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Conserved domains on  [gi|81914742|sp|Q8K4I7|]
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RecName: Full=Inactive serine protease 45; AltName: Full=Inactive testis serine protease 5; AltName: Full=Trypsin-like protease p98; 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 ...
59-289 7.55e-69

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: 214.06  E-value: 7.55e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742  59 HHWPWEASLQIED-KHVCGGALIDRSWVVSAAHCIQGN--KEYSVMLGSSTLHPNGSSWTlKIPVGDIIIHPKYwGRNFI 135
Cdd:cd00190  10 GSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQ-VIKVKKVIVHPNY-NPSTY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742 136 RSDIALLCLETPVTFNKYVQPICLPEHNFNFKVGTKCWVTGWGqvkqHSSAQLTPAPELWEAEVFIIDNKNCDSIFHKKt 215
Cdd:cd00190  88 DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG----RTSEGGPLPDVLQEVNVPIVSNAECKRAYSYG- 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81914742 216 lypqvvPLIRKNMICTTNY--GEDLCYGDPGGPLACEIDGRWILAGVFSWEKACATVPNLSVYTRITKYTIWIKDQ 289
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 ...
59-289 7.55e-69

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: 214.06  E-value: 7.55e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742  59 HHWPWEASLQIED-KHVCGGALIDRSWVVSAAHCIQGN--KEYSVMLGSSTLHPNGSSWTlKIPVGDIIIHPKYwGRNFI 135
Cdd:cd00190  10 GSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQ-VIKVKKVIVHPNY-NPSTY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742 136 RSDIALLCLETPVTFNKYVQPICLPEHNFNFKVGTKCWVTGWGqvkqHSSAQLTPAPELWEAEVFIIDNKNCDSIFHKKt 215
Cdd:cd00190  88 DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG----RTSEGGPLPDVLQEVNVPIVSNAECKRAYSYG- 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81914742 216 lypqvvPLIRKNMICTTNY--GEDLCYGDPGGPLACEIDGRWILAGVFSWEKACATVPNLSVYTRITKYTIWIKDQ 289
Cdd:cd00190 163 ------GTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
59-286 4.04e-65

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: 204.45  E-value: 4.04e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742     59 HHWPWEASLQIED-KHVCGGALIDRSWVVSAAHCIQG--NKEYSVMLGSSTLHPNGSswTLKIPVGDIIIHPKYwGRNFI 135
Cdd:smart00020  11 GSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGEE--GQVIKVSKVIIHPNY-NPSTY 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742    136 RSDIALLCLETPVTFNKYVQPICLPEHNFNFKVGTKCWVTGWGQVkqhSSAQLTPAPELWEAEVFIIDNKNCDSIFHKkt 215
Cdd:smart00020  88 DNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRT---SEGAGSLPDTLQEVNVPIVSNATCRRAYSG-- 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81914742    216 lypqvVPLIRKNMICTTNY--GEDLCYGDPGGPLACEiDGRWILAGVFSWEKACATVPNLSVYTRITKYTIWI 286
Cdd:smart00020 163 -----GGAITDNMLCAGGLegGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
59-286 6.83e-57

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 183.03  E-value: 6.83e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742    59 HHWPWEASLQIED-KHVCGGALIDRSWVVSAAHCIQGNKEYSVMLGSSTLHPNGSSwTLKIPVGDIIIHPKYwGRNFIRS 137
Cdd:pfam00089  10 GSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGG-EQKFDVEKIIVHPNY-NPDTLDN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742   138 DIALLCLETPVTFNKYVQPICLPEHNFNFKVGTKCWVTGWGQVKQHSSAQLtpapeLWEAEVFIIDNKNCDSIFHKKtly 217
Cdd:pfam00089  88 DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDT-----LQEVTVPVVSRETCRSAYGGT--- 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81914742   218 pqvvplIRKNMICTTNYGEDLCYGDPGGPLACEiDGrwILAGVFSWEKACATVPNLSVYTRITKYTIWI 286
Cdd:pfam00089 160 ------VTDTMICAGAGGKDACQGDSGGPLVCS-DG--ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
61-290 4.67e-48

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 161.74  E-value: 4.67e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742  61 WPWEASLQIED---KHVCGGALIDRSWVVSAAHCIQGN--KEYSVMLGSSTLHPNGSSwtlKIPVGDIIIHPKYWGRNFi 135
Cdd:COG5640  42 YPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLSTSGGT---VVKVARIVVHPDYDPATP- 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742 136 RSDIALLCLETPVTFnkyVQPICLPEHNFNFKVGTKCWVTGWGQVKQHSSAQltpAPELWEAEVFIIDNKNCDSifhkkt 215
Cdd:COG5640 118 GNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQ---SGTLRKADVPVVSDATCAA------ 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81914742 216 lYPQVVPlirKNMICT--TNYGEDLCYGDPGGPLACEIDGRWILAGVFSW-EKACAtvPNL-SVYTRITKYTIWIKDQV 290
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 ...
59-289 7.55e-69

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: 214.06  E-value: 7.55e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742  59 HHWPWEASLQIED-KHVCGGALIDRSWVVSAAHCIQGN--KEYSVMLGSSTLHPNGSSWTlKIPVGDIIIHPKYwGRNFI 135
Cdd:cd00190  10 GSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQ-VIKVKKVIVHPNY-NPSTY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742 136 RSDIALLCLETPVTFNKYVQPICLPEHNFNFKVGTKCWVTGWGqvkqHSSAQLTPAPELWEAEVFIIDNKNCDSIFHKKt 215
Cdd:cd00190  88 DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG----RTSEGGPLPDVLQEVNVPIVSNAECKRAYSYG- 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81914742 216 lypqvvPLIRKNMICTTNY--GEDLCYGDPGGPLACEIDGRWILAGVFSWEKACATVPNLSVYTRITKYTIWIKDQ 289
Cdd:cd00190 163 ------GTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
59-286 4.04e-65

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: 204.45  E-value: 4.04e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742     59 HHWPWEASLQIED-KHVCGGALIDRSWVVSAAHCIQG--NKEYSVMLGSSTLHPNGSswTLKIPVGDIIIHPKYwGRNFI 135
Cdd:smart00020  11 GSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGEE--GQVIKVSKVIIHPNY-NPSTY 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742    136 RSDIALLCLETPVTFNKYVQPICLPEHNFNFKVGTKCWVTGWGQVkqhSSAQLTPAPELWEAEVFIIDNKNCDSIFHKkt 215
Cdd:smart00020  88 DNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRT---SEGAGSLPDTLQEVNVPIVSNATCRRAYSG-- 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81914742    216 lypqvVPLIRKNMICTTNY--GEDLCYGDPGGPLACEiDGRWILAGVFSWEKACATVPNLSVYTRITKYTIWI 286
Cdd:smart00020 163 -----GGAITDNMLCAGGLegGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
59-286 6.83e-57

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 183.03  E-value: 6.83e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742    59 HHWPWEASLQIED-KHVCGGALIDRSWVVSAAHCIQGNKEYSVMLGSSTLHPNGSSwTLKIPVGDIIIHPKYwGRNFIRS 137
Cdd:pfam00089  10 GSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGG-EQKFDVEKIIVHPNY-NPDTLDN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742   138 DIALLCLETPVTFNKYVQPICLPEHNFNFKVGTKCWVTGWGQVKQHSSAQLtpapeLWEAEVFIIDNKNCDSIFHKKtly 217
Cdd:pfam00089  88 DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDT-----LQEVTVPVVSRETCRSAYGGT--- 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81914742   218 pqvvplIRKNMICTTNYGEDLCYGDPGGPLACEiDGrwILAGVFSWEKACATVPNLSVYTRITKYTIWI 286
Cdd:pfam00089 160 ------VTDTMICAGAGGKDACQGDSGGPLVCS-DG--ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
61-290 4.67e-48

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 161.74  E-value: 4.67e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742  61 WPWEASLQIED---KHVCGGALIDRSWVVSAAHCIQGN--KEYSVMLGSSTLHPNGSSwtlKIPVGDIIIHPKYWGRNFi 135
Cdd:COG5640  42 YPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLSTSGGT---VVKVARIVVHPDYDPATP- 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742 136 RSDIALLCLETPVTFnkyVQPICLPEHNFNFKVGTKCWVTGWGQVKQHSSAQltpAPELWEAEVFIIDNKNCDSifhkkt 215
Cdd:COG5640 118 GNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQ---SGTLRKADVPVVSDATCAA------ 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81914742 216 lYPQVVPlirKNMICT--TNYGEDLCYGDPGGPLACEIDGRWILAGVFSW-EKACAtvPNL-SVYTRITKYTIWIKDQV 290
Cdd:COG5640 186 -YGGFDG---GTMLCAgyPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWgGGPCA--AGYpGVYTRVSAYRDWIKSTA 258
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
61-176 2.66e-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: 48.70  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81914742    61 WPWEASLQIEDKHVCGGALIDRSWVVSAAHCIQG----NKEYSVMLGSSTlhpngSSWTLKIPVGDIIIHPKYWGrnFIR 136
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDtnlrHQYISVVLGGAK-----TLKSIEGPYEQIVRVDCRHD--IPE 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 81914742   137 SDIALLCLETPVTFNKYVQPICLPEHNFNFKVGTKCWVTG 176
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.
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