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Conserved domains on  [gi|6730458]
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Chain A, ELASTASE

Protein Classification

serine protease( domain architecture ID 10076129)

serine protease such as human cathepsin G with trypsin- and chymotrypsin-like specificity; also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity

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 ...
1-236 1.58e-97

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: 284.17  E-value: 1.58e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458    1 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDREL--TFRVVVGEHNLNQNNGTEQYVGVQKIV 78
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458   79 VHPYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAIC 158
Cdd:cd00190  78 VHPNYNPSTY--DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6730458  159 SSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWINNV 236
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 ...
1-236 1.58e-97

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: 284.17  E-value: 1.58e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458    1 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDREL--TFRVVVGEHNLNQNNGTEQYVGVQKIV 78
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458   79 VHPYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAIC 158
Cdd:cd00190  78 VHPNYNPSTY--DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6730458  159 SSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWINNV 236
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-233 1.16e-87

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: 259.15  E-value: 1.16e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458       1 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDR--ELTFRVVVGEHNLNqNNGTEQYVGVQKIV 78
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGR---HFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLS-SGEEGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458      79 VHPYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTR-TNGQLAQTLQQAYLPTVDYAI 157
Cdd:smart00020  78 IHPNYNPSTY--DNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6730458     158 CSSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLvNGQYAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWI 233
Cdd:smart00020 156 CRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-233 5.75e-78

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 234.26  E-value: 5.75e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458      1 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDRELTFRVVVGEHNLNQNNGTEQYVGVQKIVVH 80
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK---HFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458     81 PYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGqLAQTLQQAYLPTVDYAICSS 160
Cdd:pfam00089  78 PNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6730458    161 SsyWGSTVKNSMVCAGGDGvRSGCQGDSGGPLHCLVNgqyAVHGVTSFVsrLGCNVTRKPTVFTRVSAYISWI 233
Cdd:pfam00089 155 A--YGGTVTDTMICAGAGG-KDACQGDSGGPLVCSDG---ELIGIVSWG--YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-240 2.51e-65

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 203.34  E-value: 2.51e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458    1 VVGGTEAQRNSWPSQISLQYRSGSSwAHTCGGTLIRQNWVMTAAHCVDREL--TFRVVVGEHNLNQNNGTEqyVGVQKIV 78
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNGPS-GQFCGGTLIAPRWVLTAAHCVDGDGpsDLRVVIGSTDLSTSGGTV--VKVARIV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458   79 VHPYWNtdDVAAGYDIALLRLAQSVTLNSYVQlgvLPRAGTILANNSPCYITGWGLTRTN-GQLAQTLQQAYLPTVDYAI 157
Cdd:COG5640 108 VHPDYD--PATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVSDAT 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458  158 CSSssyWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSRlGCnVTRKPTVFTRVSAYISWINNV 236
Cdd:COG5640 183 CAA---YGGFDGGTMLCAGYpEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGG-PC-AAGYPGVYTRVSAYRDWIKST 257

                ....
gi 6730458  237 IASN 240
Cdd:COG5640 258 AGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-236 1.58e-97

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: 284.17  E-value: 1.58e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458    1 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDREL--TFRVVVGEHNLNQNNGTEQYVGVQKIV 78
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458   79 VHPYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAIC 158
Cdd:cd00190  78 VHPNYNPSTY--DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6730458  159 SSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWINNV 236
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-233 1.16e-87

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: 259.15  E-value: 1.16e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458       1 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDR--ELTFRVVVGEHNLNqNNGTEQYVGVQKIV 78
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGR---HFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLS-SGEEGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458      79 VHPYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTR-TNGQLAQTLQQAYLPTVDYAI 157
Cdd:smart00020  78 IHPNYNPSTY--DNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6730458     158 CSSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLvNGQYAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWI 233
Cdd:smart00020 156 CRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-233 5.75e-78

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 234.26  E-value: 5.75e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458      1 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDRELTFRVVVGEHNLNQNNGTEQYVGVQKIVVH 80
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK---HFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458     81 PYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGqLAQTLQQAYLPTVDYAICSS 160
Cdd:pfam00089  78 PNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6730458    161 SsyWGSTVKNSMVCAGGDGvRSGCQGDSGGPLHCLVNgqyAVHGVTSFVsrLGCNVTRKPTVFTRVSAYISWI 233
Cdd:pfam00089 155 A--YGGTVTDTMICAGAGG-KDACQGDSGGPLVCSDG---ELIGIVSWG--YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-240 2.51e-65

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 203.34  E-value: 2.51e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458    1 VVGGTEAQRNSWPSQISLQYRSGSSwAHTCGGTLIRQNWVMTAAHCVDREL--TFRVVVGEHNLNQNNGTEqyVGVQKIV 78
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNGPS-GQFCGGTLIAPRWVLTAAHCVDGDGpsDLRVVIGSTDLSTSGGTV--VKVARIV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458   79 VHPYWNtdDVAAGYDIALLRLAQSVTLNSYVQlgvLPRAGTILANNSPCYITGWGLTRTN-GQLAQTLQQAYLPTVDYAI 157
Cdd:COG5640 108 VHPDYD--PATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVSDAT 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458  158 CSSssyWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSRlGCnVTRKPTVFTRVSAYISWINNV 236
Cdd:COG5640 183 CAA---YGGFDGGTMLCAGYpEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGG-PC-AAGYPGVYTRVSAYRDWIKST 257

                ....
gi 6730458  237 IASN 240
Cdd:COG5640 258 AGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
28-208 5.45e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 54.30  E-value: 5.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458   28 HTCGGTLIRQNWVMTAAHCVDRELT------FRVVVGehnlnQNNGTEQYVGVQKIVVHPYWnTDDVAAGYDIALLRLAQ 101
Cdd:COG3591  12 GVCTGTLIGPNLVLTAGHCVYDGAGggwatnIVFVPG-----YNGGPYGTATATRFRVPPGW-VASGDAGYDYALLRLDE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6730458  102 SVTLnsyvQLGVLP-RAGTILANNSPCYITGWGLTRTNgqlAQTLQQAylptvdyaiCSSSSYWGSTVknSMVCaggdgv 180
Cdd:COG3591  86 PLGD----TTGWLGlAFNDAPLAGEPVTIIGYPGDRPK---DLSLDCS---------GRVTGVQGNRL--SYDC------ 141
                       170       180
                ....*....|....*....|....*...
gi 6730458  181 rSGCQGDSGGPLHCLVNGQYAVHGVTSF 208
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.
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