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Conserved domains on  [gi|31981542|ref|NP_035308|]
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myeloblastin precursor [Mus musculus]

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 ...
30-248 1.26e-84

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: 251.81  E-value: 1.26e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542  30 IVGGHEARPHSRPYVASLQLSRfpGSHFCGGTLIHPRFVLTAAHCLQDISWQLVTVVLGAHDLLSSEPEQQKFTISQVFQ 109
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542 110 N-NYNPEENLNDVLLLQLNRTASLGKEVAVASLPQQDQTLSQGTQCLAMGWGRLGTQAPTPRVLQELNVTVVTF-LCREH 187
Cdd:cd00190  79 HpNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNaECKRA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31981542 188 ----------NVCTLVPRRAAGICFGDSGGPLICN----GILHGVDSFVIReCASLQFPDFFARVSMYVDWIQNV 248
Cdd:cd00190 159 ysyggtitdnMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
30-248 1.26e-84

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: 251.81  E-value: 1.26e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542  30 IVGGHEARPHSRPYVASLQLSRfpGSHFCGGTLIHPRFVLTAAHCLQDISWQLVTVVLGAHDLLSSEPEQQKFTISQVFQ 109
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542 110 N-NYNPEENLNDVLLLQLNRTASLGKEVAVASLPQQDQTLSQGTQCLAMGWGRLGTQAPTPRVLQELNVTVVTF-LCREH 187
Cdd:cd00190  79 HpNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNaECKRA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31981542 188 ----------NVCTLVPRRAAGICFGDSGGPLICN----GILHGVDSFVIReCASLQFPDFFARVSMYVDWIQNV 248
Cdd:cd00190 159 ysyggtitdnMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
29-245 4.01e-78

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: 235.26  E-value: 4.01e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542     29 KIVGGHEARPHSRPYVASLQLSRfpGSHFCGGTLIHPRFVLTAAHCLQDISWQLVTVVLGAHDLLSSEpEQQKFTISQVF 108
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG--GRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGE-EGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542    109 QN-NYNPEENLNDVLLLQLNRTASLGKEVAVASLPQQDQTLSQGTQCLAMGWGRL-GTQAPTPRVLQELNVTVVT-FLCR 185
Cdd:smart00020  78 IHpNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSnATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31981542    186 EH----------NVCTLVPRRAAGICFGDSGGPLICN---GILHGVDSFVIReCASLQFPDFFARVSMYVDWI 245
Cdd:smart00020 158 RAysgggaitdnMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSG-CARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
30-245 9.12e-68

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 208.84  E-value: 9.12e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542    30 IVGGHEARPHSRPYVASLQLSRfpGSHFCGGTLIHPRFVLTAAHCLQDISwqLVTVVLGAHDLLSSEPEQQKFTISQVF- 108
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSS--GKHFCGGSLISENWVLTAAHCVSGAS--DVKVVLGAHNIVLREGGEQKFDVEKIIv 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542   109 QNNYNPEENLNDVLLLQLNRTASLGKEVAVASLPQQDQTLSQGTQCLAMGWGRLGTQAPtPRVLQELNVTVVTF-LCR-- 185
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSReTCRsa 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31981542   186 ------EHNVCTLVPRRAagICFGDSGGPLIC-NGILHGVDSFvIRECASLQFPDFFARVSMYVDWI 245
Cdd:pfam00089 156 yggtvtDTMICAGAGGKD--ACQGDSGGPLVCsDGELIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
15-253 2.40e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 188.70  E-value: 2.40e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542  15 LLLALVVGGAVQAS-KIVGGHEARPHSRPYVASLQLSRFPGSHFCGGTLIHPRFVLTAAHCLQDISWQLVTVVLGAHDLL 93
Cdd:COG5640  15 LALALAAAPAADAApAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLS 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542  94 SSEPeqQKFTISQVFQN-NYNPEENLNDVLLLQLNRTASlgkEVAVASLPQQDQTLSQGTQCLAMGWGRL-GTQAPTPRV 171
Cdd:COG5640  95 TSGG--TVVKVARIVVHpDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTsEGPGSQSGT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542 172 LQELNVTVVTF-LCR-------EHNVCTLVPRRAAGICFGDSGGPLI----CNGILHGVDSFVIRECASlQFPDFFARVS 239
Cdd:COG5640 170 LRKADVPVVSDaTCAayggfdgGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAA-GYPGVYTRVS 248
                       250
                ....*....|....
gi 31981542 240 MYVDWIQNVLRGAE 253
Cdd:COG5640 249 AYRDWIKSTAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
30-248 1.26e-84

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: 251.81  E-value: 1.26e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542  30 IVGGHEARPHSRPYVASLQLSRfpGSHFCGGTLIHPRFVLTAAHCLQDISWQLVTVVLGAHDLLSSEPEQQKFTISQVFQ 109
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTG--GRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542 110 N-NYNPEENLNDVLLLQLNRTASLGKEVAVASLPQQDQTLSQGTQCLAMGWGRLGTQAPTPRVLQELNVTVVTF-LCREH 187
Cdd:cd00190  79 HpNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNaECKRA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31981542 188 ----------NVCTLVPRRAAGICFGDSGGPLICN----GILHGVDSFVIReCASLQFPDFFARVSMYVDWIQNV 248
Cdd:cd00190 159 ysyggtitdnMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
29-245 4.01e-78

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: 235.26  E-value: 4.01e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542     29 KIVGGHEARPHSRPYVASLQLSRfpGSHFCGGTLIHPRFVLTAAHCLQDISWQLVTVVLGAHDLLSSEpEQQKFTISQVF 108
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG--GRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGE-EGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542    109 QN-NYNPEENLNDVLLLQLNRTASLGKEVAVASLPQQDQTLSQGTQCLAMGWGRL-GTQAPTPRVLQELNVTVVT-FLCR 185
Cdd:smart00020  78 IHpNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSnATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31981542    186 EH----------NVCTLVPRRAAGICFGDSGGPLICN---GILHGVDSFVIReCASLQFPDFFARVSMYVDWI 245
Cdd:smart00020 158 RAysgggaitdnMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSG-CARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
30-245 9.12e-68

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 208.84  E-value: 9.12e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542    30 IVGGHEARPHSRPYVASLQLSRfpGSHFCGGTLIHPRFVLTAAHCLQDISwqLVTVVLGAHDLLSSEPEQQKFTISQVF- 108
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSS--GKHFCGGSLISENWVLTAAHCVSGAS--DVKVVLGAHNIVLREGGEQKFDVEKIIv 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542   109 QNNYNPEENLNDVLLLQLNRTASLGKEVAVASLPQQDQTLSQGTQCLAMGWGRLGTQAPtPRVLQELNVTVVTF-LCR-- 185
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSReTCRsa 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31981542   186 ------EHNVCTLVPRRAagICFGDSGGPLIC-NGILHGVDSFvIRECASLQFPDFFARVSMYVDWI 245
Cdd:pfam00089 156 yggtvtDTMICAGAGGKD--ACQGDSGGPLVCsDGELIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
15-253 2.40e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 188.70  E-value: 2.40e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542  15 LLLALVVGGAVQAS-KIVGGHEARPHSRPYVASLQLSRFPGSHFCGGTLIHPRFVLTAAHCLQDISWQLVTVVLGAHDLL 93
Cdd:COG5640  15 LALALAAAPAADAApAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLS 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542  94 SSEPeqQKFTISQVFQN-NYNPEENLNDVLLLQLNRTASlgkEVAVASLPQQDQTLSQGTQCLAMGWGRL-GTQAPTPRV 171
Cdd:COG5640  95 TSGG--TVVKVARIVVHpDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTsEGPGSQSGT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542 172 LQELNVTVVTF-LCR-------EHNVCTLVPRRAAGICFGDSGGPLI----CNGILHGVDSFVIRECASlQFPDFFARVS 239
Cdd:COG5640 170 LRKADVPVVSDaTCAayggfdgGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAA-GYPGVYTRVS 248
                       250
                ....*....|....
gi 31981542 240 MYVDWIQNVLRGAE 253
Cdd:COG5640 249 AYRDWIKSTAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
48-210 3.07e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 43.51  E-value: 3.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542  48 QLSRFPGSHFCGGTLIHPRFVLTAAHCLQDIS----WQLVTVVLGAHDLLSSEPEQQKFTISQVFQNNYNPEenlNDVLL 123
Cdd:COG3591   4 RLETDGGGGVCTGTLIGPNLVLTAGHCVYDGAgggwATNIVFVPGYNGGPYGTATATRFRVPPGWVASGDAG---YDYAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31981542 124 LQLNR--TASLGK-EVAVASLPQQDQTLSQGTQclAMGWGRLGTQAPTPRVLQELNvTVVTFLCRehnvctlvprraagI 200
Cdd:COG3591  81 LRLDEplGDTTGWlGLAFNDAPLAGEPVTIIGY--PGDRPKDLSLDCSGRVTGVQG-NRLSYDCD--------------T 143
                       170
                ....*....|
gi 31981542 201 CFGDSGGPLI 210
Cdd:COG3591 144 TGGSSGSPVL 153
 
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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