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Conserved domains on  [gi|200513|gb|AAA39989|]
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mast cell protease-4 [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 9.90e-94

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: 274.92  E-value: 9.90e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513    21 IIGGVESRPHSRPYMAHLEITTERGFtatCGGFLITRQFVMTAAHC----SGREITVTLGAHDVSKTESTQQKIKVEKQI 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHF---CGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513    97 VHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPTSDTLREVKLRIMDKEACKN 176
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 200513   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 9.90e-94

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: 274.92  E-value: 9.90e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513    21 IIGGVESRPHSRPYMAHLEITTERGFtatCGGFLITRQFVMTAAHC----SGREITVTLGAHDVSKTESTQQKIKVEKQI 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHF---CGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513    97 VHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPTSDTLREVKLRIMDKEACKN 176
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 200513   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 6.72e-87

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: 257.22  E-value: 6.72e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513       20 EIIGGVESRPHSRPYMAHLEItteRGFTATCGGFLITRQFVMTAAHC----SGREITVTLGAHDVSKTEStQQKIKVEKQ 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEE-GQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513       96 IVHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPT-SDTLREVKLRIMDKEAC 174
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 200513      175 KNYWHYDYNL---QVCVGSPRKKRSAYKGDSGGPLLC---AGVAHGIVSYGRGDAKP--PAVFTRISSYVPWI 239
Cdd:smart00020 157 RRAYSGGGAItdnMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-239 7.56e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 218.85  E-value: 7.56e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513      21 IIGGVESRPHSRPYMAHLEITTERGFtatCGGFLITRQFVMTAAHC--SGREITVTLGAHDVSKTESTQQKIKVEKQIVH 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHF---CGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513      99 PKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPtSDTLREVKLRIMDKEACKNYW 178
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 200513     179 -HYDYNLQVCVGSprKKRSAYKGDSGGPLLCAGV-AHGIVSYGRGDAKP--PAVFTRISSYVPWI 239
Cdd:pfam00089 157 gGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-245 1.31e-60

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 191.40  E-value: 1.31e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513    13 PSGAGAEEIIGGVESRPHSRPYMAHLeITTERGFTATCGGFLITRQFVMTAAHC----SGREITVTLGAHDvsKTESTQQ 88
Cdd:COG5640  23 PAADAAPAIVGGTPATVGEYPWMVAL-QSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTD--LSTSGGT 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513    89 KIKVEKQIVHPKYNFYSNLHDIMLLKLqkkAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEP-TSDTLREVKLR 167
Cdd:COG5640 100 VVKVARIVVHPDYDPATPGNDIALLKL---ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGsQSGTLRKADVP 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513   168 IMDKEACKNYWHYDYNLQVCVGSPRKKRSAYKGDSGGPLL----CAGVAHGIVSYGRGDAKP--PAVFTRISSYVPWINR 241
Cdd:COG5640 177 VVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAgyPGVYTRVSAYRDWIKS 256

                ....
gi 200513   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 9.90e-94

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: 274.92  E-value: 9.90e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513    21 IIGGVESRPHSRPYMAHLEITTERGFtatCGGFLITRQFVMTAAHC----SGREITVTLGAHDVSKTESTQQKIKVEKQI 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHF---CGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513    97 VHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPTSDTLREVKLRIMDKEACKN 176
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 200513   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 6.72e-87

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: 257.22  E-value: 6.72e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513       20 EIIGGVESRPHSRPYMAHLEItteRGFTATCGGFLITRQFVMTAAHC----SGREITVTLGAHDVSKTEStQQKIKVEKQ 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEE-GQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513       96 IVHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPT-SDTLREVKLRIMDKEAC 174
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 200513      175 KNYWHYDYNL---QVCVGSPRKKRSAYKGDSGGPLLC---AGVAHGIVSYGRGDAKP--PAVFTRISSYVPWI 239
Cdd:smart00020 157 RRAYSGGGAItdnMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-239 7.56e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 218.85  E-value: 7.56e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513      21 IIGGVESRPHSRPYMAHLEITTERGFtatCGGFLITRQFVMTAAHC--SGREITVTLGAHDVSKTESTQQKIKVEKQIVH 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHF---CGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513      99 PKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPtSDTLREVKLRIMDKEACKNYW 178
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 200513     179 -HYDYNLQVCVGSprKKRSAYKGDSGGPLLCAGV-AHGIVSYGRGDAKP--PAVFTRISSYVPWI 239
Cdd:pfam00089 157 gGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-245 1.31e-60

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 191.40  E-value: 1.31e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513    13 PSGAGAEEIIGGVESRPHSRPYMAHLeITTERGFTATCGGFLITRQFVMTAAHC----SGREITVTLGAHDvsKTESTQQ 88
Cdd:COG5640  23 PAADAAPAIVGGTPATVGEYPWMVAL-QSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTD--LSTSGGT 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513    89 KIKVEKQIVHPKYNFYSNLHDIMLLKLqkkAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEP-TSDTLREVKLR 167
Cdd:COG5640 100 VVKVARIVVHPDYDPATPGNDIALLKL---ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGsQSGTLRKADVP 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513   168 IMDKEACKNYWHYDYNLQVCVGSPRKKRSAYKGDSGGPLL----CAGVAHGIVSYGRGDAKP--PAVFTRISSYVPWINR 241
Cdd:COG5640 177 VVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAgyPGVYTRVSAYRDWIKS 256

                ....
gi 200513   242 VIKG 245
Cdd:COG5640 257 TAGG 260
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
36-222 4.53e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 45.82  E-value: 4.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513    36 AHLEITTERGFtatCGGFLITRQFVMTAAHC-----SGR---EITVTLGAHDvskteSTQQKIKVEKQIVHPKYNFYSNL 107
Cdd:COG3591   3 GRLETDGGGGV---CTGTLIGPNLVLTAGHCvydgaGGGwatNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGDA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 200513   108 -HDIMLLKLqkkaKETPSVNVIPLP-RPSDFIKPGKMCRAAGWGRtgvTEPTSDTLREVKlRIMDKEAckNYWHYDynlq 185
Cdd:COG3591  75 gYDYALLRL----DEPLGDTTGWLGlAFNDAPLAGEPVTIIGYPG---DRPKDLSLDCSG-RVTGVQG--NRLSYD---- 140
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 200513   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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