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Conserved domains on  [gi|58331209|ref|NP_001962|]
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chymotrypsin-like elastase family member 1 [Homo sapiens]

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 ...
19-254 1.03e-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 [Multi-domain]  Cd Length: 232  Bit Score: 280.32  E-value: 1.03e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209  19 VVGGTEAGRNSWPSQISLQYRSGGsryHTCGGTLIRQNWVMTAAHCVDYQ--KTFRVVAGDHNLSQNDGTEQYVSVQKIV 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209  97 VHPYWNSDNVaaGYDIALLRLAQSVTLNSYVQLGVLPQEGAILANNSPCYITGWGKTKTNGQLAQTLQQAYLPSVDYAIC 176
Cdd:cd00190  78 VHPNYNPSTY--DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58331209 177 SSSSYWGSTVKNTMVCAGG-DGVRSGCQGDSGGPLHCLVNGKYSVHGVTSFVSsrGCNVSRKPTVFTQVSAYISWINNV 254
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 ...
19-254 1.03e-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 [Multi-domain]  Cd Length: 232  Bit Score: 280.32  E-value: 1.03e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209  19 VVGGTEAGRNSWPSQISLQYRSGGsryHTCGGTLIRQNWVMTAAHCVDYQ--KTFRVVAGDHNLSQNDGTEQYVSVQKIV 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209  97 VHPYWNSDNVaaGYDIALLRLAQSVTLNSYVQLGVLPQEGAILANNSPCYITGWGKTKTNGQLAQTLQQAYLPSVDYAIC 176
Cdd:cd00190  78 VHPNYNPSTY--DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58331209 177 SSSSYWGSTVKNTMVCAGG-DGVRSGCQGDSGGPLHCLVNGKYSVHGVTSFVSsrGCNVSRKPTVFTQVSAYISWINNV 254
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
18-251 2.24e-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: 2.24e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209     18 RVVGGTEAGRNSWPSQISLQYRSGgsrYHTCGGTLIRQNWVMTAAHCVDYQ--KTFRVVAGDHNLSqNDGTEQYVSVQKI 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGG---RHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLS-SGEEGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209     96 VVHPYWNSDNVaaGYDIALLRLAQSVTLNSYVQLGVLPQEGAILANNSPCYITGWGKTK-TNGQLAQTLQQAYLPSVDYA 174
Cdd:smart00020  77 IIHPNYNPSTY--DNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58331209    175 ICSSSSYWGSTVKNTMVCAGG-DGVRSGCQGDSGGPLHCLvNGKYSVHGVTSFVSsrGCNVSRKPTVFTQVSAYISWI 251
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
19-251 5.02e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 232.33  E-value: 5.02e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209    19 VVGGTEAGRNSWPSQISLQYRSGGsryHTCGGTLIRQNWVMTAAHCVDYQKTFRVVAGDHNLSQNDGTEQYVSVQKIVVH 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK---HFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209    99 PYWNSDNVaaGYDIALLRLAQSVTLNSYVQLGVLPQEGAILANNSPCYITGWGKTKTNGqLAQTLQQAYLPSVDYAICSS 178
Cdd:pfam00089  78 PNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58331209   179 SsyWGSTVKNTMVCAGGDGvRSGCQGDSGGPLHCLVNgkySVHGVTSFvsSRGCNVSRKPTVFTQVSAYISWI 251
Cdd:pfam00089 155 A--YGGTVTDTMICAGAGG-KDACQGDSGGPLVCSDG---ELIGIVSW--GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
8-258 1.64e-65

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 204.50  E-value: 1.64e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209   8 STQDLPETNARVVGGTEAGRNSWPSQISLQyRSGGSRYHTCGGTLIRQNWVMTAAHCVDYQ--KTFRVVAGDHNLSQNDG 85
Cdd:COG5640  20 AAAPAADAAPAIVGGTPATVGEYPWMVALQ-SSNGPSGQFCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLSTSGG 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209  86 TEqyVSVQKIVVHPYWNSdnVAAGYDIALLRLAQSVTLNSYVQlgvLPQEGAILANNSPCYITGWGKTKTN-GQLAQTLQ 164
Cdd:COG5640  99 TV--VKVARIVVHPDYDP--ATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGpGSQSGTLR 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209 165 QAYLPSVDYAICSSssyWGSTVKNTMVCAGG-DGVRSGCQGDSGGPLHCLVNGKYSVHGVTSFvSSRGCnVSRKPTVFTQ 243
Cdd:COG5640 172 KADVPVVSDATCAA---YGGFDGGTMLCAGYpEGGKDACQGDSGGPLVVKDGGGWVLVGVVSW-GGGPC-AAGYPGVYTR 246
                       250
                ....*....|....*
gi 58331209 244 VSAYISWINNVIASN 258
Cdd:COG5640 247 VSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
19-254 1.03e-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 [Multi-domain]  Cd Length: 232  Bit Score: 280.32  E-value: 1.03e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209  19 VVGGTEAGRNSWPSQISLQYRSGGsryHTCGGTLIRQNWVMTAAHCVDYQ--KTFRVVAGDHNLSQNDGTEQYVSVQKIV 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209  97 VHPYWNSDNVaaGYDIALLRLAQSVTLNSYVQLGVLPQEGAILANNSPCYITGWGKTKTNGQLAQTLQQAYLPSVDYAIC 176
Cdd:cd00190  78 VHPNYNPSTY--DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58331209 177 SSSSYWGSTVKNTMVCAGG-DGVRSGCQGDSGGPLHCLVNGKYSVHGVTSFVSsrGCNVSRKPTVFTQVSAYISWINNV 254
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
18-251 2.24e-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: 2.24e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209     18 RVVGGTEAGRNSWPSQISLQYRSGgsrYHTCGGTLIRQNWVMTAAHCVDYQ--KTFRVVAGDHNLSqNDGTEQYVSVQKI 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGG---RHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLS-SGEEGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209     96 VVHPYWNSDNVaaGYDIALLRLAQSVTLNSYVQLGVLPQEGAILANNSPCYITGWGKTK-TNGQLAQTLQQAYLPSVDYA 174
Cdd:smart00020  77 IIHPNYNPSTY--DNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58331209    175 ICSSSSYWGSTVKNTMVCAGG-DGVRSGCQGDSGGPLHCLvNGKYSVHGVTSFVSsrGCNVSRKPTVFTQVSAYISWI 251
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
19-251 5.02e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 232.33  E-value: 5.02e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209    19 VVGGTEAGRNSWPSQISLQYRSGGsryHTCGGTLIRQNWVMTAAHCVDYQKTFRVVAGDHNLSQNDGTEQYVSVQKIVVH 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK---HFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209    99 PYWNSDNVaaGYDIALLRLAQSVTLNSYVQLGVLPQEGAILANNSPCYITGWGKTKTNGqLAQTLQQAYLPSVDYAICSS 178
Cdd:pfam00089  78 PNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58331209   179 SsyWGSTVKNTMVCAGGDGvRSGCQGDSGGPLHCLVNgkySVHGVTSFvsSRGCNVSRKPTVFTQVSAYISWI 251
Cdd:pfam00089 155 A--YGGTVTDTMICAGAGG-KDACQGDSGGPLVCSDG---ELIGIVSW--GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
8-258 1.64e-65

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 204.50  E-value: 1.64e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209   8 STQDLPETNARVVGGTEAGRNSWPSQISLQyRSGGSRYHTCGGTLIRQNWVMTAAHCVDYQ--KTFRVVAGDHNLSQNDG 85
Cdd:COG5640  20 AAAPAADAAPAIVGGTPATVGEYPWMVALQ-SSNGPSGQFCGGTLIAPRWVLTAAHCVDGDgpSDLRVVIGSTDLSTSGG 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209  86 TEqyVSVQKIVVHPYWNSdnVAAGYDIALLRLAQSVTLNSYVQlgvLPQEGAILANNSPCYITGWGKTKTN-GQLAQTLQ 164
Cdd:COG5640  99 TV--VKVARIVVHPDYDP--ATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGpGSQSGTLR 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209 165 QAYLPSVDYAICSSssyWGSTVKNTMVCAGG-DGVRSGCQGDSGGPLHCLVNGKYSVHGVTSFvSSRGCnVSRKPTVFTQ 243
Cdd:COG5640 172 KADVPVVSDATCAA---YGGFDGGTMLCAGYpEGGKDACQGDSGGPLVVKDGGGWVLVGVVSW-GGGPC-AAGYPGVYTR 246
                       250
                ....*....|....*
gi 58331209 244 VSAYISWINNVIASN 258
Cdd:COG5640 247 VSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
40-226 9.45e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 56.61  E-value: 9.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209  40 SGGSRYHtCGGTLIRQNWVMTAAHCVDYQKT------FRVVAGdhnlsQNDGTEQYVSVQKIVVHPYWNSDNvAAGYDIA 113
Cdd:COG3591   7 TDGGGGV-CTGTLIGPNLVLTAGHCVYDGAGggwatnIVFVPG-----YNGGPYGTATATRFRVPPGWVASG-DAGYDYA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331209 114 LLRLAQSVTlNSYVQLGVLPQEGAilANNSPCYITGWGKTKTNgqlAQTLQQAylpsvdyaiCSSSSYWGSTVknTMVCa 193
Cdd:COG3591  80 LLRLDEPLG-DTTGWLGLAFNDAP--LAGEPVTIIGYPGDRPK---DLSLDCS---------GRVTGVQGNRL--SYDC- 141
                       170       180       190
                ....*....|....*....|....*....|...
gi 58331209 194 ggdgvrSGCQGDSGGPLHCLVNGKYSVHGVTSF 226
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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