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Conserved domains on  [gi|9506885|ref|NP_062194|]
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mast cell protease 4 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 ...
21-242 1.67e-78

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: 236.02  E-value: 1.67e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885   21 IIGGVESIPHSRPYMALLKIvteEGHVTFCGGFLISLQFVLTAAHC----HGREITVTLGAHDMSKRESTQQKIKVVKQI 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885   97 FPLKYNLFSNFRDIMLLKLEQKAVLTPSVNVIPLPQSSDIIKPGTMCLAAGWGQTGVKEPNSNTLREVMLRIMEMKACKD 176
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9506885  177 YRHYDNRF---QICVGIPQMLKLAYKGDSGGPLVC----AGVAHGIVSHGPGRGIP--PIIFTRISSYVSWINRV 242
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 ...
21-242 1.67e-78

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: 236.02  E-value: 1.67e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885   21 IIGGVESIPHSRPYMALLKIvteEGHVTFCGGFLISLQFVLTAAHC----HGREITVTLGAHDMSKRESTQQKIKVVKQI 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885   97 FPLKYNLFSNFRDIMLLKLEQKAVLTPSVNVIPLPQSSDIIKPGTMCLAAGWGQTGVKEPNSNTLREVMLRIMEMKACKD 176
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9506885  177 YRHYDNRF---QICVGIPQMLKLAYKGDSGGPLVC----AGVAHGIVSHGPGRGIP--PIIFTRISSYVSWINRV 242
Cdd:cd00190 158 AYSYGGTItdnMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-239 1.06e-73

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: 223.71  E-value: 1.06e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885      20 EIIGGVESIPHSRPYMALLKIvteEGHVTFCGGFLISLQFVLTAAHC----HGREITVTLGAHDMSKREStQQKIKVVKQ 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEE-GQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885      96 IFPLKYNLFSNFRDIMLLKLEQKAVLTPSVNVIPLPQSSDIIKPGTMCLAAGWGQT-GVKEPNSNTLREVMLRIMEMKAC 174
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9506885     175 KDYRHYDNRF---QICVGIPQMLKLAYKGDSGGPLVC---AGVAHGIVSHGPGRGIP--PIIFTRISSYVSWI 239
Cdd:smart00020 157 RRAYSGGGAItdnMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-239 3.35e-64

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 199.21  E-value: 3.35e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885     21 IIGGVESIPHSRPYMALLKIvteEGHVTFCGGFLISLQFVLTAAHC--HGREITVTLGAHDMSKRESTQQKIKVVKQIFP 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885     99 LKYNLFSNFRDIMLLKLEQKAVLTPSVNVIPLPQSSDIIKPGTMCLAAGWGQTGVKEPnSNTLREVMLRIMEMKACK-DY 177
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRsAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9506885    178 RHYDNRFQICVGIPQmlKLAYKGDSGGPLVCAGV-AHGIVSHGPGRGIP--PIIFTRISSYVSWI 239
Cdd:pfam00089 157 GGTVTDTMICAGAGG--KDACQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-246 1.10e-48

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 160.97  E-value: 1.10e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885   13 PSGAGAEEIIGGVESIPHSRPYMALLkiVTEEGHVT-FCGGFLISLQFVLTAAHCH----GREITVTLGAHDMSkrESTQ 87
Cdd:COG5640  23 PAADAAPAIVGGTPATVGEYPWMVAL--QSSNGPSGqFCGGTLIAPRWVLTAAHCVdgdgPSDLRVVIGSTDLS--TSGG 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885   88 QKIKVVKQIFPLKYNLFSNFRDIMLLKLEQKAvltPSVNVIPLPQSSDIIKPGTMCLAAGWGQTGVKEPN-SNTLREVML 166
Cdd:COG5640  99 TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSqSGTLRKADV 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885  167 RIMEMKACKDYRHYDNRFQICVGIPQMLKLAYKGDSGGPLV----CAGVAHGIVSHGPGRGIP--PIIFTRISSYVSWIN 240
Cdd:COG5640 176 PVVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAgyPGVYTRVSAYRDWIK 255

                ....*.
gi 9506885  241 RVIRGN 246
Cdd:COG5640 256 STAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
21-242 1.67e-78

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: 236.02  E-value: 1.67e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885   21 IIGGVESIPHSRPYMALLKIvteEGHVTFCGGFLISLQFVLTAAHC----HGREITVTLGAHDMSKRESTQQKIKVVKQI 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885   97 FPLKYNLFSNFRDIMLLKLEQKAVLTPSVNVIPLPQSSDIIKPGTMCLAAGWGQTGVKEPNSNTLREVMLRIMEMKACKD 176
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9506885  177 YRHYDNRF---QICVGIPQMLKLAYKGDSGGPLVC----AGVAHGIVSHGPGRGIP--PIIFTRISSYVSWINRV 242
Cdd:cd00190 158 AYSYGGTItdnMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-239 1.06e-73

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: 223.71  E-value: 1.06e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885      20 EIIGGVESIPHSRPYMALLKIvteEGHVTFCGGFLISLQFVLTAAHC----HGREITVTLGAHDMSKREStQQKIKVVKQ 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEE-GQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885      96 IFPLKYNLFSNFRDIMLLKLEQKAVLTPSVNVIPLPQSSDIIKPGTMCLAAGWGQT-GVKEPNSNTLREVMLRIMEMKAC 174
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9506885     175 KDYRHYDNRF---QICVGIPQMLKLAYKGDSGGPLVC---AGVAHGIVSHGPGRGIP--PIIFTRISSYVSWI 239
Cdd:smart00020 157 RRAYSGGGAItdnMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-239 3.35e-64

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 199.21  E-value: 3.35e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885     21 IIGGVESIPHSRPYMALLKIvteEGHVTFCGGFLISLQFVLTAAHC--HGREITVTLGAHDMSKRESTQQKIKVVKQIFP 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885     99 LKYNLFSNFRDIMLLKLEQKAVLTPSVNVIPLPQSSDIIKPGTMCLAAGWGQTGVKEPnSNTLREVMLRIMEMKACK-DY 177
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRsAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9506885    178 RHYDNRFQICVGIPQmlKLAYKGDSGGPLVCAGV-AHGIVSHGPGRGIP--PIIFTRISSYVSWI 239
Cdd:pfam00089 157 GGTVTDTMICAGAGG--KDACQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-246 1.10e-48

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 160.97  E-value: 1.10e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885   13 PSGAGAEEIIGGVESIPHSRPYMALLkiVTEEGHVT-FCGGFLISLQFVLTAAHCH----GREITVTLGAHDMSkrESTQ 87
Cdd:COG5640  23 PAADAAPAIVGGTPATVGEYPWMVAL--QSSNGPSGqFCGGTLIAPRWVLTAAHCVdgdgPSDLRVVIGSTDLS--TSGG 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885   88 QKIKVVKQIFPLKYNLFSNFRDIMLLKLEQKAvltPSVNVIPLPQSSDIIKPGTMCLAAGWGQTGVKEPN-SNTLREVML 166
Cdd:COG5640  99 TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSqSGTLRKADV 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506885  167 RIMEMKACKDYRHYDNRFQICVGIPQMLKLAYKGDSGGPLV----CAGVAHGIVSHGPGRGIP--PIIFTRISSYVSWIN 240
Cdd:COG5640 176 PVVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAgyPGVYTRVSAYRDWIK 255

                ....*.
gi 9506885  241 RVIRGN 246
Cdd:COG5640 256 STAGGL 261
 
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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