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Conserved domains on  [gi|1941159621]
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Chain DM, Cationic trypsin

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 ...
1-219 8.64e-106

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: 304.20  E-value: 8.64e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621   1 IVGGYTCGANTVPYQVSL--NSGYHFCGGSLINSQWVVSAAHCY----KSGIQVRLGEDNINVVEGNEQFISASKSIVHP 74
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCVyssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621  75 SYNSNTLNNDIMLIKLKSAASLNSRVASISLPTS--CASAGTQCLISGWGNTKSSGtSYPDVLKCLKAPILSDSSCKSAY 152
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1941159621 153 --PGQITSNMFCAGYLEGGKDSCQGDSGGPVVC----SGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQT 219
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 ...
1-219 8.64e-106

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: 304.20  E-value: 8.64e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621   1 IVGGYTCGANTVPYQVSL--NSGYHFCGGSLINSQWVVSAAHCY----KSGIQVRLGEDNINVVEGNEQFISASKSIVHP 74
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCVyssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621  75 SYNSNTLNNDIMLIKLKSAASLNSRVASISLPTS--CASAGTQCLISGWGNTKSSGtSYPDVLKCLKAPILSDSSCKSAY 152
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1941159621 153 --PGQITSNMFCAGYLEGGKDSCQGDSGGPVVC----SGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQT 219
Cdd:cd00190   160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-216 1.26e-104

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: 301.13  E-value: 1.26e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621    1 IVGGYTCGANTVPYQVSL--NSGYHFCGGSLINSQWVVSAAHC----YKSGIQVRLGEDNINVvEGNEQFISASKSIVHP 74
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLqyGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSS-GEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621   75 SYNSNTLNNDIMLIKLKSAASLNSRVASISLPTS--CASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAY 152
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1941159621  153 PGQ--ITSNMFCAGYLEGGKDSCQGDSGGPVVCSGK---LQGIVSWGSGCAQKNKPGVYTKVCNYVSWI 216
Cdd:smart00020 161 SGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-216 1.88e-86

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 255.06  E-value: 1.88e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621   1 IVGGYTCGANTVPYQVSLN--SGYHFCGGSLINSQWVVSAAHCYKSG--IQVRLGEDNINVVEGNEQFISASKSIVHPSY 76
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlsSGKHFCGGSLISENWVLTAAHCVSGAsdVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621  77 NSNTLNNDIMLIKLKSAASLNSRVASISLPTSCAS--AGTQCLISGWGNTKSSGtsYPDVLKCLKAPILSDSSCKSAYPG 154
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDlpVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1941159621 155 QITSNMFCAGYleGGKDSCQGDSGGPVVCS-GKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWI 216
Cdd:pfam00089 159 TVTDTMICAGA--GGKDACQGDSGGPLVCSdGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-223 4.93e-71

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 217.21  E-value: 4.93e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621   1 IVGGYTCGANTVPYQVSLNS----GYHFCGGSLINSQWVVSAAHCY----KSGIQVRLGEDNINVVEGneQFISASKSIV 72
Cdd:COG5640    31 IVGGTPATVGEYPWMVALQSsngpSGQFCGGTLIAPRWVLTAAHCVdgdgPSDLRVVIGSTDLSTSGG--TVVKVARIVV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621  73 HPSYNSNTLNNDIMLIKLKSAASlnsRVASISLPTS--CASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCkS 150
Cdd:COG5640   109 HPDYDPATPGNDIALLKLATPVP---GVAPAPLATSadAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATC-A 184
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1941159621 151 AYPGQITSNMFCAGYLEGGKDSCQGDSGGPVV----CSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN 223
Cdd:COG5640   185 AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-219 8.64e-106

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: 304.20  E-value: 8.64e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621   1 IVGGYTCGANTVPYQVSL--NSGYHFCGGSLINSQWVVSAAHCY----KSGIQVRLGEDNINVVEGNEQFISASKSIVHP 74
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCVyssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621  75 SYNSNTLNNDIMLIKLKSAASLNSRVASISLPTS--CASAGTQCLISGWGNTKSSGtSYPDVLKCLKAPILSDSSCKSAY 152
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1941159621 153 --PGQITSNMFCAGYLEGGKDSCQGDSGGPVVC----SGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQT 219
Cdd:cd00190   160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-216 1.26e-104

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: 301.13  E-value: 1.26e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621    1 IVGGYTCGANTVPYQVSL--NSGYHFCGGSLINSQWVVSAAHC----YKSGIQVRLGEDNINVvEGNEQFISASKSIVHP 74
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLqyGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSS-GEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621   75 SYNSNTLNNDIMLIKLKSAASLNSRVASISLPTS--CASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAY 152
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1941159621  153 PGQ--ITSNMFCAGYLEGGKDSCQGDSGGPVVCSGK---LQGIVSWGSGCAQKNKPGVYTKVCNYVSWI 216
Cdd:smart00020 161 SGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-216 1.88e-86

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 255.06  E-value: 1.88e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621   1 IVGGYTCGANTVPYQVSLN--SGYHFCGGSLINSQWVVSAAHCYKSG--IQVRLGEDNINVVEGNEQFISASKSIVHPSY 76
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlsSGKHFCGGSLISENWVLTAAHCVSGAsdVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621  77 NSNTLNNDIMLIKLKSAASLNSRVASISLPTSCAS--AGTQCLISGWGNTKSSGtsYPDVLKCLKAPILSDSSCKSAYPG 154
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDlpVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1941159621 155 QITSNMFCAGYleGGKDSCQGDSGGPVVCS-GKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWI 216
Cdd:pfam00089 159 TVTDTMICAGA--GGKDACQGDSGGPLVCSdGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-223 4.93e-71

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 217.21  E-value: 4.93e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621   1 IVGGYTCGANTVPYQVSLNS----GYHFCGGSLINSQWVVSAAHCY----KSGIQVRLGEDNINVVEGneQFISASKSIV 72
Cdd:COG5640    31 IVGGTPATVGEYPWMVALQSsngpSGQFCGGTLIAPRWVLTAAHCVdgdgPSDLRVVIGSTDLSTSGG--TVVKVARIVV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621  73 HPSYNSNTLNNDIMLIKLKSAASlnsRVASISLPTS--CASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCkS 150
Cdd:COG5640   109 HPDYDPATPGNDIALLKLATPVP---GVAPAPLATSadAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATC-A 184
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1941159621 151 AYPGQITSNMFCAGYLEGGKDSCQGDSGGPVV----CSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN 223
Cdd:COG5640   185 AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
15-196 4.53e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 45.82  E-value: 4.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621  15 QVSLNSGYHFCGGSLINSQWVVSAAHC--------YKSGIQVRLGEDNinvveGNEQFISASKSIVHPSY-NSNTLNNDI 85
Cdd:COG3591     4 RLETDGGGGVCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWvASGDAGYDY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941159621  86 MLIKLKSAASLNSRVASISLPTScASAGTQCLISGWGNTKSSGTSYpdvlkclkapilsDSSCKSAYPGQitsnmfcaGY 165
Cdd:COG3591    79 ALLRLDEPLGDTTGWLGLAFNDA-PLAGEPVTIIGYPGDRPKDLSL-------------DCSGRVTGVQG--------NR 136
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1941159621 166 LEGGKDSCQGDSGGPVV----CSGKLQGIVSWGSG 196
Cdd:COG3591   137 LSYDCDTTGGSSGSPVLddsdGGGRVVGVHSAGGA 171
 
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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