NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1371981911|ref|NP_001348566|]
View 

mast cell protease 10 isoform 2 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
13-186 4.10e-61

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: 189.79  E-value: 4.10e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911  13 GRMTVTLGAHNVRKRECTQQKIKVEKYILPPNYNVSSKFNDIVLLKLKKQANLTSAVDVVPLPAPSDFAKPGTMCWAAGW 92
Cdd:cd00190    50 SNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGW 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911  93 GRTGLKKSISRTLREVELRIMGKKACK---IFKHYKDSLQICVGSSTKVASVYMGDSGGPLLC----AGVAHGIVSSGRG 165
Cdd:cd00190   130 GRTSEGGPLPDVLQEVNVPIVSNAECKraySYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSG 209
                         170       180
                  ....*....|....*....|...
gi 1371981911 166 NAKP--PAIFTRISPHVPWINRV 186
Cdd:cd00190   210 CARPnyPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
13-186 4.10e-61

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: 189.79  E-value: 4.10e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911  13 GRMTVTLGAHNVRKRECTQQKIKVEKYILPPNYNVSSKFNDIVLLKLKKQANLTSAVDVVPLPAPSDFAKPGTMCWAAGW 92
Cdd:cd00190    50 SNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGW 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911  93 GRTGLKKSISRTLREVELRIMGKKACK---IFKHYKDSLQICVGSSTKVASVYMGDSGGPLLC----AGVAHGIVSSGRG 165
Cdd:cd00190   130 GRTSEGGPLPDVLQEVNVPIVSNAECKraySYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSG 209
                         170       180
                  ....*....|....*....|...
gi 1371981911 166 NAKP--PAIFTRISPHVPWINRV 186
Cdd:cd00190   210 CARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
13-183 2.55e-55

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: 174.79  E-value: 2.55e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911   13 GRMTVTLGAHNVRKREcTQQKIKVEKYILPPNYNVSSKFNDIVLLKLKKQANLTSAVDVVPLPAPSDFAKPGTMCWAAGW 92
Cdd:smart00020  51 SNIRVRLGSHDLSSGE-EGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGW 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911   93 GRTGL-KKSISRTLREVELRIMGKKACKifKHYK-----DSLQICVGSSTKVASVYMGDSGGPLLC---AGVAHGIVSSG 163
Cdd:smart00020 130 GRTSEgAGSLPDTLQEVNVPIVSNATCR--RAYSgggaiTDNMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWG 207
                          170       180
                   ....*....|....*....|..
gi 1371981911  164 RGNAKP--PAIFTRISPHVPWI 183
Cdd:smart00020 208 SGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
13-183 8.42e-46

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 150.29  E-value: 8.42e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911  13 GRMTVTLGAHNVRKRECTQQKIKVEKYILPPNYNVSSKFNDIVLLKLKKQANLTSAVDVVPLPAPSDFAKPGTMCWAAGW 92
Cdd:pfam00089  48 SDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGW 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911  93 GRTGLKKSiSRTLREVELRIMGKKACKifKHYKDSL---QICVGSSTKvaSVYMGDSGGPLLCAGV-AHGIVSSGRGNAK 168
Cdd:pfam00089 128 GNTKTLGP-SDTLQEVTVPVVSRETCR--SAYGGTVtdtMICAGAGGK--DACQGDSGGPLVCSDGeLIGIVSWGYGCAS 202
                         170
                  ....*....|....*..
gi 1371981911 169 P--PAIFTRISPHVPWI 183
Cdd:pfam00089 203 GnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-187 9.02e-35

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 123.22  E-value: 9.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911  13 GRMTVTLGAHNVRKREctQQKIKVEKYILPPNYNVSSKFNDIVLLKLKKQANLTSAvdvVPLPAPSDFAKPGTMCWAAGW 92
Cdd:COG5640    82 SDLRVVIGSTDLSTSG--GTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAP---APLATSADAAAPGTPATVAGW 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911  93 GRTGLKK-SISRTLREVELRIMGKKACKIFKHYKDSLQICVGSSTKVASVYMGDSGGPLL----CAGVAHGIVSSGRGNA 167
Cdd:COG5640   157 GRTSEGPgSQSGTLRKADVPVVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPC 236
                         170       180
                  ....*....|....*....|..
gi 1371981911 168 KP--PAIFTRISPHVPWINRVI 187
Cdd:COG5640   237 AAgyPGVYTRVSAYRDWIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
13-186 4.10e-61

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: 189.79  E-value: 4.10e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911  13 GRMTVTLGAHNVRKRECTQQKIKVEKYILPPNYNVSSKFNDIVLLKLKKQANLTSAVDVVPLPAPSDFAKPGTMCWAAGW 92
Cdd:cd00190    50 SNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGW 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911  93 GRTGLKKSISRTLREVELRIMGKKACK---IFKHYKDSLQICVGSSTKVASVYMGDSGGPLLC----AGVAHGIVSSGRG 165
Cdd:cd00190   130 GRTSEGGPLPDVLQEVNVPIVSNAECKraySYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSG 209
                         170       180
                  ....*....|....*....|...
gi 1371981911 166 NAKP--PAIFTRISPHVPWINRV 186
Cdd:cd00190   210 CARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
13-183 2.55e-55

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: 174.79  E-value: 2.55e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911   13 GRMTVTLGAHNVRKREcTQQKIKVEKYILPPNYNVSSKFNDIVLLKLKKQANLTSAVDVVPLPAPSDFAKPGTMCWAAGW 92
Cdd:smart00020  51 SNIRVRLGSHDLSSGE-EGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGW 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911   93 GRTGL-KKSISRTLREVELRIMGKKACKifKHYK-----DSLQICVGSSTKVASVYMGDSGGPLLC---AGVAHGIVSSG 163
Cdd:smart00020 130 GRTSEgAGSLPDTLQEVNVPIVSNATCR--RAYSgggaiTDNMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWG 207
                          170       180
                   ....*....|....*....|..
gi 1371981911  164 RGNAKP--PAIFTRISPHVPWI 183
Cdd:smart00020 208 SGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
13-183 8.42e-46

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 150.29  E-value: 8.42e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911  13 GRMTVTLGAHNVRKRECTQQKIKVEKYILPPNYNVSSKFNDIVLLKLKKQANLTSAVDVVPLPAPSDFAKPGTMCWAAGW 92
Cdd:pfam00089  48 SDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGW 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911  93 GRTGLKKSiSRTLREVELRIMGKKACKifKHYKDSL---QICVGSSTKvaSVYMGDSGGPLLCAGV-AHGIVSSGRGNAK 168
Cdd:pfam00089 128 GNTKTLGP-SDTLQEVTVPVVSRETCR--SAYGGTVtdtMICAGAGGK--DACQGDSGGPLVCSDGeLIGIVSWGYGCAS 202
                         170
                  ....*....|....*..
gi 1371981911 169 P--PAIFTRISPHVPWI 183
Cdd:pfam00089 203 GnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-187 9.02e-35

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 123.22  E-value: 9.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911  13 GRMTVTLGAHNVRKREctQQKIKVEKYILPPNYNVSSKFNDIVLLKLKKQANLTSAvdvVPLPAPSDFAKPGTMCWAAGW 92
Cdd:COG5640    82 SDLRVVIGSTDLSTSG--GTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAP---APLATSADAAAPGTPATVAGW 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911  93 GRTGLKK-SISRTLREVELRIMGKKACKIFKHYKDSLQICVGSSTKVASVYMGDSGGPLL----CAGVAHGIVSSGRGNA 167
Cdd:COG5640   157 GRTSEGPgSQSGTLRKADVPVVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPC 236
                         170       180
                  ....*....|....*....|..
gi 1371981911 168 KP--PAIFTRISPHVPWINRVI 187
Cdd:COG5640   237 AAgyPGVYTRVSAYRDWIKSTA 258
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
53-151 3.32e-03

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 36.25  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371981911  53 DIVLLKLKKQANltsAVDVVPLpAPSDFAKPGTMCWAAGWGRTGLKKSISRTlrevelRIMGKKACKIFKHYKDSLQICv 132
Cdd:pfam13365  52 DLALLRVSGDGR---GLPPLPL-GDSEPLVGGERVYAVGYPLGGEKLSLSEG------IVSGVDEGRDGGDDGRVIQTD- 120
                          90
                  ....*....|....*....
gi 1371981911 133 gsstkvASVYMGDSGGPLL 151
Cdd:pfam13365 121 ------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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH