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Conserved domains on  [gi|2462498706|ref|XP_054187853|]
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brain-specific serine protease 4 isoform X2 [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

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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 ...
50-288 4.81e-98

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: 288.41  E-value: 4.81e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706  50 VVGGEDSTDSEWPWIVSIQ-KNGTHHCAGSLLTSRWVITAAHCFKDNlnKPYLFSVLLGAWQLGNPGSRSQKVGVAWVEP 128
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS--APSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706 129 HPVYSWKeGACADIALVRLERSIQFSERVLPICLPDASIHLPPNTHCWISGWGSIQDGVPlpHPQTLQKLKVPIIDSEVC 208
Cdd:cd00190    79 HPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP--LPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706 209 SHLYWRGagqGPITEDMLCAGYLEGERDACLGDSGGPLMCQVDGAWLLAGIISWGEGCAERNRPGVYISLSAHRSWVEKI 288
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 ...
50-288 4.81e-98

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: 288.41  E-value: 4.81e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706  50 VVGGEDSTDSEWPWIVSIQ-KNGTHHCAGSLLTSRWVITAAHCFKDNlnKPYLFSVLLGAWQLGNPGSRSQKVGVAWVEP 128
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS--APSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706 129 HPVYSWKeGACADIALVRLERSIQFSERVLPICLPDASIHLPPNTHCWISGWGSIQDGVPlpHPQTLQKLKVPIIDSEVC 208
Cdd:cd00190    79 HPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP--LPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706 209 SHLYWRGagqGPITEDMLCAGYLEGERDACLGDSGGPLMCQVDGAWLLAGIISWGEGCAERNRPGVYISLSAHRSWVEKI 288
Cdd:cd00190   156 KRAYSYG---GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
49-285 5.88e-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: 278.02  E-value: 5.88e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706   49 RVVGGEDSTDSEWPWIVSIQ-KNGTHHCAGSLLTSRWVITAAHCFKDNlnKPYLFSVLLGAWQLGNPGSrSQKVGVAWVE 127
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS--DPSNIRVRLGSHDLSSGEE-GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706  128 PHPVYSwKEGACADIALVRLERSIQFSERVLPICLPDASIHLPPNTHCWISGWGSIQDGVPlPHPQTLQKLKVPIIDSEV 207
Cdd:smart00020  78 IHPNYN-PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462498706  208 CSHLYWrgaGQGPITEDMLCAGYLEGERDACLGDSGGPLMCQvDGAWLLAGIISWGEGCAERNRPGVYISLSAHRSWV 285
Cdd:smart00020 156 CRRAYS---GGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
50-285 4.88e-68

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 211.92  E-value: 4.88e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706  50 VVGGEDSTDSEWPWIVSIQ-KNGTHHCAGSLLTSRWVITAAHCFKDNLNkpylFSVLLGAWQLGNPGSRSQKVGVAWVEP 128
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASD----VKVVLGAHNIVLREGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706 129 HPVYSWkEGACADIALVRLERSIQFSERVLPICLPDASIHLPPNTHCWISGWGSIQDGVPlphPQTLQKLKVPIIDSEVC 208
Cdd:pfam00089  77 HPNYNP-DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462498706 209 shlywRGAGQGPITEDMLCAGYleGERDACLGDSGGPLMCqvdGAWLLAGIISWGEGCAERNRPGVYISLSAHRSWV 285
Cdd:pfam00089 153 -----RSAYGGTVTDTMICAGA--GGKDACQGDSGGPLVC---SDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
17-291 1.53e-63

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 201.80  E-value: 1.53e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706  17 TFTSLLLLASTAILNAARIPVPPAcgkpqqlNRVVGGEDSTDSEWPWIVSIQKNG---THHCAGSLLTSRWVITAAHCFK 93
Cdd:COG5640     5 RLLAALAAAALALALAAAPAADAA-------PAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706  94 DNLNKPYlfSVLLGAWQLGNpgSRSQKVGVAWVEPHPVYSWKEGAcADIALVRLERSIQFSErvlPICLPDASIHLPPNT 173
Cdd:COG5640    78 GDGPSDL--RVVIGSTDLST--SGGTVVKVARIVVHPDYDPATPG-NDIALLKLATPVPGVA---PAPLATSADAAAPGT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706 174 HCWISGWGSIQDGVPLPhPQTLQKLKVPIIDSEVCShlywrgAGQGPITEDMLCAGYLEGERDACLGDSGGPLMCQVDGA 253
Cdd:COG5640   150 PATVAGWGRTSEGPGSQ-SGTLRKADVPVVSDATCA------AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGG 222
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2462498706 254 WLLAGIISWGEGCAERNRPGVYISLSAHRSWVEKIVQG 291
Cdd:COG5640   223 WVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGG 260
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
50-288 4.81e-98

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: 288.41  E-value: 4.81e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706  50 VVGGEDSTDSEWPWIVSIQ-KNGTHHCAGSLLTSRWVITAAHCFKDNlnKPYLFSVLLGAWQLGNPGSRSQKVGVAWVEP 128
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS--APSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706 129 HPVYSWKeGACADIALVRLERSIQFSERVLPICLPDASIHLPPNTHCWISGWGSIQDGVPlpHPQTLQKLKVPIIDSEVC 208
Cdd:cd00190    79 HPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP--LPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706 209 SHLYWRGagqGPITEDMLCAGYLEGERDACLGDSGGPLMCQVDGAWLLAGIISWGEGCAERNRPGVYISLSAHRSWVEKI 288
Cdd:cd00190   156 KRAYSYG---GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
49-285 5.88e-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: 278.02  E-value: 5.88e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706   49 RVVGGEDSTDSEWPWIVSIQ-KNGTHHCAGSLLTSRWVITAAHCFKDNlnKPYLFSVLLGAWQLGNPGSrSQKVGVAWVE 127
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS--DPSNIRVRLGSHDLSSGEE-GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706  128 PHPVYSwKEGACADIALVRLERSIQFSERVLPICLPDASIHLPPNTHCWISGWGSIQDGVPlPHPQTLQKLKVPIIDSEV 207
Cdd:smart00020  78 IHPNYN-PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462498706  208 CSHLYWrgaGQGPITEDMLCAGYLEGERDACLGDSGGPLMCQvDGAWLLAGIISWGEGCAERNRPGVYISLSAHRSWV 285
Cdd:smart00020 156 CRRAYS---GGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
50-285 4.88e-68

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 211.92  E-value: 4.88e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706  50 VVGGEDSTDSEWPWIVSIQ-KNGTHHCAGSLLTSRWVITAAHCFKDNLNkpylFSVLLGAWQLGNPGSRSQKVGVAWVEP 128
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASD----VKVVLGAHNIVLREGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706 129 HPVYSWkEGACADIALVRLERSIQFSERVLPICLPDASIHLPPNTHCWISGWGSIQDGVPlphPQTLQKLKVPIIDSEVC 208
Cdd:pfam00089  77 HPNYNP-DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP---SDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462498706 209 shlywRGAGQGPITEDMLCAGYleGERDACLGDSGGPLMCqvdGAWLLAGIISWGEGCAERNRPGVYISLSAHRSWV 285
Cdd:pfam00089 153 -----RSAYGGTVTDTMICAGA--GGKDACQGDSGGPLVC---SDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
17-291 1.53e-63

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 201.80  E-value: 1.53e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706  17 TFTSLLLLASTAILNAARIPVPPAcgkpqqlNRVVGGEDSTDSEWPWIVSIQKNG---THHCAGSLLTSRWVITAAHCFK 93
Cdd:COG5640     5 RLLAALAAAALALALAAAPAADAA-------PAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706  94 DNLNKPYlfSVLLGAWQLGNpgSRSQKVGVAWVEPHPVYSWKEGAcADIALVRLERSIQFSErvlPICLPDASIHLPPNT 173
Cdd:COG5640    78 GDGPSDL--RVVIGSTDLST--SGGTVVKVARIVVHPDYDPATPG-NDIALLKLATPVPGVA---PAPLATSADAAAPGT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706 174 HCWISGWGSIQDGVPLPhPQTLQKLKVPIIDSEVCShlywrgAGQGPITEDMLCAGYLEGERDACLGDSGGPLMCQVDGA 253
Cdd:COG5640   150 PATVAGWGRTSEGPGSQ-SGTLRKADVPVVSDATCA------AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGG 222
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2462498706 254 WLLAGIISWGEGCAERNRPGVYISLSAHRSWVEKIVQG 291
Cdd:COG5640   223 WVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGG 260
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
70-276 9.52e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 57.38  E-value: 9.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706  70 NGTHHCAGSLLTSRWVITAAHCFKDNLNKPYLFSVLLGAWQLGNPGSRsqkVGVAWVEPHPVYSWKEGACADIALVRLER 149
Cdd:COG3591     9 GGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGPYGT---ATATRFRVPPGWVASGDAGYDYALLRLDE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706 150 SIQFSERVLPIclpDASIHLPPNTHCWISGWgsiqdgvPLPHPQTLqklkvpiidsevcshlywRGAGQGPITEdmLCAG 229
Cdd:COG3591    86 PLGDTTGWLGL---AFNDAPLAGEPVTIIGY-------PGDRPKDL------------------SLDCSGRVTG--VQGN 135
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462498706 230 YLEGERDACLGDSGGPLMCQVDGAWLLAGIISWGEgcAERNRPGVYI 276
Cdd:COG3591   136 RLSYDCDTTGGSSGSPVLDDSDGGGRVVGVHSAGG--ADRANTGVRL 180
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
61-175 1.07e-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: 52.55  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498706  61 WPWIVSIQKNGTHHCAGSLLTSRWVITAAHCFKD-NLNKPYLfSVLLGAWQ--LGNPGSRSQKVGVAWVEPHPVyswkeg 137
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDtNLRHQYI-SVVLGGAKtlKSIEGPYEQIVRVDCRHDIPE------ 73
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462498706 138 acADIALVRLERSIQFSERVLPICLPDASIHLPPNTHC 175
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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