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Conserved domains on  [gi|42543834|pdb|1UTL|M]
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Chain M, 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 ...
21-238 1.02e-112

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: 322.69  E-value: 1.02e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M       21 IVGGYECKPYSQPHQVSL--NSGYHFCGGSLVNENWVVSAAHCY----KSRVEVRLGEHNIKVTEGSEQFISSSRVIRHP 94
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCVyssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M       95 NYSSYNIDNDIMLIKLSKPATLNTYVQPVALPTS--CAPAGTMCTVSGWGNTMSSTADSNKLQCLNIPILSYSDCNNSY- 171
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYs 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1UTL_M      172 -PGMITNAMFCAGYLEGGKDSCQGDSGGPVVCN----GELQGVVSWGYGCAEPGNPGVYAKVCIFNDWLTST 238
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 ...
21-238 1.02e-112

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: 322.69  E-value: 1.02e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M       21 IVGGYECKPYSQPHQVSL--NSGYHFCGGSLVNENWVVSAAHCY----KSRVEVRLGEHNIKVTEGSEQFISSSRVIRHP 94
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCVyssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M       95 NYSSYNIDNDIMLIKLSKPATLNTYVQPVALPTS--CAPAGTMCTVSGWGNTMSSTADSNKLQCLNIPILSYSDCNNSY- 171
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYs 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1UTL_M      172 -PGMITNAMFCAGYLEGGKDSCQGDSGGPVVCN----GELQGVVSWGYGCAEPGNPGVYAKVCIFNDWLTST 238
Cdd:cd00190 161 yGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-234 6.18e-108

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: 310.38  E-value: 6.18e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M          20 KIVGGYECKPYSQPHQVSL--NSGYHFCGGSLVNENWVVSAAHC----YKSRVEVRLGEHNIKVtEGSEQFISSSRVIRH 93
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqyGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSS-GEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M          94 PNYSSYNIDNDIMLIKLSKPATLNTYVQPVALPTS--CAPAGTMCTVSGWGNTM-SSTADSNKLQCLNIPILSYSDCNNS 170
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1UTL_M         171 YPGM--ITNAMFCAGYLEGGKDSCQGDSGGPVVCN---GELQGVVSWGYGCAEPGNPGVYAKVCIFNDW 234
Cdd:smart00020 160 YSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
21-235 3.32e-95

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 277.79  E-value: 3.32e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M         21 IVGGYECKPYSQPHQVSLN--SGYHFCGGSLVNENWVVSAAHCYKSR--VEVRLGEHNIKVTEGSEQFISSSRVIRHPNY 96
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlsSGKHFCGGSLISENWVLTAAHCVSGAsdVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M         97 SSYNIDNDIMLIKLSKPATLNTYVQPVALPTSCA--PAGTMCTVSGWGNTmSSTADSNKLQCLNIPILSYSDCNNSYPGM 174
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGNT-KTLGPSDTLQEVTVPVVSRETCRSAYGGT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
1UTL_M        175 ITNAMFCAGYleGGKDSCQGDSGGPVVC-NGELQGVVSWGYGCAEPGNPGVYAKVCIFNDWL 235
Cdd:pfam00089 160 VTDTMICAGA--GGKDACQGDSGGPLVCsDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-241 2.10e-70

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 216.44  E-value: 2.10e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M        1 MISLVFVLLIGAAFATEDDKIVGGYECKPYSQPHQVSLNS----GYHFCGGSLVNENWVVSAAHCY----KSRVEVRLGE 72
Cdd:COG5640  11 AAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSsngpSGQFCGGTLIAPRWVLTAAHCVdgdgPSDLRVVIGS 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M       73 HNIKVTEGseQFISSSRVIRHPNYSSYNIDNDIMLIKLSKPATLNTYVqPVALPTSCAPAGTMCTVSGWGNTMSSTAD-S 151
Cdd:COG5640  91 TDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPA-PLATSADAAAPGTPATVAGWGRTSEGPGSqS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M      152 NKLQCLNIPILSYSDCNnSYPGMITNAMFCAGYLEGGKDSCQGDSGGPVV----CNGELQGVVSWGYGCAEPGNPGVYAK 227
Cdd:COG5640 168 GTLRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTR 246
                       250
                ....*....|....
1UTL_M      228 VCIFNDWLTSTMAS 241
Cdd:COG5640 247 VSAYRDWIKSTAGG 260
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
21-238 1.02e-112

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: 322.69  E-value: 1.02e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M       21 IVGGYECKPYSQPHQVSL--NSGYHFCGGSLVNENWVVSAAHCY----KSRVEVRLGEHNIKVTEGSEQFISSSRVIRHP 94
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCVyssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M       95 NYSSYNIDNDIMLIKLSKPATLNTYVQPVALPTS--CAPAGTMCTVSGWGNTMSSTADSNKLQCLNIPILSYSDCNNSY- 171
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYs 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1UTL_M      172 -PGMITNAMFCAGYLEGGKDSCQGDSGGPVVCN----GELQGVVSWGYGCAEPGNPGVYAKVCIFNDWLTST 238
Cdd:cd00190 161 yGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-234 6.18e-108

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: 310.38  E-value: 6.18e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M          20 KIVGGYECKPYSQPHQVSL--NSGYHFCGGSLVNENWVVSAAHC----YKSRVEVRLGEHNIKVtEGSEQFISSSRVIRH 93
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqyGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSS-GEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M          94 PNYSSYNIDNDIMLIKLSKPATLNTYVQPVALPTS--CAPAGTMCTVSGWGNTM-SSTADSNKLQCLNIPILSYSDCNNS 170
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1UTL_M         171 YPGM--ITNAMFCAGYLEGGKDSCQGDSGGPVVCN---GELQGVVSWGYGCAEPGNPGVYAKVCIFNDW 234
Cdd:smart00020 160 YSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
21-235 3.32e-95

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 277.79  E-value: 3.32e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M         21 IVGGYECKPYSQPHQVSLN--SGYHFCGGSLVNENWVVSAAHCYKSR--VEVRLGEHNIKVTEGSEQFISSSRVIRHPNY 96
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlsSGKHFCGGSLISENWVLTAAHCVSGAsdVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M         97 SSYNIDNDIMLIKLSKPATLNTYVQPVALPTSCA--PAGTMCTVSGWGNTmSSTADSNKLQCLNIPILSYSDCNNSYPGM 174
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGNT-KTLGPSDTLQEVTVPVVSRETCRSAYGGT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
1UTL_M        175 ITNAMFCAGYleGGKDSCQGDSGGPVVC-NGELQGVVSWGYGCAEPGNPGVYAKVCIFNDWL 235
Cdd:pfam00089 160 VTDTMICAGA--GGKDACQGDSGGPLVCsDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-241 2.10e-70

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 216.44  E-value: 2.10e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M        1 MISLVFVLLIGAAFATEDDKIVGGYECKPYSQPHQVSLNS----GYHFCGGSLVNENWVVSAAHCY----KSRVEVRLGE 72
Cdd:COG5640  11 AAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSsngpSGQFCGGTLIAPRWVLTAAHCVdgdgPSDLRVVIGS 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M       73 HNIKVTEGseQFISSSRVIRHPNYSSYNIDNDIMLIKLSKPATLNTYVqPVALPTSCAPAGTMCTVSGWGNTMSSTAD-S 151
Cdd:COG5640  91 TDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPA-PLATSADAAAPGTPATVAGWGRTSEGPGSqS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M      152 NKLQCLNIPILSYSDCNnSYPGMITNAMFCAGYLEGGKDSCQGDSGGPVV----CNGELQGVVSWGYGCAEPGNPGVYAK 227
Cdd:COG5640 168 GTLRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTR 246
                       250
                ....*....|....
1UTL_M      228 VCIFNDWLTSTMAS 241
Cdd:COG5640 247 VSAYRDWIKSTAGG 260
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
35-225 3.77e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 57.38  E-value: 3.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M       35 QVSLNSGYHFCGGSLVNENWVVSAAHC--------YKSRVEVRLGEHNikvteGSEQFISSSRVIRHPNY-SSYNIDNDI 105
Cdd:COG3591   4 RLETDGGGGVCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWvASGDAGYDY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UTL_M      106 MLIKLSKPATLNTYVQPVALPTScAPAGTMCTVSGwgntmsstadsnklqclnipilsysdcnnsYPG--MITNAMFCAG 183
Cdd:COG3591  79 ALLRLDEPLGDTTGWLGLAFNDA-PLAGEPVTIIG------------------------------YPGdrPKDLSLDCSG 127
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
1UTL_M      184 YLEGGK--------DSCQGDSGGPVV----CNGELQGVVSWGYgcAEPGNPGVY 225
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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