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Conserved domains on  [gi|645985789|pdb|4O3U|A]
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Chain A, Hepatocyte growth factor

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 ...
2-225 1.03e-70

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: 215.99  E-value: 1.03e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4O3U_A        2 VNGIPTR-TNIGWMVSLRYR-NKHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVhgRGDEKCKQVLNVSQLV-- 77
Cdd:cd00190   2 VGGSEAKiGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDL--SSNEGGGQVIKVKKVIvh 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4O3U_A       78 --YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGSTIPEKTSCSVYGWGYT-GLINYDGLLRVAHLYIMGNEKCSQHH 152
Cdd:cd00190  80 pnYNPStyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTsEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
4O3U_A      153 RGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKI 225
Cdd:cd00190 160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
2-225 1.03e-70

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: 215.99  E-value: 1.03e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4O3U_A        2 VNGIPTR-TNIGWMVSLRYR-NKHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVhgRGDEKCKQVLNVSQLV-- 77
Cdd:cd00190   2 VGGSEAKiGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDL--SSNEGGGQVIKVKKVIvh 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4O3U_A       78 --YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGSTIPEKTSCSVYGWGYT-GLINYDGLLRVAHLYIMGNEKCSQHH 152
Cdd:cd00190  80 pnYNPStyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTsEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
4O3U_A      153 RGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKI 225
Cdd:cd00190 160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
2-222 6.60e-70

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: 214.08  E-value: 6.60e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4O3U_A           2 VNGIPTrtNIG---WMVSLRYRN-KHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGDekcKQVLNVSQLV 77
Cdd:smart00020   3 VGGSEA--NIGsfpWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEE---GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4O3U_A          78 ----YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGSTIPEKTSCSVYGWGYT--GLINYDGLLRVAHLYIMGNEKCS 149
Cdd:smart00020  78 ihpnYNPStyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTseGAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
4O3U_A         150 QHHRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCeQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 222
Cdd:smart00020 158 RAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
2-222 8.71e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 185.34  E-value: 8.71e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4O3U_A          2 VNGIPTRTNIG-WMVSLRYR-NKHICGGSLIKESWVLTARQCFPSRdlKDYEAWLGIHDVHGRgdEKCKQVLNVSQLV-- 77
Cdd:pfam00089   2 VGGDEAQPGSFpWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLR--EGGEQKFDVEKIIvh 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4O3U_A         78 --YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGSTIPEKTSCSVYGWGYTGLINYDGLLRVAHLYIMGNEKCSQHHR 153
Cdd:pfam00089  78 pnYNPDtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
4O3U_A        154 GKVTlnESEICAGAekIGSGPCEGDYGGPLVCEQHkmrMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 222
Cdd:pfam00089 158 GTVT--DTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
2-226 1.08e-38

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 135.16  E-value: 1.08e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4O3U_A        2 VNGIP-TRTNIGWMVSLRYRN---KHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGdekcKQVLNVSQLV 77
Cdd:COG5640  32 VGGTPaTVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSG----GTVVKVARIV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4O3U_A       78 YGPE------GSDLVLMKLARPAvldDFVSTIDLPNYGSTIPEKTSCSVYGWGYT--GLINYDGLLRVAHLYIMGNEKCS 149
Cdd:COG5640 108 VHPDydpatpGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTseGPGSQSGTLRKADVPVVSDATCA 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4O3U_A      150 QHHRgkvTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKII 226
Cdd:COG5640 185 AYGG---FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
2-225 1.03e-70

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: 215.99  E-value: 1.03e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4O3U_A        2 VNGIPTR-TNIGWMVSLRYR-NKHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVhgRGDEKCKQVLNVSQLV-- 77
Cdd:cd00190   2 VGGSEAKiGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDL--SSNEGGGQVIKVKKVIvh 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4O3U_A       78 --YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGSTIPEKTSCSVYGWGYT-GLINYDGLLRVAHLYIMGNEKCSQHH 152
Cdd:cd00190  80 pnYNPStyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTsEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
4O3U_A      153 RGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKI 225
Cdd:cd00190 160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
2-222 6.60e-70

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: 214.08  E-value: 6.60e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4O3U_A           2 VNGIPTrtNIG---WMVSLRYRN-KHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGDekcKQVLNVSQLV 77
Cdd:smart00020   3 VGGSEA--NIGsfpWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEE---GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4O3U_A          78 ----YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGSTIPEKTSCSVYGWGYT--GLINYDGLLRVAHLYIMGNEKCS 149
Cdd:smart00020  78 ihpnYNPStyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTseGAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
4O3U_A         150 QHHRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCeQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 222
Cdd:smart00020 158 RAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
2-222 8.71e-59

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 185.34  E-value: 8.71e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4O3U_A          2 VNGIPTRTNIG-WMVSLRYR-NKHICGGSLIKESWVLTARQCFPSRdlKDYEAWLGIHDVHGRgdEKCKQVLNVSQLV-- 77
Cdd:pfam00089   2 VGGDEAQPGSFpWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLR--EGGEQKFDVEKIIvh 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4O3U_A         78 --YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGSTIPEKTSCSVYGWGYTGLINYDGLLRVAHLYIMGNEKCSQHHR 153
Cdd:pfam00089  78 pnYNPDtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
4O3U_A        154 GKVTlnESEICAGAekIGSGPCEGDYGGPLVCEQHkmrMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 222
Cdd:pfam00089 158 GTVT--DTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
2-226 1.08e-38

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 135.16  E-value: 1.08e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4O3U_A        2 VNGIP-TRTNIGWMVSLRYRN---KHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGdekcKQVLNVSQLV 77
Cdd:COG5640  32 VGGTPaTVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSG----GTVVKVARIV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4O3U_A       78 YGPE------GSDLVLMKLARPAvldDFVSTIDLPNYGSTIPEKTSCSVYGWGYT--GLINYDGLLRVAHLYIMGNEKCS 149
Cdd:COG5640 108 VHPDydpatpGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTseGPGSQSGTLRKADVPVVSDATCA 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4O3U_A      150 QHHRgkvTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKII 226
Cdd:COG5640 185 AYGG---FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
 
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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