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Conserved domains on  [gi|81912853|sp|Q80WM7|]
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RecName: Full=Serine protease 33; AltName: Full=Tryptase-6; Short=mT6; 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 ...
34-272 1.89e-89

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: 265.29  E-value: 1.89e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853  34 IVGGRDAQDGEWPWQTSIQHR-GAHVCGGSLIAPQWVLTAGHCFPRRVwPSEYSVLLGALSLDVRSSHELLVPVLRVLLP 112
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853 113 PDYSEDEARGDLALLQLRHPVSLSTRIQPVCLPAPGSHPPPGSPCWVTGWGSLSPGVPLPkgRPLQGVRVPLLDSRACDR 192
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP--DVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853 193 LYHVGANVPqgerivlPGNLCAGYRRGHKDACQGDSGGPLTCMESGHWVLVGVVSWGKGCALPNRPGVYTNVAKYSPWIQ 272
Cdd:cd00190 158 AYSYGGTIT-------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
34-272 1.89e-89

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: 265.29  E-value: 1.89e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853  34 IVGGRDAQDGEWPWQTSIQHR-GAHVCGGSLIAPQWVLTAGHCFPRRVwPSEYSVLLGALSLDVRSSHELLVPVLRVLLP 112
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853 113 PDYSEDEARGDLALLQLRHPVSLSTRIQPVCLPAPGSHPPPGSPCWVTGWGSLSPGVPLPkgRPLQGVRVPLLDSRACDR 192
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP--DVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853 193 LYHVGANVPqgerivlPGNLCAGYRRGHKDACQGDSGGPLTCMESGHWVLVGVVSWGKGCALPNRPGVYTNVAKYSPWIQ 272
Cdd:cd00190 158 AYSYGGTIT-------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
33-271 5.35e-83

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: 248.75  E-value: 5.35e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853     33 RIVGGRDAQDGEWPWQTSIQHRG-AHVCGGSLIAPQWVLTAGHCFPRRVwPSEYSVLLGALSLdVRSSHELLVPVLRVLL 111
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSD-PSNIRVRLGSHDL-SSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853    112 PPDYSEDEARGDLALLQLRHPVSLSTRIQPVCLPAPGSHPPPGSPCWVTGWGSLSPGVPlPKGRPLQGVRVPLLDSRACD 191
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853    192 RLYhvganvpQGERIVLPGNLCAGYRRGHKDACQGDSGGPLTCmESGHWVLVGVVSWGKGCALPNRPGVYTNVAKYSPWI 271
Cdd:smart00020 158 RAY-------SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
34-271 1.41e-64

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 201.52  E-value: 1.41e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853    34 IVGGRDAQDGEWPWQTSIQHR-GAHVCGGSLIAPQWVLTAGHCFPRRvwpSEYSVLLGALSLDVRSSHELLVPVLRVLLP 112
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA---SDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853   113 PDYSEDEARGDLALLQLRHPVSLSTRIQPVCLPAPGSHPPPGSPCWVTGWGSLSPGVPlpkGRPLQGVRVPLLDSRACDR 192
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81912853   193 LYHVGanvpqgeriVLPGNLCAGYrrGHKDACQGDSGGPLTCMesgHWVLVGVVSWGKGCALPNRPGVYTNVAKYSPWI 271
Cdd:pfam00089 155 AYGGT---------VTDTMICAGA--GGKDACQGDSGGPLVCS---DGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
23-275 4.00e-64

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 201.80  E-value: 4.00e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853  23 AACGQPRMSSRIVGGRDAQDGEWPWQTSIQHRG---AHVCGGSLIAPQWVLTAGHCFPRRVwPSEYSVLLGalSLDVRSS 99
Cdd:COG5640  20 AAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIG--STDLSTS 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853 100 HELLVPVLRVLLPPDYSEDEARGDLALLQLRHPVslsTRIQPVCLPAPGSHPPPGSPCWVTGWGSLSPGVPLPKGRpLQG 179
Cdd:COG5640  97 GGTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGT-LRK 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853 180 VRVPLLDSRACDRLyhvganvpqgERIVLPGNLCAGYRRGHKDACQGDSGGPLTCMESGHWVLVGVVSWGKGCALPNRPG 259
Cdd:COG5640 173 ADVPVVSDATCAAY----------GGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPG 242
                       250
                ....*....|....*.
gi 81912853 260 VYTNVAKYSPWIQARL 275
Cdd:COG5640 243 VYTRVSAYRDWIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
34-272 1.89e-89

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: 265.29  E-value: 1.89e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853  34 IVGGRDAQDGEWPWQTSIQHR-GAHVCGGSLIAPQWVLTAGHCFPRRVwPSEYSVLLGALSLDVRSSHELLVPVLRVLLP 112
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853 113 PDYSEDEARGDLALLQLRHPVSLSTRIQPVCLPAPGSHPPPGSPCWVTGWGSLSPGVPLPkgRPLQGVRVPLLDSRACDR 192
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP--DVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853 193 LYHVGANVPqgerivlPGNLCAGYRRGHKDACQGDSGGPLTCMESGHWVLVGVVSWGKGCALPNRPGVYTNVAKYSPWIQ 272
Cdd:cd00190 158 AYSYGGTIT-------DNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
33-271 5.35e-83

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: 248.75  E-value: 5.35e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853     33 RIVGGRDAQDGEWPWQTSIQHRG-AHVCGGSLIAPQWVLTAGHCFPRRVwPSEYSVLLGALSLdVRSSHELLVPVLRVLL 111
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSD-PSNIRVRLGSHDL-SSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853    112 PPDYSEDEARGDLALLQLRHPVSLSTRIQPVCLPAPGSHPPPGSPCWVTGWGSLSPGVPlPKGRPLQGVRVPLLDSRACD 191
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853    192 RLYhvganvpQGERIVLPGNLCAGYRRGHKDACQGDSGGPLTCmESGHWVLVGVVSWGKGCALPNRPGVYTNVAKYSPWI 271
Cdd:smart00020 158 RAY-------SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
34-271 1.41e-64

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 201.52  E-value: 1.41e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853    34 IVGGRDAQDGEWPWQTSIQHR-GAHVCGGSLIAPQWVLTAGHCFPRRvwpSEYSVLLGALSLDVRSSHELLVPVLRVLLP 112
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA---SDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853   113 PDYSEDEARGDLALLQLRHPVSLSTRIQPVCLPAPGSHPPPGSPCWVTGWGSLSPGVPlpkGRPLQGVRVPLLDSRACDR 192
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81912853   193 LYHVGanvpqgeriVLPGNLCAGYrrGHKDACQGDSGGPLTCMesgHWVLVGVVSWGKGCALPNRPGVYTNVAKYSPWI 271
Cdd:pfam00089 155 AYGGT---------VTDTMICAGA--GGKDACQGDSGGPLVCS---DGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
23-275 4.00e-64

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 201.80  E-value: 4.00e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853  23 AACGQPRMSSRIVGGRDAQDGEWPWQTSIQHRG---AHVCGGSLIAPQWVLTAGHCFPRRVwPSEYSVLLGalSLDVRSS 99
Cdd:COG5640  20 AAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIG--STDLSTS 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853 100 HELLVPVLRVLLPPDYSEDEARGDLALLQLRHPVslsTRIQPVCLPAPGSHPPPGSPCWVTGWGSLSPGVPLPKGRpLQG 179
Cdd:COG5640  97 GGTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGT-LRK 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853 180 VRVPLLDSRACDRLyhvganvpqgERIVLPGNLCAGYRRGHKDACQGDSGGPLTCMESGHWVLVGVVSWGKGCALPNRPG 259
Cdd:COG5640 173 ADVPVVSDATCAAY----------GGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPG 242
                       250
                ....*....|....*.
gi 81912853 260 VYTNVAKYSPWIQARL 275
Cdd:COG5640 243 VYTRVSAYRDWIKSTA 258
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
54-249 4.31e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 55.07  E-value: 4.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853  54 RGAHVCGGSLIAPQWVLTAGHCF---PRRVWPSEYSVLLGAlsldvRSSHELLVPVLRVLLPPDYSEDEARG-DLALLQL 129
Cdd:COG3591   9 GGGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGY-----NGGPYGTATATRFRVPPGWVASGDAGyDYALLRL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853 130 RHPVSLSTRIQPVclpAPGSHPPPGSPCWVTGWgslspgvplPKGRPLQGVRvplldSRACDRLYhvganvPQGERIVLP 209
Cdd:COG3591  84 DEPLGDTTGWLGL---AFNDAPLAGEPVTIIGY---------PGDRPKDLSL-----DCSGRVTG------VQGNRLSYD 140
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 81912853 210 GnlcagyrrghkDACQGDSGGPLTCMESGHWVLVGVVSWG 249
Cdd:COG3591 141 C-----------DTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
45-145 2.41e-05

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: 42.53  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912853    45 WPWQTSIQHRGAHVCGGSLIAPQWVLTAGHCFPRRVWPSEY-SVLLGALS--LDVRSSHEllvpvlrVLLPPDYSEDEAR 121
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYiSVVLGGAKtlKSIEGPYE-------QIVRVDCRHDIPE 73
                          90       100
                  ....*....|....*....|....
gi 81912853   122 GDLALLQLRHPVSLSTRIQPVCLP 145
Cdd:pfam09342  74 SEISLLHLASPASFSNHVLPTFVP 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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