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Conserved domains on  [gi|1191801372|ref|XP_005655631|]
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chymotrypsin-like elastase family member 1 isoform X1 [Sus scrofa]

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 ...
67-302 8.39e-99

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: 289.95  E-value: 8.39e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372  67 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDREL--TFRVVVGEHNLNQNDGTEQYVGVQKIV 144
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372 145 VHPYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAIC 224
Cdd:cd00190    78 VHPNYNPSTY--DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191801372 225 SSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWINNV 302
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 ...
67-302 8.39e-99

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: 289.95  E-value: 8.39e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372  67 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDREL--TFRVVVGEHNLNQNDGTEQYVGVQKIV 144
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372 145 VHPYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAIC 224
Cdd:cd00190    78 VHPNYNPSTY--DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191801372 225 SSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWINNV 302
Cdd:cd00190   156 KRAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
66-299 1.32e-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: 266.47  E-value: 1.32e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372   66 RVVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDR--ELTFRVVVGEHNLNqNDGTEQYVGVQKI 143
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR---HFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLS-SGEEGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372  144 VVHPYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTR-TNGQLAQTLQQAYLPTVDYA 222
Cdd:smart00020  77 IIHPNYNPSTY--DNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191801372  223 ICSSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLvNGQYAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWI 299
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
67-299 1.15e-79

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 240.81  E-value: 1.15e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372  67 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDRELTFRVVVGEHNLNQNDGTEQYVGVQKIVVH 146
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK---HFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372 147 PYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGqLAQTLQQAYLPTVDYAICSS 226
Cdd:pfam00089  78 PNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191801372 227 SsyWGSTVKNSMVCAGGDGvRSGCQGDSGGPLHClvNGQYaVHGVTSFVsrLGCNVTRKPTVFTRVSAYISWI 299
Cdd:pfam00089 155 A--YGGTVTDTMICAGAGG-KDACQGDSGGPLVC--SDGE-LIGIVSWG--YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
39-306 3.59e-67

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 210.66  E-value: 3.59e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372  39 SNMLRLLVVASLVLyGHSTQDFPETNARVVGGTEAQRNSWPSQISLQYRSGSSwAHTCGGTLIRQNWVMTAAHCVDREL- 117
Cdd:COG5640     4 RRLLAALAAAALAL-ALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGPS-GQFCGGTLIAPRWVLTAAHCVDGDGp 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372 118 -TFRVVVGEHNLNQNDGTEqyVGVQKIVVHPYWNtdDVAAGYDIALLRLAQSVTLNSYVQlgvLPRAGTILANNSPCYIT 196
Cdd:COG5640    82 sDLRVVIGSTDLSTSGGTV--VKVARIVVHPDYD--PATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372 197 GWGLTRTN-GQLAQTLQQAYLPTVDYAICSSssyWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLVNGQYAVHGVTSF 274
Cdd:COG5640   155 GWGRTSEGpGSQSGTLRKADVPVVSDATCAA---YGGFDGGTMLCAGYpEGGKDACQGDSGGPLVVKDGGGWVLVGVVSW 231
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1191801372 275 VSRlGCnVTRKPTVFTRVSAYISWINNVIASN 306
Cdd:COG5640   232 GGG-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 ...
67-302 8.39e-99

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: 289.95  E-value: 8.39e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372  67 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDREL--TFRVVVGEHNLNQNDGTEQYVGVQKIV 144
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372 145 VHPYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAIC 224
Cdd:cd00190    78 VHPNYNPSTY--DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191801372 225 SSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWINNV 302
Cdd:cd00190   156 KRAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
66-299 1.32e-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: 266.47  E-value: 1.32e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372   66 RVVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDR--ELTFRVVVGEHNLNqNDGTEQYVGVQKI 143
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR---HFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLS-SGEEGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372  144 VVHPYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTR-TNGQLAQTLQQAYLPTVDYA 222
Cdd:smart00020  77 IIHPNYNPSTY--DNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191801372  223 ICSSSSYWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLvNGQYAVHGVTSFVSrlGCNVTRKPTVFTRVSAYISWI 299
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
67-299 1.15e-79

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 240.81  E-value: 1.15e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372  67 VVGGTEAQRNSWPSQISLQYRSGSswaHTCGGTLIRQNWVMTAAHCVDRELTFRVVVGEHNLNQNDGTEQYVGVQKIVVH 146
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK---HFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372 147 PYWNTDDVaaGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGqLAQTLQQAYLPTVDYAICSS 226
Cdd:pfam00089  78 PNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191801372 227 SsyWGSTVKNSMVCAGGDGvRSGCQGDSGGPLHClvNGQYaVHGVTSFVsrLGCNVTRKPTVFTRVSAYISWI 299
Cdd:pfam00089 155 A--YGGTVTDTMICAGAGG-KDACQGDSGGPLVC--SDGE-LIGIVSWG--YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
39-306 3.59e-67

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 210.66  E-value: 3.59e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372  39 SNMLRLLVVASLVLyGHSTQDFPETNARVVGGTEAQRNSWPSQISLQYRSGSSwAHTCGGTLIRQNWVMTAAHCVDREL- 117
Cdd:COG5640     4 RRLLAALAAAALAL-ALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGPS-GQFCGGTLIAPRWVLTAAHCVDGDGp 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372 118 -TFRVVVGEHNLNQNDGTEqyVGVQKIVVHPYWNtdDVAAGYDIALLRLAQSVTLNSYVQlgvLPRAGTILANNSPCYIT 196
Cdd:COG5640    82 sDLRVVIGSTDLSTSGGTV--VKVARIVVHPDYD--PATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372 197 GWGLTRTN-GQLAQTLQQAYLPTVDYAICSSssyWGSTVKNSMVCAGG-DGVRSGCQGDSGGPLHCLVNGQYAVHGVTSF 274
Cdd:COG5640   155 GWGRTSEGpGSQSGTLRKADVPVVSDATCAA---YGGFDGGTMLCAGYpEGGKDACQGDSGGPLVVKDGGGWVLVGVVSW 231
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1191801372 275 VSRlGCnVTRKPTVFTRVSAYISWINNVIASN 306
Cdd:COG5640   232 GGG-PC-AAGYPGVYTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
94-274 3.62e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 55.45  E-value: 3.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372  94 HTCGGTLIRQNWVMTAAHCVDRELT------FRVVVGehnlnQNDGTEQYVGVQKIVVHPYWnTDDVAAGYDIALLRLAQ 167
Cdd:COG3591    12 GVCTGTLIGPNLVLTAGHCVYDGAGggwatnIVFVPG-----YNGGPYGTATATRFRVPPGW-VASGDAGYDYALLRLDE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191801372 168 SVTLnsyvQLGVLP-RAGTILANNSPCYITGWGLTRTNgqlAQTLQQAylptvdyaiCSSSSYWGSTVknSMVCaggdgv 246
Cdd:COG3591    86 PLGD----TTGWLGlAFNDAPLAGEPVTIIGYPGDRPK---DLSLDCS---------GRVTGVQGNRL--SYDC------ 141
                         170       180
                  ....*....|....*....|....*...
gi 1191801372 247 rSGCQGDSGGPLHCLVNGQYAVHGVTSF 274
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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