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Conserved domains on  [gi|114205406|ref|NP_034909|]
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mast cell protease 4 precursor [Mus musculus]

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 1.79e-93

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: 274.15  E-value: 1.79e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406  21 IIGGVESRPHSRPYMAHLEITTERGFtatCGGFLITRQFVLTAAHC----SGREITVTLGAHDVSKTESTQQKIKVEKQI 96
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHF---CGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406  97 VHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPTSDILREVKLRIMDKEACKN 176
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114205406 177 YWHYDYNL---QVCVGSPRKKRSAYKGDSGGPLLC----AGVAHGIVSYGRGDAKP--PAVFTRISSYVPWINRV 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 1.79e-93

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: 274.15  E-value: 1.79e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406  21 IIGGVESRPHSRPYMAHLEITTERGFtatCGGFLITRQFVLTAAHC----SGREITVTLGAHDVSKTESTQQKIKVEKQI 96
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHF---CGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406  97 VHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPTSDILREVKLRIMDKEACKN 176
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114205406 177 YWHYDYNL---QVCVGSPRKKRSAYKGDSGGPLLC----AGVAHGIVSYGRGDAKP--PAVFTRISSYVPWINRV 242
Cdd:cd00190  158 AYSYGGTItdnMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-239 1.29e-86

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: 256.45  E-value: 1.29e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406    20 EIIGGVESRPHSRPYMAHLEItteRGFTATCGGFLITRQFVLTAAHC----SGREITVTLGAHDVSKTEStQQKIKVEKQ 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEE-GQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406    96 IVHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPT-SDILREVKLRIMDKEAC 174
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114205406   175 KNYWHYDYNL---QVCVGSPRKKRSAYKGDSGGPLLC---AGVAHGIVSYGRGDAKP--PAVFTRISSYVPWI 239
Cdd:smart00020 157 RRAYSGGGAItdnMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-239 9.71e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 218.47  E-value: 9.71e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406   21 IIGGVESRPHSRPYMAHLEITTERGFtatCGGFLITRQFVLTAAHC--SGREITVTLGAHDVSKTESTQQKIKVEKQIVH 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHF---CGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406   99 PKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPtSDILREVKLRIMDKEACKNYW 178
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114205406  179 -HYDYNLQVCVGSprKKRSAYKGDSGGPLLCAGV-AHGIVSYGRGDAKP--PAVFTRISSYVPWI 239
Cdd:pfam00089 157 gGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-245 1.97e-61

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 193.71  E-value: 1.97e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406  13 PSGAGAEEIIGGVESRPHSRPYMAHLeITTERGFTATCGGFLITRQFVLTAAHC----SGREITVTLGAHDvsKTESTQQ 88
Cdd:COG5640   23 PAADAAPAIVGGTPATVGEYPWMVAL-QSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTD--LSTSGGT 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406  89 KIKVEKQIVHPKYNFYSNLHDIMLLKLqkkAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEP-TSDILREVKLR 167
Cdd:COG5640  100 VVKVARIVVHPDYDPATPGNDIALLKL---ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGsQSGTLRKADVP 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406 168 IMDKEACKNYWHYDYNLQVCVGSPRKKRSAYKGDSGGPLL----CAGVAHGIVSYGRGDAKP--PAVFTRISSYVPWINR 241
Cdd:COG5640  177 VVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAgyPGVYTRVSAYRDWIKS 256

                 ....
gi 114205406 242 VIKG 245
Cdd:COG5640  257 TAGG 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 1.79e-93

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: 274.15  E-value: 1.79e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406  21 IIGGVESRPHSRPYMAHLEITTERGFtatCGGFLITRQFVLTAAHC----SGREITVTLGAHDVSKTESTQQKIKVEKQI 96
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHF---CGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406  97 VHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPTSDILREVKLRIMDKEACKN 176
Cdd:cd00190   78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114205406 177 YWHYDYNL---QVCVGSPRKKRSAYKGDSGGPLLC----AGVAHGIVSYGRGDAKP--PAVFTRISSYVPWINRV 242
Cdd:cd00190  158 AYSYGGTItdnMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-239 1.29e-86

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: 256.45  E-value: 1.29e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406    20 EIIGGVESRPHSRPYMAHLEItteRGFTATCGGFLITRQFVLTAAHC----SGREITVTLGAHDVSKTEStQQKIKVEKQ 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEE-GQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406    96 IVHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPT-SDILREVKLRIMDKEAC 174
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114205406   175 KNYWHYDYNL---QVCVGSPRKKRSAYKGDSGGPLLC---AGVAHGIVSYGRGDAKP--PAVFTRISSYVPWI 239
Cdd:smart00020 157 RRAYSGGGAItdnMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-239 9.71e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 218.47  E-value: 9.71e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406   21 IIGGVESRPHSRPYMAHLEITTERGFtatCGGFLITRQFVLTAAHC--SGREITVTLGAHDVSKTESTQQKIKVEKQIVH 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHF---CGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406   99 PKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPtSDILREVKLRIMDKEACKNYW 178
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114205406  179 -HYDYNLQVCVGSprKKRSAYKGDSGGPLLCAGV-AHGIVSYGRGDAKP--PAVFTRISSYVPWI 239
Cdd:pfam00089 157 gGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-245 1.97e-61

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 193.71  E-value: 1.97e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406  13 PSGAGAEEIIGGVESRPHSRPYMAHLeITTERGFTATCGGFLITRQFVLTAAHC----SGREITVTLGAHDvsKTESTQQ 88
Cdd:COG5640   23 PAADAAPAIVGGTPATVGEYPWMVAL-QSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTD--LSTSGGT 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406  89 KIKVEKQIVHPKYNFYSNLHDIMLLKLqkkAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEP-TSDILREVKLR 167
Cdd:COG5640  100 VVKVARIVVHPDYDPATPGNDIALLKL---ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGsQSGTLRKADVP 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406 168 IMDKEACKNYWHYDYNLQVCVGSPRKKRSAYKGDSGGPLL----CAGVAHGIVSYGRGDAKP--PAVFTRISSYVPWINR 241
Cdd:COG5640  177 VVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAgyPGVYTRVSAYRDWIKS 256

                 ....
gi 114205406 242 VIKG 245
Cdd:COG5640  257 TAGG 260
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
36-222 8.41e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 45.05  E-value: 8.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406  36 AHLEITTERGFtatCGGFLITRQFVLTAAHC-----SGR---EITVTLGAHDvskteSTQQKIKVEKQIVHPKYNFYSNL 107
Cdd:COG3591    3 GRLETDGGGGV---CTGTLIGPNLVLTAGHCvydgaGGGwatNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGDA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114205406 108 -HDIMLLKLqkkaKETPSVNVIPLP-RPSDFIKPGKMCRAAGWGRTGVTEPTsdilREVKLRIMDKEAckNYWHYDynlq 185
Cdd:COG3591   75 gYDYALLRL----DEPLGDTTGWLGlAFNDAPLAGEPVTIIGYPGDRPKDLS----LDCSGRVTGVQG--NRLSYD---- 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 114205406 186 vCVGSPrkkrsaykGDSGGPLL----CAGVAHGIVSYGRGD 222
Cdd:COG3591  141 -CDTTG--------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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