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Conserved domains on  [gi|4503549|ref|NP_001963|]
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neutrophil elastase preproprotein [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 ...
30-245 1.56e-72

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: 221.77  E-value: 1.56e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549   30 IVGGRRARPHAWPFMVSLQLR-GGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTRQVFAVQRIFEN- 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHp 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549  108 GYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRGIASVLQELNVTVVT-SLCRR--- 183
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSnAECKRays 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503549  184 -------SNVCTLVRGRQAGVCFGDSGSPLVCN----GLIHGIASFVRgGCASGLYPDAFAPVAQFVNWIDSI 245
Cdd:cd00190 161 yggtitdNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGS-GCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
30-245 1.56e-72

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: 221.77  E-value: 1.56e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549   30 IVGGRRARPHAWPFMVSLQLR-GGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTRQVFAVQRIFEN- 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHp 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549  108 GYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRGIASVLQELNVTVVT-SLCRR--- 183
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSnAECKRays 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503549  184 -------SNVCTLVRGRQAGVCFGDSGSPLVCN----GLIHGIASFVRgGCASGLYPDAFAPVAQFVNWIDSI 245
Cdd:cd00190 161 yggtitdNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGS-GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
29-242 7.52e-67

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: 207.15  E-value: 7.52e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549      29 EIVGGRRARPHAWPFMVSLQLRGG-HFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTrQVFAVQRIFEN 107
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEG-QVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549     108 -GYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRG-IASVLQELNVTVVT-SLCRR- 183
Cdd:smart00020  80 pNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGsLPDTLQEVNVPIVSnATCRRa 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503549     184 ---------SNVCTLVRGRQAGVCFGDSGSPLVCN---GLIHGIASFVRgGCASGLYPDAFAPVAQFVNWI 242
Cdd:smart00020 160 ysgggaitdNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
30-242 1.42e-63

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 198.44  E-value: 1.42e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549     30 IVGGRRARPHAWPFMVSLQLRGG-HFCGATLIAPNFVMSAAHCVANVNVRAVRvvLGAHNLSRREPTRQVFAVQRIFE-N 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCVSGASDVKVV--LGAHNIVLREGGEQKFDVEKIIVhP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549    108 GYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNrGIASVLQELNVTVV-TSLCRRSN- 185
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL-GPSDTLQEVTVPVVsRETCRSAYg 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503549    186 -------VCTLVRGRqaGVCFGDSGSPLVC-NGLIHGIASFVRgGCASGLYPDAFAPVAQFVNWI 242
Cdd:pfam00089 158 gtvtdtmICAGAGGK--DACQGDSGGPLVCsDGELIGIVSWGY-GCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-246 2.65e-48

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 160.59  E-value: 2.65e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549    1 MTLGRRLACLFLACVlpALLLGGTALAS---EIVGGRRARPHAWPFMVSLQLRGG---HFCGATLIAPNFVMSAAHCVAN 74
Cdd:COG5640   1 MRRRRLLAALAAAAL--ALALAAAPAADaapAIVGGTPATVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCVDG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549   75 VNVRAVRVVLGAHNLSrrEPTRQVFAVQRIFEN-GYDPVNLLNDIVILQLNGSATinaNVQVAQLPAQGRRLGNGVQCLA 153
Cdd:COG5640  79 DGPSDLRVVIGSTDLS--TSGGTVVKVARIVVHpDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549  154 MGWGLLGRNRGIAS-VLQELNVTVV-TSLCRR-------SNVCTLVRGRQAGVCFGDSGSPLV----CNGLIHGIASFVR 220
Cdd:COG5640 154 AGWGRTSEGPGSQSgTLRKADVPVVsDATCAAyggfdggTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGG 233
                       250       260
                ....*....|....*....|....*.
gi 4503549  221 GGCASGlYPDAFAPVAQFVNWIDSII 246
Cdd:COG5640 234 GPCAAG-YPGVYTRVSAYRDWIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
30-245 1.56e-72

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: 221.77  E-value: 1.56e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549   30 IVGGRRARPHAWPFMVSLQLR-GGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTRQVFAVQRIFEN- 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHp 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549  108 GYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRGIASVLQELNVTVVT-SLCRR--- 183
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSnAECKRays 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503549  184 -------SNVCTLVRGRQAGVCFGDSGSPLVCN----GLIHGIASFVRgGCASGLYPDAFAPVAQFVNWIDSI 245
Cdd:cd00190 161 yggtitdNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGS-GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
29-242 7.52e-67

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: 207.15  E-value: 7.52e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549      29 EIVGGRRARPHAWPFMVSLQLRGG-HFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTrQVFAVQRIFEN 107
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEG-QVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549     108 -GYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRG-IASVLQELNVTVVT-SLCRR- 183
Cdd:smart00020  80 pNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGsLPDTLQEVNVPIVSnATCRRa 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503549     184 ---------SNVCTLVRGRQAGVCFGDSGSPLVCN---GLIHGIASFVRgGCASGLYPDAFAPVAQFVNWI 242
Cdd:smart00020 160 ysgggaitdNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
30-242 1.42e-63

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 198.44  E-value: 1.42e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549     30 IVGGRRARPHAWPFMVSLQLRGG-HFCGATLIAPNFVMSAAHCVANVNVRAVRvvLGAHNLSRREPTRQVFAVQRIFE-N 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCVSGASDVKVV--LGAHNIVLREGGEQKFDVEKIIVhP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549    108 GYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNrGIASVLQELNVTVV-TSLCRRSN- 185
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL-GPSDTLQEVTVPVVsRETCRSAYg 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503549    186 -------VCTLVRGRqaGVCFGDSGSPLVC-NGLIHGIASFVRgGCASGLYPDAFAPVAQFVNWI 242
Cdd:pfam00089 158 gtvtdtmICAGAGGK--DACQGDSGGPLVCsDGELIGIVSWGY-GCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-246 2.65e-48

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 160.59  E-value: 2.65e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549    1 MTLGRRLACLFLACVlpALLLGGTALAS---EIVGGRRARPHAWPFMVSLQLRGG---HFCGATLIAPNFVMSAAHCVAN 74
Cdd:COG5640   1 MRRRRLLAALAAAAL--ALALAAAPAADaapAIVGGTPATVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCVDG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549   75 VNVRAVRVVLGAHNLSrrEPTRQVFAVQRIFEN-GYDPVNLLNDIVILQLNGSATinaNVQVAQLPAQGRRLGNGVQCLA 153
Cdd:COG5640  79 DGPSDLRVVIGSTDLS--TSGGTVVKVARIVVHpDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503549  154 MGWGLLGRNRGIAS-VLQELNVTVV-TSLCRR-------SNVCTLVRGRQAGVCFGDSGSPLV----CNGLIHGIASFVR 220
Cdd:COG5640 154 AGWGRTSEGPGSQSgTLRKADVPVVsDATCAAyggfdggTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGG 233
                       250       260
                ....*....|....*....|....*.
gi 4503549  221 GGCASGlYPDAFAPVAQFVNWIDSII 246
Cdd:COG5640 234 GPCAAG-YPGVYTRVSAYRDWIKSTA 258
 
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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