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Conserved domains on  [gi|6678838|ref|NP_032597|]
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mast cell protease 2 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 ...
21-240 2.25e-90

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: 266.06  E-value: 2.25e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838   21 IIGGVEAKPHSRPYMAYLKFttkNGSKERCGGFLIAPQFVMTAAHC----NGSEISVILGAHNINKNEPTQQIIKTEKTF 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838   97 VHPKFQYLSGFYDIMLLKLQKKAELNSDVDVISLPSSSDFIKPGKMCWTAGWGKTGKNNPLSVTLREVELRIMDQEACKD 176
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678838  177 HSDYDYQL---QVCAGSPTTSKSIGQGDSGGPLVCDS----VAHGIASSYE----AKAPAVFTRISYYLPWIYKV 240
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 ...
21-240 2.25e-90

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: 266.06  E-value: 2.25e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838   21 IIGGVEAKPHSRPYMAYLKFttkNGSKERCGGFLIAPQFVMTAAHC----NGSEISVILGAHNINKNEPTQQIIKTEKTF 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838   97 VHPKFQYLSGFYDIMLLKLQKKAELNSDVDVISLPSSSDFIKPGKMCWTAGWGKTGKNNPLSVTLREVELRIMDQEACKD 176
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678838  177 HSDYDYQL---QVCAGSPTTSKSIGQGDSGGPLVCDS----VAHGIASSYE----AKAPAVFTRISYYLPWIYKV 240
Cdd:cd00190 158 AYSYGGTItdnMLCAGGLEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSgcarPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-237 1.07e-84

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: 251.83  E-value: 1.07e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838      20 EIIGGVEAKPHSRPYMAYLKFttkNGSKERCGGFLIAPQFVMTAAHC----NGSEISVILGAHNINKNEPtQQIIKTEKT 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEE-GQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838      96 FVHPKFQYLSGFYDIMLLKLQKKAELNSDVDVISLPSSSDFIKPGKMCWTAGWGKTGKNNP-LSVTLREVELRIMDQEAC 174
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGsLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678838     175 KDHSDYDYQL---QVCAGSPTTSKSIGQGDSGGPLVCDS---VAHGIASSYE----AKAPAVFTRISYYLPWI 237
Cdd:smart00020 157 RRAYSGGGAItdnMLCAGGLEGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSgcarPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-237 3.78e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 211.92  E-value: 3.78e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838     21 IIGGVEAKPHSRPYMAYLKFTtknGSKERCGGFLIAPQFVMTAAHC--NGSEISVILGAHNINKNEPTQQIIKTEKTFVH 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLS---SGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838     99 PKFQYLSGFYDIMLLKLQKKAELNSDVDVISLPSSSDFIKPGKMCWTAGWGKTGKNNPlSVTLREVELRIMDQEACK-DH 177
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRsAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678838    178 SDYDYQLQVCAGspTTSKSIGQGDSGGPLVCDSV-AHGIASSYEAKA----PAVFTRISYYLPWI 237
Cdd:pfam00089 157 GGTVTDTMICAG--AGGKDACQGDSGGPLVCSDGeLIGIVSWGYGCAsgnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-243 9.27e-55

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 176.38  E-value: 9.27e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838   13 PSGAGAEEIIGGVEAKPHSRPYMAYLkfTTKNGSKE-RCGGFLIAPQFVMTAAHC----NGSEISVILGAHNINKNEPtq 87
Cdd:COG5640  23 PAADAAPAIVGGTPATVGEYPWMVAL--QSSNGPSGqFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSGG-- 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838   88 QIIKTEKTFVHPKFQYLSGFYDIMLLKLQKKAelnSDVDVISLPSSSDFIKPGKMCWTAGWGKTGKNNP-LSVTLREVEL 166
Cdd:COG5640  99 TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGsQSGTLRKADV 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838  167 RIMDQEACKDHSDYDYQLQVCAGSPTTSKSIGQGDSGGPLVCDS----VAHGIAS----SYEAKAPAVFTRISYYLPWIY 238
Cdd:COG5640 176 PVVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDgggwVLVGVVSwgggPCAAGYPGVYTRVSAYRDWIK 255

                ....*
gi 6678838  239 KVLKS 243
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 ...
21-240 2.25e-90

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: 266.06  E-value: 2.25e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838   21 IIGGVEAKPHSRPYMAYLKFttkNGSKERCGGFLIAPQFVMTAAHC----NGSEISVILGAHNINKNEPTQQIIKTEKTF 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838   97 VHPKFQYLSGFYDIMLLKLQKKAELNSDVDVISLPSSSDFIKPGKMCWTAGWGKTGKNNPLSVTLREVELRIMDQEACKD 176
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678838  177 HSDYDYQL---QVCAGSPTTSKSIGQGDSGGPLVCDS----VAHGIASSYE----AKAPAVFTRISYYLPWIYKV 240
Cdd:cd00190 158 AYSYGGTItdnMLCAGGLEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSgcarPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-237 1.07e-84

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: 251.83  E-value: 1.07e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838      20 EIIGGVEAKPHSRPYMAYLKFttkNGSKERCGGFLIAPQFVMTAAHC----NGSEISVILGAHNINKNEPtQQIIKTEKT 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEE-GQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838      96 FVHPKFQYLSGFYDIMLLKLQKKAELNSDVDVISLPSSSDFIKPGKMCWTAGWGKTGKNNP-LSVTLREVELRIMDQEAC 174
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGsLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678838     175 KDHSDYDYQL---QVCAGSPTTSKSIGQGDSGGPLVCDS---VAHGIASSYE----AKAPAVFTRISYYLPWI 237
Cdd:smart00020 157 RRAYSGGGAItdnMLCAGGLEGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSgcarPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-237 3.78e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 211.92  E-value: 3.78e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838     21 IIGGVEAKPHSRPYMAYLKFTtknGSKERCGGFLIAPQFVMTAAHC--NGSEISVILGAHNINKNEPTQQIIKTEKTFVH 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLS---SGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838     99 PKFQYLSGFYDIMLLKLQKKAELNSDVDVISLPSSSDFIKPGKMCWTAGWGKTGKNNPlSVTLREVELRIMDQEACK-DH 177
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRsAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678838    178 SDYDYQLQVCAGspTTSKSIGQGDSGGPLVCDSV-AHGIASSYEAKA----PAVFTRISYYLPWI 237
Cdd:pfam00089 157 GGTVTDTMICAG--AGGKDACQGDSGGPLVCSDGeLIGIVSWGYGCAsgnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-243 9.27e-55

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 176.38  E-value: 9.27e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838   13 PSGAGAEEIIGGVEAKPHSRPYMAYLkfTTKNGSKE-RCGGFLIAPQFVMTAAHC----NGSEISVILGAHNINKNEPtq 87
Cdd:COG5640  23 PAADAAPAIVGGTPATVGEYPWMVAL--QSSNGPSGqFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSGG-- 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838   88 QIIKTEKTFVHPKFQYLSGFYDIMLLKLQKKAelnSDVDVISLPSSSDFIKPGKMCWTAGWGKTGKNNP-LSVTLREVEL 166
Cdd:COG5640  99 TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGsQSGTLRKADV 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678838  167 RIMDQEACKDHSDYDYQLQVCAGSPTTSKSIGQGDSGGPLVCDS----VAHGIAS----SYEAKAPAVFTRISYYLPWIY 238
Cdd:COG5640 176 PVVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDgggwVLVGVVSwgggPCAAGYPGVYTRVSAYRDWIK 255

                ....*
gi 6678838  239 KVLKS 243
Cdd:COG5640 256 STAGG 260
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
44-66 1.60e-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: 1.60e-03
                        10        20
                ....*....|....*....|...
gi 6678838   44 NGSKERCGGFLIAPQFVMTAAHC 66
Cdd:COG3591   8 DGGGGVCTGTLIGPNLVLTAGHC 30
 
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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