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Conserved domains on  [gi|755531979|ref|XP_011241266|]
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serine protease 42 isoform X1 [Mus musculus]

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 ...
24-255 5.87e-93

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: 274.15  E-value: 5.87e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979  24 IMGGVDAEEGKWPWQVSVRVR-HMHVCGGSLINSQWVLTAAHCIYSRI--QYNVKVGDRSVYRQN-TSLVIPIKTIFVHP 99
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEgGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979 100 KFSTTIVVkNDIALLKLQHPVNFTTNIYPVCIPSESFPVKAGTKCWVTGWGKLVPGAPdvPTEILQEVDQNVILYEECNE 179
Cdd:cd00190   81 NYNPSTYD-NDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP--LPDVLQEVNVPIVSNAECKR 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755531979 180 mlkkaTSSSVDLVKRGMVC-GYKERGKDACQGDSGGPMSCEFENKWVQVGVVSWGISCGRKGYPGVYTDVAFYSKWL 255
Cdd:cd00190  158 -----AYSYGGTITDNMLCaGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
24-255 5.87e-93

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: 274.15  E-value: 5.87e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979  24 IMGGVDAEEGKWPWQVSVRVR-HMHVCGGSLINSQWVLTAAHCIYSRI--QYNVKVGDRSVYRQN-TSLVIPIKTIFVHP 99
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEgGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979 100 KFSTTIVVkNDIALLKLQHPVNFTTNIYPVCIPSESFPVKAGTKCWVTGWGKLVPGAPdvPTEILQEVDQNVILYEECNE 179
Cdd:cd00190   81 NYNPSTYD-NDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP--LPDVLQEVNVPIVSNAECKR 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755531979 180 mlkkaTSSSVDLVKRGMVC-GYKERGKDACQGDSGGPMSCEFENKWVQVGVVSWGISCGRKGYPGVYTDVAFYSKWL 255
Cdd:cd00190  158 -----AYSYGGTITDNMLCaGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
23-254 3.01e-89

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: 264.54  E-value: 3.01e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979    23 KIMGGVDAEEGKWPWQVSVRVR-HMHVCGGSLINSQWVLTAAHCIYSRI--QYNVKVGDRSVYRQNTSLVIPIKTIFVHP 99
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGgGRHFCGGSLISPRWVLTAAHCVRGSDpsNIRVRLGSHDLSSGEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979   100 KFSTTIVVkNDIALLKLQHPVNFTTNIYPVCIPSESFPVKAGTKCWVTGWGKLVPGAPDVPtEILQEVDQNVILYEECNE 179
Cdd:smart00020  81 NYNPSTYD-NDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLP-DTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755531979   180 mlkkaTSSSVDLVKRGMVC-GYKERGKDACQGDSGGPMSCEfENKWVQVGVVSWGISCGRKGYPGVYTDVAFYSKW 254
Cdd:smart00020 159 -----AYSGGGAITDNMLCaGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
24-255 4.55e-68

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 210.38  E-value: 4.55e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979   24 IMGGVDAEEGKWPWQVSVRVRH-MHVCGGSLINSQWVLTAAHCIYSRIQYNVKVGDRSVYRQN-TSLVIPIKTIFVHPKF 101
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREgGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979  102 STTIVvKNDIALLKLQHPVNFTTNIYPVCIPSESFPVKAGTKCWVTGWGKlvpGAPDVPTEILQEVDQNVILYEECNeml 181
Cdd:pfam00089  81 NPDTL-DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGN---TKTLGPSDTLQEVTVPVVSRETCR--- 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755531979  182 kkatSSSVDLVKRGMVCGYkERGKDACQGDSGGPMSCEFEnkwVQVGVVSWGISCGRKGYPGVYTDVAFYSKWL 255
Cdd:pfam00089 154 ----SAYGGTVTDTMICAG-AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
23-260 5.37e-64

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 201.42  E-value: 5.37e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979  23 KIMGGVDAEEGKWPWQVSVRVR---HMHVCGGSLINSQWVLTAAHCIY--SRIQYNVKVGDRSvYRQNTSLVIPIKTIFV 97
Cdd:COG5640   30 AIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDgdGPSDLRVVIGSTD-LSTSGGTVVKVARIVV 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979  98 HPKFSTTIVVkNDIALLKLQHPVNFTTniyPVCIPSESFPVKAGTKCWVTGWGKLVPGAPDVPTeILQEVDQNVILYEEC 177
Cdd:COG5640  109 HPDYDPATPG-NDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPGSQSG-TLRKADVPVVSDATC 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979 178 NemlkkatsSSVDLVKRGMVC-GYKERGKDACQGDSGGPMSCEFENKWVQVGVVSWGISCGRKGYPGVYTDVAFYSKWLI 256
Cdd:COG5640  184 A--------AYGGFDGGTMLCaGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIK 255

                 ....
gi 755531979 257 AVVN 260
Cdd:COG5640  256 STAG 259
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
24-255 5.87e-93

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: 274.15  E-value: 5.87e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979  24 IMGGVDAEEGKWPWQVSVRVR-HMHVCGGSLINSQWVLTAAHCIYSRI--QYNVKVGDRSVYRQN-TSLVIPIKTIFVHP 99
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEgGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979 100 KFSTTIVVkNDIALLKLQHPVNFTTNIYPVCIPSESFPVKAGTKCWVTGWGKLVPGAPdvPTEILQEVDQNVILYEECNE 179
Cdd:cd00190   81 NYNPSTYD-NDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP--LPDVLQEVNVPIVSNAECKR 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755531979 180 mlkkaTSSSVDLVKRGMVC-GYKERGKDACQGDSGGPMSCEFENKWVQVGVVSWGISCGRKGYPGVYTDVAFYSKWL 255
Cdd:cd00190  158 -----AYSYGGTITDNMLCaGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
23-254 3.01e-89

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: 264.54  E-value: 3.01e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979    23 KIMGGVDAEEGKWPWQVSVRVR-HMHVCGGSLINSQWVLTAAHCIYSRI--QYNVKVGDRSVYRQNTSLVIPIKTIFVHP 99
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGgGRHFCGGSLISPRWVLTAAHCVRGSDpsNIRVRLGSHDLSSGEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979   100 KFSTTIVVkNDIALLKLQHPVNFTTNIYPVCIPSESFPVKAGTKCWVTGWGKLVPGAPDVPtEILQEVDQNVILYEECNE 179
Cdd:smart00020  81 NYNPSTYD-NDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLP-DTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755531979   180 mlkkaTSSSVDLVKRGMVC-GYKERGKDACQGDSGGPMSCEfENKWVQVGVVSWGISCGRKGYPGVYTDVAFYSKW 254
Cdd:smart00020 159 -----AYSGGGAITDNMLCaGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
24-255 4.55e-68

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 210.38  E-value: 4.55e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979   24 IMGGVDAEEGKWPWQVSVRVRH-MHVCGGSLINSQWVLTAAHCIYSRIQYNVKVGDRSVYRQN-TSLVIPIKTIFVHPKF 101
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREgGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979  102 STTIVvKNDIALLKLQHPVNFTTNIYPVCIPSESFPVKAGTKCWVTGWGKlvpGAPDVPTEILQEVDQNVILYEECNeml 181
Cdd:pfam00089  81 NPDTL-DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGN---TKTLGPSDTLQEVTVPVVSRETCR--- 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755531979  182 kkatSSSVDLVKRGMVCGYkERGKDACQGDSGGPMSCEFEnkwVQVGVVSWGISCGRKGYPGVYTDVAFYSKWL 255
Cdd:pfam00089 154 ----SAYGGTVTDTMICAG-AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
23-260 5.37e-64

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 201.42  E-value: 5.37e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979  23 KIMGGVDAEEGKWPWQVSVRVR---HMHVCGGSLINSQWVLTAAHCIY--SRIQYNVKVGDRSvYRQNTSLVIPIKTIFV 97
Cdd:COG5640   30 AIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDgdGPSDLRVVIGSTD-LSTSGGTVVKVARIVV 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979  98 HPKFSTTIVVkNDIALLKLQHPVNFTTniyPVCIPSESFPVKAGTKCWVTGWGKLVPGAPDVPTeILQEVDQNVILYEEC 177
Cdd:COG5640  109 HPDYDPATPG-NDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPGSQSG-TLRKADVPVVSDATC 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979 178 NemlkkatsSSVDLVKRGMVC-GYKERGKDACQGDSGGPMSCEFENKWVQVGVVSWGISCGRKGYPGVYTDVAFYSKWLI 256
Cdd:COG5640  184 A--------AYGGFDGGTMLCaGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIK 255

                 ....
gi 755531979 257 AVVN 260
Cdd:COG5640  256 STAG 259
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
47-233 1.61e-14

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 70.09  E-value: 1.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979  47 HVCGGSLINSQWVLTAAHCIYS----RIQYNVKVgdRSVYRQNTSLVIPIKTIFVHPKFSTTIVVKNDIALLKLQHPVNF 122
Cdd:COG3591   12 GVCTGTLIGPNLVLTAGHCVYDgaggGWATNIVF--VPGYNGGPYGTATATRFRVPPGWVASGDAGYDYALLRLDEPLGD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979 123 TTNIYPVcipSESFPVKAGTKCWVTGWGKlvpGAPDVPTeilqevdqnviLYEECnemlkKATSSSVDLVkrGMVCgyke 202
Cdd:COG3591   90 TTGWLGL---AFNDAPLAGEPVTIIGYPG---DRPKDLS-----------LDCSG-----RVTGVQGNRL--SYDC---- 141
                        170       180       190
                 ....*....|....*....|....*....|.
gi 755531979 203 rgkDACQGDSGGPMSCEFENKWVQVGVVSWG 233
Cdd:COG3591  142 ---DTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
35-148 1.09e-03

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: 37.91  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531979   35 WPWQVSVRVRHMHVCGGSLINSQWVLTAAHCIYS---RIQY-NVKVGDRSVYRQNTSlviPIKTIFVHPKFSTtiVVKND 110
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDtnlRHQYiSVVLGGAKTLKSIEG---PYEQIVRVDCRHD--IPESE 75
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 755531979  111 IALLKLQHPVNFTTNIYPVCIPSESFPVKAGTKCWVTG 148
Cdd:pfam09342  76 ISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
 
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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