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Conserved domains on  [gi|372477532|gb|AEX97001|]
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ejaculate serine protease, partial [Allonemobius socius]

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 ...
32-242 1.67e-75

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: 228.31  E-value: 1.67e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532  32 IVGGTIATPHLYPWMVAI-LNGGKMHCGGSLINDRYVLTAGHCLNWARKEDLTVVLGLHDRIAmNDGTEKIMGVDQMIVH 110
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSS-NEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532 111 EAFGSDYLHDteDIALIRLKQPVHFNAFMAPVCLAEPrGQDIYADQVAFVTGWGRTVQGGNPSRFLRKANVKVLSMAACR 190
Cdd:cd00190   80 PNYNPSTYDN--DIALLKLKRPVTLSDNVRPICLPSS-GYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 372477532 191 NTT-IGEHILDSMICA--YEFETDACQGDSGGPLVFESRPGKVeQIGVVSWGIGC 242
Cdd:cd00190  157 RAYsYGGTITDNMLCAggLEGGKDACQGDSGGPLVCNDNGRGV-LVGIVSWGSGC 210
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
32-242 1.67e-75

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: 228.31  E-value: 1.67e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532  32 IVGGTIATPHLYPWMVAI-LNGGKMHCGGSLINDRYVLTAGHCLNWARKEDLTVVLGLHDRIAmNDGTEKIMGVDQMIVH 110
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSS-NEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532 111 EAFGSDYLHDteDIALIRLKQPVHFNAFMAPVCLAEPrGQDIYADQVAFVTGWGRTVQGGNPSRFLRKANVKVLSMAACR 190
Cdd:cd00190   80 PNYNPSTYDN--DIALLKLKRPVTLSDNVRPICLPSS-GYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 372477532 191 NTT-IGEHILDSMICA--YEFETDACQGDSGGPLVFESRPGKVeQIGVVSWGIGC 242
Cdd:cd00190  157 RAYsYGGTITDNMLCAggLEGGKDACQGDSGGPLVCNDNGRGV-LVGIVSWGSGC 210
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
31-242 3.90e-73

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: 222.17  E-value: 3.90e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532    31 RIVGGTIATPHLYPWMVAILNGGKMH-CGGSLINDRYVLTAGHCLNWARKEDLTVVLGLHDRIamNDGTEKIMGVDQMIV 109
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS--SGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532   110 HEAFGSDYLHDteDIALIRLKQPVHFNAFMAPVCLAEPrGQDIYADQVAFVTGWGRTVQG-GNPSRFLRKANVKVLSMAA 188
Cdd:smart00020  79 HPNYNPSTYDN--DIALLKLKEPVTLSDNVRPICLPSS-NYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 372477532   189 CRNTTIG-EHILDSMICA--YEFETDACQGDSGGPLVFESRPGkvEQIGVVSWGIGC 242
Cdd:smart00020 156 CRRAYSGgGAITDNMLCAggLEGGKDACQGDSGGPLVCNDGRW--VLVGIVSWGSGC 210
Trypsin pfam00089
Trypsin;
32-242 2.86e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 186.49  E-value: 2.86e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532   32 IVGGTIATPHLYPWMVAILNGGKMH-CGGSLINDRYVLTAGHCLnwARKEDLTVVLGLHDrIAMNDGTEKIMGVDQMIVH 110
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCV--SGASDVKVVLGAHN-IVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532  111 EAFGSDYLHDteDIALIRLKQPVHFNAFMAPVCLAEPrGQDIYADQVAFVTGWGRTVQGGNPSRfLRKANVKVLSMAACR 190
Cdd:pfam00089  78 PNYNPDTLDN--DIALLKLESPVTLGDTVRPICLPDA-SSDLPVGTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCR 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 372477532  191 NTTIGEhILDSMICAYEFETDACQGDSGGPLVfesrPGKVEQIGVVSWGIGC 242
Cdd:pfam00089 154 SAYGGT-VTDTMICAGAGGKDACQGDSGGPLV----CSDGELIGIVSWGYGC 200
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
27-241 8.11e-56

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 179.07  E-value: 8.11e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532  27 GVSTRIVGGTIATPHLYPWMVAIL--NGGKMH-CGGSLINDRYVLTAGHCLNWARKEDLTVVLGLHDRIamNDGTEKImG 103
Cdd:COG5640   26 DAAPAIVGGTPATVGEYPWMVALQssNGPSGQfCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLS--TSGGTVV-K 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532 104 VDQMIVHEAFGSDYLHDteDIALIRLKQPVHFNafmAPVCLAEPrGQDIYADQVAFVTGWGRTVQG-GNPSRFLRKANVK 182
Cdd:COG5640  103 VARIVVHPDYDPATPGN--DIALLKLATPVPGV---APAPLATS-ADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVP 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372477532 183 VLSMAACRNttIGEHILDSMICAYEFE--TDACQGDSGGPLVFEsRPGKVEQIGVVSWGIG 241
Cdd:COG5640  177 VVSDATCAA--YGGFDGGTMLCAGYPEggKDACQGDSGGPLVVK-DGGGWVLVGVVSWGGG 234
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
32-242 1.67e-75

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: 228.31  E-value: 1.67e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532  32 IVGGTIATPHLYPWMVAI-LNGGKMHCGGSLINDRYVLTAGHCLNWARKEDLTVVLGLHDRIAmNDGTEKIMGVDQMIVH 110
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSS-NEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532 111 EAFGSDYLHDteDIALIRLKQPVHFNAFMAPVCLAEPrGQDIYADQVAFVTGWGRTVQGGNPSRFLRKANVKVLSMAACR 190
Cdd:cd00190   80 PNYNPSTYDN--DIALLKLKRPVTLSDNVRPICLPSS-GYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 372477532 191 NTT-IGEHILDSMICA--YEFETDACQGDSGGPLVFESRPGKVeQIGVVSWGIGC 242
Cdd:cd00190  157 RAYsYGGTITDNMLCAggLEGGKDACQGDSGGPLVCNDNGRGV-LVGIVSWGSGC 210
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
31-242 3.90e-73

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: 222.17  E-value: 3.90e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532    31 RIVGGTIATPHLYPWMVAILNGGKMH-CGGSLINDRYVLTAGHCLNWARKEDLTVVLGLHDRIamNDGTEKIMGVDQMIV 109
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS--SGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532   110 HEAFGSDYLHDteDIALIRLKQPVHFNAFMAPVCLAEPrGQDIYADQVAFVTGWGRTVQG-GNPSRFLRKANVKVLSMAA 188
Cdd:smart00020  79 HPNYNPSTYDN--DIALLKLKEPVTLSDNVRPICLPSS-NYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 372477532   189 CRNTTIG-EHILDSMICA--YEFETDACQGDSGGPLVFESRPGkvEQIGVVSWGIGC 242
Cdd:smart00020 156 CRRAYSGgGAITDNMLCAggLEGGKDACQGDSGGPLVCNDGRW--VLVGIVSWGSGC 210
Trypsin pfam00089
Trypsin;
32-242 2.86e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 186.49  E-value: 2.86e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532   32 IVGGTIATPHLYPWMVAILNGGKMH-CGGSLINDRYVLTAGHCLnwARKEDLTVVLGLHDrIAMNDGTEKIMGVDQMIVH 110
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCV--SGASDVKVVLGAHN-IVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532  111 EAFGSDYLHDteDIALIRLKQPVHFNAFMAPVCLAEPrGQDIYADQVAFVTGWGRTVQGGNPSRfLRKANVKVLSMAACR 190
Cdd:pfam00089  78 PNYNPDTLDN--DIALLKLESPVTLGDTVRPICLPDA-SSDLPVGTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCR 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 372477532  191 NTTIGEhILDSMICAYEFETDACQGDSGGPLVfesrPGKVEQIGVVSWGIGC 242
Cdd:pfam00089 154 SAYGGT-VTDTMICAGAGGKDACQGDSGGPLV----CSDGELIGIVSWGYGC 200
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
27-241 8.11e-56

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 179.07  E-value: 8.11e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532  27 GVSTRIVGGTIATPHLYPWMVAIL--NGGKMH-CGGSLINDRYVLTAGHCLNWARKEDLTVVLGLHDRIamNDGTEKImG 103
Cdd:COG5640   26 DAAPAIVGGTPATVGEYPWMVALQssNGPSGQfCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLS--TSGGTVV-K 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532 104 VDQMIVHEAFGSDYLHDteDIALIRLKQPVHFNafmAPVCLAEPrGQDIYADQVAFVTGWGRTVQG-GNPSRFLRKANVK 182
Cdd:COG5640  103 VARIVVHPDYDPATPGN--DIALLKLATPVPGV---APAPLATS-ADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVP 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372477532 183 VLSMAACRNttIGEHILDSMICAYEFE--TDACQGDSGGPLVFEsRPGKVEQIGVVSWGIG 241
Cdd:COG5640  177 VVSDATCAA--YGGFDGGTMLCAGYPEggKDACQGDSGGPLVVK-DGGGWVLVGVVSWGGG 234
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
51-239 8.99e-14

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 67.39  E-value: 8.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532  51 NGGKMHCGGSLINDRYVLTAGHCLNWARK----EDLTVVLGLhdriamNDGTEKIMGVDQMIVHEAFGSDYlHDTEDIAL 126
Cdd:COG3591    8 DGGGGVCTGTLIGPNLVLTAGHCVYDGAGggwaTNIVFVPGY------NGGPYGTATATRFRVPPGWVASG-DAGYDYAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532 127 IRLKQPVHFNA-FMAPVCLAEPRgqdiyADQVAFVTGWGrtvqGGNPsrflrkanvKVLSMA-ACRNTTIGEHILdsmic 204
Cdd:COG3591   81 LRLDEPLGDTTgWLGLAFNDAPL-----AGEPVTIIGYP----GDRP---------KDLSLDcSGRVTGVQGNRL----- 137
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 372477532 205 ayEFETDACQGDSGGPlVFESRPGKVEQIGVVSWG 239
Cdd:COG3591  138 --SYDCDTTGGSSGSP-VLDDSDGGGRVVGVHSAG 169
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
43-150 2.14e-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: 36.76  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372477532   43 YPWMVAILNGGKMHCGGSLINDRYVLTAGHCLNWA--RKEDLTVVLGLHDRIAMNDGT-EKIMGVDQMivheafgsDYLH 119
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTnlRHQYISVVLGGAKTLKSIEGPyEQIVRVDCR--------HDIP 72
                          90       100       110
                  ....*....|....*....|....*....|.
gi 372477532  120 DTEdIALIRLKQPVHFNAFMAPVCLAEPRGQ 150
Cdd:pfam09342  73 ESE-ISLLHLASPASFSNHVLPTFVPETRNE 102
 
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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