NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1216866469|ref|NP_001340540|]
View 

serine protease 48 isoform 2 precursor [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
28-265 1.56e-85

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: 257.98  E-value: 1.56e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469  28 VVGGQDAAAGRWPWQVSLHF-DHNFICGGSLVSERLILTAAHCIQPTwTTFSYTVWLGSITVGDSRKRVKYY-VSKIVIH 105
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIkVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469 106 PKYQDTTA--DVALLKLSSQVTFTSAILPICLPSVTKQLAIPPFCWVTGWGKVKESSDRDYHsaLQEAEVPIIDRQACEQ 183
Cdd:cd00190    80 PNYNPSTYdnDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDV--LQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469 184 LYNPIGiflpalepVIKEDKICAGDTQNMKDSCKGDSGGPLSCHIDGVWIQTGVVSWGLECG-KSLPGVYTNVIYYQKWI 262
Cdd:cd00190   158 AYSYGG--------TITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCArPNYPGVYTRVSSYLDWI 229

                  ...
gi 1216866469 263 NAT 265
Cdd:cd00190   230 QKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
28-265 1.56e-85

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: 257.98  E-value: 1.56e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469  28 VVGGQDAAAGRWPWQVSLHF-DHNFICGGSLVSERLILTAAHCIQPTwTTFSYTVWLGSITVGDSRKRVKYY-VSKIVIH 105
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIkVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469 106 PKYQDTTA--DVALLKLSSQVTFTSAILPICLPSVTKQLAIPPFCWVTGWGKVKESSDRDYHsaLQEAEVPIIDRQACEQ 183
Cdd:cd00190    80 PNYNPSTYdnDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDV--LQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469 184 LYNPIGiflpalepVIKEDKICAGDTQNMKDSCKGDSGGPLSCHIDGVWIQTGVVSWGLECG-KSLPGVYTNVIYYQKWI 262
Cdd:cd00190   158 AYSYGG--------TITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCArPNYPGVYTRVSSYLDWI 229

                  ...
gi 1216866469 263 NAT 265
Cdd:cd00190   230 QKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
27-262 2.46e-85

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: 257.22  E-value: 2.46e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469   27 RVVGGQDAAAGRWPWQVSLHF-DHNFICGGSLVSERLILTAAHCIQPTwTTFSYTVWLGSITVGDSRKRVKYYVSKIVIH 105
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469  106 PKYQDTTA--DVALLKLSSQVTFTSAILPICLPSVTKQLAIPPFCWVTGWGKVKESSDRdYHSALQEAEVPIIDRQACEQ 183
Cdd:smart00020  80 PNYNPSTYdnDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGS-LPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469  184 LYNPIgiflpalePVIKEDKICAGDTQNMKDSCKGDSGGPLSCHiDGVWIQTGVVSWGLECG-KSLPGVYTNVIYYQKWI 262
Cdd:smart00020 159 AYSGG--------GAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCArPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
4-266 8.24e-68

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 213.74  E-value: 8.24e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469   4 AGCAFTLLLLLGISVCGQPVYSSRVVGGQDAAAGRWPWQVSLHFD---HNFICGGSLVSERLILTAAHCIQPTwTTFSYT 80
Cdd:COG5640     7 LAALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469  81 VWLGSITVGDSRKRVkYYVSKIVIHPKYQDTT--ADVALLKLSSQVTFTSailPICLPSVTKQLAIPPFCWVTGWGKVKE 158
Cdd:COG5640    86 VVIGSTDLSTSGGTV-VKVARIVVHPDYDPATpgNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469 159 SSDrDYHSALQEAEVPIIDRQACEQLYNPIGiflpalepvikEDKICAGDTQNMKDSCKGDSGGPLSCHIDGVWIQTGVV 238
Cdd:COG5640   162 GPG-SQSGTLRKADVPVVSDATCAAYGGFDG-----------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVV 229
                         250       260
                  ....*....|....*....|....*....
gi 1216866469 239 SWGL-ECGKSLPGVYTNVIYYQKWINATI 266
Cdd:COG5640   230 SWGGgPCAAGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
28-262 1.79e-61

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 195.74  E-value: 1.79e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469  28 VVGGQDAAAGRWPWQVSLHFDHNF-ICGGSLVSERLILTAAHCIQptwTTFSYTVWLGSITVGDSRKRV-KYYVSKIVIH 105
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKhFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEqKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469 106 PKYQDTTA--DVALLKLSSQVTFTSAILPICLPSVTKQLAIPPFCWVTGWGKVKESSDRDYhsaLQEAEVPIIDRQACEQ 183
Cdd:pfam00089  78 PNYNPDTLdnDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDT---LQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469 184 LYNpigiflpalePVIKEDKICAGDTQnmKDSCKGDSGGPLSCHiDGvwIQTGVVSWGLECG-KSLPGVYTNVIYYQKWI 262
Cdd:pfam00089 155 AYG----------GTVTDTMICAGAGG--KDACQGDSGGPLVCS-DG--ELIGIVSWGYGCAsGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
28-265 1.56e-85

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: 257.98  E-value: 1.56e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469  28 VVGGQDAAAGRWPWQVSLHF-DHNFICGGSLVSERLILTAAHCIQPTwTTFSYTVWLGSITVGDSRKRVKYY-VSKIVIH 105
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIkVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469 106 PKYQDTTA--DVALLKLSSQVTFTSAILPICLPSVTKQLAIPPFCWVTGWGKVKESSDRDYHsaLQEAEVPIIDRQACEQ 183
Cdd:cd00190    80 PNYNPSTYdnDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDV--LQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469 184 LYNPIGiflpalepVIKEDKICAGDTQNMKDSCKGDSGGPLSCHIDGVWIQTGVVSWGLECG-KSLPGVYTNVIYYQKWI 262
Cdd:cd00190   158 AYSYGG--------TITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCArPNYPGVYTRVSSYLDWI 229

                  ...
gi 1216866469 263 NAT 265
Cdd:cd00190   230 QKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
27-262 2.46e-85

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: 257.22  E-value: 2.46e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469   27 RVVGGQDAAAGRWPWQVSLHF-DHNFICGGSLVSERLILTAAHCIQPTwTTFSYTVWLGSITVGDSRKRVKYYVSKIVIH 105
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469  106 PKYQDTTA--DVALLKLSSQVTFTSAILPICLPSVTKQLAIPPFCWVTGWGKVKESSDRdYHSALQEAEVPIIDRQACEQ 183
Cdd:smart00020  80 PNYNPSTYdnDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGS-LPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469  184 LYNPIgiflpalePVIKEDKICAGDTQNMKDSCKGDSGGPLSCHiDGVWIQTGVVSWGLECG-KSLPGVYTNVIYYQKWI 262
Cdd:smart00020 159 AYSGG--------GAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCArPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
4-266 8.24e-68

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 213.74  E-value: 8.24e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469   4 AGCAFTLLLLLGISVCGQPVYSSRVVGGQDAAAGRWPWQVSLHFD---HNFICGGSLVSERLILTAAHCIQPTwTTFSYT 80
Cdd:COG5640     7 LAALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469  81 VWLGSITVGDSRKRVkYYVSKIVIHPKYQDTT--ADVALLKLSSQVTFTSailPICLPSVTKQLAIPPFCWVTGWGKVKE 158
Cdd:COG5640    86 VVIGSTDLSTSGGTV-VKVARIVVHPDYDPATpgNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469 159 SSDrDYHSALQEAEVPIIDRQACEQLYNPIGiflpalepvikEDKICAGDTQNMKDSCKGDSGGPLSCHIDGVWIQTGVV 238
Cdd:COG5640   162 GPG-SQSGTLRKADVPVVSDATCAAYGGFDG-----------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVV 229
                         250       260
                  ....*....|....*....|....*....
gi 1216866469 239 SWGL-ECGKSLPGVYTNVIYYQKWINATI 266
Cdd:COG5640   230 SWGGgPCAAGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
28-262 1.79e-61

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 195.74  E-value: 1.79e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469  28 VVGGQDAAAGRWPWQVSLHFDHNF-ICGGSLVSERLILTAAHCIQptwTTFSYTVWLGSITVGDSRKRV-KYYVSKIVIH 105
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKhFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEqKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469 106 PKYQDTTA--DVALLKLSSQVTFTSAILPICLPSVTKQLAIPPFCWVTGWGKVKESSDRDYhsaLQEAEVPIIDRQACEQ 183
Cdd:pfam00089  78 PNYNPDTLdnDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDT---LQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469 184 LYNpigiflpalePVIKEDKICAGDTQnmKDSCKGDSGGPLSCHiDGvwIQTGVVSWGLECG-KSLPGVYTNVIYYQKWI 262
Cdd:pfam00089 155 AYG----------GTVTDTMICAGAGG--KDACQGDSGGPLVCS-DG--ELIGIVSWGYGCAsGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
50-241 9.49e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 54.68  E-value: 9.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469  50 NFICGGSLVSERLILTAAHCIqptwTTFSYTVWLGSITVG---DSRKRVKYYVSKIVIHPKYQDTTA---DVALLKLSSQ 123
Cdd:COG3591    11 GGVCTGTLIGPNLVLTAGHCV----YDGAGGGWATNIVFVpgyNGGPYGTATATRFRVPPGWVASGDagyDYALLRLDEP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469 124 VTFTSAILPIclpSVTKQLAIPPFCWVTGWGkvkesSDRDYHSALQEAEvPIIDRQACEQLYNpigiflpalepvikedk 203
Cdd:COG3591    87 LGDTTGWLGL---AFNDAPLAGEPVTIIGYP-----GDRPKDLSLDCSG-RVTGVQGNRLSYD----------------- 140
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1216866469 204 iCagdtqnmkDSCKGDSGGPLSCHIDGVWIQTGVVSWG 241
Cdd:COG3591   141 -C--------DTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
39-142 7.13e-06

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: 44.46  E-value: 7.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216866469  39 WPWQVSLHFDHNFICGGSLVSERLILTAAHCIQPTWTTFSY-TVWLGSitvGDSRKRVKYYVSKIVIHPKYQDT-TADVA 116
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYiSVVLGG---AKTLKSIEGPYEQIVRVDCRHDIpESEIS 77
                          90       100
                  ....*....|....*....|....*.
gi 1216866469 117 LLKLSSQVTFTSAILPICLPSVTKQL 142
Cdd:pfam09342  78 LLHLASPASFSNHVLPTFVPETRNEN 103
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH