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Conserved domains on  [gi|1958790936|ref|XP_038935652|]
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serine protease 57 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 ...
1-211 2.49e-71

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: 217.14  E-value: 2.49e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936   1 MASVNFE-GHHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPTQQVFGIAAVVSHPDFEPTTQANDICLL 79
Cdd:cd00190    15 QVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDNDIALL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936  80 RLNGSAVLGPAVRLLRLPRRGAKPPvAGTRCRVSGWGSVSDFEEPPPGLMEVEVRILDLSVCNSSWQ--GQLSPAMLCTh 157
Cdd:cd00190    95 KLKRPVTLSDNVRPICLPSSGYNLP-AGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYSygGTITDNMLCA- 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958790936 158 SGDRRRRGFCSADSGGPLVCGNR----AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 211
Cdd:cd00190   173 GGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSW-GSGCARPNYPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-211 2.49e-71

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: 217.14  E-value: 2.49e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936   1 MASVNFE-GHHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPTQQVFGIAAVVSHPDFEPTTQANDICLL 79
Cdd:cd00190    15 QVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDNDIALL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936  80 RLNGSAVLGPAVRLLRLPRRGAKPPvAGTRCRVSGWGSVSDFEEPPPGLMEVEVRILDLSVCNSSWQ--GQLSPAMLCTh 157
Cdd:cd00190    95 KLKRPVTLSDNVRPICLPSSGYNLP-AGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYSygGTITDNMLCA- 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958790936 158 SGDRRRRGFCSADSGGPLVCGNR----AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 211
Cdd:cd00190   173 GGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSW-GSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-211 5.80e-67

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: 205.99  E-value: 5.80e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936    1 MASVNFEG-HHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPtQQVFGIAAVVSHPDFEPTTQANDICLL 79
Cdd:smart00020  16 QVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIHPNYNPSTYDNDIALL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936   80 RLNGSAVLGPAVRLLRLPRRGAKPPvAGTRCRVSGWGSVSDFEEPPP-GLMEVEVRILDLSVCNSSWQGQ--LSPAMLCT 156
Cdd:smart00020  95 KLKEPVTLSDNVRPICLPSSNYNVP-AGTTCTVSGWGRTSEGAGSLPdTLQEVNVPIVSNATCRRAYSGGgaITDNMLCA 173
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958790936  157 hSGDRRRRGFCSADSGGPLVCGNR---AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 211
Cdd:smart00020 174 -GGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSW-GSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-211 8.75e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 184.95  E-value: 8.75e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936   1 MASVNFEGHHH-CGGFLFHAHWVLSAAHCFSDRdpSTGLVVLGAHALLTPEPTQQVFGIAAVVSHPDFEPTTQANDICLL 79
Cdd:pfam00089  15 QVSLQLSSGKHfCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPDTLDNDIALL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936  80 RLNGSAVLGPAVRLLRLPRRGAKPPVaGTRCRVSGWGSVSDFEEPPPgLMEVEVRILDLSVCNSSWQGQLSPAMLCTHSG 159
Cdd:pfam00089  93 KLESPVTLGDTVRPICLPDASSDLPV-GTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCRSAYGGTVTDTMICAGAG 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958790936 160 DrrrRGFCSADSGGPLVCGNR-AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 211
Cdd:pfam00089 171 G---KDACQGDSGGPLVCSDGeLIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
10-219 3.30e-46

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 154.04  E-value: 3.30e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936  10 HHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPtqQVFGIAAVVSHPDFEPTTQANDICLLRLNGSAVLGP 89
Cdd:COG5640    57 QFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVA 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936  90 AVRLLrlprRGAKPPVAGTRCRVSGWGSVSDFEEPPPG-LMEVEVRILDLSVCNsSWQGQLSPAMLCThSGDRRRRGFCS 168
Cdd:COG5640   135 PAPLA----TSADAAAPGTPATVAGWGRTSEGPGSQSGtLRKADVPVVSDATCA-AYGGFDGGTMLCA-GYPEGGKDACQ 208
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958790936 169 ADSGGPLV----CGNRAHGLVSFSGLWCGdPKTPDVYTQVSAFVSWIWDVVRASP 219
Cdd:COG5640   209 GDSGGPLVvkdgGGWVLVGVVSWGGGPCA-AGYPGVYTRVSAYRDWIKSTAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-211 2.49e-71

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: 217.14  E-value: 2.49e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936   1 MASVNFE-GHHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPTQQVFGIAAVVSHPDFEPTTQANDICLL 79
Cdd:cd00190    15 QVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDNDIALL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936  80 RLNGSAVLGPAVRLLRLPRRGAKPPvAGTRCRVSGWGSVSDFEEPPPGLMEVEVRILDLSVCNSSWQ--GQLSPAMLCTh 157
Cdd:cd00190    95 KLKRPVTLSDNVRPICLPSSGYNLP-AGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYSygGTITDNMLCA- 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958790936 158 SGDRRRRGFCSADSGGPLVCGNR----AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 211
Cdd:cd00190   173 GGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSW-GSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-211 5.80e-67

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: 205.99  E-value: 5.80e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936    1 MASVNFEG-HHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPtQQVFGIAAVVSHPDFEPTTQANDICLL 79
Cdd:smart00020  16 QVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIHPNYNPSTYDNDIALL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936   80 RLNGSAVLGPAVRLLRLPRRGAKPPvAGTRCRVSGWGSVSDFEEPPP-GLMEVEVRILDLSVCNSSWQGQ--LSPAMLCT 156
Cdd:smart00020  95 KLKEPVTLSDNVRPICLPSSNYNVP-AGTTCTVSGWGRTSEGAGSLPdTLQEVNVPIVSNATCRRAYSGGgaITDNMLCA 173
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958790936  157 hSGDRRRRGFCSADSGGPLVCGNR---AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 211
Cdd:smart00020 174 -GGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSW-GSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-211 8.75e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 184.95  E-value: 8.75e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936   1 MASVNFEGHHH-CGGFLFHAHWVLSAAHCFSDRdpSTGLVVLGAHALLTPEPTQQVFGIAAVVSHPDFEPTTQANDICLL 79
Cdd:pfam00089  15 QVSLQLSSGKHfCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPDTLDNDIALL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936  80 RLNGSAVLGPAVRLLRLPRRGAKPPVaGTRCRVSGWGSVSDFEEPPPgLMEVEVRILDLSVCNSSWQGQLSPAMLCTHSG 159
Cdd:pfam00089  93 KLESPVTLGDTVRPICLPDASSDLPV-GTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCRSAYGGTVTDTMICAGAG 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958790936 160 DrrrRGFCSADSGGPLVCGNR-AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 211
Cdd:pfam00089 171 G---KDACQGDSGGPLVCSDGeLIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
10-219 3.30e-46

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 154.04  E-value: 3.30e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936  10 HHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPtqQVFGIAAVVSHPDFEPTTQANDICLLRLNGSAVLGP 89
Cdd:COG5640    57 QFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVA 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936  90 AVRLLrlprRGAKPPVAGTRCRVSGWGSVSDFEEPPPG-LMEVEVRILDLSVCNsSWQGQLSPAMLCThSGDRRRRGFCS 168
Cdd:COG5640   135 PAPLA----TSADAAAPGTPATVAGWGRTSEGPGSQSGtLRKADVPVVSDATCA-AYGGFDGGTMLCA-GYPEGGKDACQ 208
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958790936 169 ADSGGPLV----CGNRAHGLVSFSGLWCGdPKTPDVYTQVSAFVSWIWDVVRASP 219
Cdd:COG5640   209 GDSGGPLVvkdgGGWVLVGVVSWGGGPCA-AGYPGVYTRVSAYRDWIKSTAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
8-116 5.46e-03

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 36.58  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790936   8 GHHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPtQQVFGIAAVVSHPDFEPTTQAN-DICLLRLNGSav 86
Cdd:COG3591    10 GGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGP-YGTATATRFRVPPGWVASGDAGyDYALLRLDEP-- 86
                          90       100       110
                  ....*....|....*....|....*....|
gi 1958790936  87 LGPAVRLLRLprRGAKPPVAGTRCRVSGWG 116
Cdd:COG3591    87 LGDTTGWLGL--AFNDAPLAGEPVTIIGYP 114
 
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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