NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1677539310|ref|NP_001295138|]
View 

serine protease 57 isoform 2 precursor [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
33-257 6.94e-73

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: 223.31  E-value: 6.94e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310  33 IIGGHEVTPHSRPYMASVRFG-GQHHCGGFLLRARWVVSAAHCFSHRDLRTGLVVLGAHVLSTAEPTQQVFGIDALTTHP 111
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310 112 DYHPMTHANDICLLRLNGSAVLGPAVGLLrPPGRRARPPTAGTRCRVAGWGFVSDFEELPPGLMEAKVRVLDPDVCNSSW 191
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPI-CLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677539310 192 KGHLTLT--MLCTrSGDSHRRGFCSADSGGPLVC----RNRAHGLVSFsGLWCGDPKTPDVYTQVSAFVAWI 257
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 ...
33-257 6.94e-73

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: 223.31  E-value: 6.94e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310  33 IIGGHEVTPHSRPYMASVRFG-GQHHCGGFLLRARWVVSAAHCFSHRDLRTGLVVLGAHVLSTAEPTQQVFGIDALTTHP 111
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310 112 DYHPMTHANDICLLRLNGSAVLGPAVGLLrPPGRRARPPTAGTRCRVAGWGFVSDFEELPPGLMEAKVRVLDPDVCNSSW 191
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPI-CLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677539310 192 KGHLTLT--MLCTrSGDSHRRGFCSADSGGPLVC----RNRAHGLVSFsGLWCGDPKTPDVYTQVSAFVAWI 257
Cdd:cd00190   160 SYGGTITdnMLCA-GGLEGGKDACQGDSGGPLVCndngRGVLVGIVSW-GSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
33-257 1.01e-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: 209.84  E-value: 1.01e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310   33 IIGGHEVTPHSRPYMASVRF-GGQHHCGGFLLRARWVVSAAHCFSHRDLRTGLVVLGAHVLSTAEPtQQVFGIDALTTHP 111
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310  112 DYHPMTHANDICLLRLNGSAVLGPAVGLLRPPGRRARPPtAGTRCRVAGWGFVSD-FEELPPGLMEAKVRVLDPDVCNSS 190
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVP-AGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677539310  191 WKGHLTLT--MLCTrSGDSHRRGFCSADSGGPLVCRNR---AHGLVSFsGLWCGDPKTPDVYTQVSAFVAWI 257
Cdd:smart00020 160 YSGGGAITdnMLCA-GGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSW-GSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
33-257 3.35e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 188.03  E-value: 3.35e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310  33 IIGGHEVTPHSRPYMASVRFGGQHH-CGGFLLRARWVVSAAHCFSHRdlRTGLVVLGAHVLSTAEPTQQVFGIDALTTHP 111
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310 112 DYHPMTHANDICLLRLNGSAVLGPAVGLLRPPGRRARPPtAGTRCRVAGWGFVSDFeELPPGLMEAKVRVLDPDVCNSSW 191
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLP-VGTTCTVSGWGNTKTL-GPSDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677539310 192 KGHLTLTMLCTRSGDshrRGFCSADSGGPLVCRNR-AHGLVSFsGLWCGDPKTPDVYTQVSAFVAWI 257
Cdd:pfam00089 157 GGTVTDTMICAGAGG---KDACQGDSGGPLVCSDGeLIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
10-265 4.63e-48

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 160.59  E-value: 4.63e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310  10 RPLLTVATALMLPVKPPGSWGAQIIGGHEVTPHSRPYMASVRFGG---QHHCGGFLLRARWVVSAAHCFSHRDLRTGLVV 86
Cdd:COG5640     8 AALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310  87 LGAHVLSTAEPtqQVFGIDALTTHPDYHPMTHANDICLLRLNGSAVLGPAVGLLrppgRRARPPTAGTRCRVAGWGFVSD 166
Cdd:COG5640    88 IGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAPLA----TSADAAAPGTPATVAGWGRTSE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310 167 FEELPPG-LMEAKVRVLDPDVCNsSWKGHLTLTMLCTRSGDShRRGFCSADSGGPLV----CRNRAHGLVSFSGLWCGdP 241
Cdd:COG5640   162 GPGSQSGtLRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEG-GKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCA-A 238
                         250       260
                  ....*....|....*....|....
gi 1677539310 242 KTPDVYTQVSAFVAWIWDVVRRSS 265
Cdd:COG5640   239 GYPGVYTRVSAYRDWIKSTAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
33-257 6.94e-73

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: 223.31  E-value: 6.94e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310  33 IIGGHEVTPHSRPYMASVRFG-GQHHCGGFLLRARWVVSAAHCFSHRDLRTGLVVLGAHVLSTAEPTQQVFGIDALTTHP 111
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310 112 DYHPMTHANDICLLRLNGSAVLGPAVGLLrPPGRRARPPTAGTRCRVAGWGFVSDFEELPPGLMEAKVRVLDPDVCNSSW 191
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPI-CLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677539310 192 KGHLTLT--MLCTrSGDSHRRGFCSADSGGPLVC----RNRAHGLVSFsGLWCGDPKTPDVYTQVSAFVAWI 257
Cdd:cd00190   160 SYGGTITdnMLCA-GGLEGGKDACQGDSGGPLVCndngRGVLVGIVSW-GSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
33-257 1.01e-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: 209.84  E-value: 1.01e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310   33 IIGGHEVTPHSRPYMASVRF-GGQHHCGGFLLRARWVVSAAHCFSHRDLRTGLVVLGAHVLSTAEPtQQVFGIDALTTHP 111
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310  112 DYHPMTHANDICLLRLNGSAVLGPAVGLLRPPGRRARPPtAGTRCRVAGWGFVSD-FEELPPGLMEAKVRVLDPDVCNSS 190
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVP-AGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677539310  191 WKGHLTLT--MLCTrSGDSHRRGFCSADSGGPLVCRNR---AHGLVSFsGLWCGDPKTPDVYTQVSAFVAWI 257
Cdd:smart00020 160 YSGGGAITdnMLCA-GGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSW-GSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
33-257 3.35e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 188.03  E-value: 3.35e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310  33 IIGGHEVTPHSRPYMASVRFGGQHH-CGGFLLRARWVVSAAHCFSHRdlRTGLVVLGAHVLSTAEPTQQVFGIDALTTHP 111
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310 112 DYHPMTHANDICLLRLNGSAVLGPAVGLLRPPGRRARPPtAGTRCRVAGWGFVSDFeELPPGLMEAKVRVLDPDVCNSSW 191
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLP-VGTTCTVSGWGNTKTL-GPSDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677539310 192 KGHLTLTMLCTRSGDshrRGFCSADSGGPLVCRNR-AHGLVSFsGLWCGDPKTPDVYTQVSAFVAWI 257
Cdd:pfam00089 157 GGTVTDTMICAGAGG---KDACQGDSGGPLVCSDGeLIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
10-265 4.63e-48

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 160.59  E-value: 4.63e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310  10 RPLLTVATALMLPVKPPGSWGAQIIGGHEVTPHSRPYMASVRFGG---QHHCGGFLLRARWVVSAAHCFSHRDLRTGLVV 86
Cdd:COG5640     8 AALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310  87 LGAHVLSTAEPtqQVFGIDALTTHPDYHPMTHANDICLLRLNGSAVLGPAVGLLrppgRRARPPTAGTRCRVAGWGFVSD 166
Cdd:COG5640    88 IGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAPLA----TSADAAAPGTPATVAGWGRTSE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677539310 167 FEELPPG-LMEAKVRVLDPDVCNsSWKGHLTLTMLCTRSGDShRRGFCSADSGGPLV----CRNRAHGLVSFSGLWCGdP 241
Cdd:COG5640   162 GPGSQSGtLRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEG-GKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCA-A 238
                         250       260
                  ....*....|....*....|....
gi 1677539310 242 KTPDVYTQVSAFVAWIWDVVRRSS 265
Cdd:COG5640   239 GYPGVYTRVSAYRDWIKSTAGGLG 262
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
45-106 5.67e-03

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: 35.99  E-value: 5.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677539310  45 PYMASVRFGGQHHCGGFLLRARWVVSAAHCFSHRDLRTGL--VVLGAH--VLSTAEPTQQVFGIDA 106
Cdd:pfam09342   2 PWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYisVVLGGAktLKSIEGPYEQIVRVDC 67
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH