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Conserved domains on  [gi|212286047|sp|Q8NF86|]
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RecName: Full=Serine protease 33; AltName: Full=Serine protease EOS; Flags: Precursor

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 ...
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 212286047  37 IVGGRDGRDGEWPWQASIQHR-GAHVCGGSLIAPQWVLTAAHCFPRRAlPAEYRVRLGALRLGSTSPRTLSVPVRRVLLP 115
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212286047 116 PDYSEDGARGDLALLQLRRPVPLSARVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVPLPEWrpLQGVRVPLLDSRTCDG 195
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDV--LQEVNVPIVSNAECKR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212286047 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 212286047  37 IVGGRDGRDGEWPWQASIQHR-GAHVCGGSLIAPQWVLTAAHCFPRRAlPAEYRVRLGALRLGSTSPRTLSVPVRRVLLP 115
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212286047 116 PDYSEDGARGDLALLQLRRPVPLSARVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVPLPEWrpLQGVRVPLLDSRTCDG 195
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDV--LQEVNVPIVSNAECKR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212286047 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 212286047    36 RIVGGRDGRDGEWPWQASIQHRG-AHVCGGSLIAPQWVLTAAHCFPRRAlPAEYRVRLGALRLGSTSPRTLsVPVRRVLL 114
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSD-PSNIRVRLGSHDLSSGEEGQV-IKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212286047   115 PPDYSEDGARGDLALLQLRRPVPLSARVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVP-LPEWrpLQGVRVPLLDSRTC 193
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGsLPDT--LQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212286047   194 DGLYHVGadvpqaeRIVLPGSLCAGYPQGHKDACQGDSGGPLTClQSGSWVLVGVVSWGKGCALPNRPGVYTSVATYSPW 273
Cdd:smart00020 157 RRAYSGG-------GAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228

                   .
gi 212286047   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 212286047  26 AACGQPRMSSRIVGGRDGRDGEWPWQASIQHRG---AHVCGGSLIAPQWVLTAAHCFPRRAlPAEYRVRLGALRLGSTSP 102
Cdd:COG5640   20 AAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212286047 103 RTlsVPVRRVLLPPDYSEDGARGDLALLQLRRPVPlsaRVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVP-LPEWrpLQ 181
Cdd:COG5640   99 TV--VKVARIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGsQSGT--LR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212286047 182 GVRVPLLDSRTCDGLyhvgadvpqaERIVLPGSLCAGYPQGHKDACQGDSGGPLTCLQSGSWVLVGVVSWGKGCALPNRP 261
Cdd:COG5640  172 KADVPVVSDATCAAY----------GGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYP 241
                        250
                 ....*....|....*..
gi 212286047 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 212286047   37 IVGGRDGRDGEWPWQASIQHR-GAHVCGGSLIAPQWVLTAAHCFPRRAlpaEYRVRLGALRLGSTSPRTLSVPVRRVLLP 115
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGAS---DVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212286047  116 PDYSEDGARGDLALLQLRRPVPLSARVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVPLpewRPLQGVRVPLLDSRTCDG 195
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPS---DTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212286047  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 212286047  37 IVGGRDGRDGEWPWQASIQHR-GAHVCGGSLIAPQWVLTAAHCFPRRAlPAEYRVRLGALRLGSTSPRTLSVPVRRVLLP 115
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212286047 116 PDYSEDGARGDLALLQLRRPVPLSARVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVPLPEWrpLQGVRVPLLDSRTCDG 195
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDV--LQEVNVPIVSNAECKR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212286047 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 212286047    36 RIVGGRDGRDGEWPWQASIQHRG-AHVCGGSLIAPQWVLTAAHCFPRRAlPAEYRVRLGALRLGSTSPRTLsVPVRRVLL 114
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSD-PSNIRVRLGSHDLSSGEEGQV-IKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212286047   115 PPDYSEDGARGDLALLQLRRPVPLSARVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVP-LPEWrpLQGVRVPLLDSRTC 193
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGsLPDT--LQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212286047   194 DGLYHVGadvpqaeRIVLPGSLCAGYPQGHKDACQGDSGGPLTClQSGSWVLVGVVSWGKGCALPNRPGVYTSVATYSPW 273
Cdd:smart00020 157 RRAYSGG-------GAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228

                   .
gi 212286047   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 212286047  26 AACGQPRMSSRIVGGRDGRDGEWPWQASIQHRG---AHVCGGSLIAPQWVLTAAHCFPRRAlPAEYRVRLGALRLGSTSP 102
Cdd:COG5640   20 AAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTDLSTSGG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212286047 103 RTlsVPVRRVLLPPDYSEDGARGDLALLQLRRPVPlsaRVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVP-LPEWrpLQ 181
Cdd:COG5640   99 TV--VKVARIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGsQSGT--LR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212286047 182 GVRVPLLDSRTCDGLyhvgadvpqaERIVLPGSLCAGYPQGHKDACQGDSGGPLTCLQSGSWVLVGVVSWGKGCALPNRP 261
Cdd:COG5640  172 KADVPVVSDATCAAY----------GGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYP 241
                        250
                 ....*....|....*..
gi 212286047 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 212286047   37 IVGGRDGRDGEWPWQASIQHR-GAHVCGGSLIAPQWVLTAAHCFPRRAlpaEYRVRLGALRLGSTSPRTLSVPVRRVLLP 115
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGAS---DVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212286047  116 PDYSEDGARGDLALLQLRRPVPLSARVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVPLpewRPLQGVRVPLLDSRTCDG 195
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPS---DTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212286047  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 212286047  57 RGAHVCGGSLIAPQWVLTAAHCF---PRRALPAEYRVRLGALRlgstsPRTLSVPVRRVLLPPDYSEDGARG-DLALLQL 132
Cdd:COG3591    9 GGGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGDAGyDYALLRL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212286047 133 RRPVPLSARVQPVclpVPGARPPPGTPCRVTGWGSLRPGVPlpewrplqgvrvplldSRTCDGLyhvgADVPQAERIVLP 212
Cdd:COG3591   84 DEPLGDTTGWLGL---AFNDAPLAGEPVTIIGYPGDRPKDL----------------SLDCSGR----VTGVQGNRLSYD 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 212286047 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 212286047   48 WPWQASIQHRGAHVCGGSLIAPQWVLTAAHCFPRRALPAEY-RVRLGalrlGSTSPRTLSVP---VRRVllppDYSEDGA 123
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYiSVVLG----GAKTLKSIEGPyeqIVRV----DCRHDIP 72
                          90       100
                  ....*....|....*....|....*
gi 212286047  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.
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