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Conserved domains on  [gi|1958732847|ref|XP_038952284|]
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putative serine protease 47 isoform X4 [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 ...
11-270 3.62e-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: 258.75  E-value: 3.62e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847  11 VFGGQDTLAGQWPWQASLLYR-GLHLCGAVLIDSHWLVSTAHCFRNKsqAPEDYEVLLGNNQLYQKTKHTQKIPVNHIIN 89
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS--APSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847  90 HPDFEKFhSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGmlsedskgkrswrgskgrekrKIRAKL 169
Cdd:cd00190    79 HPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG---------------------RTSEGG 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847 170 LPPFSLQEGEVGIIENEFCNALYGQRlgqsrNYVHEEMLCAGGLSTGKSICRGDSGGPLVCYHISAWVLVGLASWGLDCR 249
Cdd:cd00190   137 PLPDVLQEVNVPIVSNAECKRAYSYG-----GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCA 211
                         250       260
                  ....*....|....*....|.
gi 1958732847 250 PSIYPSVFTRVTYFTDWISQV 270
Cdd:cd00190   212 RPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
11-270 3.62e-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: 258.75  E-value: 3.62e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847  11 VFGGQDTLAGQWPWQASLLYR-GLHLCGAVLIDSHWLVSTAHCFRNKsqAPEDYEVLLGNNQLYQKTKHTQKIPVNHIIN 89
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS--APSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847  90 HPDFEKFhSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGmlsedskgkrswrgskgrekrKIRAKL 169
Cdd:cd00190    79 HPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG---------------------RTSEGG 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847 170 LPPFSLQEGEVGIIENEFCNALYGQRlgqsrNYVHEEMLCAGGLSTGKSICRGDSGGPLVCYHISAWVLVGLASWGLDCR 249
Cdd:cd00190   137 PLPDVLQEVNVPIVSNAECKRAYSYG-----GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCA 211
                         250       260
                  ....*....|....*....|.
gi 1958732847 250 PSIYPSVFTRVTYFTDWISQV 270
Cdd:cd00190   212 RPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
10-267 3.29e-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: 243.35  E-value: 3.29e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847   10 KVFGGQDTLAGQWPWQASLLYRGL-HLCGAVLIDSHWLVSTAHCFRNKsqAPEDYEVLLGNNQLYQKTkHTQKIPVNHII 88
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGS--DPSNIRVRLGSHDLSSGE-EGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847   89 NHPDFEKfHSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGMLSEDSKGkrswrgskgrekrkirak 168
Cdd:smart00020  78 IHPNYNP-STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGS------------------ 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847  169 llPPFSLQEGEVGIIENEFCNALYGQrlgqsRNYVHEEMLCAGGLSTGKSICRGDSGGPLVCyHISAWVLVGLASWGLDC 248
Cdd:smart00020 139 --LPDTLQEVNVPIVSNATCRRAYSG-----GGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGC 210
                          250
                   ....*....|....*....
gi 1958732847  249 RPSIYPSVFTRVTYFTDWI 267
Cdd:smart00020 211 ARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
11-267 2.65e-64

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 202.67  E-value: 2.65e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847  11 VFGGQDTLAGQWPWQASLLYRGL-HLCGAVLIDSHWLVSTAHCFRNksqaPEDYEVLLGNNQLYQKTKHTQKIPVNHIIN 89
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCVSG----ASDVKVVLGAHNIVLREGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847  90 HPDFEKFhSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGmlsedskgkRSWRGSkgrekrkirakl 169
Cdd:pfam00089  77 HPNYNPD-TLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG---------NTKTLG------------ 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847 170 lPPFSLQEGEVGIIENEFCNALYGqrlgqsrNYVHEEMLCAGGlsTGKSICRGDSGGPLVCyhiSAWVLVGLASWGLDCR 249
Cdd:pfam00089 135 -PSDTLQEVTVPVVSRETCRSAYG-------GTVTDTMICAGA--GGKDACQGDSGGPLVC---SDGELIGIVSWGYGCA 201
                         250
                  ....*....|....*...
gi 1958732847 250 PSIYPSVFTRVTYFTDWI 267
Cdd:pfam00089 202 SGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
10-270 3.87e-52

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 172.53  E-value: 3.87e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847  10 KVFGGQDTLAGQWPWQASLLYRG---LHLCGAVLIDSHWLVSTAHCFRNKSqaPEDYEVLLGNNQLyqKTKHTQKIPVNH 86
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG--PSDLRVVIGSTDL--STSGGTVVKVAR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847  87 IINHPDFEKfHSFGSDIAMLQLRLPVNFtsyVVPACLPSKDTQLSNHTSCWITGWGMLSEDskgkrswRGSKGREkrkir 166
Cdd:COG5640   106 IVVHPDYDP-ATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEG-------PGSQSGT----- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847 167 akllppfsLQEGEVGIIENEFCNALYGqrlgqsrnYVHEEMLCAGGLSTGKSICRGDSGGPLVCYHISAWVLVGLASWGL 246
Cdd:COG5640   170 --------LRKADVPVVSDATCAAYGG--------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGG 233
                         250       260
                  ....*....|....*....|....*
gi 1958732847 247 -DCRPSiYPSVFTRVTYFTDWISQV 270
Cdd:COG5640   234 gPCAAG-YPGVYTRVSAYRDWIKST 257
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
11-270 3.62e-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: 258.75  E-value: 3.62e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847  11 VFGGQDTLAGQWPWQASLLYR-GLHLCGAVLIDSHWLVSTAHCFRNKsqAPEDYEVLLGNNQLYQKTKHTQKIPVNHIIN 89
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS--APSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847  90 HPDFEKFhSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGmlsedskgkrswrgskgrekrKIRAKL 169
Cdd:cd00190    79 HPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG---------------------RTSEGG 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847 170 LPPFSLQEGEVGIIENEFCNALYGQRlgqsrNYVHEEMLCAGGLSTGKSICRGDSGGPLVCYHISAWVLVGLASWGLDCR 249
Cdd:cd00190   137 PLPDVLQEVNVPIVSNAECKRAYSYG-----GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCA 211
                         250       260
                  ....*....|....*....|.
gi 1958732847 250 PSIYPSVFTRVTYFTDWISQV 270
Cdd:cd00190   212 RPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
10-267 3.29e-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: 243.35  E-value: 3.29e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847   10 KVFGGQDTLAGQWPWQASLLYRGL-HLCGAVLIDSHWLVSTAHCFRNKsqAPEDYEVLLGNNQLYQKTkHTQKIPVNHII 88
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGS--DPSNIRVRLGSHDLSSGE-EGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847   89 NHPDFEKfHSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGMLSEDSKGkrswrgskgrekrkirak 168
Cdd:smart00020  78 IHPNYNP-STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGS------------------ 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847  169 llPPFSLQEGEVGIIENEFCNALYGQrlgqsRNYVHEEMLCAGGLSTGKSICRGDSGGPLVCyHISAWVLVGLASWGLDC 248
Cdd:smart00020 139 --LPDTLQEVNVPIVSNATCRRAYSG-----GGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGC 210
                          250
                   ....*....|....*....
gi 1958732847  249 RPSIYPSVFTRVTYFTDWI 267
Cdd:smart00020 211 ARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
11-267 2.65e-64

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 202.67  E-value: 2.65e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847  11 VFGGQDTLAGQWPWQASLLYRGL-HLCGAVLIDSHWLVSTAHCFRNksqaPEDYEVLLGNNQLYQKTKHTQKIPVNHIIN 89
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCVSG----ASDVKVVLGAHNIVLREGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847  90 HPDFEKFhSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGmlsedskgkRSWRGSkgrekrkirakl 169
Cdd:pfam00089  77 HPNYNPD-TLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG---------NTKTLG------------ 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847 170 lPPFSLQEGEVGIIENEFCNALYGqrlgqsrNYVHEEMLCAGGlsTGKSICRGDSGGPLVCyhiSAWVLVGLASWGLDCR 249
Cdd:pfam00089 135 -PSDTLQEVTVPVVSRETCRSAYG-------GTVTDTMICAGA--GGKDACQGDSGGPLVC---SDGELIGIVSWGYGCA 201
                         250
                  ....*....|....*...
gi 1958732847 250 PSIYPSVFTRVTYFTDWI 267
Cdd:pfam00089 202 SGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
10-270 3.87e-52

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 172.53  E-value: 3.87e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847  10 KVFGGQDTLAGQWPWQASLLYRG---LHLCGAVLIDSHWLVSTAHCFRNKSqaPEDYEVLLGNNQLyqKTKHTQKIPVNH 86
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG--PSDLRVVIGSTDL--STSGGTVVKVAR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847  87 IINHPDFEKfHSFGSDIAMLQLRLPVNFtsyVVPACLPSKDTQLSNHTSCWITGWGMLSEDskgkrswRGSKGREkrkir 166
Cdd:COG5640   106 IVVHPDYDP-ATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEG-------PGSQSGT----- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847 167 akllppfsLQEGEVGIIENEFCNALYGqrlgqsrnYVHEEMLCAGGLSTGKSICRGDSGGPLVCYHISAWVLVGLASWGL 246
Cdd:COG5640   170 --------LRKADVPVVSDATCAAYGG--------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGG 233
                         250       260
                  ....*....|....*....|....*
gi 1958732847 247 -DCRPSiYPSVFTRVTYFTDWISQV 270
Cdd:COG5640   234 gPCAAG-YPGVYTRVSAYRDWIKST 257
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
22-136 1.39e-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: 57.94  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732847  22 WPWQASLLYRGLHLCGAVLIDSHWLVSTAHCFRNKSQAPEDYEVLLGNNqlyqKTKHTQKIPVNHIINHPDFEKFHSfgS 101
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVLGGA----KTLKSIEGPYEQIVRVDCRHDIPE--S 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958732847 102 DIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSC 136
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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