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Conserved domains on  [gi|6435698]
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Chain B, ENTEROPEPTIDASE

Protein Classification

serine protease( domain architecture ID 10076129)

serine protease such as human cathepsin G with trypsin- and chymotrypsin-like specificity; also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity

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 ...
1-232 1.54e-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: 306.90  E-value: 1.54e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698    1 IVGGSDSREGAWPWVVALYFDD-QQVCGASLVSRDWLVSAAHCVYGRNmePSKWKAVLGLHMASNLTSPQiETRLIDQIV 79
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSNEGGG-QVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698   80 INPHYNKRRKNNDIAMMHLEMKVNYTDYIQPICLPEENQVFPPGRICSIAGWGALIYQGSTADVLQEADVPLLSNEKCQQ 159
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6435698  160 QMPE-YNITENMVCAGYEAGGVDSCQGDSGGPLMCQENNRWLLAGVTSFGYQCALPNRPGVYARVPRFTEWIQS 232
Cdd:cd00190 158 AYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-232 1.54e-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: 306.90  E-value: 1.54e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698    1 IVGGSDSREGAWPWVVALYFDD-QQVCGASLVSRDWLVSAAHCVYGRNmePSKWKAVLGLHMASNLTSPQiETRLIDQIV 79
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSNEGGG-QVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698   80 INPHYNKRRKNNDIAMMHLEMKVNYTDYIQPICLPEENQVFPPGRICSIAGWGALIYQGSTADVLQEADVPLLSNEKCQQ 159
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6435698  160 QMPE-YNITENMVCAGYEAGGVDSCQGDSGGPLMCQENNRWLLAGVTSFGYQCALPNRPGVYARVPRFTEWIQS 232
Cdd:cd00190 158 AYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-230 5.52e-101

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 [Multi-domain]  Cd Length: 229  Bit Score: 292.66  E-value: 5.52e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698       1 IVGGSDSREGAWPWVVALYFDD-QQVCGASLVSRDWLVSAAHCVYGRNmePSKWKAVLGLHMASNLTSPQieTRLIDQIV 79
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSD--PSNIRVRLGSHDLSSGEEGQ--VIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698      80 INPHYNKRRKNNDIAMMHLEMKVNYTDYIQPICLPEENQVFPPGRICSIAGWGALIY-QGSTADVLQEADVPLLSNEKCQ 158
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6435698     159 QQMPEYN-ITENMVCAGYEAGGVDSCQGDSGGPLMCQeNNRWLLAGVTSFGYQCALPNRPGVYARVPRFTEWI 230
Cdd:smart00020 158 RAYSGGGaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-230 3.07e-79

Trypsin;


Pssm-ID: 395042 [Multi-domain]  Cd Length: 219  Bit Score: 236.96  E-value: 3.07e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698      1 IVGGSDSREGAWPWVVALYF-DDQQVCGASLVSRDWLVSAAHCVYGRnmepSKWKAVLGLHmASNLTSPQIETRLIDQIV 79
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGA----SDVKVVLGAH-NIVLREGGEQKFDVEKII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698     80 INPHYNKRRKNNDIAMMHLEMKVNYTDYIQPICLPEENQVFPPGRICSIAGWGaLIYQGSTADVLQEADVPLLSNEKCQQ 159
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG-NTKTLGPSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6435698    160 QMPEYnITENMVCAGYeaGGVDSCQGDSGGPLMCQENnrwLLAGVTSFGYQCALPNRPGVYARVPRFTEWI 230
Cdd:pfam00089 155 AYGGT-VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-230 2.47e-21

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 91.48  E-value: 2.47e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698    1 IVGGSDSREGAWPWVVAL--YFDDQ---QVCGASLVSRDWLVSAAHCVYGRNmePSKWKAVLGLHMASNL-TSPQIETRl 74
Cdd:COG5640  33 IIGGSNANAGEYPSLVALvdRISDYvsgTFCGGSKLGGRYVLTAAHCADASS--PISSDVNRVVVDLNDSsQAERGHVR- 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698   75 idQIVINPHYNKRRKNNDIAMMHLEmkvnytdyiQPICLPEE---NQVFPPGRICSIAGWGAL--IYQGSTADV------ 143
Cdd:COG5640 110 --TIYVHEFYSPGNLGNDIAVLELA---------RAASLPRVkitSFDASDTFLNSVTTVSPMtnGTFGVTTPSdvprss 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698  144 -----LQEADVPLLSNEKCQQQMPEYNITENMVC-AGYEAG--GVDSCQGDSGGPLMCQENNRWLLAGVTSFGY-QCALP 214
Cdd:COG5640 179 pkgtiLHEVAVLFVPLSTCAQYKGCANASDGATGlTGFCAGrpPKDACQGDSGGPIFHKGEEGRVQRGVVSWGDgGCGGT 258
                       250
                ....*....|....*.
gi 6435698  215 NRPGVYARVPRFTEWI 230
Cdd:COG5640 259 LIPGVYTNVSNYQDWI 274
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-232 1.54e-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: 306.90  E-value: 1.54e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698    1 IVGGSDSREGAWPWVVALYFDD-QQVCGASLVSRDWLVSAAHCVYGRNmePSKWKAVLGLHMASNLTSPQiETRLIDQIV 79
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSA--PSNYTVRLGSHDLSSNEGGG-QVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698   80 INPHYNKRRKNNDIAMMHLEMKVNYTDYIQPICLPEENQVFPPGRICSIAGWGALIYQGSTADVLQEADVPLLSNEKCQQ 159
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6435698  160 QMPE-YNITENMVCAGYEAGGVDSCQGDSGGPLMCQENNRWLLAGVTSFGYQCALPNRPGVYARVPRFTEWIQS 232
Cdd:cd00190 158 AYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-230 5.52e-101

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 [Multi-domain]  Cd Length: 229  Bit Score: 292.66  E-value: 5.52e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698       1 IVGGSDSREGAWPWVVALYFDD-QQVCGASLVSRDWLVSAAHCVYGRNmePSKWKAVLGLHMASNLTSPQieTRLIDQIV 79
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSD--PSNIRVRLGSHDLSSGEEGQ--VIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698      80 INPHYNKRRKNNDIAMMHLEMKVNYTDYIQPICLPEENQVFPPGRICSIAGWGALIY-QGSTADVLQEADVPLLSNEKCQ 158
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6435698     159 QQMPEYN-ITENMVCAGYEAGGVDSCQGDSGGPLMCQeNNRWLLAGVTSFGYQCALPNRPGVYARVPRFTEWI 230
Cdd:smart00020 158 RAYSGGGaITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-230 3.07e-79

Trypsin;


Pssm-ID: 395042 [Multi-domain]  Cd Length: 219  Bit Score: 236.96  E-value: 3.07e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698      1 IVGGSDSREGAWPWVVALYF-DDQQVCGASLVSRDWLVSAAHCVYGRnmepSKWKAVLGLHmASNLTSPQIETRLIDQIV 79
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGA----SDVKVVLGAH-NIVLREGGEQKFDVEKII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698     80 INPHYNKRRKNNDIAMMHLEMKVNYTDYIQPICLPEENQVFPPGRICSIAGWGaLIYQGSTADVLQEADVPLLSNEKCQQ 159
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG-NTKTLGPSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6435698    160 QMPEYnITENMVCAGYeaGGVDSCQGDSGGPLMCQENnrwLLAGVTSFGYQCALPNRPGVYARVPRFTEWI 230
Cdd:pfam00089 155 AYGGT-VTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-230 2.47e-21

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 91.48  E-value: 2.47e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698    1 IVGGSDSREGAWPWVVAL--YFDDQ---QVCGASLVSRDWLVSAAHCVYGRNmePSKWKAVLGLHMASNL-TSPQIETRl 74
Cdd:COG5640  33 IIGGSNANAGEYPSLVALvdRISDYvsgTFCGGSKLGGRYVLTAAHCADASS--PISSDVNRVVVDLNDSsQAERGHVR- 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698   75 idQIVINPHYNKRRKNNDIAMMHLEmkvnytdyiQPICLPEE---NQVFPPGRICSIAGWGAL--IYQGSTADV------ 143
Cdd:COG5640 110 --TIYVHEFYSPGNLGNDIAVLELA---------RAASLPRVkitSFDASDTFLNSVTTVSPMtnGTFGVTTPSdvprss 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435698  144 -----LQEADVPLLSNEKCQQQMPEYNITENMVC-AGYEAG--GVDSCQGDSGGPLMCQENNRWLLAGVTSFGY-QCALP 214
Cdd:COG5640 179 pkgtiLHEVAVLFVPLSTCAQYKGCANASDGATGlTGFCAGrpPKDACQGDSGGPIFHKGEEGRVQRGVVSWGDgGCGGT 258
                       250
                ....*....|....*.
gi 6435698  215 NRPGVYARVPRFTEWI 230
Cdd:COG5640 259 LIPGVYTNVSNYQDWI 274
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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