NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1872048497|ref|NP_001372391|]
View 

serine protease 33 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 ...
37-275 8.46e-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: 294.18  E-value: 8.46e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497  37 IVGGRDGRDGEWPWQASIQHR-GAHVCGGSLIAPQWVLTAAHCFPRRAlPAEYRVRLGALRLGSTSPRTLSVPVRRVLLP 115
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497 116 PDYSEDGARGDLALLQLRRPVPLSARVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVPLPEWrpLQGVRVPLLDSRTCDG 195
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDV--LQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497 196 LYHVGadvpqaeRIVLPGSLCAGYPQGHKDACQGDSGGPLTCLQSGSWVLVGVVSWGKGCALPNRPGVYTSVATYSPWIQ 275
Cdd:cd00190   158 AYSYG-------GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
37-275 8.46e-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: 294.18  E-value: 8.46e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497  37 IVGGRDGRDGEWPWQASIQHR-GAHVCGGSLIAPQWVLTAAHCFPRRAlPAEYRVRLGALRLGSTSPRTLSVPVRRVLLP 115
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497 116 PDYSEDGARGDLALLQLRRPVPLSARVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVPLPEWrpLQGVRVPLLDSRTCDG 195
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDV--LQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497 196 LYHVGadvpqaeRIVLPGSLCAGYPQGHKDACQGDSGGPLTCLQSGSWVLVGVVSWGKGCALPNRPGVYTSVATYSPWIQ 275
Cdd:cd00190   158 AYSYG-------GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
36-274 1.24e-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: 278.41  E-value: 1.24e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497   36 RIVGGRDGRDGEWPWQASIQHRG-AHVCGGSLIAPQWVLTAAHCFPRRAlPAEYRVRLGALRLGSTSPRTLsVPVRRVLL 114
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSD-PSNIRVRLGSHDLSSGEEGQV-IKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497  115 PPDYSEDGARGDLALLQLRRPVPLSARVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVP-LPEWrpLQGVRVPLLDSRTC 193
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGsLPDT--LQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497  194 DGLYHVGadvpqaeRIVLPGSLCAGYPQGHKDACQGDSGGPLTClQSGSWVLVGVVSWGKGCALPNRPGVYTSVATYSPW 273
Cdd:smart00020 157 RRAYSGG-------GAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228

                   .
gi 1872048497  274 I 274
Cdd:smart00020 229 I 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
26-278 2.32e-74

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 228.00  E-value: 2.32e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497  26 AACGQPRMSSRIVGGRDGRDGEWPWQASIQHRG---AHVCGGSLIAPQWVLTAAHCFPRRAlPAEYRVRLGALRLGSTSP 102
Cdd:COG5640    20 AAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497 103 RTlsVPVRRVLLPPDYSEDGARGDLALLQLRRPVPlsaRVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVP-LPEWrpLQ 181
Cdd:COG5640    99 TV--VKVARIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGsQSGT--LR 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497 182 GVRVPLLDSRTCDGLyhvgadvpqaERIVLPGSLCAGYPQGHKDACQGDSGGPLTCLQSGSWVLVGVVSWGKGCALPNRP 261
Cdd:COG5640   172 KADVPVVSDATCAAY----------GGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYP 241
                         250
                  ....*....|....*..
gi 1872048497 262 GVYTSVATYSPWIQARV 278
Cdd:COG5640   242 GVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
37-274 2.29e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 221.55  E-value: 2.29e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497  37 IVGGRDGRDGEWPWQASIQHR-GAHVCGGSLIAPQWVLTAAHCFPRRAlpaEYRVRLGALRLGSTSPRTLSVPVRRVLLP 115
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGAS---DVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497 116 PDYSEDGARGDLALLQLRRPVPLSARVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVPLpewRPLQGVRVPLLDSRTCDG 195
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPS---DTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1872048497 196 LYHVGadvpqaeriVLPGSLCAGYpqGHKDACQGDSGGPLTCLQSgswVLVGVVSWGKGCALPNRPGVYTSVATYSPWI 274
Cdd:pfam00089 155 AYGGT---------VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
37-275 8.46e-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: 294.18  E-value: 8.46e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497  37 IVGGRDGRDGEWPWQASIQHR-GAHVCGGSLIAPQWVLTAAHCFPRRAlPAEYRVRLGALRLGSTSPRTLSVPVRRVLLP 115
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497 116 PDYSEDGARGDLALLQLRRPVPLSARVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVPLPEWrpLQGVRVPLLDSRTCDG 195
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDV--LQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497 196 LYHVGadvpqaeRIVLPGSLCAGYPQGHKDACQGDSGGPLTCLQSGSWVLVGVVSWGKGCALPNRPGVYTSVATYSPWIQ 275
Cdd:cd00190   158 AYSYG-------GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
36-274 1.24e-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: 278.41  E-value: 1.24e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497   36 RIVGGRDGRDGEWPWQASIQHRG-AHVCGGSLIAPQWVLTAAHCFPRRAlPAEYRVRLGALRLGSTSPRTLsVPVRRVLL 114
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSD-PSNIRVRLGSHDLSSGEEGQV-IKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497  115 PPDYSEDGARGDLALLQLRRPVPLSARVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVP-LPEWrpLQGVRVPLLDSRTC 193
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGsLPDT--LQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497  194 DGLYHVGadvpqaeRIVLPGSLCAGYPQGHKDACQGDSGGPLTClQSGSWVLVGVVSWGKGCALPNRPGVYTSVATYSPW 273
Cdd:smart00020 157 RRAYSGG-------GAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228

                   .
gi 1872048497  274 I 274
Cdd:smart00020 229 I 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
26-278 2.32e-74

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 228.00  E-value: 2.32e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497  26 AACGQPRMSSRIVGGRDGRDGEWPWQASIQHRG---AHVCGGSLIAPQWVLTAAHCFPRRAlPAEYRVRLGALRLGSTSP 102
Cdd:COG5640    20 AAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497 103 RTlsVPVRRVLLPPDYSEDGARGDLALLQLRRPVPlsaRVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVP-LPEWrpLQ 181
Cdd:COG5640    99 TV--VKVARIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGsQSGT--LR 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497 182 GVRVPLLDSRTCDGLyhvgadvpqaERIVLPGSLCAGYPQGHKDACQGDSGGPLTCLQSGSWVLVGVVSWGKGCALPNRP 261
Cdd:COG5640   172 KADVPVVSDATCAAY----------GGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYP 241
                         250
                  ....*....|....*..
gi 1872048497 262 GVYTSVATYSPWIQARV 278
Cdd:COG5640   242 GVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
37-274 2.29e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 221.55  E-value: 2.29e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497  37 IVGGRDGRDGEWPWQASIQHR-GAHVCGGSLIAPQWVLTAAHCFPRRAlpaEYRVRLGALRLGSTSPRTLSVPVRRVLLP 115
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGAS---DVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497 116 PDYSEDGARGDLALLQLRRPVPLSARVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVPLpewRPLQGVRVPLLDSRTCDG 195
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPS---DTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1872048497 196 LYHVGadvpqaeriVLPGSLCAGYpqGHKDACQGDSGGPLTCLQSgswVLVGVVSWGKGCALPNRPGVYTSVATYSPWI 274
Cdd:pfam00089 155 AYGGT---------VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
57-252 1.33e-14

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 70.48  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497  57 RGAHVCGGSLIAPQWVLTAAHCF---PRRALPAEYRVRLGALRlgstsPRTLSVPVRRVLLPPDYSEDGARG-DLALLQL 132
Cdd:COG3591     9 GGGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGDAGyDYALLRL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497 133 RRPVPLSARVQPVclpVPGARPPPGTPCRVTGWGSLRPGVPlpewrplqgvrvplldSRTCDGLyhvgADVPQAERIVLP 212
Cdd:COG3591    84 DEPLGDTTGWLGL---AFNDAPLAGEPVTIIGYPGDRPKDL----------------SLDCSGR----VTGVQGNRLSYD 140
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1872048497 213 GslcagypqghkDACQGDSGGPLTCLQSGSWVLVGVVSWG 252
Cdd:COG3591   141 C-----------DTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
48-148 7.68e-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: 44.08  E-value: 7.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1872048497  48 WPWQASIQHRGAHVCGGSLIAPQWVLTAAHCFPRRALPAEY-RVRLGalrlGSTSPRTLSVP---VRRVllppDYSEDGA 123
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYiSVVLG----GAKTLKSIEGPyeqIVRV----DCRHDIP 72
                          90       100
                  ....*....|....*....|....*
gi 1872048497 124 RGDLALLQLRRPVPLSARVQPVCLP 148
Cdd:pfam09342  73 ESEISLLHLASPASFSNHVLPTFVP 97
 
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