NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|76825467|gb|AAI07232|]
View 

BC107230 protein [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
50-280 4.28e-68

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: 212.14  E-value: 4.28e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467  50 HHWPWEASLQIED-KHVCGGALIDRSWVVSAAHCIQGN--KEYSVMLGSSTLHPNGSSWTlKIPVGDIIIHPKYwGRNFI 126
Cdd:cd00190  10 GSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQ-VIKVKKVIVHPNY-NPSTY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467 127 RSDIALLCLETPVTFNKYVQPICLPEHNFNFKIGTKCWVTGWGqvkqHSSAQLTPAPELWEAEVFIIDNKNCDSIFHKKt 206
Cdd:cd00190  88 DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG----RTSEGGPLPDVLQEVNVPIVSNAECKRAYSYG- 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 76825467 207 lypqvvPLIRKNMICTTNY--GEDLCYGDPGGPLACEIDGRWILAGVFSWEKACATVPNLSVYTRITKYTIWIKDQ 280
Cdd:cd00190 163 ------GTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
50-280 4.28e-68

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: 212.14  E-value: 4.28e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467  50 HHWPWEASLQIED-KHVCGGALIDRSWVVSAAHCIQGN--KEYSVMLGSSTLHPNGSSWTlKIPVGDIIIHPKYwGRNFI 126
Cdd:cd00190  10 GSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQ-VIKVKKVIVHPNY-NPSTY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467 127 RSDIALLCLETPVTFNKYVQPICLPEHNFNFKIGTKCWVTGWGqvkqHSSAQLTPAPELWEAEVFIIDNKNCDSIFHKKt 206
Cdd:cd00190  88 DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG----RTSEGGPLPDVLQEVNVPIVSNAECKRAYSYG- 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 76825467 207 lypqvvPLIRKNMICTTNY--GEDLCYGDPGGPLACEIDGRWILAGVFSWEKACATVPNLSVYTRITKYTIWIKDQ 280
Cdd:cd00190 163 ------GTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
50-277 2.79e-64

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: 202.14  E-value: 2.79e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467     50 HHWPWEASLQIED-KHVCGGALIDRSWVVSAAHCIQG--NKEYSVMLGSSTLHPNGSswTLKIPVGDIIIHPKYwGRNFI 126
Cdd:smart00020  11 GSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGEE--GQVIKVSKVIIHPNY-NPSTY 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467    127 RSDIALLCLETPVTFNKYVQPICLPEHNFNFKIGTKCWVTGWGQVkqhSSAQLTPAPELWEAEVFIIDNKNCDSIFHKkt 206
Cdd:smart00020  88 DNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRT---SEGAGSLPDTLQEVNVPIVSNATCRRAYSG-- 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 76825467    207 lypqvVPLIRKNMICTTNY--GEDLCYGDPGGPLACEiDGRWILAGVFSWEKACATVPNLSVYTRITKYTIWI 277
Cdd:smart00020 163 -----GGAITDNMLCAGGLegGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
50-277 2.05e-56

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 181.49  E-value: 2.05e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467    50 HHWPWEASLQIED-KHVCGGALIDRSWVVSAAHCIQGNKEYSVMLGSSTLHPNGSSwTLKIPVGDIIIHPKYwGRNFIRS 128
Cdd:pfam00089  10 GSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGG-EQKFDVEKIIVHPNY-NPDTLDN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467   129 DIALLCLETPVTFNKYVQPICLPEHNFNFKIGTKCWVTGWGQVKQHSSAQLtpapeLWEAEVFIIDNKNCDSIFHKKtly 208
Cdd:pfam00089  88 DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDT-----LQEVTVPVVSRETCRSAYGGT--- 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 76825467   209 pqvvplIRKNMICTTNYGEDLCYGDPGGPLACEiDGrwILAGVFSWEKACATVPNLSVYTRITKYTIWI 277
Cdd:pfam00089 160 ------VTDTMICAGAGGKDACQGDSGGPLVCS-DG--ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
52-281 1.45e-47

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 160.20  E-value: 1.45e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467  52 WPWEASLQIED---KHVCGGALIDRSWVVSAAHCIQGN--KEYSVMLGSSTLHPNGSSwtlKIPVGDIIIHPKYWGRNFi 126
Cdd:COG5640  42 YPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLSTSGGT---VVKVARIVVHPDYDPATP- 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467 127 RSDIALLCLETPVTFnkyVQPICLPEHNFNFKIGTKCWVTGWGQVKQHSSAQltpAPELWEAEVFIIDNKNCDSifhkkt 206
Cdd:COG5640 118 GNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQ---SGTLRKADVPVVSDATCAA------ 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 76825467 207 lYPQVVPlirKNMICTTNY--GEDLCYGDPGGPLACEIDGRWILAGVFSW-EKACAtvPNL-SVYTRITKYTIWIKDQV 281
Cdd:COG5640 186 -YGGFDG---GTMLCAGYPegGKDACQGDSGGPLVVKDGGGWVLVGVVSWgGGPCA--AGYpGVYTRVSAYRDWIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
50-280 4.28e-68

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: 212.14  E-value: 4.28e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467  50 HHWPWEASLQIED-KHVCGGALIDRSWVVSAAHCIQGN--KEYSVMLGSSTLHPNGSSWTlKIPVGDIIIHPKYwGRNFI 126
Cdd:cd00190  10 GSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQ-VIKVKKVIVHPNY-NPSTY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467 127 RSDIALLCLETPVTFNKYVQPICLPEHNFNFKIGTKCWVTGWGqvkqHSSAQLTPAPELWEAEVFIIDNKNCDSIFHKKt 206
Cdd:cd00190  88 DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG----RTSEGGPLPDVLQEVNVPIVSNAECKRAYSYG- 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 76825467 207 lypqvvPLIRKNMICTTNY--GEDLCYGDPGGPLACEIDGRWILAGVFSWEKACATVPNLSVYTRITKYTIWIKDQ 280
Cdd:cd00190 163 ------GTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
50-277 2.79e-64

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: 202.14  E-value: 2.79e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467     50 HHWPWEASLQIED-KHVCGGALIDRSWVVSAAHCIQG--NKEYSVMLGSSTLHPNGSswTLKIPVGDIIIHPKYwGRNFI 126
Cdd:smart00020  11 GSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGEE--GQVIKVSKVIIHPNY-NPSTY 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467    127 RSDIALLCLETPVTFNKYVQPICLPEHNFNFKIGTKCWVTGWGQVkqhSSAQLTPAPELWEAEVFIIDNKNCDSIFHKkt 206
Cdd:smart00020  88 DNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRT---SEGAGSLPDTLQEVNVPIVSNATCRRAYSG-- 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 76825467    207 lypqvVPLIRKNMICTTNY--GEDLCYGDPGGPLACEiDGRWILAGVFSWEKACATVPNLSVYTRITKYTIWI 277
Cdd:smart00020 163 -----GGAITDNMLCAGGLegGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
50-277 2.05e-56

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 181.49  E-value: 2.05e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467    50 HHWPWEASLQIED-KHVCGGALIDRSWVVSAAHCIQGNKEYSVMLGSSTLHPNGSSwTLKIPVGDIIIHPKYwGRNFIRS 128
Cdd:pfam00089  10 GSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGG-EQKFDVEKIIVHPNY-NPDTLDN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467   129 DIALLCLETPVTFNKYVQPICLPEHNFNFKIGTKCWVTGWGQVKQHSSAQLtpapeLWEAEVFIIDNKNCDSIFHKKtly 208
Cdd:pfam00089  88 DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDT-----LQEVTVPVVSRETCRSAYGGT--- 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 76825467   209 pqvvplIRKNMICTTNYGEDLCYGDPGGPLACEiDGrwILAGVFSWEKACATVPNLSVYTRITKYTIWI 277
Cdd:pfam00089 160 ------VTDTMICAGAGGKDACQGDSGGPLVCS-DG--ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
52-281 1.45e-47

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 160.20  E-value: 1.45e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467  52 WPWEASLQIED---KHVCGGALIDRSWVVSAAHCIQGN--KEYSVMLGSSTLHPNGSSwtlKIPVGDIIIHPKYWGRNFi 126
Cdd:COG5640  42 YPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLSTSGGT---VVKVARIVVHPDYDPATP- 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467 127 RSDIALLCLETPVTFnkyVQPICLPEHNFNFKIGTKCWVTGWGQVKQHSSAQltpAPELWEAEVFIIDNKNCDSifhkkt 206
Cdd:COG5640 118 GNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQ---SGTLRKADVPVVSDATCAA------ 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 76825467 207 lYPQVVPlirKNMICTTNY--GEDLCYGDPGGPLACEIDGRWILAGVFSW-EKACAtvPNL-SVYTRITKYTIWIKDQV 281
Cdd:COG5640 186 -YGGFDG---GTMLCAGYPegGKDACQGDSGGPLVVKDGGGWVLVGVVSWgGGPCA--AGYpGVYTRVSAYRDWIKSTA 258
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
52-167 3.36e-07

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: 48.31  E-value: 3.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76825467    52 WPWEASLQIEDKHVCGGALIDRSWVVSAAHCIQG----NKEYSVMLGSSTlhpngSSWTLKIPVGDIIIHPKYWGrnFIR 127
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDtnlrHQYISVVLGGAK-----TLKSIEGPYEQIVRVDCRHD--IPE 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 76825467   128 SDIALLCLETPVTFNKYVQPICLPEHNFNFKIGTKCWVTG 167
Cdd:pfam09342  74 SEISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH