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Conserved domains on  [gi|2289229208|ref|NP_001398261|]
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tryptase gamma 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

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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 ...
14-157 2.00e-64

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: 198.65  E-value: 2.00e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289229208  14 DIALVQLSSPVALSSQVQPVCLPEASADFYPGMQCWVTGWGYTGEGEPLkpPYNLQEAKVSVVDVKTCSQAYnsPNGSLI 93
Cdd:cd00190    90 DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNAECKRAY--SYGGTI 165
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2289229208  94 QPDMLCARGPG---DACQDDSGGPLVCQVAGTWQQAGVVSWGEGCGRPDRPGVYARVTAYVNWIHHH 157
Cdd:cd00190   166 TDNMLCAGGLEggkDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
14-157 2.00e-64

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: 198.65  E-value: 2.00e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289229208  14 DIALVQLSSPVALSSQVQPVCLPEASADFYPGMQCWVTGWGYTGEGEPLkpPYNLQEAKVSVVDVKTCSQAYnsPNGSLI 93
Cdd:cd00190    90 DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNAECKRAY--SYGGTI 165
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2289229208  94 QPDMLCARGPG---DACQDDSGGPLVCQVAGTWQQAGVVSWGEGCGRPDRPGVYARVTAYVNWIHHH 157
Cdd:cd00190   166 TDNMLCAGGLEggkDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
14-154 1.29e-60

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: 189.04  E-value: 1.29e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289229208   14 DIALVQLSSPVALSSQVQPVCLPEASADFYPGMQCWVTGWGYTGEGEPlKPPYNLQEAKVSVVDVKTCSQAYnsPNGSLI 93
Cdd:smart00020  90 DIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNATCRRAY--SGGGAI 166
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2289229208   94 QPDMLCARGPG---DACQDDSGGPLVCQVaGTWQQAGVVSWGEGCGRPDRPGVYARVTAYVNWI 154
Cdd:smart00020 167 TDNMLCAGGLEggkDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
14-154 1.05e-46

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 153.37  E-value: 1.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289229208  14 DIALVQLSSPVALSSQVQPVCLPEASADFYPGMQCWVTGWGYTGEgepLKPPYNLQEAKVSVVDVKTCSQAYNSPngslI 93
Cdd:pfam00089  88 DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKT---LGPSDTLQEVTVPVVSRETCRSAYGGT----V 160
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2289229208  94 QPDMLCARGPG-DACQDDSGGPLVCqvaGTWQQAGVVSWGEGCGRPDRPGVYARVTAYVNWI 154
Cdd:pfam00089 161 TDTMICAGAGGkDACQGDSGGPLVC---SDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
14-162 5.66e-39

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 134.78  E-value: 5.66e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289229208  14 DIALVQLSSPValsSQVQPVCLPEASADFYPGMQCWVTGWGYTGEGEPLKPPYnLQEAKVSVVDVKTCsQAYNSPNGSli 93
Cdd:COG5640   120 DIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGT-LRKADVPVVSDATC-AAYGGFDGG-- 192
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2289229208  94 qpDMLCA---RGPGDACQDDSGGPLVCQVAGTWQQAGVVSWGEGCGRPDRPGVYARVTAYVNWIHHHIPEAG 162
Cdd:COG5640   193 --TMLCAgypEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
14-157 2.00e-64

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: 198.65  E-value: 2.00e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289229208  14 DIALVQLSSPVALSSQVQPVCLPEASADFYPGMQCWVTGWGYTGEGEPLkpPYNLQEAKVSVVDVKTCSQAYnsPNGSLI 93
Cdd:cd00190    90 DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPL--PDVLQEVNVPIVSNAECKRAY--SYGGTI 165
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2289229208  94 QPDMLCARGPG---DACQDDSGGPLVCQVAGTWQQAGVVSWGEGCGRPDRPGVYARVTAYVNWIHHH 157
Cdd:cd00190   166 TDNMLCAGGLEggkDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
14-154 1.29e-60

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: 189.04  E-value: 1.29e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289229208   14 DIALVQLSSPVALSSQVQPVCLPEASADFYPGMQCWVTGWGYTGEGEPlKPPYNLQEAKVSVVDVKTCSQAYnsPNGSLI 93
Cdd:smart00020  90 DIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAG-SLPDTLQEVNVPIVSNATCRRAY--SGGGAI 166
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2289229208   94 QPDMLCARGPG---DACQDDSGGPLVCQVaGTWQQAGVVSWGEGCGRPDRPGVYARVTAYVNWI 154
Cdd:smart00020 167 TDNMLCAGGLEggkDACQGDSGGPLVCND-GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
14-154 1.05e-46

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 153.37  E-value: 1.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289229208  14 DIALVQLSSPVALSSQVQPVCLPEASADFYPGMQCWVTGWGYTGEgepLKPPYNLQEAKVSVVDVKTCSQAYNSPngslI 93
Cdd:pfam00089  88 DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKT---LGPSDTLQEVTVPVVSRETCRSAYGGT----V 160
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2289229208  94 QPDMLCARGPG-DACQDDSGGPLVCqvaGTWQQAGVVSWGEGCGRPDRPGVYARVTAYVNWI 154
Cdd:pfam00089 161 TDTMICAGAGGkDACQGDSGGPLVC---SDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
14-162 5.66e-39

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 134.78  E-value: 5.66e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289229208  14 DIALVQLSSPValsSQVQPVCLPEASADFYPGMQCWVTGWGYTGEGEPLKPPYnLQEAKVSVVDVKTCsQAYNSPNGSli 93
Cdd:COG5640   120 DIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGT-LRKADVPVVSDATC-AAYGGFDGG-- 192
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2289229208  94 qpDMLCA---RGPGDACQDDSGGPLVCQVAGTWQQAGVVSWGEGCGRPDRPGVYARVTAYVNWIHHHIPEAG 162
Cdd:COG5640   193 --TMLCAgypEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 262
 
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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