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Conserved domains on  [gi|200515|gb|AAA39990|]
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mast cell protease-like [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 ...
21-242 3.47e-82

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: 245.65  E-value: 3.47e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515    21 IIGGVESEPHSRPYMAYVntfRRKGYVAICGGFLITPQFVMTAAHC----RGRRMTVTLGAHNVRKRECTQQKIKVEKYI 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515    97 LPPNYNVSSKFNDIVLLKLKKQANLTSAVDVVPLPGPSDFAKPGTMCWAAGWGRTGVKKIISHTLREVELKIVGEKACK- 175
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKr 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 200515   176 --IFRHYKDSLQICVGSSTKVASVYMGDSGGPLLC----AGVAHGIVSSGRGNAKP--PAIFTRISPHVPWINRV 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 3.47e-82

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: 245.65  E-value: 3.47e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515    21 IIGGVESEPHSRPYMAYVntfRRKGYVAICGGFLITPQFVMTAAHC----RGRRMTVTLGAHNVRKRECTQQKIKVEKYI 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515    97 LPPNYNVSSKFNDIVLLKLKKQANLTSAVDVVPLPGPSDFAKPGTMCWAAGWGRTGVKKIISHTLREVELKIVGEKACK- 175
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKr 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 200515   176 --IFRHYKDSLQICVGSSTKVASVYMGDSGGPLLC----AGVAHGIVSSGRGNAKP--PAIFTRISPHVPWINRV 242
Cdd:cd00190 158 aySYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-239 3.27e-76

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: 230.26  E-value: 3.27e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515       20 EIIGGVESEPHSRPYMAYVntfRRKGYVAICGGFLITPQFVMTAAHC----RGRRMTVTLGAHNVRKREcTQQKIKVEKY 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSL---QYGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGE-EGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515       96 ILPPNYNVSSKFNDIVLLKLKKQANLTSAVDVVPLPGPSDFAKPGTMCWAAGWGRT-GVKKIISHTLREVELKIVGEKAC 174
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 200515      175 KifRHYK-----DSLQICVGSSTKVASVYMGDSGGPLLC---AGVAHGIVSSGRGNAKP--PAIFTRISPHVPWI 239
Cdd:smart00020 157 R--RAYSgggaiTDNMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-239 6.11e-63

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 196.12  E-value: 6.11e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515      21 IIGGVESEPHSRPYMAyvnTFRRKGYVAICGGFLITPQFVMTAAHC--RGRRMTVTLGAHNVRKRECTQQKIKVEKYILP 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQV---SLQLSSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515      99 PNYNVSSKFNDIVLLKLKKQANLTSAVDVVPLPGPSDFAKPGTMCWAAGWGRTGVKKiISHTLREVELKIVGEKACKifR 178
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCR--S 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 200515     179 HYKDSL---QICVGSSTKvaSVYMGDSGGPLLCAGV-AHGIVSSGRGNAKP--PAIFTRISPHVPWI 239
Cdd:pfam00089 155 AYGGTVtdtMICAGAGGK--DACQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-245 5.40e-48

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 159.04  E-value: 5.40e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515    13 PSGAGAEEIIGGVESEPHSRPYMAYVntFRRKGYVA-ICGGFLITPQFVMTAAHC----RGRRMTVTLGAHNVRKREctQ 87
Cdd:COG5640  23 PAADAAPAIVGGTPATVGEYPWMVAL--QSSNGPSGqFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSG--G 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515    88 QKIKVEKYILPPNYNVSSKFNDIVLLKLKKQANLTSAvdvVPLPGPSDFAKPGTMCWAAGWGRTGVKK-IISHTLREVEL 166
Cdd:COG5640  99 TVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAP---APLATSADAAAPGTPATVAGWGRTSEGPgSQSGTLRKADV 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515   167 KIVGEKACKIFRHYKDSLQICVGSSTKVASVYMGDSGGPLL----CAGVAHGIVSSGRGNAKP--PAIFTRISPHVPWIN 240
Cdd:COG5640 176 PVVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAgyPGVYTRVSAYRDWIK 255

                ....*
gi 200515   241 RVIKG 245
Cdd:COG5640 256 STAGG 260
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
21-242 3.47e-82

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: 245.65  E-value: 3.47e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515    21 IIGGVESEPHSRPYMAYVntfRRKGYVAICGGFLITPQFVMTAAHC----RGRRMTVTLGAHNVRKRECTQQKIKVEKYI 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515    97 LPPNYNVSSKFNDIVLLKLKKQANLTSAVDVVPLPGPSDFAKPGTMCWAAGWGRTGVKKIISHTLREVELKIVGEKACK- 175
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKr 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 200515   176 --IFRHYKDSLQICVGSSTKVASVYMGDSGGPLLC----AGVAHGIVSSGRGNAKP--PAIFTRISPHVPWINRV 242
Cdd:cd00190 158 aySYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-239 3.27e-76

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: 230.26  E-value: 3.27e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515       20 EIIGGVESEPHSRPYMAYVntfRRKGYVAICGGFLITPQFVMTAAHC----RGRRMTVTLGAHNVRKREcTQQKIKVEKY 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSL---QYGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGE-EGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515       96 ILPPNYNVSSKFNDIVLLKLKKQANLTSAVDVVPLPGPSDFAKPGTMCWAAGWGRT-GVKKIISHTLREVELKIVGEKAC 174
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 200515      175 KifRHYK-----DSLQICVGSSTKVASVYMGDSGGPLLC---AGVAHGIVSSGRGNAKP--PAIFTRISPHVPWI 239
Cdd:smart00020 157 R--RAYSgggaiTDNMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-239 6.11e-63

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 196.12  E-value: 6.11e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515      21 IIGGVESEPHSRPYMAyvnTFRRKGYVAICGGFLITPQFVMTAAHC--RGRRMTVTLGAHNVRKRECTQQKIKVEKYILP 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQV---SLQLSSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515      99 PNYNVSSKFNDIVLLKLKKQANLTSAVDVVPLPGPSDFAKPGTMCWAAGWGRTGVKKiISHTLREVELKIVGEKACKifR 178
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCR--S 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 200515     179 HYKDSL---QICVGSSTKvaSVYMGDSGGPLLCAGV-AHGIVSSGRGNAKP--PAIFTRISPHVPWI 239
Cdd:pfam00089 155 AYGGTVtdtMICAGAGGK--DACQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-245 5.40e-48

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 159.04  E-value: 5.40e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515    13 PSGAGAEEIIGGVESEPHSRPYMAYVntFRRKGYVA-ICGGFLITPQFVMTAAHC----RGRRMTVTLGAHNVRKREctQ 87
Cdd:COG5640  23 PAADAAPAIVGGTPATVGEYPWMVAL--QSSNGPSGqFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSG--G 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515    88 QKIKVEKYILPPNYNVSSKFNDIVLLKLKKQANLTSAvdvVPLPGPSDFAKPGTMCWAAGWGRTGVKK-IISHTLREVEL 166
Cdd:COG5640  99 TVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAP---APLATSADAAAPGTPATVAGWGRTSEGPgSQSGTLRKADV 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515   167 KIVGEKACKIFRHYKDSLQICVGSSTKVASVYMGDSGGPLL----CAGVAHGIVSSGRGNAKP--PAIFTRISPHVPWIN 240
Cdd:COG5640 176 PVVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAgyPGVYTRVSAYRDWIK 255

                ....*
gi 200515   241 RVIKG 245
Cdd:COG5640 256 STAGG 260
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
45-236 9.50e-08

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 50.83  E-value: 9.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515    45 GYVAICGGFLITPQFVMTAAHC--------RGRRMTVTLGAHNVRKRECTqqkikVEKYILPPNYNVSSKFN-DIVLLKL 115
Cdd:COG3591   9 GGGGVCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNGGPYGTAT-----ATRFRVPPGWVASGDAGyDYALLRL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515   116 KkqANLTSAVDVVPLpGPSDFAKPGTMCWAAGWGRTGVKKIishTLREvelkivgekACKIFRHYKDSLQIcvgsstkVA 195
Cdd:COG3591  84 D--EPLGDTTGWLGL-AFNDAPLAGEPVTIIGYPGDRPKDL---SLDC---------SGRVTGVQGNRLSY-------DC 141
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 200515   196 SVYMGDSGGPLL----CAGVAHGIVSSgrGNAKPPAIFTRISPHV 236
Cdd:COG3591 142 DTTGGSSGSPVLddsdGGGRVVGVHSA--GGADRANTGVRLTSAI 184
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
52-207 3.47e-05

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 42.41  E-value: 3.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200515      52 GFLITPQ-FVMTAAHCRGRRMTVTLGAHNVRKRECTQQKIKVEKYilPPNYnvsskfnDIVLLKLKKQANltsAVDVVPL 130
Cdd:pfam13365   3 GFVVSSDgLVLTNAHVVDDAEEAAVELVSVVLADGREYPATVVAR--DPDL-------DLALLRVSGDGR---GLPPLPL 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 200515     131 pGPSDFAKPGTMCWAAGWGRTGVKKIISHTlrevelKIVGEKACKIFRHYKDSLQICvgsstkvASVYMGDSGGPLL 207
Cdd:pfam13365  71 -GDSEPLVGGERVYAVGYPLGGEKLSLSEG------IVSGVDEGRDGGDDGRVIQTD-------AALSPGSSGGPVF 133
 
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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