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Conserved domains on  [gi|74759052|sp|Q7RTY3|]
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PUTATIVE PSEUDOGENE: RecName: Full=Putative serine protease 45; AltName: Full=Serine protease 45, pseudogene; AltName: Full=Testis serine protease 5

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 ...
5-232 1.40e-77

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: 234.48  E-value: 1.40e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052   5 WPWEVSLRME-NEHVCGGALIDPSWVVTAAHCIQGT--KEYSVVLGTSKLQPMNFSRALwVPVRDIIMHPKYwGRAFIMG 81
Cdd:cd00190  12 FPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQV-IKVKKVIVHPNY-NPSTYDN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052  82 DVALVHLQTPVTFSEYVQPICLPEPNFNLKVGTQCWVTGWSQVKQRFSANSmltpELQEAEVFIMDNKRCDRHYKKSFFp 161
Cdd:cd00190  90 DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD----VLQEVNVPIVSNAECKRAYSYGGT- 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74759052 162 pvvplVLGDMICATNY--GENLCYGDSGGPLACEVEGRWILAGVLSWEKACVKAQNPGVYTRITKYTKWIKKQ 232
Cdd:cd00190 165 -----ITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
5-232 1.40e-77

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: 234.48  E-value: 1.40e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052   5 WPWEVSLRME-NEHVCGGALIDPSWVVTAAHCIQGT--KEYSVVLGTSKLQPMNFSRALwVPVRDIIMHPKYwGRAFIMG 81
Cdd:cd00190  12 FPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQV-IKVKKVIVHPNY-NPSTYDN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052  82 DVALVHLQTPVTFSEYVQPICLPEPNFNLKVGTQCWVTGWSQVKQRFSANSmltpELQEAEVFIMDNKRCDRHYKKSFFp 161
Cdd:cd00190  90 DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD----VLQEVNVPIVSNAECKRAYSYGGT- 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74759052 162 pvvplVLGDMICATNY--GENLCYGDSGGPLACEVEGRWILAGVLSWEKACVKAQNPGVYTRITKYTKWIKKQ 232
Cdd:cd00190 165 -----ITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
5-229 8.34e-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: 8.34e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052      5 WPWEVSLRMEN-EHVCGGALIDPSWVVTAAHCIQG--TKEYSVVLGTSKLQPMNFSRAlwVPVRDIIMHPKYwGRAFIMG 81
Cdd:smart00020  13 FPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGEEGQV--IKVSKVIIHPNY-NPSTYDN 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052     82 DVALVHLQTPVTFSEYVQPICLPEPNFNLKVGTQCWVTGWSQVKQRFSANSmltPELQEAEVFIMDNKRCDRHYKKSFFp 161
Cdd:smart00020  90 DIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLP---DTLQEVNVPIVSNATCRRAYSGGGA- 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052    162 pvvplVLGDMICATNY--GENLCYGDSGGPLACEVeGRWILAGVLSWEKACVKAQNPGVYTRITKYTKWI 229
Cdd:smart00020 166 -----ITDNMLCAGGLegGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
3-229 1.90e-61

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 192.66  E-value: 1.90e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052     3 RHWPWEVSLRME-NEHVCGGALIDPSWVVTAAHCIQGTKEYSVVLGTSKLQpMNFSRALWVPVRDIIMHPKYWGRAfIMG 81
Cdd:pfam00089  10 GSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIV-LREGGEQKFDVEKIIVHPNYNPDT-LDN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052    82 DVALVHLQTPVTFSEYVQPICLPEPNFNLKVGTQCWVTGWSQVKQRFSANSmltpeLQEAEVFIMDNKRCDRHYKKSffp 161
Cdd:pfam00089  88 DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDT-----LQEVTVPVVSRETCRSAYGGT--- 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74759052   162 pvvplVLGDMICATNYGENLCYGDSGGPLACEVEgrwILAGVLSWEKACVKAQNPGVYTRITKYTKWI 229
Cdd:pfam00089 160 -----VTDTMICAGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
5-233 1.72e-56

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 181.39  E-value: 1.72e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052   5 WPWEVSLRMEN---EHVCGGALIDPSWVVTAAHCIQGT--KEYSVVLGTSKLQPmnfSRALWVPVRDIIMHPKYWGRAFi 79
Cdd:COG5640  42 YPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLST---SGGTVVKVARIVVHPDYDPATP- 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052  80 MGDVALVHLQTPVTFseyVQPICLPEPNFNLKVGTQCWVTGWSQVKQRFSANSmltPELQEAEVFIMDNKRCdrhykkSF 159
Cdd:COG5640 118 GNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQS---GTLRKADVPVVSDATC------AA 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74759052 160 FPPVVPlvlGDMICATNY--GENLCYGDSGGPLACEVEGRWILAGVLSWEKACVKAQNPGVYTRITKYTKWIKKQM 233
Cdd:COG5640 186 YGGFDG---GTMLCAGYPegGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
5-232 1.40e-77

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: 234.48  E-value: 1.40e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052   5 WPWEVSLRME-NEHVCGGALIDPSWVVTAAHCIQGT--KEYSVVLGTSKLQPMNFSRALwVPVRDIIMHPKYwGRAFIMG 81
Cdd:cd00190  12 FPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQV-IKVKKVIVHPNY-NPSTYDN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052  82 DVALVHLQTPVTFSEYVQPICLPEPNFNLKVGTQCWVTGWSQVKQRFSANSmltpELQEAEVFIMDNKRCDRHYKKSFFp 161
Cdd:cd00190  90 DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPD----VLQEVNVPIVSNAECKRAYSYGGT- 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74759052 162 pvvplVLGDMICATNY--GENLCYGDSGGPLACEVEGRWILAGVLSWEKACVKAQNPGVYTRITKYTKWIKKQ 232
Cdd:cd00190 165 -----ITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
5-229 8.34e-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: 8.34e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052      5 WPWEVSLRMEN-EHVCGGALIDPSWVVTAAHCIQG--TKEYSVVLGTSKLQPMNFSRAlwVPVRDIIMHPKYwGRAFIMG 81
Cdd:smart00020  13 FPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGEEGQV--IKVSKVIIHPNY-NPSTYDN 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052     82 DVALVHLQTPVTFSEYVQPICLPEPNFNLKVGTQCWVTGWSQVKQRFSANSmltPELQEAEVFIMDNKRCDRHYKKSFFp 161
Cdd:smart00020  90 DIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLP---DTLQEVNVPIVSNATCRRAYSGGGA- 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052    162 pvvplVLGDMICATNY--GENLCYGDSGGPLACEVeGRWILAGVLSWEKACVKAQNPGVYTRITKYTKWI 229
Cdd:smart00020 166 -----ITDNMLCAGGLegGKDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
3-229 1.90e-61

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 192.66  E-value: 1.90e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052     3 RHWPWEVSLRME-NEHVCGGALIDPSWVVTAAHCIQGTKEYSVVLGTSKLQpMNFSRALWVPVRDIIMHPKYWGRAfIMG 81
Cdd:pfam00089  10 GSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIV-LREGGEQKFDVEKIIVHPNYNPDT-LDN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052    82 DVALVHLQTPVTFSEYVQPICLPEPNFNLKVGTQCWVTGWSQVKQRFSANSmltpeLQEAEVFIMDNKRCDRHYKKSffp 161
Cdd:pfam00089  88 DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDT-----LQEVTVPVVSRETCRSAYGGT--- 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74759052   162 pvvplVLGDMICATNYGENLCYGDSGGPLACEVEgrwILAGVLSWEKACVKAQNPGVYTRITKYTKWI 229
Cdd:pfam00089 160 -----VTDTMICAGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
5-233 1.72e-56

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 181.39  E-value: 1.72e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052   5 WPWEVSLRMEN---EHVCGGALIDPSWVVTAAHCIQGT--KEYSVVLGTSKLQPmnfSRALWVPVRDIIMHPKYWGRAFi 79
Cdd:COG5640  42 YPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLST---SGGTVVKVARIVVHPDYDPATP- 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052  80 MGDVALVHLQTPVTFseyVQPICLPEPNFNLKVGTQCWVTGWSQVKQRFSANSmltPELQEAEVFIMDNKRCdrhykkSF 159
Cdd:COG5640 118 GNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQS---GTLRKADVPVVSDATC------AA 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74759052 160 FPPVVPlvlGDMICATNY--GENLCYGDSGGPLACEVEGRWILAGVLSWEKACVKAQNPGVYTRITKYTKWIKKQM 233
Cdd:COG5640 186 YGGFDG---GTMLCAGYPegGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
5-120 1.48e-09

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: 54.48  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052     5 WPWEVSLRMENEHVCGGALIDPSWVVTAAHCIQGTK---EY-SVVLGTSKLQpmnfsRALWVPVRDIIMHPKYWGraFIM 80
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNlrhQYiSVVLGGAKTL-----KSIEGPYEQIVRVDCRHD--IPE 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 74759052    81 GDVALVHLQTPVTFSEYVQPICLPEPNFNLKVGTQCWVTG 120
Cdd:pfam09342  74 SEISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
17-206 6.13e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 45.82  E-value: 6.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052  17 HVCGGALIDPSWVVTAAHCI--QGTKEYSVVLgtsKLQPmNFSRALW--VPVRDIIMHPKYWGRAFIMGDVALVHLQTPV 92
Cdd:COG3591  12 GVCTGTLIGPNLVLTAGHCVydGAGGGWATNI---VFVP-GYNGGPYgtATATRFRVPPGWVASGDAGYDYALLRLDEPL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74759052  93 TFSEYVQPIclpEPNFNLKVGTQCWVTGWSQvkqrfsansmltpelqeaevfimdnkrcDRHYKKSFFP--PVVPLVLGD 170
Cdd:COG3591  88 GDTTGWLGL---AFNDAPLAGEPVTIIGYPG----------------------------DRPKDLSLDCsgRVTGVQGNR 136
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 74759052 171 MIcatnYGENLCYGDSGGPLACEVEGRWILAGVLSW 206
Cdd:COG3591 137 LS----YDCDTTGGSSGSPVLDDSDGGGRVVGVHSA 168
 
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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