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Conserved domains on  [gi|50979297|ref|NP_998988|]
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chymotrypsin-like elastase family member 1 preproprotein [Sus scrofa]

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

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 ...
27-262 6.93e-95

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: 278.39  E-value: 6.93e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297  27 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDREL--TFRVVVGEHNLNQNDGTEQYVGVQKIV 104
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297 105 VHPYWNTDDVaaGYDIALLRLGQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAIL 184
Cdd:cd00190  78 VHPNYNPSTY--DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50979297 185 SSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWINNV 262
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
27-262 6.93e-95

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: 278.39  E-value: 6.93e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297  27 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDREL--TFRVVVGEHNLNQNDGTEQYVGVQKIV 104
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297 105 VHPYWNTDDVaaGYDIALLRLGQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAIL 184
Cdd:cd00190  78 VHPNYNPSTY--DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50979297 185 SSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWINNV 262
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
26-259 8.51e-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: 255.30  E-value: 8.51e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297     26 RVVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDR--ELTFRVVVGEHNLNqNDGTEQYVGVQKI 103
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR---HFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLS-SGEEGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297    104 VVHPYWNTDDVaaGYDIALLRLGQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTR-TNGQLAQTLQQAYLPTVDYA 182
Cdd:smart00020  77 IIHPNYNPSTY--DNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50979297    183 ILSSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLvNGQYAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWI 259
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
27-259 1.68e-76

Trypsin;


Pssm-ID: 333831  Cd Length: 219  Bit Score: 231.17  E-value: 1.68e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297    27 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDRELTFRVVVGEHNLNQNDGTEQYVGVQKIVVH 106
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK---HFCGGSLISENWVLTAAHCVSGSSDVQVVLGEHNIVLREGGEQKFDVEKVIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297   107 PYWNTDDVaaGYDIALLRLGQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGqLAQTLQQAYLPTVDYAilSS 186
Cdd:pfam00089  78 PNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDAGSDLPVGTTCTVSGWGNTKTLG-RPDTLQEVTVPVVSRE--TC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50979297   187 SSYWGSTVKNSMVCAGGDGvRSGCQGDSGGPLHCLVNgqyAVHGVTSFVsrLGCNVTRKPTVFTRVSAYISWI 259
Cdd:pfam00089 153 RSAYGGTVTDNMICAGAGG-KDACQGDSGGPLVCSDG---ELIGIVSWG--YGCASGNKPGVYTRVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
22-259 6.19e-23

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 96.48  E-value: 6.19e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297  22 ETNARVVGGTEAQRNSWPSQISLQYRSGSSWAHT-CGGTLIRQNWVMTAAHCVDRE-----LTFRVVVGEHNLNQNDGte 95
Cdd:COG5640  28 EVSSRIIGGSNANAGEYPSLVALVDRISDYVSGTfCGGSKLGGRYVLTAAHCADASspissDVNRVVVDLNDSSQAER-- 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297  96 qyVGVQKIVVHPYWNTDDVaaGYDIALLRLGQSVTLNSYVQLGVLPRAG--TILANNSPCYITGWGLTR--------TNG 165
Cdd:COG5640 106 --GHVRTIYVHEFYSPGNL--GNDIAVLELARAASLPRVKITSFDASDTflNSVTTVSPMTNGTFGVTTpsdvprssPKG 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297 166 QLAQTLQQAYLPTVDYAILSSSSYWGSTVKNSM-VCAGGDGvRSGCQGDSGGPLHCLVNGQYAVHGVTSFvSRLGCNVTR 244
Cdd:COG5640 182 TILHEVAVLFVPLSTCAQYKGCANASDGATGLTgFCAGRPP-KDACQGDSGGPIFHKGEEGRVQRGVVSW-GDGGCGGTL 259
                       250
                ....*....|....*
gi 50979297 245 KPTVFTRVSAYISWI 259
Cdd:COG5640 260 IPGVYTNVSNYQDWI 274
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
27-262 6.93e-95

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: 278.39  E-value: 6.93e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297  27 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDREL--TFRVVVGEHNLNQNDGTEQYVGVQKIV 104
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297 105 VHPYWNTDDVaaGYDIALLRLGQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAIL 184
Cdd:cd00190  78 VHPNYNPSTY--DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50979297 185 SSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWINNV 262
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
26-259 8.51e-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: 255.30  E-value: 8.51e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297     26 RVVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDR--ELTFRVVVGEHNLNqNDGTEQYVGVQKI 103
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR---HFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLS-SGEEGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297    104 VVHPYWNTDDVaaGYDIALLRLGQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTR-TNGQLAQTLQQAYLPTVDYA 182
Cdd:smart00020  77 IIHPNYNPSTY--DNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50979297    183 ILSSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLvNGQYAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWI 259
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
27-259 1.68e-76

Trypsin;


Pssm-ID: 333831  Cd Length: 219  Bit Score: 231.17  E-value: 1.68e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297    27 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDRELTFRVVVGEHNLNQNDGTEQYVGVQKIVVH 106
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK---HFCGGSLISENWVLTAAHCVSGSSDVQVVLGEHNIVLREGGEQKFDVEKVIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297   107 PYWNTDDVaaGYDIALLRLGQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGqLAQTLQQAYLPTVDYAilSS 186
Cdd:pfam00089  78 PNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDAGSDLPVGTTCTVSGWGNTKTLG-RPDTLQEVTVPVVSRE--TC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50979297   187 SSYWGSTVKNSMVCAGGDGvRSGCQGDSGGPLHCLVNgqyAVHGVTSFVsrLGCNVTRKPTVFTRVSAYISWI 259
Cdd:pfam00089 153 RSAYGGTVTDNMICAGAGG-KDACQGDSGGPLVCSDG---ELIGIVSWG--YGCASGNKPGVYTRVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
22-259 6.19e-23

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 96.48  E-value: 6.19e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297  22 ETNARVVGGTEAQRNSWPSQISLQYRSGSSWAHT-CGGTLIRQNWVMTAAHCVDRE-----LTFRVVVGEHNLNQNDGte 95
Cdd:COG5640  28 EVSSRIIGGSNANAGEYPSLVALVDRISDYVSGTfCGGSKLGGRYVLTAAHCADASspissDVNRVVVDLNDSSQAER-- 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297  96 qyVGVQKIVVHPYWNTDDVaaGYDIALLRLGQSVTLNSYVQLGVLPRAG--TILANNSPCYITGWGLTR--------TNG 165
Cdd:COG5640 106 --GHVRTIYVHEFYSPGNL--GNDIAVLELARAASLPRVKITSFDASDTflNSVTTVSPMTNGTFGVTTpsdvprssPKG 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297 166 QLAQTLQQAYLPTVDYAILSSSSYWGSTVKNSM-VCAGGDGvRSGCQGDSGGPLHCLVNGQYAVHGVTSFvSRLGCNVTR 244
Cdd:COG5640 182 TILHEVAVLFVPLSTCAQYKGCANASDGATGLTgFCAGRPP-KDACQGDSGGPIFHKGEEGRVQRGVVSW-GDGGCGGTL 259
                       250
                ....*....|....*
gi 50979297 245 KPTVFTRVSAYISWI 259
Cdd:COG5640 260 IPGVYTNVSNYQDWI 274
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
36-151 2.28e-03

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


Pssm-ID: 226119  Cd Length: 251  Bit Score: 38.14  E-value: 2.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50979297  36 NSWPSQISLQYRSGSSwAHTCGGTLIRQNWVMTAAHCVDRELTFRVVVGEHNLNQNDGTEQYVGVQKIVVHPY---WNTD 112
Cdd:COG3591  47 TQFPYSAVVQFEAATG-RLCTAATLIGPNTVLTAGHCIYSPDYGEDDIAAAPPGVNSDGGPFYGITKIEIRVYpgeLYKE 125
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 50979297 113 DvAAGYDIALLRLGQSVTLNSYVQLGVLPRAGTILANNS 151
Cdd:COG3591 126 D-GASYDVGEAALESGINIGDVVNYLKRNTASEAKANDR 163
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
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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