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Conserved domains on  [gi|755547931|ref|XP_011243282|]
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mast cell protease 2 isoform X1 [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 ...
53-179 1.53e-44

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: 147.04  E-value: 1.53e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755547931  53 ELQKKAELNSDVDVISLPSSSDFIKPGKMCWTAGWGKTGKNNPLSVTLREVELRIMDQEACKDHSDYDYQL---QVCAGS 129
Cdd:cd00190   95 KLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYSYGGTItdnMLCAGG 174
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755547931 130 PTTSKSIGQGDSGGPLVCDS----VAHGIASSYE----AKAPAVFTRISYYLPWIYKV 179
Cdd:cd00190  175 LEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSgcarPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
53-179 1.53e-44

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: 147.04  E-value: 1.53e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755547931  53 ELQKKAELNSDVDVISLPSSSDFIKPGKMCWTAGWGKTGKNNPLSVTLREVELRIMDQEACKDHSDYDYQL---QVCAGS 129
Cdd:cd00190   95 KLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYSYGGTItdnMLCAGG 174
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755547931 130 PTTSKSIGQGDSGGPLVCDS----VAHGIASSYE----AKAPAVFTRISYYLPWIYKV 179
Cdd:cd00190  175 LEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSgcarPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
53-176 1.65e-41

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: 139.35  E-value: 1.65e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755547931    53 ELQKKAELNSDVDVISLPSSSDFIKPGKMCWTAGWGKTGKNNP-LSVTLREVELRIMDQEACKDHSDYDYQL---QVCAG 128
Cdd:smart00020  95 KLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGsLPDTLQEVNVPIVSNATCRRAYSGGGAItdnMLCAG 174
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 755547931   129 SPTTSKSIGQGDSGGPLVCDS---VAHGIASSYE----AKAPAVFTRISYYLPWI 176
Cdd:smart00020 175 GLEGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSgcarPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
54-176 1.02e-28

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 105.99  E-value: 1.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755547931   54 LQKKAELNSDVDVISLPSSSDFIKPGKMCWTAGWGKTGKNNPlSVTLREVELRIMDQEACK-DHSDYDYQLQVCAGspTT 132
Cdd:pfam00089  94 LESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRsAYGGTVTDTMICAG--AG 170
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 755547931  133 SKSIGQGDSGGPLVCDSV-AHGIASSYEAKA----PAVFTRISYYLPWI 176
Cdd:pfam00089 171 GKDACQGDSGGPLVCSDGeLIGIVSWGYGCAsgnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
59-182 1.08e-25

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 99.34  E-value: 1.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755547931  59 ELNSDVD---VISLPSSSDFIKPGKMCWTAGWGKTGKNNP-LSVTLREVELRIMDQEACKDHSDYDYQLQVCAGSPTTSK 134
Cdd:COG5640  125 KLATPVPgvaPAPLATSADAAAPGTPATVAGWGRTSEGPGsQSGTLRKADVPVVSDATCAAYGGFDGGTMLCAGYPEGGK 204
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755547931 135 SIGQGDSGGPLVCDS----VAHGIAS----SYEAKAPAVFTRISYYLPWIYKVLKS 182
Cdd:COG5640  205 DACQGDSGGPLVVKDgggwVLVGVVSwgggPCAAGYPGVYTRVSAYRDWIKSTAGG 260
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
53-179 1.53e-44

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: 147.04  E-value: 1.53e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755547931  53 ELQKKAELNSDVDVISLPSSSDFIKPGKMCWTAGWGKTGKNNPLSVTLREVELRIMDQEACKDHSDYDYQL---QVCAGS 129
Cdd:cd00190   95 KLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYSYGGTItdnMLCAGG 174
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755547931 130 PTTSKSIGQGDSGGPLVCDS----VAHGIASSYE----AKAPAVFTRISYYLPWIYKV 179
Cdd:cd00190  175 LEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSgcarPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
53-176 1.65e-41

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: 139.35  E-value: 1.65e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755547931    53 ELQKKAELNSDVDVISLPSSSDFIKPGKMCWTAGWGKTGKNNP-LSVTLREVELRIMDQEACKDHSDYDYQL---QVCAG 128
Cdd:smart00020  95 KLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGsLPDTLQEVNVPIVSNATCRRAYSGGGAItdnMLCAG 174
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 755547931   129 SPTTSKSIGQGDSGGPLVCDS---VAHGIASSYE----AKAPAVFTRISYYLPWI 176
Cdd:smart00020 175 GLEGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSgcarPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
54-176 1.02e-28

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 105.99  E-value: 1.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755547931   54 LQKKAELNSDVDVISLPSSSDFIKPGKMCWTAGWGKTGKNNPlSVTLREVELRIMDQEACK-DHSDYDYQLQVCAGspTT 132
Cdd:pfam00089  94 LESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRsAYGGTVTDTMICAG--AG 170
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 755547931  133 SKSIGQGDSGGPLVCDSV-AHGIASSYEAKA----PAVFTRISYYLPWI 176
Cdd:pfam00089 171 GKDACQGDSGGPLVCSDGeLIGIVSWGYGCAsgnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
59-182 1.08e-25

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 99.34  E-value: 1.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755547931  59 ELNSDVD---VISLPSSSDFIKPGKMCWTAGWGKTGKNNP-LSVTLREVELRIMDQEACKDHSDYDYQLQVCAGSPTTSK 134
Cdd:COG5640  125 KLATPVPgvaPAPLATSADAAAPGTPATVAGWGRTSEGPGsQSGTLRKADVPVVSDATCAAYGGFDGGTMLCAGYPEGGK 204
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755547931 135 SIGQGDSGGPLVCDS----VAHGIAS----SYEAKAPAVFTRISYYLPWIYKVLKS 182
Cdd:COG5640  205 DACQGDSGGPLVVKDgggwVLVGVVSwgggPCAAGYPGVYTRVSAYRDWIKSTAGG 260
 
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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