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Conserved domains on  [gi|312191312|gb|ADQ43543|]
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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 ...
36-268 1.60e-90

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: 267.99  E-value: 1.60e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312  36 IVGGTIATPHLYPWMVAI-LNGGKMHCGGSLINDRYVLTAGHCLNWARKEDLTVVLGLHDRIAmNDGTEKIMGVDQMIVH 114
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSS-NEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312 115 EAFGSDYLHDteDIALIRLKQPVHFNAFMAPVCLAEPrGQDIYADQVAFVTGWGRTVQGGNPSRFLRKANVKVLSMAACR 194
Cdd:cd00190   80 PNYNPSTYDN--DIALLKLKRPVTLSDNVRPICLPSS-GYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312191312 195 NTT-IGEHILDSMICA--YEFETDACQGDSGGPLVFESRPGKVeQIGVVSWGIGCARPGMPGVYTTVSYYLDWIRAH 268
Cdd:cd00190  157 RAYsYGGTITDNMLCAggLEGGKDACQGDSGGPLVCNDNGRGV-LVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
36-268 1.60e-90

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: 267.99  E-value: 1.60e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312  36 IVGGTIATPHLYPWMVAI-LNGGKMHCGGSLINDRYVLTAGHCLNWARKEDLTVVLGLHDRIAmNDGTEKIMGVDQMIVH 114
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSS-NEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312 115 EAFGSDYLHDteDIALIRLKQPVHFNAFMAPVCLAEPrGQDIYADQVAFVTGWGRTVQGGNPSRFLRKANVKVLSMAACR 194
Cdd:cd00190   80 PNYNPSTYDN--DIALLKLKRPVTLSDNVRPICLPSS-GYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312191312 195 NTT-IGEHILDSMICA--YEFETDACQGDSGGPLVFESRPGKVeQIGVVSWGIGCARPGMPGVYTTVSYYLDWIRAH 268
Cdd:cd00190  157 RAYsYGGTITDNMLCAggLEGGKDACQGDSGGPLVCNDNGRGV-LVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
35-265 1.27e-87

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: 260.69  E-value: 1.27e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312    35 RIVGGTIATPHLYPWMVAILNGGKMH-CGGSLINDRYVLTAGHCLNWARKEDLTVVLGLHDRIamNDGTEKIMGVDQMIV 113
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS--SGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312   114 HEAFGSDYLHDteDIALIRLKQPVHFNAFMAPVCLAEPrGQDIYADQVAFVTGWGRTVQG-GNPSRFLRKANVKVLSMAA 192
Cdd:smart00020  79 HPNYNPSTYDN--DIALLKLKEPVTLSDNVRPICLPSS-NYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312191312   193 CRNTTIG-EHILDSMICA--YEFETDACQGDSGGPLVFESRPGkvEQIGVVSWGIGCARPGMPGVYTTVSYYLDWI 265
Cdd:smart00020 156 CRRAYSGgGAITDNMLCAggLEGGKDACQGDSGGPLVCNDGRW--VLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
36-265 1.38e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 214.61  E-value: 1.38e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312   36 IVGGTIATPHLYPWMVAILNGGKMH-CGGSLINDRYVLTAGHCLnwARKEDLTVVLGLHDrIAMNDGTEKIMGVDQMIVH 114
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCV--SGASDVKVVLGAHN-IVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312  115 EAFGSDYLHDteDIALIRLKQPVHFNAFMAPVCLAEPrGQDIYADQVAFVTGWGRTVQGGNPSRfLRKANVKVLSMAACR 194
Cdd:pfam00089  78 PNYNPDTLDN--DIALLKLESPVTLGDTVRPICLPDA-SSDLPVGTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312191312  195 NTTIGEhILDSMICAYEFETDACQGDSGGPLVfesrPGKVEQIGVVSWGIGCARPGMPGVYTTVSYYLDWI 265
Cdd:pfam00089 154 SAYGGT-VTDTMICAGAGGKDACQGDSGGPLV----CSDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
31-269 2.81e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 207.58  E-value: 2.81e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312  31 GVSTRIVGGTIATPHLYPWMVAIL--NGGKMH-CGGSLINDRYVLTAGHCLNWARKEDLTVVLGLHDRIamNDGTEKImG 107
Cdd:COG5640   26 DAAPAIVGGTPATVGEYPWMVALQssNGPSGQfCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLS--TSGGTVV-K 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312 108 VDQMIVHEAFGSDYLHDteDIALIRLKQPVHFNAfmaPVCLAEPrGQDIYADQVAFVTGWGRTVQG-GNPSRFLRKANVK 186
Cdd:COG5640  103 VARIVVHPDYDPATPGN--DIALLKLATPVPGVA---PAPLATS-ADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVP 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312 187 VLSMAACRNttIGEHILDSMICAYEFE--TDACQGDSGGPLVFEsRPGKVEQIGVVSWGIGCARPGMPGVYTTVSYYLDW 264
Cdd:COG5640  177 VVSDATCAA--YGGFDGGTMLCAGYPEggKDACQGDSGGPLVVK-DGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                 ....*
gi 312191312 265 IRAHT 269
Cdd:COG5640  254 IKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
36-268 1.60e-90

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: 267.99  E-value: 1.60e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312  36 IVGGTIATPHLYPWMVAI-LNGGKMHCGGSLINDRYVLTAGHCLNWARKEDLTVVLGLHDRIAmNDGTEKIMGVDQMIVH 114
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSS-NEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312 115 EAFGSDYLHDteDIALIRLKQPVHFNAFMAPVCLAEPrGQDIYADQVAFVTGWGRTVQGGNPSRFLRKANVKVLSMAACR 194
Cdd:cd00190   80 PNYNPSTYDN--DIALLKLKRPVTLSDNVRPICLPSS-GYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312191312 195 NTT-IGEHILDSMICA--YEFETDACQGDSGGPLVFESRPGKVeQIGVVSWGIGCARPGMPGVYTTVSYYLDWIRAH 268
Cdd:cd00190  157 RAYsYGGTITDNMLCAggLEGGKDACQGDSGGPLVCNDNGRGV-LVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
35-265 1.27e-87

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: 260.69  E-value: 1.27e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312    35 RIVGGTIATPHLYPWMVAILNGGKMH-CGGSLINDRYVLTAGHCLNWARKEDLTVVLGLHDRIamNDGTEKIMGVDQMIV 113
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS--SGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312   114 HEAFGSDYLHDteDIALIRLKQPVHFNAFMAPVCLAEPrGQDIYADQVAFVTGWGRTVQG-GNPSRFLRKANVKVLSMAA 192
Cdd:smart00020  79 HPNYNPSTYDN--DIALLKLKEPVTLSDNVRPICLPSS-NYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312191312   193 CRNTTIG-EHILDSMICA--YEFETDACQGDSGGPLVFESRPGkvEQIGVVSWGIGCARPGMPGVYTTVSYYLDWI 265
Cdd:smart00020 156 CRRAYSGgGAITDNMLCAggLEGGKDACQGDSGGPLVCNDGRW--VLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
36-265 1.38e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 214.61  E-value: 1.38e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312   36 IVGGTIATPHLYPWMVAILNGGKMH-CGGSLINDRYVLTAGHCLnwARKEDLTVVLGLHDrIAMNDGTEKIMGVDQMIVH 114
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCV--SGASDVKVVLGAHN-IVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312  115 EAFGSDYLHDteDIALIRLKQPVHFNAFMAPVCLAEPrGQDIYADQVAFVTGWGRTVQGGNPSRfLRKANVKVLSMAACR 194
Cdd:pfam00089  78 PNYNPDTLDN--DIALLKLESPVTLGDTVRPICLPDA-SSDLPVGTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312191312  195 NTTIGEhILDSMICAYEFETDACQGDSGGPLVfesrPGKVEQIGVVSWGIGCARPGMPGVYTTVSYYLDWI 265
Cdd:pfam00089 154 SAYGGT-VTDTMICAGAGGKDACQGDSGGPLV----CSDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
31-269 2.81e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 207.58  E-value: 2.81e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312  31 GVSTRIVGGTIATPHLYPWMVAIL--NGGKMH-CGGSLINDRYVLTAGHCLNWARKEDLTVVLGLHDRIamNDGTEKImG 107
Cdd:COG5640   26 DAAPAIVGGTPATVGEYPWMVALQssNGPSGQfCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLS--TSGGTVV-K 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312 108 VDQMIVHEAFGSDYLHDteDIALIRLKQPVHFNAfmaPVCLAEPrGQDIYADQVAFVTGWGRTVQG-GNPSRFLRKANVK 186
Cdd:COG5640  103 VARIVVHPDYDPATPGN--DIALLKLATPVPGVA---PAPLATS-ADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVP 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312 187 VLSMAACRNttIGEHILDSMICAYEFE--TDACQGDSGGPLVFEsRPGKVEQIGVVSWGIGCARPGMPGVYTTVSYYLDW 264
Cdd:COG5640  177 VVSDATCAA--YGGFDGGTMLCAGYPEggKDACQGDSGGPLVVK-DGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                 ....*
gi 312191312 265 IRAHT 269
Cdd:COG5640  254 IKSTA 258
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
55-243 3.70e-13

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 66.62  E-value: 3.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312  55 NGGKMHCGGSLINDRYVLTAGHCLNWARK----EDLTVVLGLhdriamNDGTEKIMGVDQMIVHEAFGSDYlHDTEDIAL 130
Cdd:COG3591    8 DGGGGVCTGTLIGPNLVLTAGHCVYDGAGggwaTNIVFVPGY------NGGPYGTATATRFRVPPGWVASG-DAGYDYAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312 131 IRLKQPVHFNA-FMAPVCLAEPRgqdiyADQVAFVTGWGrtvqGGNPsrflrkanvKVLSMA-ACRNTTIGEHILdsmic 208
Cdd:COG3591   81 LRLDEPLGDTTgWLGLAFNDAPL-----AGEPVTIIGYP----GDRP---------KDLSLDcSGRVTGVQGNRL----- 137
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 312191312 209 ayEFETDACQGDSGGPlVFESRPGKVEQIGVVSWG 243
Cdd:COG3591  138 --SYDCDTTGGSSGSP-VLDDSDGGGRVVGVHSAG 169
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
47-154 2.95e-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: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312191312   47 YPWMVAILNGGKMHCGGSLINDRYVLTAGHCLNWA--RKEDLTVVLGLHDRIAMNDGT-EKIMGVDQMivheafgsDYLH 123
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTnlRHQYISVVLGGAKTLKSIEGPyEQIVRVDCR--------HDIP 72
                          90       100       110
                  ....*....|....*....|....*....|.
gi 312191312  124 DTEdIALIRLKQPVHFNAFMAPVCLAEPRGQ 154
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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