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Conserved domains on  [gi|6681297|ref|NP_031945|]
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chymotrypsin-like elastase family member 2A preproprotein [Mus musculus]

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

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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 ...
31-267 7.71e-101

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: 293.80  E-value: 7.71e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297   31 VVGGQEATPNTWPWQVSLQVlssGRWRHNCGGSLVANNWVLTAAHCLSNYQ--TYRVLLGAHSLSNPGAGSAAVQVSKLV 108
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297  109 VHQRWNSQNVGNgyDIALIKLASPVTLSKNIQTACLPPAGTILPRNYVCYVTGWGLLQTNGNSPDTLRQGRLLVVDYATC 188
Cdd:cd00190  78 VHPNYNPSTYDN--DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297  189 SSASWWGSSVKSSMVCAGG-DGVTSSCNGDSGGPLNCRaSNGQWQVHGIVSFGSslGCNYPRKPSVFTRVSNYIDWINSV 267
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCN-DNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
31-267 7.71e-101

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: 293.80  E-value: 7.71e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297   31 VVGGQEATPNTWPWQVSLQVlssGRWRHNCGGSLVANNWVLTAAHCLSNYQ--TYRVLLGAHSLSNPGAGSAAVQVSKLV 108
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297  109 VHQRWNSQNVGNgyDIALIKLASPVTLSKNIQTACLPPAGTILPRNYVCYVTGWGLLQTNGNSPDTLRQGRLLVVDYATC 188
Cdd:cd00190  78 VHPNYNPSTYDN--DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297  189 SSASWWGSSVKSSMVCAGG-DGVTSSCNGDSGGPLNCRaSNGQWQVHGIVSFGSslGCNYPRKPSVFTRVSNYIDWINSV 267
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCN-DNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
30-264 2.13e-95

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: 279.95  E-value: 2.13e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297      30 RVVGGQEATPNTWPWQVSLQVlssGRWRHNCGGSLVANNWVLTAAHCLSNY--QTYRVLLGAHSLSNPGaGSAAVQVSKL 107
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLSSGE-EGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297     108 VVHQRWNSQNVGNgyDIALIKLASPVTLSKNIQTACLPPAGTILPRNYVCYVTGWGLLQ-TNGNSPDTLRQGRLLVVDYA 186
Cdd:smart00020  77 IIHPNYNPSTYDN--DIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6681297     187 TCSSASWWGSSVKSSMVCAGG-DGVTSSCNGDSGGPLNCRasNGQWQVHGIVSFGSslGCNYPRKPSVFTRVSNYIDWI 264
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
31-264 3.33e-74

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 225.78  E-value: 3.33e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297     31 VVGGQEATPNTWPWQVSLQVLSSGrwrHNCGGSLVANNWVLTAAHCLSNYQTYRVLLGAHSLSNPGAGSAAVQVSKLVVH 110
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK---HFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297    111 QRWNSQNVGNgyDIALIKLASPVTLSKNIQTACLPPAGTILPRNYVCYVTGWGLLQTNGnSPDTLRQGRLLVVDYATCSS 190
Cdd:pfam00089  78 PNYNPDTLDN--DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6681297    191 AswWGSSVKSSMVCAGGDGVtSSCNGDSGGPLNCraSNGqwQVHGIVSFGssLGCNYPRKPSVFTRVSNYIDWI 264
Cdd:pfam00089 155 A--YGGTVTDTMICAGAGGK-DACQGDSGGPLVC--SDG--ELIGIVSWG--YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-271 6.07e-72

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 221.45  E-value: 6.07e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297    1 MIRTLLLSALVAGALSCGYPTYEVEDDVSRVVGGQEATPNTWPWQVSLQVlSSGRWRHNCGGSLVANNWVLTAAHCLSNY 80
Cdd:COG5640   1 MRRRRLLAALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQS-SNGPSGQFCGGTLIAPRWVLTAAHCVDGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297   81 Q--TYRVLLGAHSLSNPGAgsAAVQVSKLVVHQRWNSQNvgNGYDIALIKLASPVTlskNIQTACLPPAGTILPRNYVCY 158
Cdd:COG5640  80 GpsDLRVVIGSTDLSTSGG--TVVKVARIVVHPDYDPAT--PGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPAT 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297  159 VTGWGLLQTN-GNSPDTLRQGRLLVVDYATCSSaswWGSSVKSSMVCAGG-DGVTSSCNGDSGGPLnCRASNGQWQVHGI 236
Cdd:COG5640 153 VAGWGRTSEGpGSQSGTLRKADVPVVSDATCAA---YGGFDGGTMLCAGYpEGGKDACQGDSGGPL-VVKDGGGWVLVGV 228
                       250       260       270
                ....*....|....*....|....*....|....*
gi 6681297  237 VSFGSSlGCnYPRKPSVFTRVSNYIDWINSVMARN 271
Cdd:COG5640 229 VSWGGG-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 ...
31-267 7.71e-101

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: 293.80  E-value: 7.71e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297   31 VVGGQEATPNTWPWQVSLQVlssGRWRHNCGGSLVANNWVLTAAHCLSNYQ--TYRVLLGAHSLSNPGAGSAAVQVSKLV 108
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297  109 VHQRWNSQNVGNgyDIALIKLASPVTLSKNIQTACLPPAGTILPRNYVCYVTGWGLLQTNGNSPDTLRQGRLLVVDYATC 188
Cdd:cd00190  78 VHPNYNPSTYDN--DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297  189 SSASWWGSSVKSSMVCAGG-DGVTSSCNGDSGGPLNCRaSNGQWQVHGIVSFGSslGCNYPRKPSVFTRVSNYIDWINSV 267
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCN-DNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
30-264 2.13e-95

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: 279.95  E-value: 2.13e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297      30 RVVGGQEATPNTWPWQVSLQVlssGRWRHNCGGSLVANNWVLTAAHCLSNY--QTYRVLLGAHSLSNPGaGSAAVQVSKL 107
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLSSGE-EGQVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297     108 VVHQRWNSQNVGNgyDIALIKLASPVTLSKNIQTACLPPAGTILPRNYVCYVTGWGLLQ-TNGNSPDTLRQGRLLVVDYA 186
Cdd:smart00020  77 IIHPNYNPSTYDN--DIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6681297     187 TCSSASWWGSSVKSSMVCAGG-DGVTSSCNGDSGGPLNCRasNGQWQVHGIVSFGSslGCNYPRKPSVFTRVSNYIDWI 264
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
31-264 3.33e-74

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 225.78  E-value: 3.33e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297     31 VVGGQEATPNTWPWQVSLQVLSSGrwrHNCGGSLVANNWVLTAAHCLSNYQTYRVLLGAHSLSNPGAGSAAVQVSKLVVH 110
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK---HFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297    111 QRWNSQNVGNgyDIALIKLASPVTLSKNIQTACLPPAGTILPRNYVCYVTGWGLLQTNGnSPDTLRQGRLLVVDYATCSS 190
Cdd:pfam00089  78 PNYNPDTLDN--DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6681297    191 AswWGSSVKSSMVCAGGDGVtSSCNGDSGGPLNCraSNGqwQVHGIVSFGssLGCNYPRKPSVFTRVSNYIDWI 264
Cdd:pfam00089 155 A--YGGTVTDTMICAGAGGK-DACQGDSGGPLVC--SDG--ELIGIVSWG--YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-271 6.07e-72

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 221.45  E-value: 6.07e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297    1 MIRTLLLSALVAGALSCGYPTYEVEDDVSRVVGGQEATPNTWPWQVSLQVlSSGRWRHNCGGSLVANNWVLTAAHCLSNY 80
Cdd:COG5640   1 MRRRRLLAALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQS-SNGPSGQFCGGTLIAPRWVLTAAHCVDGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297   81 Q--TYRVLLGAHSLSNPGAgsAAVQVSKLVVHQRWNSQNvgNGYDIALIKLASPVTlskNIQTACLPPAGTILPRNYVCY 158
Cdd:COG5640  80 GpsDLRVVIGSTDLSTSGG--TVVKVARIVVHPDYDPAT--PGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPAT 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297  159 VTGWGLLQTN-GNSPDTLRQGRLLVVDYATCSSaswWGSSVKSSMVCAGG-DGVTSSCNGDSGGPLnCRASNGQWQVHGI 236
Cdd:COG5640 153 VAGWGRTSEGpGSQSGTLRKADVPVVSDATCAA---YGGFDGGTMLCAGYpEGGKDACQGDSGGPL-VVKDGGGWVLVGV 228
                       250       260       270
                ....*....|....*....|....*....|....*
gi 6681297  237 VSFGSSlGCnYPRKPSVFTRVSNYIDWINSVMARN 271
Cdd:COG5640 229 VSWGGG-PC-AAGYPGVYTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
51-242 4.90e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 60.46  E-value: 4.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297   51 LSSGRWRHNCGGSLVANNWVLTAAHCLSNYQT------YRVLLGAHslsnpGAGSAAVQVSKLVVHQRWnSQNVGNGYDI 124
Cdd:COG3591   5 LETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGggwatnIVFVPGYN-----GGPYGTATATRFRVPPGW-VASGDAGYDY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681297  125 ALIKLASPVTLSK---NIQTACLPPAGTILprnyvcYVTGWGllqtnGNSPDTLRQgrllvvdYATCSSASWWGSSVksS 201
Cdd:COG3591  79 ALLRLDEPLGDTTgwlGLAFNDAPLAGEPV------TIIGYP-----GDRPKDLSL-------DCSGRVTGVQGNRL--S 138
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 6681297  202 MVCaggdgvtSSCNGDSGGPLnCRASNGQWQVHGIVSFGSS 242
Cdd:COG3591 139 YDC-------DTTGGSSGSPV-LDDSDGGGRVVGVHSAGGA 171
 
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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