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Conserved domains on  [gi|1958732850|ref|XP_038952285|]
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putative serine protease 47 isoform X6 [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 ...
83-294 1.37e-57

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: 184.79  E-value: 1.37e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850  83 VFGGQDTLAGQWPWQASLLYR-GLHLCGAVLIDSHWLVSTAHCFRNKsqAPEDYEVLLGNNQLYQKTKHTQKIPVNHIIN 161
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS--APSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850 162 HPDFEKFhSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGmlsedskgkrswrgskgrekrKIRAKL 241
Cdd:cd00190    79 HPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG---------------------RTSEGG 136
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958732850 242 LPPFSLQEGEVGIIENEFCNALYGQrlgqsRNYVHEEMLCAGGLSTGKSICRG 294
Cdd:cd00190   137 PLPDVLQEVNVPIVSNAECKRAYSY-----GGTITDNMLCAGGLEGGKDACQG 184
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
83-294 1.37e-57

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: 184.79  E-value: 1.37e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850  83 VFGGQDTLAGQWPWQASLLYR-GLHLCGAVLIDSHWLVSTAHCFRNKsqAPEDYEVLLGNNQLYQKTKHTQKIPVNHIIN 161
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS--APSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850 162 HPDFEKFhSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGmlsedskgkrswrgskgrekrKIRAKL 241
Cdd:cd00190    79 HPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG---------------------RTSEGG 136
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958732850 242 LPPFSLQEGEVGIIENEFCNALYGQrlgqsRNYVHEEMLCAGGLSTGKSICRG 294
Cdd:cd00190   137 PLPDVLQEVNVPIVSNAECKRAYSY-----GGTITDNMLCAGGLEGGKDACQG 184
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
82-294 2.01e-53

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: 174.02  E-value: 2.01e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850   82 KVFGGQDTLAGQWPWQASLLYRGL-HLCGAVLIDSHWLVSTAHCFRNKsqAPEDYEVLLGNNQLYQKTkHTQKIPVNHII 160
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGS--DPSNIRVRLGSHDLSSGE-EGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850  161 NHPDFEKfHSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGMLSEDSKGkrswrgskgrekrkirak 240
Cdd:smart00020  78 IHPNYNP-STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGS------------------ 138
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958732850  241 llPPFSLQEGEVGIIENEFCNALYGQrlgqsRNYVHEEMLCAGGLSTGKSICRG 294
Cdd:smart00020 139 --LPDTLQEVNVPIVSNATCRRAYSG-----GGAITDNMLCAGGLEGGKDACQG 185
Trypsin pfam00089
Trypsin;
83-294 1.76e-43

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 147.97  E-value: 1.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850  83 VFGGQDTLAGQWPWQASLLYRGL-HLCGAVLIDSHWLVSTAHCFRNksqaPEDYEVLLGNNQLYQKTKHTQKIPVNHIIN 161
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCVSG----ASDVKVVLGAHNIVLREGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850 162 HPDFEKFhSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGmlsedskgkRSWRGSkgrekrkirakl 241
Cdd:pfam00089  77 HPNYNPD-TLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG---------NTKTLG------------ 134
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958732850 242 lPPFSLQEGEVGIIENEFCNALYGqrlgqsrNYVHEEMLCAGGlsTGKSICRG 294
Cdd:pfam00089 135 -PSDTLQEVTVPVVSRETCRSAYG-------GTVTDTMICAGA--GGKDACQG 177
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
82-294 2.12e-29

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 112.44  E-value: 2.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850  82 KVFGGQDTLAGQWPWQASLLYRG---LHLCGAVLIDSHWLVSTAHCFRNksQAPEDYEVLLGNNQLyqKTKHTQKIPVNH 158
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDG--DGPSDLRVVIGSTDL--STSGGTVVKVAR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850 159 IINHPDFEKfHSFGSDIAMLQLRLPVNFtsyVVPACLPSKDTQLSNHTSCWITGWGMLSEDskgkrswRGSKGREkrkir 238
Cdd:COG5640   106 IVVHPDYDP-ATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEG-------PGSQSGT----- 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958732850 239 akllppfsLQEGEVGIIENEFCNALYGqrlgqsrnYVHEEMLCAGGLSTGKSICRG 294
Cdd:COG5640   170 --------LRKADVPVVSDATCAAYGG--------FDGGTMLCAGYPEGGKDACQG 209
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
83-294 1.37e-57

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: 184.79  E-value: 1.37e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850  83 VFGGQDTLAGQWPWQASLLYR-GLHLCGAVLIDSHWLVSTAHCFRNKsqAPEDYEVLLGNNQLYQKTKHTQKIPVNHIIN 161
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS--APSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850 162 HPDFEKFhSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGmlsedskgkrswrgskgrekrKIRAKL 241
Cdd:cd00190    79 HPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG---------------------RTSEGG 136
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958732850 242 LPPFSLQEGEVGIIENEFCNALYGQrlgqsRNYVHEEMLCAGGLSTGKSICRG 294
Cdd:cd00190   137 PLPDVLQEVNVPIVSNAECKRAYSY-----GGTITDNMLCAGGLEGGKDACQG 184
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
82-294 2.01e-53

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: 174.02  E-value: 2.01e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850   82 KVFGGQDTLAGQWPWQASLLYRGL-HLCGAVLIDSHWLVSTAHCFRNKsqAPEDYEVLLGNNQLYQKTkHTQKIPVNHII 160
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGS--DPSNIRVRLGSHDLSSGE-EGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850  161 NHPDFEKfHSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGMLSEDSKGkrswrgskgrekrkirak 240
Cdd:smart00020  78 IHPNYNP-STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGS------------------ 138
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958732850  241 llPPFSLQEGEVGIIENEFCNALYGQrlgqsRNYVHEEMLCAGGLSTGKSICRG 294
Cdd:smart00020 139 --LPDTLQEVNVPIVSNATCRRAYSG-----GGAITDNMLCAGGLEGGKDACQG 185
Trypsin pfam00089
Trypsin;
83-294 1.76e-43

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 147.97  E-value: 1.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850  83 VFGGQDTLAGQWPWQASLLYRGL-HLCGAVLIDSHWLVSTAHCFRNksqaPEDYEVLLGNNQLYQKTKHTQKIPVNHIIN 161
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCVSG----ASDVKVVLGAHNIVLREGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850 162 HPDFEKFhSFGSDIAMLQLRLPVNFTSYVVPACLPSKDTQLSNHTSCWITGWGmlsedskgkRSWRGSkgrekrkirakl 241
Cdd:pfam00089  77 HPNYNPD-TLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG---------NTKTLG------------ 134
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958732850 242 lPPFSLQEGEVGIIENEFCNALYGqrlgqsrNYVHEEMLCAGGlsTGKSICRG 294
Cdd:pfam00089 135 -PSDTLQEVTVPVVSRETCRSAYG-------GTVTDTMICAGA--GGKDACQG 177
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
82-294 2.12e-29

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 112.44  E-value: 2.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850  82 KVFGGQDTLAGQWPWQASLLYRG---LHLCGAVLIDSHWLVSTAHCFRNksQAPEDYEVLLGNNQLyqKTKHTQKIPVNH 158
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDG--DGPSDLRVVIGSTDL--STSGGTVVKVAR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850 159 IINHPDFEKfHSFGSDIAMLQLRLPVNFtsyVVPACLPSKDTQLSNHTSCWITGWGMLSEDskgkrswRGSKGREkrkir 238
Cdd:COG5640   106 IVVHPDYDP-ATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEG-------PGSQSGT----- 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958732850 239 akllppfsLQEGEVGIIENEFCNALYGqrlgqsrnYVHEEMLCAGGLSTGKSICRG 294
Cdd:COG5640   170 --------LRKADVPVVSDATCAAYGG--------FDGGTMLCAGYPEGGKDACQG 209
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
94-208 5.54e-11

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: 58.71  E-value: 5.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732850  94 WPWQASLLYRGLHLCGAVLIDSHWLVSTAHCFRNKSQAPEDYEVLLGNNqlyqKTKHTQKIPVNHIINHPDFEKFHSfgS 173
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVLGGA----KTLKSIEGPYEQIVRVDCRHDIPE--S 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958732850 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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