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Conserved domains on  [gi|158563985|sp|Q6IE59|]
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RecName: Full=Serine protease 57; AltName: Full=Complement factor D-like protein; AltName: Full=Neutrophil serine protease 4; Short=NSP4; AltName: Full=Serine protease 1-like protein 1; Flags: Precursor

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 ...
34-258 1.62e-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: 239.87  E-value: 1.62e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985  34 IVGGHEVKPHARPYMASVNFE-GHHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPTQQVFGIAAVVSHP 112
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985 113 DFEPTTQANDICLLRLNGSAVLGPAVRLLRLPRRGAKPPvAGTRCRVSGWGSVSDFEEPPPGLMEVEVRILDLSVCNSSW 192
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLP-AGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158563985 193 Q--GQLSPAMLCThSGDRRRRGFCSADSGGPLVCGNR----AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 258
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 ...
34-258 1.62e-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: 239.87  E-value: 1.62e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985  34 IVGGHEVKPHARPYMASVNFE-GHHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPTQQVFGIAAVVSHP 112
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985 113 DFEPTTQANDICLLRLNGSAVLGPAVRLLRLPRRGAKPPvAGTRCRVSGWGSVSDFEEPPPGLMEVEVRILDLSVCNSSW 192
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLP-AGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158563985 193 Q--GQLSPAMLCThSGDRRRRGFCSADSGGPLVCGNR----AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 258
Cdd:cd00190  160 SygGTITDNMLCA-GGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSW-GSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
33-258 6.13e-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: 228.33  E-value: 6.13e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985    33 HIVGGHEVKPHARPYMASVNFEG-HHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPtQQVFGIAAVVSH 111
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985   112 PDFEPTTQANDICLLRLNGSAVLGPAVRLLRLPRRGAKPPvAGTRCRVSGWGSVSDFEEPPP-GLMEVEVRILDLSVCNS 190
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVP-AGTTCTVSGWGRTSEGAGSLPdTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158563985   191 SWQGQ--LSPAMLCThSGDRRRRGFCSADSGGPLVCGNR---AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 258
Cdd:smart00020 159 AYSGGgaITDNMLCA-GGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSW-GSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
34-258 1.09e-65

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 204.21  E-value: 1.09e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985   34 IVGGHEVKPHARPYMASVNFEGHHH-CGGFLFHAHWVLSAAHCFSDRdpSTGLVVLGAHALLTPEPTQQVFGIAAVVSHP 112
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985  113 DFEPTTQANDICLLRLNGSAVLGPAVRLLRLPRRGAKPPVaGTRCRVSGWGSVSDFEEPPPgLMEVEVRILDLSVCNSSW 192
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPV-GTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158563985  193 QGQLSPAMLCTHSGDrrrRGFCSADSGGPLVCGNR-AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 258
Cdd:pfam00089 157 GGTVTDTMICAGAGG---KDACQGDSGGPLVCSDGeLIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
14-266 1.67e-50

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 166.75  E-value: 1.67e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985  14 LVVATALTQLLWLPGCCGSH----IVGGHEVKPHARPYMASVNFEG---HHHCGGFLFHAHWVLSAAHCFSDRDPSTGLV 86
Cdd:COG5640    7 LAALAAAALALALAAAPAADaapaIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985  87 VLGAHALLTPEPtqQVFGIAAVVSHPDFEPTTQANDICLLRLNGSAVLGPAVRLLrlprRGAKPPVAGTRCRVSGWGSVS 166
Cdd:COG5640   87 VIGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAPLA----TSADAAAPGTPATVAGWGRTS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985 167 DFEEPPPG-LMEVEVRILDLSVCNsSWQGQLSPAMLCThSGDRRRRGFCSADSGGPLV----CGNRAHGLVSFSGLWCGd 241
Cdd:COG5640  161 EGPGSQSGtLRKADVPVVSDATCA-AYGGFDGGTMLCA-GYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCA- 237
                        250       260
                 ....*....|....*....|....*
gi 158563985 242 PKTPDVYTQVSAFVSWIWDVVRASP 266
Cdd:COG5640  238 AGYPGVYTRVSAYRDWIKSTAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
34-258 1.62e-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: 239.87  E-value: 1.62e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985  34 IVGGHEVKPHARPYMASVNFE-GHHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPTQQVFGIAAVVSHP 112
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985 113 DFEPTTQANDICLLRLNGSAVLGPAVRLLRLPRRGAKPPvAGTRCRVSGWGSVSDFEEPPPGLMEVEVRILDLSVCNSSW 192
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLP-AGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158563985 193 Q--GQLSPAMLCThSGDRRRRGFCSADSGGPLVCGNR----AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 258
Cdd:cd00190  160 SygGTITDNMLCA-GGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSW-GSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
33-258 6.13e-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: 228.33  E-value: 6.13e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985    33 HIVGGHEVKPHARPYMASVNFEG-HHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPtQQVFGIAAVVSH 111
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985   112 PDFEPTTQANDICLLRLNGSAVLGPAVRLLRLPRRGAKPPvAGTRCRVSGWGSVSDFEEPPP-GLMEVEVRILDLSVCNS 190
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVP-AGTTCTVSGWGRTSEGAGSLPdTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158563985   191 SWQGQ--LSPAMLCThSGDRRRRGFCSADSGGPLVCGNR---AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 258
Cdd:smart00020 159 AYSGGgaITDNMLCA-GGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSW-GSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
34-258 1.09e-65

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 204.21  E-value: 1.09e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985   34 IVGGHEVKPHARPYMASVNFEGHHH-CGGFLFHAHWVLSAAHCFSDRdpSTGLVVLGAHALLTPEPTQQVFGIAAVVSHP 112
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985  113 DFEPTTQANDICLLRLNGSAVLGPAVRLLRLPRRGAKPPVaGTRCRVSGWGSVSDFEEPPPgLMEVEVRILDLSVCNSSW 192
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPV-GTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158563985  193 QGQLSPAMLCTHSGDrrrRGFCSADSGGPLVCGNR-AHGLVSFsGLWCGDPKTPDVYTQVSAFVSWI 258
Cdd:pfam00089 157 GGTVTDTMICAGAGG---KDACQGDSGGPLVCSDGeLIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
14-266 1.67e-50

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 166.75  E-value: 1.67e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985  14 LVVATALTQLLWLPGCCGSH----IVGGHEVKPHARPYMASVNFEG---HHHCGGFLFHAHWVLSAAHCFSDRDPSTGLV 86
Cdd:COG5640    7 LAALAAAALALALAAAPAADaapaIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985  87 VLGAHALLTPEPtqQVFGIAAVVSHPDFEPTTQANDICLLRLNGSAVLGPAVRLLrlprRGAKPPVAGTRCRVSGWGSVS 166
Cdd:COG5640   87 VIGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAPLA----TSADAAAPGTPATVAGWGRTS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985 167 DFEEPPPG-LMEVEVRILDLSVCNsSWQGQLSPAMLCThSGDRRRRGFCSADSGGPLV----CGNRAHGLVSFSGLWCGd 241
Cdd:COG5640  161 EGPGSQSGtLRKADVPVVSDATCA-AYGGFDGGTMLCA-GYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCA- 237
                        250       260
                 ....*....|....*....|....*
gi 158563985 242 PKTPDVYTQVSAFVSWIWDVVRASP 266
Cdd:COG5640  238 AGYPGVYTRVSAYRDWIKSTAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
55-163 9.59e-03

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 36.19  E-value: 9.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158563985  55 GHHHCGGFLFHAHWVLSAAHCFSDRDPSTGLVVLGAHALLTPEPtQQVFGIAAVVSHPDFEPTTQAN-DICLLRLNGSav 133
Cdd:COG3591   10 GGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGP-YGTATATRFRVPPGWVASGDAGyDYALLRLDEP-- 86
                         90       100       110
                 ....*....|....*....|....*....|
gi 158563985 134 LGPAVRLLRLprRGAKPPVAGTRCRVSGWG 163
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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