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Conserved domains on  [gi|62526043|ref|NP_009203|]
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chymotrypsin-C preproprotein [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 ...
30-265 4.86e-98

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: 286.48  E-value: 4.86e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043  30 VVGGEDARPHSWPWQISLQYlknDTWRHTCGGTLIASNFVLTAAHCISNT--RTYRVAVGKNNLEVEdEEGSLFVGVDTI 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSN-EGGGQVIKVKKV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043 108 HVHKRWNALLLRNDIALIKLAEHVELSDTIQVACLPEKDSLLPKDYPCYVTGWGRLWTNGPIADKLQQGLQPVVDHATCS 187
Cdd:cd00190  77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62526043 188 RIDWWGFRVKKTMVCAGG-DGVISACNGDSGGPLNCQLeNGSWEVFGIVSFGSrrGCNTRKKPVVYTRVSAYIDWINEK 265
Cdd:cd00190 157 RAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
30-265 4.86e-98

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: 286.48  E-value: 4.86e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043  30 VVGGEDARPHSWPWQISLQYlknDTWRHTCGGTLIASNFVLTAAHCISNT--RTYRVAVGKNNLEVEdEEGSLFVGVDTI 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSN-EGGGQVIKVKKV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043 108 HVHKRWNALLLRNDIALIKLAEHVELSDTIQVACLPEKDSLLPKDYPCYVTGWGRLWTNGPIADKLQQGLQPVVDHATCS 187
Cdd:cd00190  77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62526043 188 RIDWWGFRVKKTMVCAGG-DGVISACNGDSGGPLNCQLeNGSWEVFGIVSFGSrrGCNTRKKPVVYTRVSAYIDWINEK 265
Cdd:cd00190 157 RAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
29-262 2.02e-94

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: 277.25  E-value: 2.02e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043     29 RVVGGEDARPHSWPWQISLQYlknDTWRHTCGGTLIASNFVLTAAHCISN--TRTYRVAVGKNNLEVEDEEgsLFVGVDT 106
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGEEG--QVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043    107 IHVHKRWNALLLRNDIALIKLAEHVELSDTIQVACLPEKDSLLPKDYPCYVTGWGRL-WTNGPIADKLQQGLQPVVDHAT 185
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62526043    186 CSRIDWWGFRVKKTMVCAGG-DGVISACNGDSGGPLNCQleNGSWEVFGIVSFGSrrGCNTRKKPVVYTRVSAYIDWI 262
Cdd:smart00020 156 CRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
30-262 1.55e-76

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 231.56  E-value: 1.55e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043    30 VVGGEDARPHSWPWQISLQYlknDTWRHTCGGTLIASNFVLTAAHCISNTRTYRVAVGKNNLEVeDEEGSLFVGVDTIHV 109
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVL-REGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043   110 HKRWNALLLRNDIALIKLAEHVELSDTIQVACLPEKDSLLPKDYPCYVTGWGRLWTNGPiADKLQQGLQPVVDHATCSRi 189
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRS- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62526043   190 dWWGFRVKKTMVCAGGDGViSACNGDSGGPLNCqlENGswEVFGIVSFGsrRGCNTRKKPVVYTRVSAYIDWI 262
Cdd:pfam00089 155 -AYGGTVTDTMICAGAGGK-DACQGDSGGPLVC--SDG--ELIGIVSWG--YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-266 1.17e-64

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 202.57  E-value: 1.17e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043   1 MLGITVLAALLACASSCGVPSFPPN-LSARVVGGEDARPHSWPWQISLQYlKNDTWRHTCGGTLIASNFVLTAAHCISNT 79
Cdd:COG5640   1 MRRRRLLAALAAAALALALAAAPAAdAAPAIVGGTPATVGEYPWMVALQS-SNGPSGQFCGGTLIAPRWVLTAAHCVDGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043  80 R--TYRVAVGKNNLEVEDEEgslFVGVDTIHVHKRWNALLLRNDIALIKLAEHVelsDTIQVACLPEKDSLLPKDYPCYV 157
Cdd:COG5640  80 GpsDLRVVIGSTDLSTSGGT---VVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043 158 TGWGRLWTN-GPIADKLQQGLQPVVDHATCSRidwWGFRVKKTMVCAGG-DGVISACNGDSGGPLnCQLENGSWEVFGIV 235
Cdd:COG5640 154 AGWGRTSEGpGSQSGTLRKADVPVVSDATCAA---YGGFDGGTMLCAGYpEGGKDACQGDSGGPL-VVKDGGGWVLVGVV 229
                       250       260       270
                ....*....|....*....|....*....|.
gi 62526043 236 SFGSrRGCNTrKKPVVYTRVSAYIDWINEKM 266
Cdd:COG5640 230 SWGG-GPCAA-GYPGVYTRVSAYRDWIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
30-265 4.86e-98

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: 286.48  E-value: 4.86e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043  30 VVGGEDARPHSWPWQISLQYlknDTWRHTCGGTLIASNFVLTAAHCISNT--RTYRVAVGKNNLEVEdEEGSLFVGVDTI 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSN-EGGGQVIKVKKV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043 108 HVHKRWNALLLRNDIALIKLAEHVELSDTIQVACLPEKDSLLPKDYPCYVTGWGRLWTNGPIADKLQQGLQPVVDHATCS 187
Cdd:cd00190  77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62526043 188 RIDWWGFRVKKTMVCAGG-DGVISACNGDSGGPLNCQLeNGSWEVFGIVSFGSrrGCNTRKKPVVYTRVSAYIDWINEK 265
Cdd:cd00190 157 RAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
29-262 2.02e-94

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: 277.25  E-value: 2.02e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043     29 RVVGGEDARPHSWPWQISLQYlknDTWRHTCGGTLIASNFVLTAAHCISN--TRTYRVAVGKNNLEVEDEEgsLFVGVDT 106
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGEEG--QVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043    107 IHVHKRWNALLLRNDIALIKLAEHVELSDTIQVACLPEKDSLLPKDYPCYVTGWGRL-WTNGPIADKLQQGLQPVVDHAT 185
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62526043    186 CSRIDWWGFRVKKTMVCAGG-DGVISACNGDSGGPLNCQleNGSWEVFGIVSFGSrrGCNTRKKPVVYTRVSAYIDWI 262
Cdd:smart00020 156 CRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
30-262 1.55e-76

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 231.56  E-value: 1.55e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043    30 VVGGEDARPHSWPWQISLQYlknDTWRHTCGGTLIASNFVLTAAHCISNTRTYRVAVGKNNLEVeDEEGSLFVGVDTIHV 109
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVL-REGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043   110 HKRWNALLLRNDIALIKLAEHVELSDTIQVACLPEKDSLLPKDYPCYVTGWGRLWTNGPiADKLQQGLQPVVDHATCSRi 189
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRS- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62526043   190 dWWGFRVKKTMVCAGGDGViSACNGDSGGPLNCqlENGswEVFGIVSFGsrRGCNTRKKPVVYTRVSAYIDWI 262
Cdd:pfam00089 155 -AYGGTVTDTMICAGAGGK-DACQGDSGGPLVC--SDG--ELIGIVSWG--YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-266 1.17e-64

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 202.57  E-value: 1.17e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043   1 MLGITVLAALLACASSCGVPSFPPN-LSARVVGGEDARPHSWPWQISLQYlKNDTWRHTCGGTLIASNFVLTAAHCISNT 79
Cdd:COG5640   1 MRRRRLLAALAAAALALALAAAPAAdAAPAIVGGTPATVGEYPWMVALQS-SNGPSGQFCGGTLIAPRWVLTAAHCVDGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043  80 R--TYRVAVGKNNLEVEDEEgslFVGVDTIHVHKRWNALLLRNDIALIKLAEHVelsDTIQVACLPEKDSLLPKDYPCYV 157
Cdd:COG5640  80 GpsDLRVVIGSTDLSTSGGT---VVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043 158 TGWGRLWTN-GPIADKLQQGLQPVVDHATCSRidwWGFRVKKTMVCAGG-DGVISACNGDSGGPLnCQLENGSWEVFGIV 235
Cdd:COG5640 154 AGWGRTSEGpGSQSGTLRKADVPVVSDATCAA---YGGFDGGTMLCAGYpEGGKDACQGDSGGPL-VVKDGGGWVLVGVV 229
                       250       260       270
                ....*....|....*....|....*....|.
gi 62526043 236 SFGSrRGCNTrKKPVVYTRVSAYIDWINEKM 266
Cdd:COG5640 230 SWGG-GPCAA-GYPGVYTRVSAYRDWIKSTA 258
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
49-245 1.88e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 58.92  E-value: 1.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043  49 YLKNDTWRHTCGGTLIASNFVLTAAHCISNTRTYRVAVgknNLEVE---DEEGSLFVGVDTIHVHKRW-NALLLRNDIAL 124
Cdd:COG3591   4 RLETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWAT---NIVFVpgyNGGPYGTATATRFRVPPGWvASGDAGYDYAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526043 125 IKLAEHVELsdtiQVACLP-EKDSLLPKDYPCYVTGWGrlwtngpiADKLQQglqpVVDHATCSRIDWWGFRVkkTMVCa 203
Cdd:COG3591  81 LRLDEPLGD----TTGWLGlAFNDAPLAGEPVTIIGYP--------GDRPKD----LSLDCSGRVTGVQGNRL--SYDC- 141
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 62526043 204 ggdgviSACNGDSGGPLnCQLENGSWEVFGIVSFGSRRGCNT 245
Cdd:COG3591 142 ------DTTGGSSGSPV-LDDSDGGGRVVGVHSAGGADRANT 176
 
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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