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Conserved domains on  [gi|1958790919|ref|XP_038935644|]
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serine protease 57 isoform X1 [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 ...
46-270 1.68e-79

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: 240.26  E-value: 1.68e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919  46 IVGGHEVKPHARPYMASVNFE-GHHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPTQQVFGIAAVVSHP 124
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919 125 DFEPTTQANDICLLRLNGSAVLGPAVRLLRLPRRGAKPPvAGTRCRVSGWGSVSDFEEPPPGLMEVEVRILDLSVCNSSW 204
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLP-AGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958790919 205 Q--GQLSPAMLCThSGDRRRRGFCSADSGGPLVCGNR----AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 270
Cdd:cd00190   160 SygGTITDNMLCA-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 ...
46-270 1.68e-79

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: 240.26  E-value: 1.68e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919  46 IVGGHEVKPHARPYMASVNFE-GHHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPTQQVFGIAAVVSHP 124
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919 125 DFEPTTQANDICLLRLNGSAVLGPAVRLLRLPRRGAKPPvAGTRCRVSGWGSVSDFEEPPPGLMEVEVRILDLSVCNSSW 204
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLP-AGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958790919 205 Q--GQLSPAMLCThSGDRRRRGFCSADSGGPLVCGNR----AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 270
Cdd:cd00190   160 SygGTITDNMLCA-GGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSW-GSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
45-270 5.38e-75

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: 228.72  E-value: 5.38e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919   45 HIVGGHEVKPHARPYMASVNFEG-HHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPtQQVFGIAAVVSH 123
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919  124 PDFEPTTQANDICLLRLNGSAVLGPAVRLLRLPRRGAKPPvAGTRCRVSGWGSVSDFEEPPP-GLMEVEVRILDLSVCNS 202
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVP-AGTTCTVSGWGRTSEGAGSLPdTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958790919  203 SWQGQ--LSPAMLCThSGDRRRRGFCSADSGGPLVCGNR---AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 270
Cdd:smart00020 159 AYSGGgaITDNMLCA-GGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSW-GSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
46-270 1.19e-65

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 204.60  E-value: 1.19e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919  46 IVGGHEVKPHARPYMASVNFEGHHH-CGGFLFHAHWVLSAAHCFSDRdpSTGLVVLGAHALLTPEPTQQVFGIAAVVSHP 124
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919 125 DFEPTTQANDICLLRLNGSAVLGPAVRLLRLPRRGAKPPVaGTRCRVSGWGSVSDFEEPPPgLMEVEVRILDLSVCNSSW 204
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPV-GTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958790919 205 QGQLSPAMLCTHSGDrrrRGFCSADSGGPLVCGNR-AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 270
Cdd:pfam00089 157 GGTVTDTMICAGAGG---KDACQGDSGGPLVCSDGeLIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
46-278 3.58e-50

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 166.36  E-value: 3.58e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919  46 IVGGHEVKPHARPYMASVNFEG---HHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPtqQVFGIAAVVS 122
Cdd:COG5640    31 IVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGG--TVVKVARIVV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919 123 HPDFEPTTQANDICLLRLNGSAVLGPAVRLLrlprRGAKPPVAGTRCRVSGWGSVSDFEEPPPG-LMEVEVRILDLSVCN 201
Cdd:COG5640   109 HPDYDPATPGNDIALLKLATPVPGVAPAPLA----TSADAAAPGTPATVAGWGRTSEGPGSQSGtLRKADVPVVSDATCA 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919 202 sSWQGQLSPAMLCThSGDRRRRGFCSADSGGPLV----CGNRAHGLVSFSGLWCGdPKTPDVYTQVSAFVSWIWDVVRAS 277
Cdd:COG5640   185 -AYGGFDGGTMLCA-GYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCA-AGYPGVYTRVSAYRDWIKSTAGGL 261

                  .
gi 1958790919 278 P 278
Cdd:COG5640   262 G 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
46-270 1.68e-79

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: 240.26  E-value: 1.68e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919  46 IVGGHEVKPHARPYMASVNFE-GHHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPTQQVFGIAAVVSHP 124
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919 125 DFEPTTQANDICLLRLNGSAVLGPAVRLLRLPRRGAKPPvAGTRCRVSGWGSVSDFEEPPPGLMEVEVRILDLSVCNSSW 204
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLP-AGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958790919 205 Q--GQLSPAMLCThSGDRRRRGFCSADSGGPLVCGNR----AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 270
Cdd:cd00190   160 SygGTITDNMLCA-GGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSW-GSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
45-270 5.38e-75

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: 228.72  E-value: 5.38e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919   45 HIVGGHEVKPHARPYMASVNFEG-HHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPtQQVFGIAAVVSH 123
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919  124 PDFEPTTQANDICLLRLNGSAVLGPAVRLLRLPRRGAKPPvAGTRCRVSGWGSVSDFEEPPP-GLMEVEVRILDLSVCNS 202
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVP-AGTTCTVSGWGRTSEGAGSLPdTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958790919  203 SWQGQ--LSPAMLCThSGDRRRRGFCSADSGGPLVCGNR---AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 270
Cdd:smart00020 159 AYSGGgaITDNMLCA-GGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSW-GSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
46-270 1.19e-65

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 204.60  E-value: 1.19e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919  46 IVGGHEVKPHARPYMASVNFEGHHH-CGGFLFHAHWVLSAAHCFSDRdpSTGLVVLGAHALLTPEPTQQVFGIAAVVSHP 124
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919 125 DFEPTTQANDICLLRLNGSAVLGPAVRLLRLPRRGAKPPVaGTRCRVSGWGSVSDFEEPPPgLMEVEVRILDLSVCNSSW 204
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPV-GTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958790919 205 QGQLSPAMLCTHSGDrrrRGFCSADSGGPLVCGNR-AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 270
Cdd:pfam00089 157 GGTVTDTMICAGAGG---KDACQGDSGGPLVCSDGeLIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
46-278 3.58e-50

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 166.36  E-value: 3.58e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919  46 IVGGHEVKPHARPYMASVNFEG---HHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPtqQVFGIAAVVS 122
Cdd:COG5640    31 IVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGG--TVVKVARIVV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919 123 HPDFEPTTQANDICLLRLNGSAVLGPAVRLLrlprRGAKPPVAGTRCRVSGWGSVSDFEEPPPG-LMEVEVRILDLSVCN 201
Cdd:COG5640   109 HPDYDPATPGNDIALLKLATPVPGVAPAPLA----TSADAAAPGTPATVAGWGRTSEGPGSQSGtLRKADVPVVSDATCA 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919 202 sSWQGQLSPAMLCThSGDRRRRGFCSADSGGPLV----CGNRAHGLVSFSGLWCGdPKTPDVYTQVSAFVSWIWDVVRAS 277
Cdd:COG5640   185 -AYGGFDGGTMLCA-GYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCA-AGYPGVYTRVSAYRDWIKSTAGGL 261

                  .
gi 1958790919 278 P 278
Cdd:COG5640   262 G 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
67-175 9.24e-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: 9.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790919  67 GHHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPtQQVFGIAAVVSHPDFEPTTQAN-DICLLRLNGSav 145
Cdd:COG3591    10 GGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGP-YGTATATRFRVPPGWVASGDAGyDYALLRLDEP-- 86
                          90       100       110
                  ....*....|....*....|....*....|
gi 1958790919 146 LGPAVRLLRLprRGAKPPVAGTRCRVSGWG 175
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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