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Conserved domains on  [gi|66730380|ref|NP_001019435|]
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myeloblastin precursor [Rattus norvegicus]

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 ...
30-248 6.45e-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: 250.27  E-value: 6.45e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380  30 IVGGHEARPHSRPYVASLQlsRSPGSHFCGGTLIHPRFVLTAAHCLQDISWQLVTVVLGAHDLLSSEPEQQKFTITQVFE 109
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQ--YTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380 110 N-NYNPEETLNDVLLLQLNRPASLGKQVAVASLPQQDQSLSQGTQCLAMGWGRLGTRAPTPRVLHELNVTVVTF-LCREH 187
Cdd:cd00190  79 HpNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNaECKRA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66730380 188 ----------NVCTLVPRRAAGICFGDSGGPLICN----GILHGVDSFVIReCASLQFPDFFARVSMYVNWIHSV 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 6.45e-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: 250.27  E-value: 6.45e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380  30 IVGGHEARPHSRPYVASLQlsRSPGSHFCGGTLIHPRFVLTAAHCLQDISWQLVTVVLGAHDLLSSEPEQQKFTITQVFE 109
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQ--YTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380 110 N-NYNPEETLNDVLLLQLNRPASLGKQVAVASLPQQDQSLSQGTQCLAMGWGRLGTRAPTPRVLHELNVTVVTF-LCREH 187
Cdd:cd00190  79 HpNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNaECKRA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66730380 188 ----------NVCTLVPRRAAGICFGDSGGPLICN----GILHGVDSFVIReCASLQFPDFFARVSMYVNWIHSV 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 3.64e-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: 235.65  E-value: 3.64e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380     29 KIVGGHEARPHSRPYVASLQLSRspGSHFCGGTLIHPRFVLTAAHCLQDISWQLVTVVLGAHDLLSSEpEQQKFTITQVF 108
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG--GRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGE-EGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380    109 EN-NYNPEETLNDVLLLQLNRPASLGKQVAVASLPQQDQSLSQGTQCLAMGWGRLGTRAPT-PRVLHELNVTVVT-FLCR 185
Cdd:smart00020  78 IHpNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSnATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66730380    186 EH----------NVCTLVPRRAAGICFGDSGGPLICN---GILHGVDSFVIReCASLQFPDFFARVSMYVNWI 245
Cdd:smart00020 158 RAysgggaitdnMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSG-CARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
30-245 4.93e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 211.92  E-value: 4.93e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380    30 IVGGHEARPHSRPYVASLQLSRspGSHFCGGTLIHPRFVLTAAHCLQDISwqLVTVVLGAHDLLSSEPEQQKFTITQVFE 109
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSS--GKHFCGGSLISENWVLTAAHCVSGAS--DVKVVLGAHNIVLREGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380   110 -NNYNPEETLNDVLLLQLNRPASLGKQVAVASLPQQDQSLSQGTQCLAMGWGRLGTRAPtPRVLHELNVTVVTF-LCR-- 185
Cdd:pfam00089  77 hPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSReTCRsa 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66730380   186 ------EHNVCTLVPRRAagICFGDSGGPLIC-NGILHGVDSFvIRECASLQFPDFFARVSMYVNWI 245
Cdd:pfam00089 156 yggtvtDTMICAGAGGKD--ACQGDSGGPLVCsDGELIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
15-253 2.02e-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: 2.02e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380  15 LLLALVFGGAVQAS-KIVGGHEARPHSRPYVASLQLSRSPGSHFCGGTLIHPRFVLTAAHCLQDISWQLVTVVLGAHDLL 93
Cdd:COG5640  15 LALALAAAPAADAApAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLS 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380  94 SSEPeqQKFTITQVFEN-NYNPEETLNDVLLLQLNRPASLgkqVAVASLPQQDQSLSQGTQCLAMGWGRL-GTRAPTPRV 171
Cdd:COG5640  95 TSGG--TVVKVARIVVHpDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTsEGPGSQSGT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380 172 LHELNVTVVTF-LCR-------EHNVCTLVPRRAAGICFGDSGGPLI----CNGILHGVDSFVIRECASlQFPDFFARVS 239
Cdd:COG5640 170 LRKADVPVVSDaTCAayggfdgGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAA-GYPGVYTRVS 248
                       250
                ....*....|....
gi 66730380 240 MYVNWIHSVLRSAE 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 6.45e-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: 250.27  E-value: 6.45e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380  30 IVGGHEARPHSRPYVASLQlsRSPGSHFCGGTLIHPRFVLTAAHCLQDISWQLVTVVLGAHDLLSSEPEQQKFTITQVFE 109
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQ--YTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380 110 N-NYNPEETLNDVLLLQLNRPASLGKQVAVASLPQQDQSLSQGTQCLAMGWGRLGTRAPTPRVLHELNVTVVTF-LCREH 187
Cdd:cd00190  79 HpNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNaECKRA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66730380 188 ----------NVCTLVPRRAAGICFGDSGGPLICN----GILHGVDSFVIReCASLQFPDFFARVSMYVNWIHSV 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 3.64e-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: 235.65  E-value: 3.64e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380     29 KIVGGHEARPHSRPYVASLQLSRspGSHFCGGTLIHPRFVLTAAHCLQDISWQLVTVVLGAHDLLSSEpEQQKFTITQVF 108
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG--GRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGE-EGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380    109 EN-NYNPEETLNDVLLLQLNRPASLGKQVAVASLPQQDQSLSQGTQCLAMGWGRLGTRAPT-PRVLHELNVTVVT-FLCR 185
Cdd:smart00020  78 IHpNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSnATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66730380    186 EH----------NVCTLVPRRAAGICFGDSGGPLICN---GILHGVDSFVIReCASLQFPDFFARVSMYVNWI 245
Cdd:smart00020 158 RAysgggaitdnMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSG-CARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
30-245 4.93e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 211.92  E-value: 4.93e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380    30 IVGGHEARPHSRPYVASLQLSRspGSHFCGGTLIHPRFVLTAAHCLQDISwqLVTVVLGAHDLLSSEPEQQKFTITQVFE 109
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSS--GKHFCGGSLISENWVLTAAHCVSGAS--DVKVVLGAHNIVLREGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380   110 -NNYNPEETLNDVLLLQLNRPASLGKQVAVASLPQQDQSLSQGTQCLAMGWGRLGTRAPtPRVLHELNVTVVTF-LCR-- 185
Cdd:pfam00089  77 hPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSReTCRsa 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66730380   186 ------EHNVCTLVPRRAagICFGDSGGPLIC-NGILHGVDSFvIRECASLQFPDFFARVSMYVNWI 245
Cdd:pfam00089 156 yggtvtDTMICAGAGGKD--ACQGDSGGPLVCsDGELIGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
15-253 2.02e-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: 2.02e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380  15 LLLALVFGGAVQAS-KIVGGHEARPHSRPYVASLQLSRSPGSHFCGGTLIHPRFVLTAAHCLQDISWQLVTVVLGAHDLL 93
Cdd:COG5640  15 LALALAAAPAADAApAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLS 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380  94 SSEPeqQKFTITQVFEN-NYNPEETLNDVLLLQLNRPASLgkqVAVASLPQQDQSLSQGTQCLAMGWGRL-GTRAPTPRV 171
Cdd:COG5640  95 TSGG--TVVKVARIVVHpDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTsEGPGSQSGT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380 172 LHELNVTVVTF-LCR-------EHNVCTLVPRRAAGICFGDSGGPLI----CNGILHGVDSFVIRECASlQFPDFFARVS 239
Cdd:COG5640 170 LRKADVPVVSDaTCAayggfdgGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAA-GYPGVYTRVS 248
                       250
                ....*....|....
gi 66730380 240 MYVNWIHSVLRSAE 253
Cdd:COG5640 249 AYRDWIKSTAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
48-210 9.97e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 47.75  E-value: 9.97e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380  48 QLSRSPGSHFCGGTLIHPRFVLTAAHCLQDIS----WQLVTVVLGAHDLLSSEPEQQKFTITQVFENNYNPEetlNDVLL 123
Cdd:COG3591   4 RLETDGGGGVCTGTLIGPNLVLTAGHCVYDGAgggwATNIVFVPGYNGGPYGTATATRFRVPPGWVASGDAG---YDYAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730380 124 LQLNRPasLGKQVAVASLPQQDQSLSqGTQCLAMGWGrlGTRAPTPRVLHELNVTVVTFLCREHNvctlvprraAGICFG 203
Cdd:COG3591  81 LRLDEP--LGDTTGWLGLAFNDAPLA-GEPVTIIGYP--GDRPKDLSLDCSGRVTGVQGNRLSYD---------CDTTGG 146

                ....*..
gi 66730380 204 DSGGPLI 210
Cdd:COG3591 147 SSGSPVL 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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