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Conserved domains on  [gi|1958732842|ref|XP_038952283|]
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putative serine protease 47 isoform X2 [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

 Zoom to residue level

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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 ...
83-334 4.86e-86

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: 260.67  E-value: 4.86e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842  83 VFGGQDTLAGQWPWQASLLYR-GLHLCGAVLIDSHWLVSTAHCFRNKsqAPEDYEVLLGNNQLYQKTKHTQKIPVNHIIN 161
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS--APSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842 162 HPDFEKFhSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGMLSEDSKgkrswrgskakllPPFSLQE 241
Cdd:cd00190    79 HPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-------------LPDVLQE 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842 242 GEVGIIENEFCNALYGQRlgqsrNYVHEEMLCAGGLSTGKSICRGDSGGPLVCYHISAWVLVGLASWGLDCRPSIYPSVF 321
Cdd:cd00190   145 VNVPIVSNAECKRAYSYG-----GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVY 219
                         250
                  ....*....|...
gi 1958732842 322 TRVTYFTDWISQV 334
Cdd:cd00190   220 TRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
83-334 4.86e-86

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: 260.67  E-value: 4.86e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842  83 VFGGQDTLAGQWPWQASLLYR-GLHLCGAVLIDSHWLVSTAHCFRNKsqAPEDYEVLLGNNQLYQKTKHTQKIPVNHIIN 161
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS--APSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842 162 HPDFEKFhSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGMLSEDSKgkrswrgskakllPPFSLQE 241
Cdd:cd00190    79 HPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-------------LPDVLQE 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842 242 GEVGIIENEFCNALYGQRlgqsrNYVHEEMLCAGGLSTGKSICRGDSGGPLVCYHISAWVLVGLASWGLDCRPSIYPSVF 321
Cdd:cd00190   145 VNVPIVSNAECKRAYSYG-----GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVY 219
                         250
                  ....*....|...
gi 1958732842 322 TRVTYFTDWISQV 334
Cdd:cd00190   220 TRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
82-331 5.02e-80

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: 245.28  E-value: 5.02e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842   82 KVFGGQDTLAGQWPWQASLLYRGL-HLCGAVLIDSHWLVSTAHCFRNKsqAPEDYEVLLGNNQLYQKTkHTQKIPVNHII 160
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGS--DPSNIRVRLGSHDLSSGE-EGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842  161 NHPDFEKfHSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGMLSEDSKGkrswrgskakllPPFSLQ 240
Cdd:smart00020  78 IHPNYNP-STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGS------------LPDTLQ 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842  241 EGEVGIIENEFCNALYGQrlgqsRNYVHEEMLCAGGLSTGKSICRGDSGGPLVCyHISAWVLVGLASWGLDCRPSIYPSV 320
Cdd:smart00020 145 EVNVPIVSNATCRRAYSG-----GGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGV 218
                          250
                   ....*....|.
gi 1958732842  321 FTRVTYFTDWI 331
Cdd:smart00020 219 YTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
83-331 1.02e-63

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 203.06  E-value: 1.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842  83 VFGGQDTLAGQWPWQASLLYRGL-HLCGAVLIDSHWLVSTAHCFRNksqaPEDYEVLLGNNQLYQKTKHTQKIPVNHIIN 161
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCVSG----ASDVKVVLGAHNIVLREGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842 162 HPDFEKFhSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGmlsedskgkRSWRGSkakllPPFSLQE 241
Cdd:pfam00089  77 HPNYNPD-TLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG---------NTKTLG-----PSDTLQE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842 242 GEVGIIENEFCNALYGqrlgqsrNYVHEEMLCAGGlsTGKSICRGDSGGPLVCyhiSAWVLVGLASWGLDCRPSIYPSVF 321
Cdd:pfam00089 142 VTVPVVSRETCRSAYG-------GTVTDTMICAGA--GGKDACQGDSGGPLVC---SDGELIGIVSWGYGCASGNYPGVY 209
                         250
                  ....*....|
gi 1958732842 322 TRVTYFTDWI 331
Cdd:pfam00089 210 TPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
82-334 8.66e-51

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 170.99  E-value: 8.66e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842  82 KVFGGQDTLAGQWPWQASLLYRG---LHLCGAVLIDSHWLVSTAHCFRNksQAPEDYEVLLGNNQLyqKTKHTQKIPVNH 158
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDG--DGPSDLRVVIGSTDL--STSGGTVVKVAR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842 159 IINHPDFEKfHSFGSDIAMLQLRLPVNFtsyVVPACLPSKDTQLSNHTSCWITGWGMLSEDskgkrswRGSkakllPPFS 238
Cdd:COG5640   106 IVVHPDYDP-ATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEG-------PGS-----QSGT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842 239 LQEGEVGIIENEFCNALYGqrlgqsrnYVHEEMLCAGGLSTGKSICRGDSGGPLVCYHISAWVLVGLASWGL-DCRPSiY 317
Cdd:COG5640   170 LRKADVPVVSDATCAAYGG--------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGgPCAAG-Y 240
                         250
                  ....*....|....*..
gi 1958732842 318 PSVFTRVTYFTDWISQV 334
Cdd:COG5640   241 PGVYTRVSAYRDWIKST 257
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
83-334 4.86e-86

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: 260.67  E-value: 4.86e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842  83 VFGGQDTLAGQWPWQASLLYR-GLHLCGAVLIDSHWLVSTAHCFRNKsqAPEDYEVLLGNNQLYQKTKHTQKIPVNHIIN 161
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS--APSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842 162 HPDFEKFhSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGMLSEDSKgkrswrgskakllPPFSLQE 241
Cdd:cd00190    79 HPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-------------LPDVLQE 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842 242 GEVGIIENEFCNALYGQRlgqsrNYVHEEMLCAGGLSTGKSICRGDSGGPLVCYHISAWVLVGLASWGLDCRPSIYPSVF 321
Cdd:cd00190   145 VNVPIVSNAECKRAYSYG-----GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVY 219
                         250
                  ....*....|...
gi 1958732842 322 TRVTYFTDWISQV 334
Cdd:cd00190   220 TRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
82-331 5.02e-80

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: 245.28  E-value: 5.02e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842   82 KVFGGQDTLAGQWPWQASLLYRGL-HLCGAVLIDSHWLVSTAHCFRNKsqAPEDYEVLLGNNQLYQKTkHTQKIPVNHII 160
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGS--DPSNIRVRLGSHDLSSGE-EGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842  161 NHPDFEKfHSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGMLSEDSKGkrswrgskakllPPFSLQ 240
Cdd:smart00020  78 IHPNYNP-STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGS------------LPDTLQ 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842  241 EGEVGIIENEFCNALYGQrlgqsRNYVHEEMLCAGGLSTGKSICRGDSGGPLVCyHISAWVLVGLASWGLDCRPSIYPSV 320
Cdd:smart00020 145 EVNVPIVSNATCRRAYSG-----GGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGV 218
                          250
                   ....*....|.
gi 1958732842  321 FTRVTYFTDWI 331
Cdd:smart00020 219 YTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
83-331 1.02e-63

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 203.06  E-value: 1.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842  83 VFGGQDTLAGQWPWQASLLYRGL-HLCGAVLIDSHWLVSTAHCFRNksqaPEDYEVLLGNNQLYQKTKHTQKIPVNHIIN 161
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCVSG----ASDVKVVLGAHNIVLREGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842 162 HPDFEKFhSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGmlsedskgkRSWRGSkakllPPFSLQE 241
Cdd:pfam00089  77 HPNYNPD-TLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG---------NTKTLG-----PSDTLQE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842 242 GEVGIIENEFCNALYGqrlgqsrNYVHEEMLCAGGlsTGKSICRGDSGGPLVCyhiSAWVLVGLASWGLDCRPSIYPSVF 321
Cdd:pfam00089 142 VTVPVVSRETCRSAYG-------GTVTDTMICAGA--GGKDACQGDSGGPLVC---SDGELIGIVSWGYGCASGNYPGVY 209
                         250
                  ....*....|
gi 1958732842 322 TRVTYFTDWI 331
Cdd:pfam00089 210 TPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
82-334 8.66e-51

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 170.99  E-value: 8.66e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842  82 KVFGGQDTLAGQWPWQASLLYRG---LHLCGAVLIDSHWLVSTAHCFRNksQAPEDYEVLLGNNQLyqKTKHTQKIPVNH 158
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDG--DGPSDLRVVIGSTDL--STSGGTVVKVAR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842 159 IINHPDFEKfHSFGSDIAMLQLRLPVNFtsyVVPACLPSKDTQLSNHTSCWITGWGMLSEDskgkrswRGSkakllPPFS 238
Cdd:COG5640   106 IVVHPDYDP-ATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEG-------PGS-----QSGT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842 239 LQEGEVGIIENEFCNALYGqrlgqsrnYVHEEMLCAGGLSTGKSICRGDSGGPLVCYHISAWVLVGLASWGL-DCRPSiY 317
Cdd:COG5640   170 LRKADVPVVSDATCAAYGG--------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGgPCAAG-Y 240
                         250
                  ....*....|....*..
gi 1958732842 318 PSVFTRVTYFTDWISQV 334
Cdd:COG5640   241 PGVYTRVSAYRDWIKST 257
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
94-208 1.28e-10

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: 58.33  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732842  94 WPWQASLLYRGLHLCGAVLIDSHWLVSTAHCFRNKSQAPEDYEVLLGNNqlyqKTKHTQKIPVNHIINHPDFEKFHSfgS 173
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVLGGA----KTLKSIEGPYEQIVRVDCRHDIPE--S 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958732842 174 DIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSC 208
Cdd:pfam09342  75 EISLLHLASPASFSNHVLPTFVPETRNENEKDNEC 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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