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Conserved domains on  [gi|307568208|pdb|3L33|B]
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Chain B, Trypsin-3

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 ...
1-219 1.76e-106

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: 306.13  E-value: 1.76e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B        1 IVGGYTCEENSLPYQVSL--NSGSHFCGGSLISEQWVVSAAHC----YKTRIQVRLGEHNIKVLEGNEQFINAAKIIRHP 74
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B       75 KYNRDTLDNDIMLIKLSSPAVINARVSTISLPT--APPAAGTECLISGWGNTlSFGADYPDELKCLDAPVLTQAECKASY 152
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3L33_B      153 --PGKITNSMFCVGFLEGGKDSCQRDAGGPVVCN----GQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDT 219
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 ...
1-219 1.76e-106

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: 306.13  E-value: 1.76e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B        1 IVGGYTCEENSLPYQVSL--NSGSHFCGGSLISEQWVVSAAHC----YKTRIQVRLGEHNIKVLEGNEQFINAAKIIRHP 74
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B       75 KYNRDTLDNDIMLIKLSSPAVINARVSTISLPT--APPAAGTECLISGWGNTlSFGADYPDELKCLDAPVLTQAECKASY 152
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3L33_B      153 --PGKITNSMFCVGFLEGGKDSCQRDAGGPVVCN----GQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDT 219
Cdd:cd00190 160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-216 1.36e-103

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: 298.82  E-value: 1.36e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B           1 IVGGYTCEENSLPYQVSL--NSGSHFCGGSLISEQWVVSAAHC----YKTRIQVRLGEHNIKVlEGNEQFINAAKIIRHP 74
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLqyGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSS-GEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B          75 KYNRDTLDNDIMLIKLSSPAVINARVSTISLPTA--PPAAGTECLISGWGNTLSFGADYPDELKCLDAPVLTQAECKASY 152
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
3L33_B         153 PG--KITNSMFCVGFLEGGKDSCQRDAGGPVVCN---GQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWI 216
Cdd:smart00020 161 SGggAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-216 1.32e-88

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 260.45  E-value: 1.32e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B          1 IVGGYTCEENSLPYQVSLN--SGSHFCGGSLISEQWVVSAAHCYK--TRIQVRLGEHNIKVLEGNEQFINAAKIIRHPKY 76
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlsSGKHFCGGSLISENWVLTAAHCVSgaSDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B         77 NRDTLDNDIMLIKLSSPAVINARVSTISLPTA--PPAAGTECLISGWGNTLSFGadYPDELKCLDAPVLTQAECKASYPG 154
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDAssDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
3L33_B        155 KITNSMFCVGFleGGKDSCQRDAGGPVVCNGQ-LQGVVSWGHGCAWKNRPGVYTKVYNYVDWI 216
Cdd:pfam00089 159 TVTDTMICAGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-224 2.26e-69

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 212.97  E-value: 2.26e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B        1 IVGGYTCEENSLPYQVSLNS----GSHFCGGSLISEQWVVSAAHCY----KTRIQVRLGEHNIKVLEGneQFINAAKIIR 72
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSsngpSGQFCGGTLIAPRWVLTAAHCVdgdgPSDLRVVIGSTDLSTSGG--TVVKVARIVV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B       73 HPKYNRDTLDNDIMLIKLSSPAvinARVSTISLPTAP--PAAGTECLISGWGNTLSFGADYPDELKCLDAPVLTQAECKA 150
Cdd:COG5640 109 HPDYDPATPGNDIALLKLATPV---PGVAPAPLATSAdaAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATCAA 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3L33_B      151 sYPGKITNSMFCVGFLEGGKDSCQRDAGGPVV----CNGQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDTIAANS 224
Cdd:COG5640 186 -YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-219 1.76e-106

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: 306.13  E-value: 1.76e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B        1 IVGGYTCEENSLPYQVSL--NSGSHFCGGSLISEQWVVSAAHC----YKTRIQVRLGEHNIKVLEGNEQFINAAKIIRHP 74
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B       75 KYNRDTLDNDIMLIKLSSPAVINARVSTISLPT--APPAAGTECLISGWGNTlSFGADYPDELKCLDAPVLTQAECKASY 152
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3L33_B      153 --PGKITNSMFCVGFLEGGKDSCQRDAGGPVVCN----GQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDT 219
Cdd:cd00190 160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-216 1.36e-103

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: 298.82  E-value: 1.36e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B           1 IVGGYTCEENSLPYQVSL--NSGSHFCGGSLISEQWVVSAAHC----YKTRIQVRLGEHNIKVlEGNEQFINAAKIIRHP 74
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLqyGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSS-GEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B          75 KYNRDTLDNDIMLIKLSSPAVINARVSTISLPTA--PPAAGTECLISGWGNTLSFGADYPDELKCLDAPVLTQAECKASY 152
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
3L33_B         153 PG--KITNSMFCVGFLEGGKDSCQRDAGGPVVCN---GQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWI 216
Cdd:smart00020 161 SGggAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-216 1.32e-88

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 260.45  E-value: 1.32e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B          1 IVGGYTCEENSLPYQVSLN--SGSHFCGGSLISEQWVVSAAHCYK--TRIQVRLGEHNIKVLEGNEQFINAAKIIRHPKY 76
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlsSGKHFCGGSLISENWVLTAAHCVSgaSDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B         77 NRDTLDNDIMLIKLSSPAVINARVSTISLPTA--PPAAGTECLISGWGNTLSFGadYPDELKCLDAPVLTQAECKASYPG 154
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDAssDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
3L33_B        155 KITNSMFCVGFleGGKDSCQRDAGGPVVCNGQ-LQGVVSWGHGCAWKNRPGVYTKVYNYVDWI 216
Cdd:pfam00089 159 TVTDTMICAGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-224 2.26e-69

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 212.97  E-value: 2.26e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B        1 IVGGYTCEENSLPYQVSLNS----GSHFCGGSLISEQWVVSAAHCY----KTRIQVRLGEHNIKVLEGneQFINAAKIIR 72
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSsngpSGQFCGGTLIAPRWVLTAAHCVdgdgPSDLRVVIGSTDLSTSGG--TVVKVARIVV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B       73 HPKYNRDTLDNDIMLIKLSSPAvinARVSTISLPTAP--PAAGTECLISGWGNTLSFGADYPDELKCLDAPVLTQAECKA 150
Cdd:COG5640 109 HPDYDPATPGNDIALLKLATPV---PGVAPAPLATSAdaAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATCAA 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3L33_B      151 sYPGKITNSMFCVGFLEGGKDSCQRDAGGPVV----CNGQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDTIAANS 224
Cdd:COG5640 186 -YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
15-222 6.74e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 48.13  E-value: 6.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B       15 QVSLNSGSHFCGGSLISEQWVVSAAHC--------YKTRIQVRLGEHNikvleGNEQFINAAKIIRHPKYNRDTLDN-DI 85
Cdd:COG3591   4 RLETDGGGGVCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGDAGyDY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3L33_B       86 MLIKLSSPavINARVSTISL-PTAPPAAGTECLISGwgntlsFGADYPDELKCldapvltQAECKASYPGKITNSMFCvg 164
Cdd:COG3591  79 ALLRLDEP--LGDTTGWLGLaFNDAPLAGEPVTIIG------YPGDRPKDLSL-------DCSGRVTGVQGNRLSYDC-- 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
3L33_B      165 fleggkDSCQRDAGGPVV----CNGQLQGVVSWGhGCAWKNRpGVYTkVYNYVDWIKDTIAA 222
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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