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Conserved domains on  [gi|1407939183|pdb|1HJ8|A]
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Chain A, TRYPSIN I

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 ...
1-218 3.30e-111

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: 318.07  E-value: 3.30e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A        1 IVGGYECKAYSQPHQVSL--NSGYHFCGGSLVNENWVVSAAHC----YKSRVEVRLGEHNIKVTEGSEQFISSSRVIRHP 74
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A       75 NYSSYNIDNDIMLIKLSKPATLNTYVQPVALPTS--CAPAGTMCTVSGWGNTMSSTADSNKLQCLNIPILSYSDCNNSY- 151
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYs 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1HJ8_A      152 -PGMITNAMFCAGYLEGGKDSCQGDSGGPVVCN----GELQGVVSWGYGCAEPGNPGVYAKVCIFNDWLTST 218
Cdd:cd00190 161 yGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-218 3.30e-111

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: 318.07  E-value: 3.30e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A        1 IVGGYECKAYSQPHQVSL--NSGYHFCGGSLVNENWVVSAAHC----YKSRVEVRLGEHNIKVTEGSEQFISSSRVIRHP 74
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A       75 NYSSYNIDNDIMLIKLSKPATLNTYVQPVALPTS--CAPAGTMCTVSGWGNTMSSTADSNKLQCLNIPILSYSDCNNSY- 151
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYs 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1HJ8_A      152 -PGMITNAMFCAGYLEGGKDSCQGDSGGPVVCN----GELQGVVSWGYGCAEPGNPGVYAKVCIFNDWLTST 218
Cdd:cd00190 161 yGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-214 3.60e-106

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: 304.99  E-value: 3.60e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A           1 IVGGYECKAYSQPHQVSL--NSGYHFCGGSLVNENWVVSAAHC----YKSRVEVRLGEHNIKVtEGSEQFISSSRVIRHP 74
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLqyGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSS-GEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A          75 NYSSYNIDNDIMLIKLSKPATLNTYVQPVALPTS--CAPAGTMCTVSGWGNTM-SSTADSNKLQCLNIPILSYSDCNNSY 151
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1HJ8_A         152 PGM--ITNAMFCAGYLEGGKDSCQGDSGGPVVCN---GELQGVVSWGYGCAEPGNPGVYAKVCIFNDW 214
Cdd:smart00020 161 SGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
1-215 7.22e-94

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 273.55  E-value: 7.22e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A          1 IVGGYECKAYSQPHQVSLN--SGYHFCGGSLVNENWVVSAAHCYKSR--VEVRLGEHNIKVTEGSEQFISSSRVIRHPNY 76
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlsSGKHFCGGSLISENWVLTAAHCVSGAsdVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A         77 SSYNIDNDIMLIKLSKPATLNTYVQPVALPTSCA--PAGTMCTVSGWGNTmSSTADSNKLQCLNIPILSYSDCNNSYPGM 154
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGNT-KTLGPSDTLQEVTVPVVSRETCRSAYGGT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
1HJ8_A        155 ITNAMFCAGYleGGKDSCQGDSGGPVVC-NGELQGVVSWGYGCAEPGNPGVYAKVCIFNDWL 215
Cdd:pfam00089 160 VTDTMICAGA--GGKDACQGDSGGPLVCsDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-221 9.43e-69

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 211.43  E-value: 9.43e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A        1 IVGGYECKAYSQPHQVSLNS----GYHFCGGSLVNENWVVSAAHCY----KSRVEVRLGEHNIKVTEGseQFISSSRVIR 72
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSsngpSGQFCGGTLIAPRWVLTAAHCVdgdgPSDLRVVIGSTDLSTSGG--TVVKVARIVV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A       73 HPNYSSYNIDNDIMLIKLSKPATLNTYVqPVALPTSCAPAGTMCTVSGWGNTMSSTAD-SNKLQCLNIPILSYSDCNnSY 151
Cdd:COG5640 109 HPDYDPATPGNDIALLKLATPVPGVAPA-PLATSADAAAPGTPATVAGWGRTSEGPGSqSGTLRKADVPVVSDATCA-AY 186
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1HJ8_A      152 PGMITNAMFCAGYLEGGKDSCQGDSGGPVV----CNGELQGVVSWGYGCAEPGNPGVYAKVCIFNDWLTSTMAS 221
Cdd:COG5640 187 GGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGG 260
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-218 3.30e-111

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: 318.07  E-value: 3.30e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A        1 IVGGYECKAYSQPHQVSL--NSGYHFCGGSLVNENWVVSAAHC----YKSRVEVRLGEHNIKVTEGSEQFISSSRVIRHP 74
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A       75 NYSSYNIDNDIMLIKLSKPATLNTYVQPVALPTS--CAPAGTMCTVSGWGNTMSSTADSNKLQCLNIPILSYSDCNNSY- 151
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYs 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1HJ8_A      152 -PGMITNAMFCAGYLEGGKDSCQGDSGGPVVCN----GELQGVVSWGYGCAEPGNPGVYAKVCIFNDWLTST 218
Cdd:cd00190 161 yGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-214 3.60e-106

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: 304.99  E-value: 3.60e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A           1 IVGGYECKAYSQPHQVSL--NSGYHFCGGSLVNENWVVSAAHC----YKSRVEVRLGEHNIKVtEGSEQFISSSRVIRHP 74
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLqyGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSS-GEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A          75 NYSSYNIDNDIMLIKLSKPATLNTYVQPVALPTS--CAPAGTMCTVSGWGNTM-SSTADSNKLQCLNIPILSYSDCNNSY 151
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1HJ8_A         152 PGM--ITNAMFCAGYLEGGKDSCQGDSGGPVVCN---GELQGVVSWGYGCAEPGNPGVYAKVCIFNDW 214
Cdd:smart00020 161 SGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
1-215 7.22e-94

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 273.55  E-value: 7.22e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A          1 IVGGYECKAYSQPHQVSLN--SGYHFCGGSLVNENWVVSAAHCYKSR--VEVRLGEHNIKVTEGSEQFISSSRVIRHPNY 76
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlsSGKHFCGGSLISENWVLTAAHCVSGAsdVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A         77 SSYNIDNDIMLIKLSKPATLNTYVQPVALPTSCA--PAGTMCTVSGWGNTmSSTADSNKLQCLNIPILSYSDCNNSYPGM 154
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGNT-KTLGPSDTLQEVTVPVVSRETCRSAYGGT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
1HJ8_A        155 ITNAMFCAGYleGGKDSCQGDSGGPVVC-NGELQGVVSWGYGCAEPGNPGVYAKVCIFNDWL 215
Cdd:pfam00089 160 VTDTMICAGA--GGKDACQGDSGGPLVCsDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-221 9.43e-69

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 211.43  E-value: 9.43e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A        1 IVGGYECKAYSQPHQVSLNS----GYHFCGGSLVNENWVVSAAHCY----KSRVEVRLGEHNIKVTEGseQFISSSRVIR 72
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSsngpSGQFCGGTLIAPRWVLTAAHCVdgdgPSDLRVVIGSTDLSTSGG--TVVKVARIVV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A       73 HPNYSSYNIDNDIMLIKLSKPATLNTYVqPVALPTSCAPAGTMCTVSGWGNTMSSTAD-SNKLQCLNIPILSYSDCNnSY 151
Cdd:COG5640 109 HPDYDPATPGNDIALLKLATPVPGVAPA-PLATSADAAAPGTPATVAGWGRTSEGPGSqSGTLRKADVPVVSDATCA-AY 186
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1HJ8_A      152 PGMITNAMFCAGYLEGGKDSCQGDSGGPVV----CNGELQGVVSWGYGCAEPGNPGVYAKVCIFNDWLTSTMAS 221
Cdd:COG5640 187 GGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGG 260
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
15-205 4.98e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 56.99  E-value: 4.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A       15 QVSLNSGYHFCGGSLVNENWVVSAAHC--------YKSRVEVRLGEHNikvteGSEQFISSSRVIRHPNY-SSYNIDNDI 85
Cdd:COG3591   4 RLETDGGGGVCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWvASGDAGYDY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HJ8_A       86 MLIKLSKPATLNTYVQPVALPTScAPAGTMCTVSGwgntmsstadsnklqclnipilsysdcnnsYPG--MITNAMFCAG 163
Cdd:COG3591  79 ALLRLDEPLGDTTGWLGLAFNDA-PLAGEPVTIIG------------------------------YPGdrPKDLSLDCSG 127
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
1HJ8_A      164 YLEGGK--------DSCQGDSGGPVV----CNGELQGVVSWGYgcAEPGNPGVY 205
Cdd:COG3591 128 RVTGVQgnrlsydcDTTGGSSGSPVLddsdGGGRVVGVHSAGG--ADRANTGVR 179
 
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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