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Conserved domains on  [gi|586500063|pdb|3W94|B]
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Chain B, Enteropeptidase-1

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 ...
1-233 4.36e-106

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: 305.74  E-value: 4.36e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B        1 VVGGVNAEKGAWPWMVSLHWR-GRHGCGASLIGRDWLLTAAHCVYGKNTHLqyWSAVLGLHAQSSMNSQEvQIRQVDRII 79
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSN--YTVRLGSHDLSSNEGGG-QVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B       80 INKNYNRRTKEADIAMMHLQQPVNFTEWVLPVCLASEDQHFPAGRRCFIAGWGRDAEGGSLPDILQEAEVPLVDQDECQR 159
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3W94_B      160 LLPE-YTFTSSMLCAGYPEGGVDSCQGDSGGPLMCLEDARWTLIGVTSFGVGCGRPERPGAYARVSAFTSWIAET 233
Cdd:cd00190 158 AYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-233 4.36e-106

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: 305.74  E-value: 4.36e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B        1 VVGGVNAEKGAWPWMVSLHWR-GRHGCGASLIGRDWLLTAAHCVYGKNTHLqyWSAVLGLHAQSSMNSQEvQIRQVDRII 79
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSN--YTVRLGSHDLSSNEGGG-QVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B       80 INKNYNRRTKEADIAMMHLQQPVNFTEWVLPVCLASEDQHFPAGRRCFIAGWGRDAEGGSLPDILQEAEVPLVDQDECQR 159
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3W94_B      160 LLPE-YTFTSSMLCAGYPEGGVDSCQGDSGGPLMCLEDARWTLIGVTSFGVGCGRPERPGAYARVSAFTSWIAET 233
Cdd:cd00190 158 AYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-230 9.16e-102

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: 294.59  E-value: 9.16e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B           1 VVGGVNAEKGAWPWMVSLHWRG-RHGCGASLIGRDWLLTAAHCVYGKNTHLqyWSAVLGLHAQSSmnSQEVQIRQVDRII 79
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSN--IRVRLGSHDLSS--GEEGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B          80 INKNYNRRTKEADIAMMHLQQPVNFTEWVLPVCLASEDQHFPAGRRCFIAGWGRDAEG-GSLPDILQEAEVPLVDQDECQ 158
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3W94_B         159 RLLPEY-TFTSSMLCAGYPEGGVDSCQGDSGGPLMClEDARWTLIGVTSFGVGCGRPERPGAYARVSAFTSWI 230
Cdd:smart00020 158 RAYSGGgAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-230 1.31e-79

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 238.11  E-value: 1.31e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B          1 VVGGVNAEKGAWPWMVSLHWR-GRHGCGASLIGRDWLLTAAHCVYGKNThlqyWSAVLGLHaQSSMNSQEVQIRQVDRII 79
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGASD----VKVVLGAH-NIVLREGGEQKFDVEKII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B         80 INKNYNRRTKEADIAMMHLQQPVNFTEWVLPVCLASEDQHFPAGRRCFIAGWGRDAEGGsLPDILQEAEVPLVDQDECQR 159
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3W94_B        160 LLPEYTfTSSMLCAGYpeGGVDSCQGDSGGPLMCLEDarwTLIGVTSFGVGCGRPERPGAYARVSAFTSWI 230
Cdd:pfam00089 155 AYGGTV-TDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-233 1.92e-76

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 231.46  E-value: 1.92e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B        1 VVGGVNAEKGAWPWMVSLHWRG---RHGCGASLIGRDWLLTAAHCVYGKNTHLqyWSAVLGLHaqsSMNSQEVQIRQVDR 77
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSD--LRVVIGST---DLSTSGGTVVKVAR 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B       78 IIINKNYNRRTKEADIAMMHLQQPVNFTEwvlPVCLASEDQHFPAGRRCFIAGWGRDAEG-GSLPDILQEAEVPLVDQDE 156
Cdd:COG5640 106 IVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVSDAT 182
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3W94_B      157 CQRLLPEYTftSSMLCAGYPEGGVDSCQGDSGGPLMCLEDARWTLIGVTSFGVGCGRPERPGAYARVSAFTSWIAET 233
Cdd:COG5640 183 CAAYGGFDG--GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKST 257
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-233 4.36e-106

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: 305.74  E-value: 4.36e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B        1 VVGGVNAEKGAWPWMVSLHWR-GRHGCGASLIGRDWLLTAAHCVYGKNTHLqyWSAVLGLHAQSSMNSQEvQIRQVDRII 79
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSN--YTVRLGSHDLSSNEGGG-QVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B       80 INKNYNRRTKEADIAMMHLQQPVNFTEWVLPVCLASEDQHFPAGRRCFIAGWGRDAEGGSLPDILQEAEVPLVDQDECQR 159
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3W94_B      160 LLPE-YTFTSSMLCAGYPEGGVDSCQGDSGGPLMCLEDARWTLIGVTSFGVGCGRPERPGAYARVSAFTSWIAET 233
Cdd:cd00190 158 AYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-230 9.16e-102

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: 294.59  E-value: 9.16e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B           1 VVGGVNAEKGAWPWMVSLHWRG-RHGCGASLIGRDWLLTAAHCVYGKNTHLqyWSAVLGLHAQSSmnSQEVQIRQVDRII 79
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSN--IRVRLGSHDLSS--GEEGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B          80 INKNYNRRTKEADIAMMHLQQPVNFTEWVLPVCLASEDQHFPAGRRCFIAGWGRDAEG-GSLPDILQEAEVPLVDQDECQ 158
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3W94_B         159 RLLPEY-TFTSSMLCAGYPEGGVDSCQGDSGGPLMClEDARWTLIGVTSFGVGCGRPERPGAYARVSAFTSWI 230
Cdd:smart00020 158 RAYSGGgAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-230 1.31e-79

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 238.11  E-value: 1.31e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B          1 VVGGVNAEKGAWPWMVSLHWR-GRHGCGASLIGRDWLLTAAHCVYGKNThlqyWSAVLGLHaQSSMNSQEVQIRQVDRII 79
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGASD----VKVVLGAH-NIVLREGGEQKFDVEKII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B         80 INKNYNRRTKEADIAMMHLQQPVNFTEWVLPVCLASEDQHFPAGRRCFIAGWGRDAEGGsLPDILQEAEVPLVDQDECQR 159
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3W94_B        160 LLPEYTfTSSMLCAGYpeGGVDSCQGDSGGPLMCLEDarwTLIGVTSFGVGCGRPERPGAYARVSAFTSWI 230
Cdd:pfam00089 155 AYGGTV-TDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-233 1.92e-76

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 231.46  E-value: 1.92e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B        1 VVGGVNAEKGAWPWMVSLHWRG---RHGCGASLIGRDWLLTAAHCVYGKNTHLqyWSAVLGLHaqsSMNSQEVQIRQVDR 77
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSD--LRVVIGST---DLSTSGGTVVKVAR 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B       78 IIINKNYNRRTKEADIAMMHLQQPVNFTEwvlPVCLASEDQHFPAGRRCFIAGWGRDAEG-GSLPDILQEAEVPLVDQDE 156
Cdd:COG5640 106 IVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVSDAT 182
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3W94_B      157 CQRLLPEYTftSSMLCAGYPEGGVDSCQGDSGGPLMCLEDARWTLIGVTSFGVGCGRPERPGAYARVSAFTSWIAET 233
Cdd:COG5640 183 CAAYGGFDG--GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKST 257
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
21-210 3.30e-14

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 68.55  E-value: 3.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B       21 RGRHGCGASLIGRDWLLTAAHCVYGKNTHLQYWSavlgLHAQSSMNSQEVQIRQVDRIIINKNYNRRTKEA-DIAMMHLQ 99
Cdd:COG3591   9 GGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATN----IVFVPGYNGGPYGTATATRFRVPPGWVASGDAGyDYALLRLD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B      100 QPVNFTEWVLPVclaSEDQHFPAGRRCFIAGWGRDAEGGslpdilqeaevpLVDQDECqRLLPEYTFTSSMLCagypegg 179
Cdd:COG3591  85 EPLGDTTGWLGL---AFNDAPLAGEPVTIIGYPGDRPKD------------LSLDCSG-RVTGVQGNRLSYDC------- 141
                       170       180       190
                ....*....|....*....|....*....|.
3W94_B      180 vDSCQGDSGGPLMCLEDARWTLIGVTSFGVG 210
Cdd:COG3591 142 -DTTGGSSGSPVLDDSDGGGRVVGVHSAGGA 171
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
12-130 2.75e-11

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: 58.71  E-value: 2.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3W94_B         12 WPWMVSLHWRGRHGCGASLIGRDWLLTAAHCVYGKNTHLQYWSAVLGLH-AQSSMNSQEVQIRQVDriiinknYNRRTKE 90
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVLGGAkTLKSIEGPYEQIVRVD-------CRHDIPE 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
3W94_B         91 ADIAMMHLQQPVNFTEWVLPVCLASEDQHFPAGRRCFIAG 130
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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