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Conserved domains on  [gi|61557348|ref|NP_001013244|]
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serine protease 40 precursor [Rattus norvegicus]

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 ...
70-312 4.45e-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: 237.17  E-value: 4.45e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348  70 IYGGSIAKAERWPWQASLIFR-GRHICGAVLIDKNWVASAAHCFKRSlKPSDYRILLGYNELSNPSNYSRQMTLSKVIVH 148
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348 149 EDYNKLHSqEKDIVLIQLHLPVRYSSHIFPVCVPDQTTKEPSDESCWISGWGMVTDDKFLqaPFPLLDSEVFLMNDQECE 228
Cdd:cd00190  80 PNYNPSTY-DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348 229 AFFQTPqisiteyDAIKDDMICAGDITNQKSTCRGDSGGPLVCLLDSYWYLVGLASWSGACLEPiHSPSIFTRVSHFSDW 308
Cdd:cd00190 157 RAYSYG-------GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARP-NYPGVYTRVSSYLDW 228

                ....
gi 61557348 309 IEKK 312
Cdd:cd00190 229 IQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
70-312 4.45e-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: 237.17  E-value: 4.45e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348  70 IYGGSIAKAERWPWQASLIFR-GRHICGAVLIDKNWVASAAHCFKRSlKPSDYRILLGYNELSNPSNYSRQMTLSKVIVH 148
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348 149 EDYNKLHSqEKDIVLIQLHLPVRYSSHIFPVCVPDQTTKEPSDESCWISGWGMVTDDKFLqaPFPLLDSEVFLMNDQECE 228
Cdd:cd00190  80 PNYNPSTY-DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348 229 AFFQTPqisiteyDAIKDDMICAGDITNQKSTCRGDSGGPLVCLLDSYWYLVGLASWSGACLEPiHSPSIFTRVSHFSDW 308
Cdd:cd00190 157 RAYSYG-------GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARP-NYPGVYTRVSSYLDW 228

                ....
gi 61557348 309 IEKK 312
Cdd:cd00190 229 IQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
69-309 1.19e-72

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: 225.63  E-value: 1.19e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348     69 KIYGGSIAKAERWPWQASLIFRG-RHICGAVLIDKNWVASAAHCFkRSLKPSDYRILLGYNELSNPsNYSRQMTLSKVIV 147
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSG-EEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348    148 HEDYNKLHSqEKDIVLIQLHLPVRYSSHIFPVCVPDQTTKEPSDESCWISGWGmVTDDKFLQAPFPLLDSEVFLMNDQEC 227
Cdd:smart00020  79 HPNYNPSTY-DNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWG-RTSEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348    228 EAFFQTpqisiteYDAIKDDMICAGDITNQKSTCRGDSGGPLVClLDSYWYLVGLASWSGACLEPiHSPSIFTRVSHFSD 307
Cdd:smart00020 157 RRAYSG-------GGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARP-GKPGVYTRVSSYLD 227

                   ..
gi 61557348    308 WI 309
Cdd:smart00020 228 WI 229
Trypsin pfam00089
Trypsin;
70-309 2.31e-54

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 178.40  E-value: 2.31e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348    70 IYGGSIAKAERWPWQASLIFR-GRHICGAVLIDKNWVASAAHCFKRSlkpSDYRILLGYNELSNPSNYSRQMTLSKVIVH 148
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA---SDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348   149 EDYNKLhSQEKDIVLIQLHLPVRYSSHIFPVCVPDQTTKEPSDESCWISGWGmvtDDKFLQAPFPLLDSEVFLMNDQECE 228
Cdd:pfam00089  78 PNYNPD-TLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG---NTKTLGPSDTLQEVTVPVVSRETCR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348   229 AFFQTPqisiteydaIKDDMICAGdiTNQKSTCRGDSGGPLVCLLDsywYLVGLASWSGAClEPIHSPSIFTRVSHFSDW 308
Cdd:pfam00089 154 SAYGGT---------VTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGC-ASGNYPGVYTPVSSYLDW 218

                  .
gi 61557348   309 I 309
Cdd:pfam00089 219 I 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
67-310 1.38e-50

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 169.83  E-value: 1.38e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348  67 QGKIYGGSIAKAERWPWQASLIFRG---RHICGAVLIDKNWVASAAHCFKRSlKPSDYRILLGYNELSNPSNYSRqmTLS 143
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGSTDLSTSGGTVV--KVA 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348 144 KVIVHEDYNKlHSQEKDIVLIQLHLPVRYSShifPVCVPDQTTKEPSDESCWISGWGMVTDDkflQAPFP--LLDSEVFL 221
Cdd:COG5640 105 RIVVHPDYDP-ATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEG---PGSQSgtLRKADVPV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348 222 MNDQECEAFFqtpqisiteyDAIKDDMICAGDITNQKSTCRGDSGGPLVCLLDSYWYLVGLASWS-GAClePIHSPSIFT 300
Cdd:COG5640 178 VSDATCAAYG----------GFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGgGPC--AAGYPGVYT 245
                       250
                ....*....|
gi 61557348 301 RVSHFSDWIE 310
Cdd:COG5640 246 RVSAYRDWIK 255
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
70-312 4.45e-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: 237.17  E-value: 4.45e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348  70 IYGGSIAKAERWPWQASLIFR-GRHICGAVLIDKNWVASAAHCFKRSlKPSDYRILLGYNELSNPSNYSRQMTLSKVIVH 148
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348 149 EDYNKLHSqEKDIVLIQLHLPVRYSSHIFPVCVPDQTTKEPSDESCWISGWGMVTDDKFLqaPFPLLDSEVFLMNDQECE 228
Cdd:cd00190  80 PNYNPSTY-DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348 229 AFFQTPqisiteyDAIKDDMICAGDITNQKSTCRGDSGGPLVCLLDSYWYLVGLASWSGACLEPiHSPSIFTRVSHFSDW 308
Cdd:cd00190 157 RAYSYG-------GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARP-NYPGVYTRVSSYLDW 228

                ....
gi 61557348 309 IEKK 312
Cdd:cd00190 229 IQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
69-309 1.19e-72

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: 225.63  E-value: 1.19e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348     69 KIYGGSIAKAERWPWQASLIFRG-RHICGAVLIDKNWVASAAHCFkRSLKPSDYRILLGYNELSNPsNYSRQMTLSKVIV 147
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSG-EEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348    148 HEDYNKLHSqEKDIVLIQLHLPVRYSSHIFPVCVPDQTTKEPSDESCWISGWGmVTDDKFLQAPFPLLDSEVFLMNDQEC 227
Cdd:smart00020  79 HPNYNPSTY-DNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWG-RTSEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348    228 EAFFQTpqisiteYDAIKDDMICAGDITNQKSTCRGDSGGPLVClLDSYWYLVGLASWSGACLEPiHSPSIFTRVSHFSD 307
Cdd:smart00020 157 RRAYSG-------GGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARP-GKPGVYTRVSSYLD 227

                   ..
gi 61557348    308 WI 309
Cdd:smart00020 228 WI 229
Trypsin pfam00089
Trypsin;
70-309 2.31e-54

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 178.40  E-value: 2.31e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348    70 IYGGSIAKAERWPWQASLIFR-GRHICGAVLIDKNWVASAAHCFKRSlkpSDYRILLGYNELSNPSNYSRQMTLSKVIVH 148
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA---SDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348   149 EDYNKLhSQEKDIVLIQLHLPVRYSSHIFPVCVPDQTTKEPSDESCWISGWGmvtDDKFLQAPFPLLDSEVFLMNDQECE 228
Cdd:pfam00089  78 PNYNPD-TLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG---NTKTLGPSDTLQEVTVPVVSRETCR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348   229 AFFQTPqisiteydaIKDDMICAGdiTNQKSTCRGDSGGPLVCLLDsywYLVGLASWSGAClEPIHSPSIFTRVSHFSDW 308
Cdd:pfam00089 154 SAYGGT---------VTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGC-ASGNYPGVYTPVSSYLDW 218

                  .
gi 61557348   309 I 309
Cdd:pfam00089 219 I 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
67-310 1.38e-50

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 169.83  E-value: 1.38e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348  67 QGKIYGGSIAKAERWPWQASLIFRG---RHICGAVLIDKNWVASAAHCFKRSlKPSDYRILLGYNELSNPSNYSRqmTLS 143
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGSTDLSTSGGTVV--KVA 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348 144 KVIVHEDYNKlHSQEKDIVLIQLHLPVRYSShifPVCVPDQTTKEPSDESCWISGWGMVTDDkflQAPFP--LLDSEVFL 221
Cdd:COG5640 105 RIVVHPDYDP-ATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEG---PGSQSgtLRKADVPV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348 222 MNDQECEAFFqtpqisiteyDAIKDDMICAGDITNQKSTCRGDSGGPLVCLLDSYWYLVGLASWS-GAClePIHSPSIFT 300
Cdd:COG5640 178 VSDATCAAYG----------GFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGgGPC--AAGYPGVYT 245
                       250
                ....*....|
gi 61557348 301 RVSHFSDWIE 310
Cdd:COG5640 246 RVSAYRDWIK 255
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
81-194 8.07e-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: 52.94  E-value: 8.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557348    81 WPWQASLIFRGRHICGAVLIDKNWVASAAHCFKR-SLKPSDYRILLGYNE--LSNPSNYSRqmtLSKVIVHEDYnklhsQ 157
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDtNLRHQYISVVLGGAKtlKSIEGPYEQ---IVRVDCRHDI-----P 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 61557348   158 EKDIVLIQLHLPVRYSSHIFPVCVPDQTTKEPSDESC 194
Cdd:pfam09342  73 ESEISLLHLASPASFSNHVLPTFVPETRNENEKDNEC 109
 
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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