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Conserved domains on  [gi|2462550111|ref|XP_054169579|]
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brain-specific serine protease 4 isoform X3 [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

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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 ...
158-396 6.04e-96

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: 287.25  E-value: 6.04e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 158 VVGGEDSTDSEWPWIVSIQ-KNGTHHCAGSLLTSRWVITAAHCFKDNlnKPYLFSVLLGAWQLGNPGSRSQKVGVAWVEP 236
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS--APSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 237 HPVYSWKeGACADIALVRLERSIQFSERVLPICLPDASIHLPPNTHCWISGWGSIQDGVPlpHPQTLQKLKVPIIDSEVC 316
Cdd:cd00190    79 HPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP--LPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 317 SHLYWRGagqGPITEDMLCAGYLEGERDACLGDSGGPLMCQVDGAWLLAGIISWGEGCAERNRPGVYISLSAHRSWVEKI 396
Cdd:cd00190   156 KRAYSYG---GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
158-396 6.04e-96

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: 287.25  E-value: 6.04e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 158 VVGGEDSTDSEWPWIVSIQ-KNGTHHCAGSLLTSRWVITAAHCFKDNlnKPYLFSVLLGAWQLGNPGSRSQKVGVAWVEP 236
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS--APSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 237 HPVYSWKeGACADIALVRLERSIQFSERVLPICLPDASIHLPPNTHCWISGWGSIQDGVPlpHPQTLQKLKVPIIDSEVC 316
Cdd:cd00190    79 HPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP--LPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 317 SHLYWRGagqGPITEDMLCAGYLEGERDACLGDSGGPLMCQVDGAWLLAGIISWGEGCAERNRPGVYISLSAHRSWVEKI 396
Cdd:cd00190   156 KRAYSYG---GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
157-393 1.49e-91

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: 276.10  E-value: 1.49e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111  157 RVVGGEDSTDSEWPWIVSIQ-KNGTHHCAGSLLTSRWVITAAHCFKDNlnKPYLFSVLLGAWQLGNPGSrSQKVGVAWVE 235
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS--DPSNIRVRLGSHDLSSGEE-GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111  236 PHPVYSwKEGACADIALVRLERSIQFSERVLPICLPDASIHLPPNTHCWISGWGSIQDGVPlPHPQTLQKLKVPIIDSEV 315
Cdd:smart00020  78 IHPNYN-PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462550111  316 CSHLYWrgaGQGPITEDMLCAGYLEGERDACLGDSGGPLMCQvDGAWLLAGIISWGEGCAERNRPGVYISLSAHRSWV 393
Cdd:smart00020 156 CRRAYS---GGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
158-393 3.02e-66

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 210.76  E-value: 3.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 158 VVGGEDSTDSEWPWIVSIQ-KNGTHHCAGSLLTSRWVITAAHCFKDNLNkpylFSVLLGAWQLGNPGSRSQKVGVAWVEP 236
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASD----VKVVLGAHNIVLREGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 237 HPVYSWkEGACADIALVRLERSIQFSERVLPICLPDASIHLPPNTHCWISGWGSIQDGVPlphPQTLQKLKVPIIDSEVC 316
Cdd:pfam00089  77 HPNYNP-DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462550111 317 shlywRGAGQGPITEDMLCAGYleGERDACLGDSGGPLMCqvdGAWLLAGIISWGEGCAERNRPGVYISLSAHRSWV 393
Cdd:pfam00089 153 -----RSAYGGTVTDTMICAGA--GGKDACQGDSGGPLVC---SDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
157-399 6.67e-61

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 198.33  E-value: 6.67e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 157 RVVGGEDSTDSEWPWIVSIQKNG---THHCAGSLLTSRWVITAAHCFKDNLNKPYlfSVLLGAWQLGNpgSRSQKVGVAW 233
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDL--RVVIGSTDLST--SGGTVVKVAR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 234 VEPHPVYSWKEGAcADIALVRLERSIQFSErvlPICLPDASIHLPPNTHCWISGWGSIQDGVPLPhPQTLQKLKVPIIDS 313
Cdd:COG5640   106 IVVHPDYDPATPG-NDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPGSQ-SGTLRKADVPVVSD 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 314 EVCShlywrgAGQGPITEDMLCAGYLEGERDACLGDSGGPLMCQVDGAWLLAGIISWGEGCAERNRPGVYISLSAHRSWV 393
Cdd:COG5640   181 ATCA------AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254

                  ....*.
gi 2462550111 394 EKIVQG 399
Cdd:COG5640   255 KSTAGG 260
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
158-396 6.04e-96

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: 287.25  E-value: 6.04e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 158 VVGGEDSTDSEWPWIVSIQ-KNGTHHCAGSLLTSRWVITAAHCFKDNlnKPYLFSVLLGAWQLGNPGSRSQKVGVAWVEP 236
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS--APSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 237 HPVYSWKeGACADIALVRLERSIQFSERVLPICLPDASIHLPPNTHCWISGWGSIQDGVPlpHPQTLQKLKVPIIDSEVC 316
Cdd:cd00190    79 HPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP--LPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 317 SHLYWRGagqGPITEDMLCAGYLEGERDACLGDSGGPLMCQVDGAWLLAGIISWGEGCAERNRPGVYISLSAHRSWVEKI 396
Cdd:cd00190   156 KRAYSYG---GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
157-393 1.49e-91

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: 276.10  E-value: 1.49e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111  157 RVVGGEDSTDSEWPWIVSIQ-KNGTHHCAGSLLTSRWVITAAHCFKDNlnKPYLFSVLLGAWQLGNPGSrSQKVGVAWVE 235
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS--DPSNIRVRLGSHDLSSGEE-GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111  236 PHPVYSwKEGACADIALVRLERSIQFSERVLPICLPDASIHLPPNTHCWISGWGSIQDGVPlPHPQTLQKLKVPIIDSEV 315
Cdd:smart00020  78 IHPNYN-PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462550111  316 CSHLYWrgaGQGPITEDMLCAGYLEGERDACLGDSGGPLMCQvDGAWLLAGIISWGEGCAERNRPGVYISLSAHRSWV 393
Cdd:smart00020 156 CRRAYS---GGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
158-393 3.02e-66

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 210.76  E-value: 3.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 158 VVGGEDSTDSEWPWIVSIQ-KNGTHHCAGSLLTSRWVITAAHCFKDNLNkpylFSVLLGAWQLGNPGSRSQKVGVAWVEP 236
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASD----VKVVLGAHNIVLREGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 237 HPVYSWkEGACADIALVRLERSIQFSERVLPICLPDASIHLPPNTHCWISGWGSIQDGVPlphPQTLQKLKVPIIDSEVC 316
Cdd:pfam00089  77 HPNYNP-DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462550111 317 shlywRGAGQGPITEDMLCAGYleGERDACLGDSGGPLMCqvdGAWLLAGIISWGEGCAERNRPGVYISLSAHRSWV 393
Cdd:pfam00089 153 -----RSAYGGTVTDTMICAGA--GGKDACQGDSGGPLVC---SDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
157-399 6.67e-61

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 198.33  E-value: 6.67e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 157 RVVGGEDSTDSEWPWIVSIQKNG---THHCAGSLLTSRWVITAAHCFKDNLNKPYlfSVLLGAWQLGNpgSRSQKVGVAW 233
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDL--RVVIGSTDLST--SGGTVVKVAR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 234 VEPHPVYSWKEGAcADIALVRLERSIQFSErvlPICLPDASIHLPPNTHCWISGWGSIQDGVPLPhPQTLQKLKVPIIDS 313
Cdd:COG5640   106 IVVHPDYDPATPG-NDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPGSQ-SGTLRKADVPVVSD 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 314 EVCShlywrgAGQGPITEDMLCAGYLEGERDACLGDSGGPLMCQVDGAWLLAGIISWGEGCAERNRPGVYISLSAHRSWV 393
Cdd:COG5640   181 ATCA------AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254

                  ....*.
gi 2462550111 394 EKIVQG 399
Cdd:COG5640   255 KSTAGG 260
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
178-384 1.93e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 56.99  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 178 NGTHHCAGSLLTSRWVITAAHCFKDNLNKPYLFSVLLGAWQLGNPGSRsqkVGVAWVEPHPVYSWKEGACADIALVRLER 257
Cdd:COG3591     9 GGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGPYGT---ATATRFRVPPGWVASGDAGYDYALLRLDE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 258 SIQFSERVLPIclpDASIHLPPNTHCWISGWgsiqdgvPLPHPQTLqklkvpiidsevcshlywRGAGQGPITEdmLCAG 337
Cdd:COG3591    86 PLGDTTGWLGL---AFNDAPLAGEPVTIIGY-------PGDRPKDL------------------SLDCSGRVTG--VQGN 135
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462550111 338 YLEGERDACLGDSGGPLMCQVDGAWLLAGIISWGEgcAERNRPGVYI 384
Cdd:COG3591   136 RLSYDCDTTGGSSGSPVLDDSDGGGRVVGVHSAGG--ADRANTGVRL 180
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
169-283 1.15e-08

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: 52.94  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550111 169 WPWIVSIQKNGTHHCAGSLLTSRWVITAAHCFKD-NLNKPYLfSVLLGAWQ--LGNPGSRSQKVGVAWVEPHPVyswkeg 245
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDtNLRHQYI-SVVLGGAKtlKSIEGPYEQIVRVDCRHDIPE------ 73
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462550111 246 acADIALVRLERSIQFSERVLPICLPDASIHLPPNTHC 283
Cdd:pfam09342  74 --SEISLLHLASPASFSNHVLPTFVPETRNENEKDNEC 109
 
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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