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Conserved domains on  [gi|61680579|pdb|1YBW|A]
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Chain A, Hepatocyte growth factor activator 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

 Zoom to residue level

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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 ...
36-271 5.53e-97

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: 284.55  E-value: 5.53e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A       36 IIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFSHSPPRdSVSVVLGQHFFNRTTDVTQTFGIEKYIPY 113
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGrhFCGGSLISPRWVLTAAHCVYSSAPS-NYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A      114 TLYSVfNPSDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSgYSSSLREALVPLVADH 193
Cdd:cd00190  80 PNYNP-STYDNDIALLKLKRP----VTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1YBW_A      194 KCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACEKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWIND 271
Cdd:cd00190 154 ECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
36-271 5.53e-97

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: 284.55  E-value: 5.53e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A       36 IIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFSHSPPRdSVSVVLGQHFFNRTTDVTQTFGIEKYIPY 113
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGrhFCGGSLISPRWVLTAAHCVYSSAPS-NYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A      114 TLYSVfNPSDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSgYSSSLREALVPLVADH 193
Cdd:cd00190  80 PNYNP-STYDNDIALLKLKRP----VTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1YBW_A      194 KCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACEKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWIND 271
Cdd:cd00190 154 ECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
35-269 1.11e-92

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: 273.40  E-value: 1.11e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A          35 RIIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFsHSPPRDSVSVVLGQHFFNRTTDvTQTFGIEKYIP 112
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrhFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A         113 YTLYSVfNPSDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSGYSSSLREALVPLVAD 192
Cdd:smart00020  79 HPNYNP-STYDNDIALLKLKEP----VTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSN 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1YBW_A         193 HKCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACeKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWI 269
Cdd:smart00020 154 ATCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
36-269 1.96e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 234.26  E-value: 1.96e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A         36 IIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFSHsppRDSVSVVLGQHFFNRTTDVTQTFGIEKYIPY 113
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkhFCGGSLISENWVLTAAHCVSG---ASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A        114 TLYSVFNPsDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENvsGYSSSLREALVPLVADH 193
Cdd:pfam00089  78 PNYNPDTL-DNDIALLKLESP----VTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRE 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1YBW_A        194 KCSSpeVYGADISPNMLCAGYfdCKSDACQGDSGGPLACEKNgvaYLYGIISWGDGCGRLHKPGVYTRVANYVDWI 269
Cdd:pfam00089 151 TCRS--AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
34-274 2.18e-63

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 200.26  E-value: 2.18e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A       34 PRIIGGSSSLPGSHPWLAAIYIGDS----FCAGSLVHTCWVVSAAHCFSHSPPrDSVSVVLGQHffNRTTDVTQTFGIEK 109
Cdd:COG5640  29 PAIVGGTPATVGEYPWMVALQSSNGpsgqFCGGTLIAPRWVLTAAHCVDGDGP-SDLRVVIGST--DLSTSGGTVVKVAR 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A      110 YIPYTLYSVFNPsDHDLVLIRLkkkgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSGYSSSLREALVPL 189
Cdd:COG5640 106 IVVHPDYDPATP-GNDIALLKL-------ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A      190 VADHKCSSpevYGADISPNMLCAGYFDCKSDACQGDSGGPLACEKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWI 269
Cdd:COG5640 178 VSDATCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254

                ....*
1YBW_A      270 NDRIR 274
Cdd:COG5640 255 KSTAG 259
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
36-271 5.53e-97

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: 284.55  E-value: 5.53e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A       36 IIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFSHSPPRdSVSVVLGQHFFNRTTDVTQTFGIEKYIPY 113
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGrhFCGGSLISPRWVLTAAHCVYSSAPS-NYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A      114 TLYSVfNPSDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSgYSSSLREALVPLVADH 193
Cdd:cd00190  80 PNYNP-STYDNDIALLKLKRP----VTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1YBW_A      194 KCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACEKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWIND 271
Cdd:cd00190 154 ECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
35-269 1.11e-92

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: 273.40  E-value: 1.11e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A          35 RIIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFsHSPPRDSVSVVLGQHFFNRTTDvTQTFGIEKYIP 112
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrhFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A         113 YTLYSVfNPSDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSGYSSSLREALVPLVAD 192
Cdd:smart00020  79 HPNYNP-STYDNDIALLKLKEP----VTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSN 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1YBW_A         193 HKCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACeKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWI 269
Cdd:smart00020 154 ATCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
36-269 1.96e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 234.26  E-value: 1.96e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A         36 IIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFSHsppRDSVSVVLGQHFFNRTTDVTQTFGIEKYIPY 113
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkhFCGGSLISENWVLTAAHCVSG---ASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A        114 TLYSVFNPsDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENvsGYSSSLREALVPLVADH 193
Cdd:pfam00089  78 PNYNPDTL-DNDIALLKLESP----VTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRE 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1YBW_A        194 KCSSpeVYGADISPNMLCAGYfdCKSDACQGDSGGPLACEKNgvaYLYGIISWGDGCGRLHKPGVYTRVANYVDWI 269
Cdd:pfam00089 151 TCRS--AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
34-274 2.18e-63

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 200.26  E-value: 2.18e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A       34 PRIIGGSSSLPGSHPWLAAIYIGDS----FCAGSLVHTCWVVSAAHCFSHSPPrDSVSVVLGQHffNRTTDVTQTFGIEK 109
Cdd:COG5640  29 PAIVGGTPATVGEYPWMVALQSSNGpsgqFCGGTLIAPRWVLTAAHCVDGDGP-SDLRVVIGST--DLSTSGGTVVKVAR 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A      110 YIPYTLYSVFNPsDHDLVLIRLkkkgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSGYSSSLREALVPL 189
Cdd:COG5640 106 IVVHPDYDPATP-GNDIALLKL-------ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A      190 VADHKCSSpevYGADISPNMLCAGYFDCKSDACQGDSGGPLACEKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWI 269
Cdd:COG5640 178 VSDATCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254

                ....*
1YBW_A      270 NDRIR 274
Cdd:COG5640 255 KSTAG 259
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
56-249 7.00e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 39.66  E-value: 7.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A       56 GDSFCAGSLVHTCWVVSAAHCFsHSPPRDSVSVVLgqHF-FNRTTDVTQTFGIEKYIPYTLYSVFNPSDHDLVLIRLKKk 134
Cdd:COG3591  10 GGGVCTGTLIGPNLVLTAGHCV-YDGAGGGWATNI--VFvPGYNGGPYGTATATRFRVPPGWVASGDAGYDYALLRLDE- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YBW_A      135 gdrcatrsqfvqpiclPEPGSTFPAGHKCQIAGWGHLDENVSGYSSSLREALVplvADHKCSSpevygADISPNMLcagY 214
Cdd:COG3591  86 ----------------PLGDTTGWLGLAFNDAPLAGEPVTIIGYPGDRPKDLS---LDCSGRV-----TGVQGNRL---S 138
                       170       180       190
                ....*....|....*....|....*....|....*
1YBW_A      215 FDCksDACQGDSGGPLACEKNGVAYLYGIISWGDG 249
Cdd:COG3591 139 YDC--DTTGGSSGSPVLDDSDGGGRVVGVHSAGGA 171
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
48-93 8.31e-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: 35.60  E-value: 8.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
1YBW_A         48 PWLAAIYI-GDSFCAGSLVHTCWVVSAAHCFSHSPPRDS-VSVVLGQH 93
Cdd:pfam09342   2 PWIAKVYLdGNMICSGVLIDASWVIVSGSCLRDTNLRHQyISVVLGGA 49
 
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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