMWLPGCCGS----YIVGGHEVTPHSRPYMASVSFEG---HHYCGGFLIHTHWVVSAAHCFSDRDPSMG 90
Cdd:COG5640    5 RLLAALAAAALALALAAAPAAdaapAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469  91 LVVLGAHALLAPEPtqQTFSIAAAVSHPDFQPATQANDICLLRLNGSAVLGPAVRLLrlprRNAKPPAAGTRCHVSGWGF 170
Cdd:COG5640   85 RVVIGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAPLA----TSADAAAPGTPATVAGWGR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469 171 VSDFEEPPPG-LMEVEVRILDLSVCNsSWQGQLNPAMLCThSGDRRRRGFCSADSGGPLV----CGRRAHGLVSFSGLWC 245
Cdd:COG5640  159 TSEGPGSQSGtLRKADVPVVSDATCA-AYGGFDGGTMLCA-GYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPC 236
                        250       260
                 ....*....|....*....|....*..
gi 111607469 246 GdPKTPDVYTQVSAFVTWIWDVVRASS 272
Cdd:COG5640  237 A-AGYPGVYTRVSAYRDWIKSTAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
40-264 1.12e-77

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: 235.63  E-value: 1.12e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469  40 IVGGHEVTPHSRPYMASVSFE-GHHYCGGFLIHTHWVVSAAHCFSDRDPSMGLVVLGAHALLAPEPTQQTFSIAAAVSHP 118
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469 119 DFQPATQANDICLLRLNGSAVLGPAVRLLRLPRRNAKPPaAGTRCHVSGWGFVSDFEEPPPGLMEVEVRILDLSVCNSSW 198
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLP-AGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111607469 199 Q--GQLNPAMLCThSGDRRRRGFCSADSGGPLVCGRR----AHGLVSFsGLWCGDPKTPDVYTQVSAFVTWI 264
Cdd:cd00190  160 SygGTITDNMLCA-GGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSW-GSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
40-264 1.32e-73

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: 224.86  E-value: 1.32e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469    40 IVGGHEVTPHSRPYMASVSFEG-HHYCGGFLIHTHWVVSAAHCFSDRDPSMGLVVLGAHALLAPEPtQQTFSIAAAVSHP 118
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469   119 DFQPATQANDICLLRLNGSAVLGPAVRLLRLPRRNAkPPAAGTRCHVSGWGFVSDFEEPPP-GLMEVEVRILDLSVCNSS 197
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNY-NVPAGTTCTVSGWGRTSEGAGSLPdTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111607469   198 WQGQ--LNPAMLCThSGDRRRRGFCSADSGGPLVCGRR---AHGLVSFsGLWCGDPKTPDVYTQVSAFVTWI 264
Cdd:smart00020 160 YSGGgaITDNMLCA-GGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSW-GSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
40-264 6.19e-64

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 199.98  E-value: 6.19e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469   40 IVGGHEVTPHSRPYMASVSFE-GHHYCGGFLIHTHWVVSAAHCFSDRdpSMGLVVLGAHALLAPEPTQQTFSIAAAVSHP 118
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469  119 DFQPATQANDICLLRLNGSAVLGPAVRLLRLPRRNAKPPaAGTRCHVSGWGFVSDFEEPPPgLMEVEVRILDLSVCNSSW 198
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLP-VGTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 111607469  199 QGQLNPAMLCTHSGDrrrRGFCSADSGGPLVC-GRRAHGLVSFsGLWCGDPKTPDVYTQVSAFVTWI 264
Cdd:pfam00089 157 GGTVTDTMICAGAGG---KDACQGDSGGPLVCsDGELIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
18-272 1.38e-48

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 162.13  E-value: 1.38e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469  18 LVLTTAAALTQLMWLPGCCGS----YIVGGHEVTPHSRPYMASVSFEG---HHYCGGFLIHTHWVVSAAHCFSDRDPSMG 90
Cdd:COG5640    5 RLLAALAAAALALALAAAPAAdaapAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469  91 LVVLGAHALLAPEPtqQTFSIAAAVSHPDFQPATQANDICLLRLNGSAVLGPAVRLLrlprRNAKPPAAGTRCHVSGWGF 170
Cdd:COG5640   85 RVVIGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAPLA----TSADAAAPGTPATVAGWGR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469 171 VSDFEEPPPG-LMEVEVRILDLSVCNsSWQGQLNPAMLCThSGDRRRRGFCSADSGGPLV----CGRRAHGLVSFSGLWC 245
Cdd:COG5640  159 TSEGPGSQSGtLRKADVPVVSDATCA-AYGGFDGGTMLCA-GYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPC 236
                        250       260
                 ....*....|....*....|....*..
gi 111607469 246 GdPKTPDVYTQVSAFVTWIWDVVRASS 272
Cdd:COG5640  237 A-AGYPGVYTRVSAYRDWIKSTAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
61-169 6.53e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 40.04  E-value: 6.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111607469  61 GHHYCGGFLIHTHWVVSAAHCFSDRD----PSMGLVVLGAHAllapePTQQTFSIAAAVSHPDFQPATQAN-DICLLRLN 135
Cdd:COG3591   10 GGGVCTGTLIGPNLVLTAGHCVYDGAgggwATNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGDAGyDYALLRLD 84
                         90       100       110
                 ....*....|....*....|....*....|....
gi 111607469 136 GSavLGPAVRLLRLprRNAKPPAAGTRCHVSGWG 169
Cdd:COG3591   85 EP--LGDTTGWLGL--AFNDAPLAGEPVTIIGYP 114
 
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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