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Conserved domains on  [gi|2041616042|emb|CAF3514728|]
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unnamed protein product [Didymodactylos carnosus]

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 ...
133-378 3.17e-46

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: 157.82  E-value: 3.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 133 NTVRRGEMPWLVRLESRTNLQSlylsmCGGTIIHPQWILTAAHCLLDSNtetlyaADGVSVYVGHSSRRQIGDDTVRVNP 212
Cdd:cd00190     5 SEAKIGSFPWQVSLQYTGGRHF-----CGGSLISPRWVLTAAHCVYSSA------PSNYTVRLGSHDLSSNEGGGQVIKV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 213 AMYILHPKFRIGRYSapvHDLALIKLATPLKLNKNTDIICLPEKTDDLTDGTLAHTAGWGRSSDNSPVVDEARRARIRI- 291
Cdd:cd00190    74 KKVIVHPNYNPSTYD---NDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIv 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 292 SPDACRKLPMNRTI----HIC-GRNEKGNNICSGDSGSGLYVRagiingtsTTWKWHVFGVASFGrEECQvSVNHDNAFS 366
Cdd:cd00190   151 SNAECKRAYSYGGTitdnMLCaGGLEGGKDACQGDSGGPLVCN--------DNGRGVLVGIVSWG-SGCA-RPNYPGVYT 220
                         250
                  ....*....|..
gi 2041616042 367 SVAADIDWIKSV 378
Cdd:cd00190   221 RVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
133-378 3.17e-46

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: 157.82  E-value: 3.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 133 NTVRRGEMPWLVRLESRTNLQSlylsmCGGTIIHPQWILTAAHCLLDSNtetlyaADGVSVYVGHSSRRQIGDDTVRVNP 212
Cdd:cd00190     5 SEAKIGSFPWQVSLQYTGGRHF-----CGGSLISPRWVLTAAHCVYSSA------PSNYTVRLGSHDLSSNEGGGQVIKV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 213 AMYILHPKFRIGRYSapvHDLALIKLATPLKLNKNTDIICLPEKTDDLTDGTLAHTAGWGRSSDNSPVVDEARRARIRI- 291
Cdd:cd00190    74 KKVIVHPNYNPSTYD---NDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIv 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 292 SPDACRKLPMNRTI----HIC-GRNEKGNNICSGDSGSGLYVRagiingtsTTWKWHVFGVASFGrEECQvSVNHDNAFS 366
Cdd:cd00190   151 SNAECKRAYSYGGTitdnMLCaGGLEGGKDACQGDSGGPLVCN--------DNGRGVLVGIVSWG-SGCA-RPNYPGVYT 220
                         250
                  ....*....|..
gi 2041616042 367 SVAADIDWIKSV 378
Cdd:cd00190   221 RVSSYLDWIQKT 232
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
134-381 1.55e-44

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 154.42  E-value: 1.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 134 TVRRGEMPWLVRLESRTNLQSLYlsmCGGTIIHPQWILTAAHCLLDSntetlyAADGVSVYVGhsSRRQIGDDTVRVNPA 213
Cdd:COG5640    36 PATVGEYPWMVALQSSNGPSGQF---CGGTLIAPRWVLTAAHCVDGD------GPSDLRVVIG--STDLSTSGGTVVKVA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 214 MYILHPKFrigRYSAPVHDLALIKLATPLKLNKntdIICLPEKTDDLTDGTLAHTAGWGRSSDNSPVV-DEARRARIRIS 292
Cdd:COG5640   105 RIVVHPDY---DPATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPGSQsGTLRKADVPVV 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 293 PDA-CRKLPMNRT-IHIC-GRNEKGNNICSGDSGSGLYVRAGiingtsttWKWHVFGVASFGREECqvSVNHDNAFSSVA 369
Cdd:COG5640   179 SDAtCAAYGGFDGgTMLCaGYPEGGKDACQGDSGGPLVVKDG--------GGWVLVGVVSWGGGPC--AAGYPGVYTRVS 248
                         250
                  ....*....|..
gi 2041616042 370 ADIDWIKSVIRT 381
Cdd:COG5640   249 AYRDWIKSTAGG 260
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
135-375 8.88e-44

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: 151.68  E-value: 8.88e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042  135 VRRGEMPWLVRLESRTNLQSlylsmCGGTIIHPQWILTAAHCLLDSNtetlyaADGVSVYVGhSSRRQIGDDTVRVNPAM 214
Cdd:smart00020   8 ANIGSFPWQVSLQYGGGRHF-----CGGSLISPRWVLTAAHCVRGSD------PSNIRVRLG-SHDLSSGEEGQVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042  215 YILHPKFRIGRYSapvHDLALIKLATPLKLNKNTDIICLPEKTDDLTDGTLAHTAGWGRSSDNSPVV-DEARRARIRI-S 292
Cdd:smart00020  76 VIIHPNYNPSTYD---NDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpDTLQEVNVPIvS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042  293 PDACRK-LPMNRTI---HIC-GRNEKGNNICSGDSGSGLYVRAGIingtsttwkWHVFGVASFGrEECQvSVNHDNAFSS 367
Cdd:smart00020 153 NATCRRaYSGGGAItdnMLCaGGLEGGKDACQGDSGGPLVCNDGR---------WVLVGIVSWG-SGCA-RPGKPGVYTR 221

                   ....*...
gi 2041616042  368 VAADIDWI 375
Cdd:smart00020 222 VSSYLDWI 229
Trypsin pfam00089
Trypsin;
135-375 1.07e-26

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 105.99  E-value: 1.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 135 VRRGEMPWLVRLESRTNLQslylsMCGGTIIHPQWILTAAHClldsntetLYAADGVSVYVGHSSRRQIGDDTVRVNPAM 214
Cdd:pfam00089   7 AQPGSFPWQVSLQLSSGKH-----FCGGSLISENWVLTAAHC--------VSGASDVKVVLGAHNIVLREGGEQKFDVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 215 YILHPKFRIGRYSapvHDLALIKLATPLKLNKNTDIICLPEKTDDLTDGTLAHTAGWGRSSDNSPvVDEARRARIRI-SP 293
Cdd:pfam00089  74 IIVHPNYNPDTLD---NDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVvSR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 294 DACRKlPMNRTI---HICGRnEKGNNICSGDSGSGLYVRAGIingtsttwkwhVFGVASFGREECQvsVNHDNAFSSVAA 370
Cdd:pfam00089 150 ETCRS-AYGGTVtdtMICAG-AGGKDACQGDSGGPLVCSDGE-----------LIGIVSWGYGCAS--GNYPGVYTPVSS 214

                  ....*
gi 2041616042 371 DIDWI 375
Cdd:pfam00089 215 YLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
133-378 3.17e-46

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: 157.82  E-value: 3.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 133 NTVRRGEMPWLVRLESRTNLQSlylsmCGGTIIHPQWILTAAHCLLDSNtetlyaADGVSVYVGHSSRRQIGDDTVRVNP 212
Cdd:cd00190     5 SEAKIGSFPWQVSLQYTGGRHF-----CGGSLISPRWVLTAAHCVYSSA------PSNYTVRLGSHDLSSNEGGGQVIKV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 213 AMYILHPKFRIGRYSapvHDLALIKLATPLKLNKNTDIICLPEKTDDLTDGTLAHTAGWGRSSDNSPVVDEARRARIRI- 291
Cdd:cd00190    74 KKVIVHPNYNPSTYD---NDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIv 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 292 SPDACRKLPMNRTI----HIC-GRNEKGNNICSGDSGSGLYVRagiingtsTTWKWHVFGVASFGrEECQvSVNHDNAFS 366
Cdd:cd00190   151 SNAECKRAYSYGGTitdnMLCaGGLEGGKDACQGDSGGPLVCN--------DNGRGVLVGIVSWG-SGCA-RPNYPGVYT 220
                         250
                  ....*....|..
gi 2041616042 367 SVAADIDWIKSV 378
Cdd:cd00190   221 RVSSYLDWIQKT 232
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
134-381 1.55e-44

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 154.42  E-value: 1.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 134 TVRRGEMPWLVRLESRTNLQSLYlsmCGGTIIHPQWILTAAHCLLDSntetlyAADGVSVYVGhsSRRQIGDDTVRVNPA 213
Cdd:COG5640    36 PATVGEYPWMVALQSSNGPSGQF---CGGTLIAPRWVLTAAHCVDGD------GPSDLRVVIG--STDLSTSGGTVVKVA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 214 MYILHPKFrigRYSAPVHDLALIKLATPLKLNKntdIICLPEKTDDLTDGTLAHTAGWGRSSDNSPVV-DEARRARIRIS 292
Cdd:COG5640   105 RIVVHPDY---DPATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPGSQsGTLRKADVPVV 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 293 PDA-CRKLPMNRT-IHIC-GRNEKGNNICSGDSGSGLYVRAGiingtsttWKWHVFGVASFGREECqvSVNHDNAFSSVA 369
Cdd:COG5640   179 SDAtCAAYGGFDGgTMLCaGYPEGGKDACQGDSGGPLVVKDG--------GGWVLVGVVSWGGGPC--AAGYPGVYTRVS 248
                         250
                  ....*....|..
gi 2041616042 370 ADIDWIKSVIRT 381
Cdd:COG5640   249 AYRDWIKSTAGG 260
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
135-375 8.88e-44

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: 151.68  E-value: 8.88e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042  135 VRRGEMPWLVRLESRTNLQSlylsmCGGTIIHPQWILTAAHCLLDSNtetlyaADGVSVYVGhSSRRQIGDDTVRVNPAM 214
Cdd:smart00020   8 ANIGSFPWQVSLQYGGGRHF-----CGGSLISPRWVLTAAHCVRGSD------PSNIRVRLG-SHDLSSGEEGQVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042  215 YILHPKFRIGRYSapvHDLALIKLATPLKLNKNTDIICLPEKTDDLTDGTLAHTAGWGRSSDNSPVV-DEARRARIRI-S 292
Cdd:smart00020  76 VIIHPNYNPSTYD---NDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpDTLQEVNVPIvS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042  293 PDACRK-LPMNRTI---HIC-GRNEKGNNICSGDSGSGLYVRAGIingtsttwkWHVFGVASFGrEECQvSVNHDNAFSS 367
Cdd:smart00020 153 NATCRRaYSGGGAItdnMLCaGGLEGGKDACQGDSGGPLVCNDGR---------WVLVGIVSWG-SGCA-RPGKPGVYTR 221

                   ....*...
gi 2041616042  368 VAADIDWI 375
Cdd:smart00020 222 VSSYLDWI 229
Trypsin pfam00089
Trypsin;
135-375 1.07e-26

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 105.99  E-value: 1.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 135 VRRGEMPWLVRLESRTNLQslylsMCGGTIIHPQWILTAAHClldsntetLYAADGVSVYVGHSSRRQIGDDTVRVNPAM 214
Cdd:pfam00089   7 AQPGSFPWQVSLQLSSGKH-----FCGGSLISENWVLTAAHC--------VSGASDVKVVLGAHNIVLREGGEQKFDVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 215 YILHPKFRIGRYSapvHDLALIKLATPLKLNKNTDIICLPEKTDDLTDGTLAHTAGWGRSSDNSPvVDEARRARIRI-SP 293
Cdd:pfam00089  74 IIVHPNYNPDTLD---NDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVvSR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 294 DACRKlPMNRTI---HICGRnEKGNNICSGDSGSGLYVRAGIingtsttwkwhVFGVASFGREECQvsVNHDNAFSSVAA 370
Cdd:pfam00089 150 ETCRS-AYGGTVtdtMICAG-AGGKDACQGDSGGPLVCSDGE-----------LIGIVSWGYGCAS--GNYPGVYTPVSS 214

                  ....*
gi 2041616042 371 DIDWI 375
Cdd:pfam00089 215 YLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
158-355 6.18e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 61.23  E-value: 6.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 158 SMCGGTIIHPQWILTAAHCLLDSNTETlyAADGVSVYVGHSSRRQIGDDTVRvnpamYILHPKFRIGrySAPVHDLALIK 237
Cdd:COG3591    12 GVCTGTLIGPNLVLTAGHCVYDGAGGG--WATNIVFVPGYNGGPYGTATATR-----FRVPPGWVAS--GDAGYDYALLR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616042 238 LATPLklnkNTDIICLP-EKTDDLTDGTLAHTAGWGRSSDNSPVVDEARRARIRISpdacrklpmNRTIHICgrnekgnN 316
Cdd:COG3591    83 LDEPL----GDTTGWLGlAFNDAPLAGEPVTIIGYPGDRPKDLSLDCSGRVTGVQG---------NRLSYDC-------D 142
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2041616042 317 ICSGDSGSGLYVRagiingtsTTWKWHVFGVASFGREEC 355
Cdd:COG3591   143 TTGGSSGSPVLDD--------SDGGGRVVGVHSAGGADR 173
 
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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