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Conserved domains on  [gi|767912400|ref|XP_011542477|]
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serine protease 38 isoform X1 [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

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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 ...
60-192 3.49e-40

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: 137.79  E-value: 3.49e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912400  60 ILGGVPAPERKWPWQVSVHY-AGLHVCGGSILNEYWVLSAAHCFhRDKNIKIYDMYVGLVNLRVAGNHTQWYEVNRVILH 138
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767912400 139 PTYEMyHPIGGDVALVQLKTRIVFSESVLPVCLATPEVNLTS-ANCWATGWGLVS 192
Cdd:cd00190   80 PNYNP-STYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAgTTCTVSGWGRTS 133
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
60-192 3.49e-40

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: 137.79  E-value: 3.49e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912400  60 ILGGVPAPERKWPWQVSVHY-AGLHVCGGSILNEYWVLSAAHCFhRDKNIKIYDMYVGLVNLRVAGNHTQWYEVNRVILH 138
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767912400 139 PTYEMyHPIGGDVALVQLKTRIVFSESVLPVCLATPEVNLTS-ANCWATGWGLVS 192
Cdd:cd00190   80 PNYNP-STYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAgTTCTVSGWGRTS 133
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
59-192 1.93e-38

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: 133.19  E-value: 1.93e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912400    59 KILGGVPAPERKWPWQVSVHYAGL-HVCGGSILNEYWVLSAAHCFhRDKNIKIYDMYVGLVNLRVaGNHTQWYEVNRVIL 137
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSS-GEEGQVIKVSKVII 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912400   138 HPTYEMYhPIGGDVALVQLKTRIVFSESVLPVCLATPEVNL-TSANCWATGWGLVS 192
Cdd:smart00020  79 HPNYNPS-TYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVpAGTTCTVSGWGRTS 133
Trypsin pfam00089
Trypsin;
60-192 2.90e-28

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 106.37  E-value: 2.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912400   60 ILGGVPAPERKWPWQVSVHY-AGLHVCGGSILNEYWVLSAAHCFHRDKNIKIydmYVGLVNLRVAGNHTQWYEVNRVILH 138
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVKV---VLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767912400  139 PTYEMYHpIGGDVALVQLKTRIVFSESVLPVCLAT----PEVNLTsanCWATGWGLVS 192
Cdd:pfam00089  78 PNYNPDT-LDNDIALLKLESPVTLGDTVRPICLPDassdLPVGTT---CTVSGWGNTK 131
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
49-192 7.27e-23

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 93.18  E-value: 7.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912400  49 VACGRPSMEGKILGGVPAPERKWPWQVSVHYAG---LHVCGGSILNEYWVLSAAHCFhRDKNIKIYDMYVGLVNLRVAGn 125
Cdd:COG5640   20 AAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCV-DGDGPSDLRVVIGSTDLSTSG- 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912400 126 hTQWYEVNRVILHPTYEMYHPiGGDVALVQLKTRIvfsESVLPVCLATPEVNLTS-ANCWATGWGLVS 192
Cdd:COG5640   98 -GTVVKVARIVVHPDYDPATP-GNDIALLKLATPV---PGVAPAPLATSADAAAPgTPATVAGWGRTS 160
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
60-192 3.49e-40

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: 137.79  E-value: 3.49e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912400  60 ILGGVPAPERKWPWQVSVHY-AGLHVCGGSILNEYWVLSAAHCFhRDKNIKIYDMYVGLVNLRVAGNHTQWYEVNRVILH 138
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767912400 139 PTYEMyHPIGGDVALVQLKTRIVFSESVLPVCLATPEVNLTS-ANCWATGWGLVS 192
Cdd:cd00190   80 PNYNP-STYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAgTTCTVSGWGRTS 133
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
59-192 1.93e-38

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: 133.19  E-value: 1.93e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912400    59 KILGGVPAPERKWPWQVSVHYAGL-HVCGGSILNEYWVLSAAHCFhRDKNIKIYDMYVGLVNLRVaGNHTQWYEVNRVIL 137
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSS-GEEGQVIKVSKVII 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912400   138 HPTYEMYhPIGGDVALVQLKTRIVFSESVLPVCLATPEVNL-TSANCWATGWGLVS 192
Cdd:smart00020  79 HPNYNPS-TYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVpAGTTCTVSGWGRTS 133
Trypsin pfam00089
Trypsin;
60-192 2.90e-28

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 106.37  E-value: 2.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912400   60 ILGGVPAPERKWPWQVSVHY-AGLHVCGGSILNEYWVLSAAHCFHRDKNIKIydmYVGLVNLRVAGNHTQWYEVNRVILH 138
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVKV---VLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767912400  139 PTYEMYHpIGGDVALVQLKTRIVFSESVLPVCLAT----PEVNLTsanCWATGWGLVS 192
Cdd:pfam00089  78 PNYNPDT-LDNDIALLKLESPVTLGDTVRPICLPDassdLPVGTT---CTVSGWGNTK 131
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
49-192 7.27e-23

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 93.18  E-value: 7.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912400  49 VACGRPSMEGKILGGVPAPERKWPWQVSVHYAG---LHVCGGSILNEYWVLSAAHCFhRDKNIKIYDMYVGLVNLRVAGn 125
Cdd:COG5640   20 AAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCV-DGDGPSDLRVVIGSTDLSTSG- 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912400 126 hTQWYEVNRVILHPTYEMYHPiGGDVALVQLKTRIvfsESVLPVCLATPEVNLTS-ANCWATGWGLVS 192
Cdd:COG5640   98 -GTVVKVARIVVHPDYDPATP-GNDIALLKLATPV---PGVAPAPLATSADAAAPgTPATVAGWGRTS 160
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
71-187 7.34e-06

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: 43.69  E-value: 7.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912400   71 WPWQVSVHYAGLHVCGGSILNEYWVLSAAHCFhrdKNIKIYDMYVGLV------NLRVAGNHTQWYEVNrvILHPTYEmy 144
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCL---RDTNLRHQYISVVlggaktLKSIEGPYEQIVRVD--CRHDIPE-- 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 767912400  145 hpigGDVALVQLKTRIVFSESVLPVCLA-TPEVNLTSANCWATG 187
Cdd:pfam09342  74 ----SEISLLHLASPASFSNHVLPTFVPeTRNENEKDNECLAVG 113
 
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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