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Conserved domains on  [gi|71361688|ref|NP_002768|]
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myeloblastin precursor [Homo sapiens]

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 ...
28-246 7.33e-86

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: 255.28  E-value: 7.33e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688  28 IVGGHEAQPHSRPYMASLQMRGnpGSHFCGGTLIHPSFVLTAAHCLRDIPQRLVNVVLGAHNVRTQEPTQQHFSVAQVFL 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688 108 N-NYDAENKLNDVLLIQLSSPANLSASVATVQLPQQDQPVPHGTQCLAMGWGRVGAHDPPAQVLQELNVTVVTF-FCR-- 183
Cdd:cd00190  79 HpNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNaECKra 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71361688 184 --------PHNICTFVPRRKAGICFGDSGGPLICD----GIIQGIDSFVIwGCATRLFPDFFTRVALYVDWIRST 246
Cdd:cd00190 159 ysyggtitDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGS-GCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
28-246 7.33e-86

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: 255.28  E-value: 7.33e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688  28 IVGGHEAQPHSRPYMASLQMRGnpGSHFCGGTLIHPSFVLTAAHCLRDIPQRLVNVVLGAHNVRTQEPTQQHFSVAQVFL 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688 108 N-NYDAENKLNDVLLIQLSSPANLSASVATVQLPQQDQPVPHGTQCLAMGWGRVGAHDPPAQVLQELNVTVVTF-FCR-- 183
Cdd:cd00190  79 HpNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNaECKra 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71361688 184 --------PHNICTFVPRRKAGICFGDSGGPLICD----GIIQGIDSFVIwGCATRLFPDFFTRVALYVDWIRST 246
Cdd:cd00190 159 ysyggtitDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGS-GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
27-243 4.10e-81

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: 242.97  E-value: 4.10e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688     27 EIVGGHEAQPHSRPYMASLQMRGnpGSHFCGGTLIHPSFVLTAAHCLRDIPQRLVNVVLGAHNvRTQEPTQQHFSVAQVF 106
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG--GRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHD-LSSGEEGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688    107 LN-NYDAENKLNDVLLIQLSSPANLSASVATVQLPQQDQPVPHGTQCLAMGWGRV-GAHDPPAQVLQELNVTVVT-FFCR 183
Cdd:smart00020  78 IHpNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSnATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71361688    184 ----------PHNICTFVPRRKAGICFGDSGGPLICD---GIIQGIDSFVIwGCATRLFPDFFTRVALYVDWI 243
Cdd:smart00020 158 raysgggaitDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
28-243 2.30e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 223.09  E-value: 2.30e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688    28 IVGGHEAQPHSRPYMASLQMRGnpGSHFCGGTLIHPSFVLTAAHCLRDIPQrlVNVVLGAHNVRTQEPTQQHFSVAQVFL 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSS--GKHFCGGSLISENWVLTAAHCVSGASD--VKVVLGAHNIVLREGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688   108 -NNYDAENKLNDVLLIQLSSPANLSASVATVQLPQQDQPVPHGTQCLAMGWGRVGAHDPPaQVLQELNVTVVTF-FCR-- 183
Cdd:pfam00089  77 hPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPS-DTLQEVTVPVVSReTCRsa 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71361688   184 ------PHNICTFVprRKAGICFGDSGGPLIC-DGIIQGIDSFvIWGCATRLFPDFFTRVALYVDWI 243
Cdd:pfam00089 156 yggtvtDTMICAGA--GGKDACQGDSGGPLVCsDGELIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
28-248 2.94e-53

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 173.30  E-value: 2.94e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688  28 IVGGHEAQPHSRPYMASLQMRGNPGSHFCGGTLIHPSFVLTAAHCLRDIPQRLVNVVLGAHNVRTQEPTQqhFSVAQVFL 107
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTV--VKVARIVV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688 108 N-NYDAENKLNDVLLIQLSSPANlsaSVATVQLPQQDQPVPHGTQCLAMGWGRVGAHDP-PAQVLQELNVTVVTF----- 180
Cdd:COG5640 109 HpDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGsQSGTLRKADVPVVSDatcaa 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71361688 181 ---FCRPHNICTFVPRRKAGICFGDSGGPLI----CDGIIQGIDSFVIWGCATRlFPDFFTRVALYVDWIRSTLR 248
Cdd:COG5640 186 yggFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAG-YPGVYTRVSAYRDWIKSTAG 259
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
28-246 7.33e-86

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: 255.28  E-value: 7.33e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688  28 IVGGHEAQPHSRPYMASLQMRGnpGSHFCGGTLIHPSFVLTAAHCLRDIPQRLVNVVLGAHNVRTQEPTQQHFSVAQVFL 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688 108 N-NYDAENKLNDVLLIQLSSPANLSASVATVQLPQQDQPVPHGTQCLAMGWGRVGAHDPPAQVLQELNVTVVTF-FCR-- 183
Cdd:cd00190  79 HpNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNaECKra 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71361688 184 --------PHNICTFVPRRKAGICFGDSGGPLICD----GIIQGIDSFVIwGCATRLFPDFFTRVALYVDWIRST 246
Cdd:cd00190 159 ysyggtitDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGS-GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
27-243 4.10e-81

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: 242.97  E-value: 4.10e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688     27 EIVGGHEAQPHSRPYMASLQMRGnpGSHFCGGTLIHPSFVLTAAHCLRDIPQRLVNVVLGAHNvRTQEPTQQHFSVAQVF 106
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG--GRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHD-LSSGEEGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688    107 LN-NYDAENKLNDVLLIQLSSPANLSASVATVQLPQQDQPVPHGTQCLAMGWGRV-GAHDPPAQVLQELNVTVVT-FFCR 183
Cdd:smart00020  78 IHpNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSnATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71361688    184 ----------PHNICTFVPRRKAGICFGDSGGPLICD---GIIQGIDSFVIwGCATRLFPDFFTRVALYVDWI 243
Cdd:smart00020 158 raysgggaitDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
28-243 2.30e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 223.09  E-value: 2.30e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688    28 IVGGHEAQPHSRPYMASLQMRGnpGSHFCGGTLIHPSFVLTAAHCLRDIPQrlVNVVLGAHNVRTQEPTQQHFSVAQVFL 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSS--GKHFCGGSLISENWVLTAAHCVSGASD--VKVVLGAHNIVLREGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688   108 -NNYDAENKLNDVLLIQLSSPANLSASVATVQLPQQDQPVPHGTQCLAMGWGRVGAHDPPaQVLQELNVTVVTF-FCR-- 183
Cdd:pfam00089  77 hPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPS-DTLQEVTVPVVSReTCRsa 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71361688   184 ------PHNICTFVprRKAGICFGDSGGPLIC-DGIIQGIDSFvIWGCATRLFPDFFTRVALYVDWI 243
Cdd:pfam00089 156 yggtvtDTMICAGA--GGKDACQGDSGGPLVCsDGELIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
28-248 2.94e-53

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 173.30  E-value: 2.94e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688  28 IVGGHEAQPHSRPYMASLQMRGNPGSHFCGGTLIHPSFVLTAAHCLRDIPQRLVNVVLGAHNVRTQEPTQqhFSVAQVFL 107
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTV--VKVARIVV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688 108 N-NYDAENKLNDVLLIQLSSPANlsaSVATVQLPQQDQPVPHGTQCLAMGWGRVGAHDP-PAQVLQELNVTVVTF----- 180
Cdd:COG5640 109 HpDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGsQSGTLRKADVPVVSDatcaa 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71361688 181 ---FCRPHNICTFVPRRKAGICFGDSGGPLI----CDGIIQGIDSFVIWGCATRlFPDFFTRVALYVDWIRSTLR 248
Cdd:COG5640 186 yggFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAG-YPGVYTRVSAYRDWIKSTAG 259
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
46-236 8.78e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 48.13  E-value: 8.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688  46 QMRGNPGSHFCGGTLIHPSFVLTAAHCLRDIPQ----RLVNVVLGAHNVRTQEPTQQHFSVAQVFLNNYDAEnklNDVLL 121
Cdd:COG3591   4 RLETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGggwaTNIVFVPGYNGGPYGTATATRFRVPPGWVASGDAG---YDYAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688 122 IQLSSPanLSASVATVQLPQQDQPVPhGTQCLAMGWgrvGAHDPPAQVLQElnvtvvtfFCRPHNICTFVPRRKAGICFG 201
Cdd:COG3591  81 LRLDEP--LGDTTGWLGLAFNDAPLA-GEPVTIIGY---PGDRPKDLSLDC--------SGRVTGVQGNRLSYDCDTTGG 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 71361688 202 DSGGPLI----CDGIIQGIDSFVIWGC---ATRLFPDFFTRV 236
Cdd:COG3591 147 SSGSPVLddsdGGGRVVGVHSAGGADRantGVRLTSAIVAAL 188
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
40-156 2.84e-04

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: 39.45  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71361688    40 PYMASLQMRGNpgsHFCGGTLIHPSFVLTAAHCLRDIPQR--LVNVVLGAHNVR--TQEPTQQHFSVaQVFLNNYDAEnk 115
Cdd:pfam09342   2 PWIAKVYLDGN---MICSGVLIDASWVIVSGSCLRDTNLRhqYISVVLGGAKTLksIEGPYEQIVRV-DCRHDIPESE-- 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 71361688   116 lndVLLIQLSSPANLSASVATVQLPQQDQPVPHGTQCLAMG 156
Cdd:pfam09342  76 ---ISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 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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