NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|119253|sp|P00772|]
View 

RecName: Full=Chymotrypsin-like elastase family member 1; AltName: Full=Elastase-1; Flags: Precursor

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 1.18e-98

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: 288.02  E-value: 1.18e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253    27 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDREL--TFRVVVGEHNLNQNDGTEQYVGVQKIV 104
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253   105 VHPYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAIC 184
Cdd:cd00190  78 VHPNYNPSTY--DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119253   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 1.18e-98

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: 288.02  E-value: 1.18e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253    27 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDREL--TFRVVVGEHNLNQNDGTEQYVGVQKIV 104
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253   105 VHPYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAIC 184
Cdd:cd00190  78 VHPNYNPSTY--DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119253   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 1.66e-89

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: 264.93  E-value: 1.66e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253       26 RVVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDR--ELTFRVVVGEHNLNqNDGTEQYVGVQKI 103
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR---HFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLS-SGEEGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253      104 VVHPYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTR-TNGQLAQTLQQAYLPTVDYA 182
Cdd:smart00020  77 IIHPNYNPSTY--DNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119253      183 ICSSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLvNGQYAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWI 259
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
27-259 2.99e-79

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 238.50  E-value: 2.99e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253      27 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDRELTFRVVVGEHNLNQNDGTEQYVGVQKIVVH 106
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK---HFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253     107 PYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGqLAQTLQQAYLPTVDYAICSS 186
Cdd:pfam00089  78 PNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119253     187 SsyWGSTVKNSMVCAGGDGvRSGCQGDSGGPLHClvNGQYaVHGVTSFVsrLGCNVTRKPTVFTRVSAYISWI 259
Cdd:pfam00089 155 A--YGGTVTDTMICAGAGG-KDACQGDSGGPLVC--SDGE-LIGIVSWG--YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-266 1.06e-67

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 210.28  E-value: 1.06e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253     1 MLRLLVVASLVLyGHSTQDFPETNARVVGGTEAQRNSWPSQISLQYRSGSSwAHTCGGTLIRQNWVMTAAHCVDREL--T 78
Cdd:COG5640   6 LLAALAAAALAL-ALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGPS-GQFCGGTLIAPRWVLTAAHCVDGDGpsD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253    79 FRVVVGEHNLNQNDGTEqyVGVQKIVVHPYWNtdDVAAGYDIALLRLAQSVTLNSYVQlgvLPRAGTILANNSPCYITGW 158
Cdd:COG5640  84 LRVVIGSTDLSTSGGTV--VKVARIVVHPDYD--PATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGW 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253   159 GLTRTN-GQLAQTLQQAYLPTVDYAICSSssyWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVS 236
Cdd:COG5640 157 GRTSEGpGSQSGTLRKADVPVVSDATCAA---YGGFDGGTMLCAGYpEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGG 233
                       250       260       270
                ....*....|....*....|....*....|
gi 119253   237 RlGCnVTRKPTVFTRVSAYISWINNVIASN 266
Cdd:COG5640 234 G-PC-AAGYPGVYTRVSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
27-262 1.18e-98

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: 288.02  E-value: 1.18e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253    27 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDREL--TFRVVVGEHNLNQNDGTEQYVGVQKIV 104
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253   105 VHPYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAIC 184
Cdd:cd00190  78 VHPNYNPSTY--DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119253   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 1.66e-89

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: 264.93  E-value: 1.66e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253       26 RVVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDR--ELTFRVVVGEHNLNqNDGTEQYVGVQKI 103
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR---HFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLS-SGEEGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253      104 VVHPYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTR-TNGQLAQTLQQAYLPTVDYA 182
Cdd:smart00020  77 IIHPNYNPSTY--DNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119253      183 ICSSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLvNGQYAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWI 259
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
27-259 2.99e-79

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 238.50  E-value: 2.99e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253      27 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDRELTFRVVVGEHNLNQNDGTEQYVGVQKIVVH 106
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK---HFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253     107 PYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGqLAQTLQQAYLPTVDYAICSS 186
Cdd:pfam00089  78 PNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119253     187 SsyWGSTVKNSMVCAGGDGvRSGCQGDSGGPLHClvNGQYaVHGVTSFVsrLGCNVTRKPTVFTRVSAYISWI 259
Cdd:pfam00089 155 A--YGGTVTDTMICAGAGG-KDACQGDSGGPLVC--SDGE-LIGIVSWG--YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-266 1.06e-67

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 210.28  E-value: 1.06e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253     1 MLRLLVVASLVLyGHSTQDFPETNARVVGGTEAQRNSWPSQISLQYRSGSSwAHTCGGTLIRQNWVMTAAHCVDREL--T 78
Cdd:COG5640   6 LLAALAAAALAL-ALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGPS-GQFCGGTLIAPRWVLTAAHCVDGDGpsD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253    79 FRVVVGEHNLNQNDGTEqyVGVQKIVVHPYWNtdDVAAGYDIALLRLAQSVTLNSYVQlgvLPRAGTILANNSPCYITGW 158
Cdd:COG5640  84 LRVVIGSTDLSTSGGTV--VKVARIVVHPDYD--PATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGW 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253   159 GLTRTN-GQLAQTLQQAYLPTVDYAICSSssyWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVS 236
Cdd:COG5640 157 GRTSEGpGSQSGTLRKADVPVVSDATCAA---YGGFDGGTMLCAGYpEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGG 233
                       250       260       270
                ....*....|....*....|....*....|
gi 119253   237 RlGCnVTRKPTVFTRVSAYISWINNVIASN 266
Cdd:COG5640 234 G-PC-AAGYPGVYTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
54-234 4.17e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 55.07  E-value: 4.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253    54 HTCGGTLIRQNWVMTAAHCVDRELT------FRVVVGehnlnQNDGTEQYVGVQKIVVHPYWnTDDVAAGYDIALLRLAQ 127
Cdd:COG3591  12 GVCTGTLIGPNLVLTAGHCVYDGAGggwatnIVFVPG-----YNGGPYGTATATRFRVPPGW-VASGDAGYDYALLRLDE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119253   128 SVTLnsyvQLGVLP-RAGTILANNSPCYITGWGLTRTNgqlAQTLQQAylptvdyaiCSSSSYWGSTVknSMVCaggdgv 206
Cdd:COG3591  86 PLGD----TTGWLGlAFNDAPLAGEPVTIIGYPGDRPK---DLSLDCS---------GRVTGVQGNRL--SYDC------ 141
                       170       180
                ....*....|....*....|....*...
gi 119253   207 rSGCQGDSGGPLHCLVNGQYAVHGVTSF 234
Cdd:COG3591 142 -DTTGGSSGSPVLDDSDGGGRVVGVHSA 168
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH