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Conserved domains on  [gi|25282393|ref|NP_742041|]
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mast cell protease 1 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 2.95e-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: 255.66  E-value: 2.95e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393  21 IIGGVESIPHSRPYMAHLDIvteKGLRVICGGFLISRQFVLTAAHCKGR----EITVILGAHDVRKRESTQQKIKVEKQI 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSsapsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393  97 IHESYNSVPNLHDIMLLKLEKKVELTPAVNVVPLPSPSDFIHPGAMCWAAGWGKTGVRDPTSYTLREVELRIMDEKACVD 176
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25282393 177 YRYYEYKF---QVCVGSPTTLRAAFMGDSGGPLLC----AGVAHGIVSYGHPDAKP--PAIFTRVSTYVPWINAV 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 2.95e-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: 255.66  E-value: 2.95e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393  21 IIGGVESIPHSRPYMAHLDIvteKGLRVICGGFLISRQFVLTAAHCKGR----EITVILGAHDVRKRESTQQKIKVEKQI 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSsapsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393  97 IHESYNSVPNLHDIMLLKLEKKVELTPAVNVVPLPSPSDFIHPGAMCWAAGWGKTGVRDPTSYTLREVELRIMDEKACVD 176
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25282393 177 YRYYEYKF---QVCVGSPTTLRAAFMGDSGGPLLC----AGVAHGIVSYGHPDAKP--PAIFTRVSTYVPWINAV 242
Cdd:cd00190 158 AYSYGGTItdnMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-239 9.00e-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: 241.81  E-value: 9.00e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393     20 EIIGGVESIPHSRPYMAHLDIvteKGLRVICGGFLISRQFVLTAAHCKGR----EITVILGAHDVRKREStQQKIKVEKQ 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRGsdpsNIRVRLGSHDLSSGEE-GQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393     96 IIHESYNSVPNLHDIMLLKLEKKVELTPAVNVVPLPSPSDFIHPGAMCWAAGWGKTGVRDPT-SYTLREVELRIMDEKAC 174
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25282393    175 VDYRYYEYKF---QVCVGSPTTLRAAFMGDSGGPLLC---AGVAHGIVSYGHPDAKP--PAIFTRVSTYVPWI 239
Cdd:smart00020 157 RRAYSGGGAItdnMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-239 4.26e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 219.62  E-value: 4.26e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393    21 IIGGVESIPHSRPYMAHLDIvteKGLRVICGGFLISRQFVLTAAHCK--GREITVILGAHDVRKRESTQQKIKVEKQIIH 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393    99 ESYNSVPNLHDIMLLKLEKKVELTPAVNVVPLPSPSDFIHPGAMCWAAGWGKTGVRDPtSYTLREVELRIMDEKACV-DY 177
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRsAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25282393   178 RYYEYKFQVCVGspTTLRAAFMGDSGGPLLCAGV-AHGIVSYGHPDAKP--PAIFTRVSTYVPWI 239
Cdd:pfam00089 157 GGTVTDTMICAG--AGGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-247 2.50e-51

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 167.90  E-value: 2.50e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393  13 PSGAGAEEIIGGVESIPHSRPYMAHLdIVTEKGLRVICGGFLISRQFVLTAAHC----KGREITVILGAHDvrKRESTQQ 88
Cdd:COG5640  23 PAADAAPAIVGGTPATVGEYPWMVAL-QSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTD--LSTSGGT 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393  89 KIKVEKQIIHESYNSVPNLHDIMLLKLEKKVeltPAVNVVPLPSPSDFIHPGAMCWAAGWGKTGV-RDPTSYTLREVELR 167
Cdd:COG5640 100 VVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVP 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393 168 IMDEKACVDYRYYEYKFQVCVGSPTTLRAAFMGDSGGPLL----CAGVAHGIVSYGHPDAKP--PAIFTRVSTYVPWINA 241
Cdd:COG5640 177 VVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAgyPGVYTRVSAYRDWIKS 256

                ....*.
gi 25282393 242 VINTSS 247
Cdd:COG5640 257 TAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
21-242 2.95e-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: 255.66  E-value: 2.95e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393  21 IIGGVESIPHSRPYMAHLDIvteKGLRVICGGFLISRQFVLTAAHCKGR----EITVILGAHDVRKRESTQQKIKVEKQI 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSsapsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393  97 IHESYNSVPNLHDIMLLKLEKKVELTPAVNVVPLPSPSDFIHPGAMCWAAGWGKTGVRDPTSYTLREVELRIMDEKACVD 176
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25282393 177 YRYYEYKF---QVCVGSPTTLRAAFMGDSGGPLLC----AGVAHGIVSYGHPDAKP--PAIFTRVSTYVPWINAV 242
Cdd:cd00190 158 AYSYGGTItdnMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-239 9.00e-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: 241.81  E-value: 9.00e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393     20 EIIGGVESIPHSRPYMAHLDIvteKGLRVICGGFLISRQFVLTAAHCKGR----EITVILGAHDVRKREStQQKIKVEKQ 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRGsdpsNIRVRLGSHDLSSGEE-GQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393     96 IIHESYNSVPNLHDIMLLKLEKKVELTPAVNVVPLPSPSDFIHPGAMCWAAGWGKTGVRDPT-SYTLREVELRIMDEKAC 174
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25282393    175 VDYRYYEYKF---QVCVGSPTTLRAAFMGDSGGPLLC---AGVAHGIVSYGHPDAKP--PAIFTRVSTYVPWI 239
Cdd:smart00020 157 RRAYSGGGAItdnMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-239 4.26e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 219.62  E-value: 4.26e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393    21 IIGGVESIPHSRPYMAHLDIvteKGLRVICGGFLISRQFVLTAAHCK--GREITVILGAHDVRKRESTQQKIKVEKQIIH 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393    99 ESYNSVPNLHDIMLLKLEKKVELTPAVNVVPLPSPSDFIHPGAMCWAAGWGKTGVRDPtSYTLREVELRIMDEKACV-DY 177
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRsAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25282393   178 RYYEYKFQVCVGspTTLRAAFMGDSGGPLLCAGV-AHGIVSYGHPDAKP--PAIFTRVSTYVPWI 239
Cdd:pfam00089 157 GGTVTDTMICAG--AGGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-247 2.50e-51

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 167.90  E-value: 2.50e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393  13 PSGAGAEEIIGGVESIPHSRPYMAHLdIVTEKGLRVICGGFLISRQFVLTAAHC----KGREITVILGAHDvrKRESTQQ 88
Cdd:COG5640  23 PAADAAPAIVGGTPATVGEYPWMVAL-QSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTD--LSTSGGT 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393  89 KIKVEKQIIHESYNSVPNLHDIMLLKLEKKVeltPAVNVVPLPSPSDFIHPGAMCWAAGWGKTGV-RDPTSYTLREVELR 167
Cdd:COG5640 100 VVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVP 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393 168 IMDEKACVDYRYYEYKFQVCVGSPTTLRAAFMGDSGGPLL----CAGVAHGIVSYGHPDAKP--PAIFTRVSTYVPWINA 241
Cdd:COG5640 177 VVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAgyPGVYTRVSAYRDWIKS 256

                ....*.
gi 25282393 242 VINTSS 247
Cdd:COG5640 257 TAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
41-222 1.65e-03

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 38.50  E-value: 1.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393  41 VTEKGLRVICGGFLISRQFVLTAAHC-----KGR---EITVILGAHDvrkreSTQQKIKVEKQIIHESYNSVPNL-HDIM 111
Cdd:COG3591   5 LETDGGGGVCTGTLIGPNLVLTAGHCvydgaGGGwatNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGDAgYDYA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25282393 112 LLKLEKKVELTpavnVVPLP-SPSDFIHPGAMCWAAGWGKTgvrDPTSYTLREvELRIMDEKAcvDYRYYEykfqvCVGS 190
Cdd:COG3591  80 LLRLDEPLGDT----TGWLGlAFNDAPLAGEPVTIIGYPGD---RPKDLSLDC-SGRVTGVQG--NRLSYD-----CDTT 144
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 25282393 191 PttlraafmGDSGGPLL----CAGVAHGIVSYGHPD 222
Cdd:COG3591 145 G--------GSSGSPVLddsdGGGRVVGVHSAGGAD 172
 
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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