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Conserved domains on  [gi|62897905|dbj|BAD96892|]
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chymotrypsin-like variant, partial [Homo sapiens]

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 ...
34-260 9.61e-101

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: 293.41  E-value: 9.61e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905  34 IVNGENAVLGSWPWQVSLQDSSGFHFCGGSLISQSWVVTAAHC--NVSPGRHFVVLGEYDRSSNAEPLQVLSVSRAITHP 111
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCvySSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905 112 SWNSTTMNNDVTLLKLASPAQYTTRISPVCLASSNEALTEGLTCVTTGWGRLSGVGNvTPAHLQQVALPLVTVNQCRQYW 191
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62897905 192 --GSSITDSMICTGGA--GASSCQGDSGGPLVCQKGNTWVLIGIVSWGTkNCNV-RAPAVYTRVSKFSTWINQV 260
Cdd:cd00190 160 syGGTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS-GCARpNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
34-260 9.61e-101

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: 293.41  E-value: 9.61e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905  34 IVNGENAVLGSWPWQVSLQDSSGFHFCGGSLISQSWVVTAAHC--NVSPGRHFVVLGEYDRSSNAEPLQVLSVSRAITHP 111
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCvySSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905 112 SWNSTTMNNDVTLLKLASPAQYTTRISPVCLASSNEALTEGLTCVTTGWGRLSGVGNvTPAHLQQVALPLVTVNQCRQYW 191
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62897905 192 --GSSITDSMICTGGA--GASSCQGDSGGPLVCQKGNTWVLIGIVSWGTkNCNV-RAPAVYTRVSKFSTWINQV 260
Cdd:cd00190 160 syGGTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS-GCARpNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
33-257 2.06e-99

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: 289.96  E-value: 2.06e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905     33 RIVNGENAVLGSWPWQVSLQDSSGFHFCGGSLISQSWVVTAAHC--NVSPGRHFVVLGEYDRSSNaEPLQVLSVSRAITH 110
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCvrGSDPSNIRVRLGSHDLSSG-EEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905    111 PSWNSTTMNNDVTLLKLASPAQYTTRISPVCLASSNEALTEGLTCVTTGWGRLSGVGNVTPAHLQQVALPLVTVNQCRQY 190
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62897905    191 WG--SSITDSMICTGGA--GASSCQGDSGGPLVCQkGNTWVLIGIVSWGTKNCNVRAPAVYTRVSKFSTWI 257
Cdd:smart00020 160 YSggGAITDNMLCAGGLegGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
26-262 1.68e-79

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 240.32  E-value: 1.68e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905  26 PALSFSQRIVNGENAVLGSWPWQVSLQDSSGF--HFCGGSLISQSWVVTAAHC--NVSPGRHFVVLGEYDRSSNAEplQV 101
Cdd:COG5640  23 PAADAAPAIVGGTPATVGEYPWMVALQSSNGPsgQFCGGTLIAPRWVLTAAHCvdGDGPSDLRVVIGSTDLSTSGG--TV 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905 102 LSVSRAITHPSWNSTTMNNDVTLLKLASPAqytTRISPVCLASSNEALTEGLTCVTTGWGRLSGVGNVTPAHLQQVALPL 181
Cdd:COG5640 101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905 182 VTVNQCRQYwGSSITDSMICTGGA--GASSCQGDSGGPLVCQKGNTWVLIGIVSWGTKNCNVRAPAVYTRVSKFSTWINQ 259
Cdd:COG5640 178 VSDATCAAY-GGFDGGTMLCAGYPegGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKS 256

                ...
gi 62897905 260 VIA 262
Cdd:COG5640 257 TAG 259
Trypsin pfam00089
Trypsin;
34-257 8.94e-79

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 236.96  E-value: 8.94e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905    34 IVNGENAVLGSWPWQVSLQDSSGFHFCGGSLISQSWVVTAAHCNVSPGRHFVVLGEYDRSSNAEPLQVLSVSRAITHPSW 113
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905   114 NSTTMNNDVTLLKLASPAQYTTRISPVCLASSNEALTEGLTCVTTGWGRLSGVGnvTPAHLQQVALPLVTVNQCRQYWGS 193
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62897905   194 SITDSMICTGGAGASSCQGDSGGPLVCQKGntwVLIGIVSWGTKNCNVRAPAVYTRVSKFSTWI 257
Cdd:pfam00089 159 TVTDTMICAGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
34-260 9.61e-101

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: 293.41  E-value: 9.61e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905  34 IVNGENAVLGSWPWQVSLQDSSGFHFCGGSLISQSWVVTAAHC--NVSPGRHFVVLGEYDRSSNAEPLQVLSVSRAITHP 111
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCvySSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905 112 SWNSTTMNNDVTLLKLASPAQYTTRISPVCLASSNEALTEGLTCVTTGWGRLSGVGNvTPAHLQQVALPLVTVNQCRQYW 191
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62897905 192 --GSSITDSMICTGGA--GASSCQGDSGGPLVCQKGNTWVLIGIVSWGTkNCNV-RAPAVYTRVSKFSTWINQV 260
Cdd:cd00190 160 syGGTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS-GCARpNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
33-257 2.06e-99

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: 289.96  E-value: 2.06e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905     33 RIVNGENAVLGSWPWQVSLQDSSGFHFCGGSLISQSWVVTAAHC--NVSPGRHFVVLGEYDRSSNaEPLQVLSVSRAITH 110
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCvrGSDPSNIRVRLGSHDLSSG-EEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905    111 PSWNSTTMNNDVTLLKLASPAQYTTRISPVCLASSNEALTEGLTCVTTGWGRLSGVGNVTPAHLQQVALPLVTVNQCRQY 190
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62897905    191 WG--SSITDSMICTGGA--GASSCQGDSGGPLVCQkGNTWVLIGIVSWGTKNCNVRAPAVYTRVSKFSTWI 257
Cdd:smart00020 160 YSggGAITDNMLCAGGLegGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
26-262 1.68e-79

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 240.32  E-value: 1.68e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905  26 PALSFSQRIVNGENAVLGSWPWQVSLQDSSGF--HFCGGSLISQSWVVTAAHC--NVSPGRHFVVLGEYDRSSNAEplQV 101
Cdd:COG5640  23 PAADAAPAIVGGTPATVGEYPWMVALQSSNGPsgQFCGGTLIAPRWVLTAAHCvdGDGPSDLRVVIGSTDLSTSGG--TV 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905 102 LSVSRAITHPSWNSTTMNNDVTLLKLASPAqytTRISPVCLASSNEALTEGLTCVTTGWGRLSGVGNVTPAHLQQVALPL 181
Cdd:COG5640 101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905 182 VTVNQCRQYwGSSITDSMICTGGA--GASSCQGDSGGPLVCQKGNTWVLIGIVSWGTKNCNVRAPAVYTRVSKFSTWINQ 259
Cdd:COG5640 178 VSDATCAAY-GGFDGGTMLCAGYPegGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKS 256

                ...
gi 62897905 260 VIA 262
Cdd:COG5640 257 TAG 259
Trypsin pfam00089
Trypsin;
34-257 8.94e-79

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 236.96  E-value: 8.94e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905    34 IVNGENAVLGSWPWQVSLQDSSGFHFCGGSLISQSWVVTAAHCNVSPGRHFVVLGEYDRSSNAEPLQVLSVSRAITHPSW 113
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905   114 NSTTMNNDVTLLKLASPAQYTTRISPVCLASSNEALTEGLTCVTTGWGRLSGVGnvTPAHLQQVALPLVTVNQCRQYWGS 193
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62897905   194 SITDSMICTGGAGASSCQGDSGGPLVCQKGntwVLIGIVSWGTKNCNVRAPAVYTRVSKFSTWI 257
Cdd:pfam00089 159 TVTDTMICAGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
51-250 2.82e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 60.85  E-value: 2.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905  51 LQDSSGFHFCGGSLISQSWVVTAAHCNVSPGR-------HFVVlgeydrSSNAEPLQVLSVSRAITHPSW-NSTTMNNDV 122
Cdd:COG3591   5 LETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGggwatniVFVP------GYNGGPYGTATATRFRVPPGWvASGDAGYDY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905 123 TLLKLASPAQYTTRISPVclaSSNEALTEGLTCVTTGWGRlsgvgnvtpAHLQQVALplvtVNQCRqywGSSITDSMICT 202
Cdd:COG3591  79 ALLRLDEPLGDTTGWLGL---AFNDAPLAGEPVTIIGYPG---------DRPKDLSL----DCSGR---VTGVQGNRLSY 139
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 62897905 203 ggaGASSCQGDSGGPLVCQKGNTWVLIGIVSWGTKNCNVRAPAVYTRV 250
Cdd:COG3591 140 ---DCDTTGGSSGSPVLDDSDGGGRVVGVHSAGGADRANTGVRLTSAI 184
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
69-231 1.49e-03

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 38.17  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905    69 WVVTAAHCnVSPGRHFVVLGEYDRSSNAEPLQVLSVSRaithpswnstTMNNDVTLLKLASPAqytTRISPVCLASSnEA 148
Cdd:pfam13365  11 LVLTNAHV-VDDAEEAAVELVSVVLADGREYPATVVAR----------DPDLDLALLRVSGDG---RGLPPLPLGDS-EP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905   149 LTEGLTCVTTGWGRLSGVGNVTPAhlqqvalplvTVNQCRQYWGSSITDSMICTGGAGASscqGDSGGPLVCQKGNtwvL 228
Cdd:pfam13365  76 LVGGERVYAVGYPLGGEKLSLSEG----------IVSGVDEGRDGGDDGRVIQTDAALSP---GSSGGPVFDADGR---V 139

                  ...
gi 62897905   229 IGI 231
Cdd:pfam13365 140 VGI 142
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
45-159 9.97e-03

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: 35.22  E-value: 9.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62897905    45 WPWQVSLQdSSGFHFCGGSLISQSWVVTAAHC--NVSPGRHF--VVLGEYD--RSSNAEPLQVLSVSRAITHPSWNsttm 118
Cdd:pfam09342   1 WPWIAKVY-LDGNMICSGVLIDASWVIVSGSClrDTNLRHQYisVVLGGAKtlKSIEGPYEQIVRVDCRHDIPESE---- 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 62897905   119 nndVTLLKLASPAQYTTRISPVCLASSNEALTEGLTCVTTG 159
Cdd:pfam09342  76 ---ISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 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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