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Conserved domains on  [gi|1840526823|ref|NP_031369|]
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trypsin-3 isoform 1 preproprotein [Homo sapiens]

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 ...
1-134 8.44e-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: 186.71  E-value: 8.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840526823   1 MLIKLSSPAVINARVSTISLPTT--PPAAGTECLISGWGNTlSFGADYPDELKCLDAPVLTQAECKASY--PGKITNSMF 76
Cdd:cd00190    92 ALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAECKRAYsyGGTITDNML 170
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1840526823  77 CVGFLEGGKDSCQRDSGGPVVCN----GQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDT 134
Cdd:cd00190   171 CAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-134 8.44e-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: 186.71  E-value: 8.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840526823   1 MLIKLSSPAVINARVSTISLPTT--PPAAGTECLISGWGNTlSFGADYPDELKCLDAPVLTQAECKASY--PGKITNSMF 76
Cdd:cd00190    92 ALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAECKRAYsyGGTITDNML 170
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1840526823  77 CVGFLEGGKDSCQRDSGGPVVCN----GQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDT 134
Cdd:cd00190   171 CAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-131 7.53e-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: 184.03  E-value: 7.53e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840526823    1 MLIKLSSPAVINARVSTISLPTT--PPAAGTECLISGWGNTLSFGADYPDELKCLDAPVLTQAECKASYPG--KITNSMF 76
Cdd:smart00020  92 ALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGggAITDNML 171
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1840526823   77 CVGFLEGGKDSCQRDSGGPVVCN---GQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWI 131
Cdd:smart00020 172 CAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-131 1.47e-46

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 149.90  E-value: 1.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840526823   1 MLIKLSSPAVINARVSTISLPTT--PPAAGTECLISGWGNTLSFGadYPDELKCLDAPVLTQAECKASYPGKITNSMFCV 78
Cdd:pfam00089  90 ALLKLESPVTLGDTVRPICLPDAssDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAYGGTVTDTMICA 167
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1840526823  79 GFleGGKDSCQRDSGGPVVCNGQ-LQGVVSWGHGCAWKNRPGVYTKVYNYVDWI 131
Cdd:pfam00089 168 GA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
2-139 2.14e-38

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 130.54  E-value: 2.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840526823   2 LIKLSSPAvinARVSTISLPTTP--PAAGTECLISGWGNTLSFGADYPDELKCLDAPVLTQAECKAsYPGKITNSMFCVG 79
Cdd:COG5640   123 LLKLATPV---PGVAPAPLATSAdaAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATCAA-YGGFDGGTMLCAG 198
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1840526823  80 FLEGGKDSCQRDSGGPVV----CNGQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDTIAANS 139
Cdd:COG5640   199 YPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-134 8.44e-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: 186.71  E-value: 8.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840526823   1 MLIKLSSPAVINARVSTISLPTT--PPAAGTECLISGWGNTlSFGADYPDELKCLDAPVLTQAECKASY--PGKITNSMF 76
Cdd:cd00190    92 ALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAECKRAYsyGGTITDNML 170
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1840526823  77 CVGFLEGGKDSCQRDSGGPVVCN----GQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDT 134
Cdd:cd00190   171 CAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-131 7.53e-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: 184.03  E-value: 7.53e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840526823    1 MLIKLSSPAVINARVSTISLPTT--PPAAGTECLISGWGNTLSFGADYPDELKCLDAPVLTQAECKASYPG--KITNSMF 76
Cdd:smart00020  92 ALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGggAITDNML 171
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1840526823   77 CVGFLEGGKDSCQRDSGGPVVCN---GQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWI 131
Cdd:smart00020 172 CAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-131 1.47e-46

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 149.90  E-value: 1.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840526823   1 MLIKLSSPAVINARVSTISLPTT--PPAAGTECLISGWGNTLSFGadYPDELKCLDAPVLTQAECKASYPGKITNSMFCV 78
Cdd:pfam00089  90 ALLKLESPVTLGDTVRPICLPDAssDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAYGGTVTDTMICA 167
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1840526823  79 GFleGGKDSCQRDSGGPVVCNGQ-LQGVVSWGHGCAWKNRPGVYTKVYNYVDWI 131
Cdd:pfam00089 168 GA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
2-139 2.14e-38

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 130.54  E-value: 2.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840526823   2 LIKLSSPAvinARVSTISLPTTP--PAAGTECLISGWGNTLSFGADYPDELKCLDAPVLTQAECKAsYPGKITNSMFCVG 79
Cdd:COG5640   123 LLKLATPV---PGVAPAPLATSAdaAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATCAA-YGGFDGGTMLCAG 198
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1840526823  80 FLEGGKDSCQRDSGGPVV----CNGQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDTIAANS 139
Cdd:COG5640   199 YPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 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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