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Conserved domains on  [gi|157834015]
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Protein Classification

serine protease (domain architecture ID 12184331)

trypsin-like serine protease such as snake venom serine proteases and trypsin, which preferentially cleaves peptide bonds after arginine and lysine residues

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-220 2.05e-86

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: 254.91  E-value: 2.05e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015     1 IVGGTSASAGDFPFIVSISRNGGP-WCGGSLLNANTVLTAAHCVSGYAQSGFQIRAGSLSRTSGG--ITSSLSSVRVHPS 77
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEegQVIKVSKVIIHPN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015    78 YSGNN--NDLAILKLSTSIPSGGNIGYARLAASGSDPVAGSSATVAGWGATSEGGSSTPVNLLKVTVPIVSRATCRAQY- 154
Cdd:smart00020  82 YNPSTydNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYs 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157834015   155 GTSAITNQMFCAGVSSGGKDSCQGDSGGPIV--DSSNTLIGAVSWGNGCARPNYSGVYASVGALRSFI 220
Cdd:smart00020 162 GGGAITDNMLCAGGLEGGKDACQGDSGGPLVcnDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-220 2.05e-86

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: 254.91  E-value: 2.05e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015     1 IVGGTSASAGDFPFIVSISRNGGP-WCGGSLLNANTVLTAAHCVSGYAQSGFQIRAGSLSRTSGG--ITSSLSSVRVHPS 77
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEegQVIKVSKVIIHPN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015    78 YSGNN--NDLAILKLSTSIPSGGNIGYARLAASGSDPVAGSSATVAGWGATSEGGSSTPVNLLKVTVPIVSRATCRAQY- 154
Cdd:smart00020  82 YNPSTydNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYs 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157834015   155 GTSAITNQMFCAGVSSGGKDSCQGDSGGPIV--DSSNTLIGAVSWGNGCARPNYSGVYASVGALRSFI 220
Cdd:smart00020 162 GGGAITDNMLCAGGLEGGKDACQGDSGGPLVcnDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-221 2.40e-84

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  Cd Length: 232  Bit Score: 249.89  E-value: 2.40e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015   1 IVGGTSASAGDFPFIVSISRNGGP-WCGGSLLNANTVLTAAHCVSGYAQSGFQIRAGSLSRTS---GGITSSLSSVRVHP 76
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSnegGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015  77 SYSGN--NNDLAILKLSTSIPSGGNIGYARLAASGSDPVAGSSATVAGWGATSEGGsSTPVNLLKVTVPIVSRATCRAQY 154
Cdd:cd00190   81 NYNPStyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157834015 155 GT-SAITNQMFCAGVSSGGKDSCQGDSGGPIV---DSSNTLIGAVSWGNGCARPNYSGVYASVGALRSFID 221
Cdd:cd00190  160 SYgGTITDNMLCAGGLEGGKDACQGDSGGPLVcndNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
Trypsin pfam00089
Trypsin.
1-220 6.50e-61

Trypsin.


Pssm-ID: 365866  Cd Length: 219  Bit Score: 189.96  E-value: 6.50e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015    1 IVGGTSASAGDFPFIVSIS-RNGGPWCGGSLLNANTVLTAAHCVSGYAQsgFQIRAGSLSRTS---GGITSSLSSVRVHP 76
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASD--VQVVLGEHNIVLregGEQKFDVAKVIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015   77 SYSGNN--NDLAILKLSTSIPSGGNIGYARLAASGSDPVAGSSATVAGWGATSEGGssTPVNLLKVTVPIVSRATCRAQY 154
Cdd:pfam00089  79 NYNPDTldNDIALLKLESPVTLGDTVRPICLPDAGADLPVGTTCTVSGWGNTKTLG--PPDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157834015  155 GTsAITNQMFCAGvsSGGKDSCQGDSGGPIVDSSNTLIGAVSWGNGCARPNYSGVYASVGALRSFI 220
Cdd:pfam00089 157 GG-TVTDTMICAG--AGGKDACQGDSGGPLVCSDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-221 1.19e-25

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 103.03  E-value: 1.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015   1 IVGGTSASAGDFPFIVSISRNGGP-----WCGGSLLNANTVLTAAHCV--SGYAQSGFQIRAGSLSRTSGGITSSLSSVR 73
Cdd:COG5640   33 IIGGSNANAGEYPSLVALVDRISDyvsgtFCGGSKLGGRYVLTAAHCAdaSSPISSDVNRVVVDLNDSSQAERGHVRTIY 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015  74 VHPSYSGNN--NDLAILKLS--TSIPSGGNIGYARLAASGSDPVAGSSATVAGWGAT--SEGGSSTPVN--LLKVTVPIV 145
Cdd:COG5640  113 VHEFYSPGNlgNDIAVLELAraASLPRVKITSFDASDTFLNSVTTVSPMTNGTFGVTtpSDVPRSSPKGtiLHEVAVLFV 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015 146 SRATCRAQYG-------TSAITNqmFCAGvsSGGKDSCQGDSGGPIV-DSSNT--LIGAVSWG-NGCARPNYSGVYASVG 214
Cdd:COG5640  193 PLSTCAQYKGcanasdgATGLTG--FCAG--RPPKDACQGDSGGPIFhKGEEGrvQRGVVSWGdGGCGGTLIPGVYTNVS 268

                 ....*..
gi 157834015 215 ALRSFID 221
Cdd:COG5640  269 NYQDWIA 275
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-220 2.05e-86

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: 254.91  E-value: 2.05e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015     1 IVGGTSASAGDFPFIVSISRNGGP-WCGGSLLNANTVLTAAHCVSGYAQSGFQIRAGSLSRTSGG--ITSSLSSVRVHPS 77
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEegQVIKVSKVIIHPN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015    78 YSGNN--NDLAILKLSTSIPSGGNIGYARLAASGSDPVAGSSATVAGWGATSEGGSSTPVNLLKVTVPIVSRATCRAQY- 154
Cdd:smart00020  82 YNPSTydNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYs 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157834015   155 GTSAITNQMFCAGVSSGGKDSCQGDSGGPIV--DSSNTLIGAVSWGNGCARPNYSGVYASVGALRSFI 220
Cdd:smart00020 162 GGGAITDNMLCAGGLEGGKDACQGDSGGPLVcnDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-221 2.40e-84

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  Cd Length: 232  Bit Score: 249.89  E-value: 2.40e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015   1 IVGGTSASAGDFPFIVSISRNGGP-WCGGSLLNANTVLTAAHCVSGYAQSGFQIRAGSLSRTS---GGITSSLSSVRVHP 76
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSnegGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015  77 SYSGN--NNDLAILKLSTSIPSGGNIGYARLAASGSDPVAGSSATVAGWGATSEGGsSTPVNLLKVTVPIVSRATCRAQY 154
Cdd:cd00190   81 NYNPStyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157834015 155 GT-SAITNQMFCAGVSSGGKDSCQGDSGGPIV---DSSNTLIGAVSWGNGCARPNYSGVYASVGALRSFID 221
Cdd:cd00190  160 SYgGTITDNMLCAGGLEGGKDACQGDSGGPLVcndNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
Trypsin pfam00089
Trypsin.
1-220 6.50e-61

Trypsin.


Pssm-ID: 365866  Cd Length: 219  Bit Score: 189.96  E-value: 6.50e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015    1 IVGGTSASAGDFPFIVSIS-RNGGPWCGGSLLNANTVLTAAHCVSGYAQsgFQIRAGSLSRTS---GGITSSLSSVRVHP 76
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASD--VQVVLGEHNIVLregGEQKFDVAKVIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015   77 SYSGNN--NDLAILKLSTSIPSGGNIGYARLAASGSDPVAGSSATVAGWGATSEGGssTPVNLLKVTVPIVSRATCRAQY 154
Cdd:pfam00089  79 NYNPDTldNDIALLKLESPVTLGDTVRPICLPDAGADLPVGTTCTVSGWGNTKTLG--PPDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157834015  155 GTsAITNQMFCAGvsSGGKDSCQGDSGGPIVDSSNTLIGAVSWGNGCARPNYSGVYASVGALRSFI 220
Cdd:pfam00089 157 GG-TVTDTMICAG--AGGKDACQGDSGGPLVCSDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-221 1.19e-25

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 103.03  E-value: 1.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015   1 IVGGTSASAGDFPFIVSISRNGGP-----WCGGSLLNANTVLTAAHCV--SGYAQSGFQIRAGSLSRTSGGITSSLSSVR 73
Cdd:COG5640   33 IIGGSNANAGEYPSLVALVDRISDyvsgtFCGGSKLGGRYVLTAAHCAdaSSPISSDVNRVVVDLNDSSQAERGHVRTIY 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015  74 VHPSYSGNN--NDLAILKLS--TSIPSGGNIGYARLAASGSDPVAGSSATVAGWGAT--SEGGSSTPVN--LLKVTVPIV 145
Cdd:COG5640  113 VHEFYSPGNlgNDIAVLELAraASLPRVKITSFDASDTFLNSVTTVSPMTNGTFGVTtpSDVPRSSPKGtiLHEVAVLFV 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015 146 SRATCRAQYG-------TSAITNqmFCAGvsSGGKDSCQGDSGGPIV-DSSNT--LIGAVSWG-NGCARPNYSGVYASVG 214
Cdd:COG5640  193 PLSTCAQYKGcanasdgATGLTG--FCAG--RPPKDACQGDSGGPIFhKGEEGrvQRGVVSWGdGGCGGTLIPGVYTNVS 268

                 ....*..
gi 157834015 215 ALRSFID 221
Cdd:COG5640  269 NYQDWIA 275
Trypsin_2 pfam13365
Trypsin-like peptidase domain. This family includes trypsin-like peptidase domains.
34-193 2.60e-04

Trypsin-like peptidase domain. This family includes trypsin-like peptidase domains.


Pssm-ID: 379142  Cd Length: 143  Bit Score: 39.72  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015   34 NTVLTAAHCVSGYAqsGFQIRAGSLSRTSGGITsslssVRVHPSYSGNNNDLAILKLSTSipsGGNIGYARLAASgSDPV 113
Cdd:pfam13365  10 GLVLTNAHVVDDAD--EAAVTVVEEVVLADGRE-----YPATVVARDPELDLALLRVEGD---GAGLPPLPLGDS-EPLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157834015  114 AGSSATVAGWGATSEGGSSTPVNLLKVTVPIVSRATCRAQYGTSAITNqmfcagvssggkdscqGDSGGPIVDSSNTLIG 193
Cdd:pfam13365  79 GGERVYAVGYPLGGPKLSLSEGRVSGVSRPAPGGDDDRFIQTDAALSP----------------GSSGGPVFDADGRVVG 142
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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