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Conserved domains on  [gi|2217377829|ref|XP_047279558|]
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trypsin-3 isoform X2 [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 ...
24-242 8.92e-109

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: 313.06  E-value: 8.92e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829  24 IVGGYTCEENSLPYQVSL--NSGSHFCGGSLISEQWVVSAAHC----YKTRIQVRLGEHNIKVLEGNEQFINAAKIIRHP 97
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829  98 KYNRDTLDNDIMLIKLSSPAVINARVSTISLPTT--PPAAGTECLISGWGNTlSFGADYPDELKCLDAPVLTQAECKASY 175
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217377829 176 --PGKITNSMFCVGFLEGGKDSCQRDSGGPVVCN----GQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDT 242
Cdd:cd00190   160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
24-242 8.92e-109

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: 313.06  E-value: 8.92e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829  24 IVGGYTCEENSLPYQVSL--NSGSHFCGGSLISEQWVVSAAHC----YKTRIQVRLGEHNIKVLEGNEQFINAAKIIRHP 97
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829  98 KYNRDTLDNDIMLIKLSSPAVINARVSTISLPTT--PPAAGTECLISGWGNTlSFGADYPDELKCLDAPVLTQAECKASY 175
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217377829 176 --PGKITNSMFCVGFLEGGKDSCQRDSGGPVVCN----GQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDT 242
Cdd:cd00190   160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
23-239 4.30e-106

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: 306.14  E-value: 4.30e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829   23 KIVGGYTCEENSLPYQVSL--NSGSHFCGGSLISEQWVVSAAHC----YKTRIQVRLGEHNIKVlEGNEQFINAAKIIRH 96
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqyGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSS-GEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829   97 PKYNRDTLDNDIMLIKLSSPAVINARVSTISLPTT--PPAAGTECLISGWGNTLSFGADYPDELKCLDAPVLTQAECKAS 174
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829  175 YPG--KITNSMFCVGFLEGGKDSCQRDSGGPVVCN---GQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWI 239
Cdd:smart00020 160 YSGggAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
24-239 5.20e-90

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 265.07  E-value: 5.20e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829  24 IVGGYTCEENSLPYQVSLN--SGSHFCGGSLISEQWVVSAAHCYK--TRIQVRLGEHNIKVLEGNEQFINAAKIIRHPKY 99
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlsSGKHFCGGSLISENWVLTAAHCVSgaSDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829 100 NRDTLDNDIMLIKLSSPAVINARVSTISLPTT--PPAAGTECLISGWGNTLSFGadYPDELKCLDAPVLTQAECKASYPG 177
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDAssDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217377829 178 KITNSMFCVGFleGGKDSCQRDSGGPVVCNGQ-LQGVVSWGHGCAWKNRPGVYTKVYNYVDWI 239
Cdd:pfam00089 159 TVTDTMICAGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
5-247 3.19e-73

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 223.76  E-value: 3.19e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829   5 LILAFVGAAVAVPFDDDDKIVGGYTCEENSLPYQVSLNS----GSHFCGGSLISEQWVVSAAHCY----KTRIQVRLGEH 76
Cdd:COG5640    12 AAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSsngpSGQFCGGTLIAPRWVLTAAHCVdgdgPSDLRVVIGST 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829  77 NIKVLEGneQFINAAKIIRHPKYNRDTLDNDIMLIKLSSPAvinARVSTISLPTTP--PAAGTECLISGWGNTLSFGADY 154
Cdd:COG5640    92 DLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSAdaAAPGTPATVAGWGRTSEGPGSQ 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829 155 PDELKCLDAPVLTQAECKAsYPGKITNSMFCVGFLEGGKDSCQRDSGGPVV----CNGQLQGVVSWGHGCAWKNRPGVYT 230
Cdd:COG5640   167 SGTLRKADVPVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYT 245
                         250
                  ....*....|....*..
gi 2217377829 231 KVYNYVDWIKDTIAANS 247
Cdd:COG5640   246 RVSAYRDWIKSTAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
24-242 8.92e-109

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: 313.06  E-value: 8.92e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829  24 IVGGYTCEENSLPYQVSL--NSGSHFCGGSLISEQWVVSAAHC----YKTRIQVRLGEHNIKVLEGNEQFINAAKIIRHP 97
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829  98 KYNRDTLDNDIMLIKLSSPAVINARVSTISLPTT--PPAAGTECLISGWGNTlSFGADYPDELKCLDAPVLTQAECKASY 175
Cdd:cd00190    81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAECKRAY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217377829 176 --PGKITNSMFCVGFLEGGKDSCQRDSGGPVVCN----GQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDT 242
Cdd:cd00190   160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
23-239 4.30e-106

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: 306.14  E-value: 4.30e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829   23 KIVGGYTCEENSLPYQVSL--NSGSHFCGGSLISEQWVVSAAHC----YKTRIQVRLGEHNIKVlEGNEQFINAAKIIRH 96
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqyGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSS-GEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829   97 PKYNRDTLDNDIMLIKLSSPAVINARVSTISLPTT--PPAAGTECLISGWGNTLSFGADYPDELKCLDAPVLTQAECKAS 174
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829  175 YPG--KITNSMFCVGFLEGGKDSCQRDSGGPVVCN---GQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWI 239
Cdd:smart00020 160 YSGggAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
24-239 5.20e-90

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 265.07  E-value: 5.20e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829  24 IVGGYTCEENSLPYQVSLN--SGSHFCGGSLISEQWVVSAAHCYK--TRIQVRLGEHNIKVLEGNEQFINAAKIIRHPKY 99
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlsSGKHFCGGSLISENWVLTAAHCVSgaSDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829 100 NRDTLDNDIMLIKLSSPAVINARVSTISLPTT--PPAAGTECLISGWGNTLSFGadYPDELKCLDAPVLTQAECKASYPG 177
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDAssDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217377829 178 KITNSMFCVGFleGGKDSCQRDSGGPVVCNGQ-LQGVVSWGHGCAWKNRPGVYTKVYNYVDWI 239
Cdd:pfam00089 159 TVTDTMICAGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
5-247 3.19e-73

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 223.76  E-value: 3.19e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829   5 LILAFVGAAVAVPFDDDDKIVGGYTCEENSLPYQVSLNS----GSHFCGGSLISEQWVVSAAHCY----KTRIQVRLGEH 76
Cdd:COG5640    12 AAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSsngpSGQFCGGTLIAPRWVLTAAHCVdgdgPSDLRVVIGST 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829  77 NIKVLEGneQFINAAKIIRHPKYNRDTLDNDIMLIKLSSPAvinARVSTISLPTTP--PAAGTECLISGWGNTLSFGADY 154
Cdd:COG5640    92 DLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSAdaAAPGTPATVAGWGRTSEGPGSQ 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829 155 PDELKCLDAPVLTQAECKAsYPGKITNSMFCVGFLEGGKDSCQRDSGGPVV----CNGQLQGVVSWGHGCAWKNRPGVYT 230
Cdd:COG5640   167 SGTLRKADVPVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYT 245
                         250
                  ....*....|....*..
gi 2217377829 231 KVYNYVDWIKDTIAANS 247
Cdd:COG5640   246 RVSAYRDWIKSTAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
38-245 3.06e-08

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 52.37  E-value: 3.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829  38 QVSLNSGSHFCGGSLISEQWVVSAAHC--------YKTRIQVRLGEHNikvleGNEQFINAAKIIRHPKYNRDTLDN-DI 108
Cdd:COG3591     4 RLETDGGGGVCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGDAGyDY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217377829 109 MLIKLSSPavINARVSTISL-PTTPPAAGTECLISGwgntlsFGADYPDELKCldapvltQAECKASYPGKITNSMFCvg 187
Cdd:COG3591    79 ALLRLDEP--LGDTTGWLGLaFNDAPLAGEPVTIIG------YPGDRPKDLSL-------DCSGRVTGVQGNRLSYDC-- 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217377829 188 fleggkDSCQRDSGGPVV----CNGQLQGVVSWGhGCAWKNRpGVYTkVYNYVDWIKDTIAA 245
Cdd:COG3591   142 ------DTTGGSSGSPVLddsdGGGRVVGVHSAG-GADRANT-GVRL-TSAIVAALRAWASA 194
 
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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