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Conserved domains on  [gi|6978803|ref|NP_036685|]
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chymotrypsin-like elastase family member 2A precursor [Rattus norvegicus]

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

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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 2.64e-104

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: 302.66  E-value: 2.64e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803   31 VVGGQEASPNSWPWQVSLQYlssGKWHHTCGGSLVANNWVLTAAHCISNS--RTYRVLLGRHSLSTSESGSLAVQVSKLV 108
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803  109 VHEKWNAQklSNGNDIALVKLASPVALTSKIQTACLPPAGTILPNNYPCYVTGWGRLQTNGATPDVLQQGRLLVVDYATC 188
Cdd:cd00190  78 VHPNYNPS--TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803  189 SSASWWGSSVKTNMVCAGG-DGVTSSCNGDSGGPLNCQaSNGQWQVHGIVSFGStlGCNYPRKPSVFTRVSNYIDWINSV 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 2.64e-104

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: 302.66  E-value: 2.64e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803   31 VVGGQEASPNSWPWQVSLQYlssGKWHHTCGGSLVANNWVLTAAHCISNS--RTYRVLLGRHSLSTSESGSLAVQVSKLV 108
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803  109 VHEKWNAQklSNGNDIALVKLASPVALTSKIQTACLPPAGTILPNNYPCYVTGWGRLQTNGATPDVLQQGRLLVVDYATC 188
Cdd:cd00190  78 VHPNYNPS--TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803  189 SSASWWGSSVKTNMVCAGG-DGVTSSCNGDSGGPLNCQaSNGQWQVHGIVSFGStlGCNYPRKPSVFTRVSNYIDWINSV 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 1.20e-98

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: 288.04  E-value: 1.20e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803      30 RVVGGQEASPNSWPWQVSLQYlssGKWHHTCGGSLVANNWVLTAAHCISNS--RTYRVLLGRHSLSTSESGsLAVQVSKL 107
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLSSGEEG-QVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803     108 VVHEKWNAQklSNGNDIALVKLASPVALTSKIQTACLPPAGTILPNNYPCYVTGWGRLQ-TNGATPDVLQQGRLLVVDYA 186
Cdd:smart00020  77 IIHPNYNPS--TYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6978803     187 TCSSASWWGSSVKTNMVCAGG-DGVTSSCNGDSGGPLNCQasNGQWQVHGIVSFGStlGCNYPRKPSVFTRVSNYIDWI 264
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
31-264 5.69e-78

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 235.41  E-value: 5.69e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803     31 VVGGQEASPNSWPWQVSLQYLSSgkwHHTCGGSLVANNWVLTAAHCISNSRTYRVLLGRHSLSTSESGSLAVQVSKLVVH 110
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSG---KHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803    111 EKWNAQKLsnGNDIALVKLASPVALTSKIQTACLPPAGTILPNNYPCYVTGWGRLQTNGaTPDVLQQGRLLVVDYATCSS 190
Cdd:pfam00089  78 PNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6978803    191 AswWGSSVKTNMVCAGGDGVtSSCNGDSGGPLNCqaSNGqwQVHGIVSFGstLGCNYPRKPSVFTRVSNYIDWI 264
Cdd:pfam00089 155 A--YGGTVTDTMICAGAGGK-DACQGDSGGPLVC--SDG--ELIGIVSWG--YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-271 1.59e-72

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 222.99  E-value: 1.59e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803    1 MIRTLLLSALVAGALSCGYPTYEVQHDVSRVVGGQEASPNSWPWQVSLQYlSSGKWHHTCGGSLVANNWVLTAAHCISNS 80
Cdd:COG5640   1 MRRRRLLAALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQS-SNGPSGQFCGGTLIAPRWVLTAAHCVDGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803   81 R--TYRVLLGRHSLSTSEsGSLaVQVSKLVVHEKWNAQklSNGNDIALVKLASPValtSKIQTACLPPAGTILPNNYPCY 158
Cdd:COG5640  80 GpsDLRVVIGSTDLSTSG-GTV-VKVARIVVHPDYDPA--TPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPAT 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803  159 VTGWGRLQTN-GATPDVLQQGRLLVVDYATCSSaswWGSSVKTNMVCAGG-DGVTSSCNGDSGGPLnCQASNGQWQVHGI 236
Cdd:COG5640 153 VAGWGRTSEGpGSQSGTLRKADVPVVSDATCAA---YGGFDGGTMLCAGYpEGGKDACQGDSGGPL-VVKDGGGWVLVGV 228
                       250       260       270
                ....*....|....*....|....*....|....*
gi 6978803  237 VSFGSTlGCnYPRKPSVFTRVSNYIDWINSVIAKN 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 2.64e-104

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: 302.66  E-value: 2.64e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803   31 VVGGQEASPNSWPWQVSLQYlssGKWHHTCGGSLVANNWVLTAAHCISNS--RTYRVLLGRHSLSTSESGSLAVQVSKLV 108
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803  109 VHEKWNAQklSNGNDIALVKLASPVALTSKIQTACLPPAGTILPNNYPCYVTGWGRLQTNGATPDVLQQGRLLVVDYATC 188
Cdd:cd00190  78 VHPNYNPS--TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803  189 SSASWWGSSVKTNMVCAGG-DGVTSSCNGDSGGPLNCQaSNGQWQVHGIVSFGStlGCNYPRKPSVFTRVSNYIDWINSV 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 1.20e-98

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: 288.04  E-value: 1.20e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803      30 RVVGGQEASPNSWPWQVSLQYlssGKWHHTCGGSLVANNWVLTAAHCISNS--RTYRVLLGRHSLSTSESGsLAVQVSKL 107
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDLSSGEEG-QVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803     108 VVHEKWNAQklSNGNDIALVKLASPVALTSKIQTACLPPAGTILPNNYPCYVTGWGRLQ-TNGATPDVLQQGRLLVVDYA 186
Cdd:smart00020  77 IIHPNYNPS--TYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6978803     187 TCSSASWWGSSVKTNMVCAGG-DGVTSSCNGDSGGPLNCQasNGQWQVHGIVSFGStlGCNYPRKPSVFTRVSNYIDWI 264
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
31-264 5.69e-78

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 235.41  E-value: 5.69e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803     31 VVGGQEASPNSWPWQVSLQYLSSgkwHHTCGGSLVANNWVLTAAHCISNSRTYRVLLGRHSLSTSESGSLAVQVSKLVVH 110
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSG---KHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803    111 EKWNAQKLsnGNDIALVKLASPVALTSKIQTACLPPAGTILPNNYPCYVTGWGRLQTNGaTPDVLQQGRLLVVDYATCSS 190
Cdd:pfam00089  78 PNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6978803    191 AswWGSSVKTNMVCAGGDGVtSSCNGDSGGPLNCqaSNGqwQVHGIVSFGstLGCNYPRKPSVFTRVSNYIDWI 264
Cdd:pfam00089 155 A--YGGTVTDTMICAGAGGK-DACQGDSGGPLVC--SDG--ELIGIVSWG--YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-271 1.59e-72

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 222.99  E-value: 1.59e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803    1 MIRTLLLSALVAGALSCGYPTYEVQHDVSRVVGGQEASPNSWPWQVSLQYlSSGKWHHTCGGSLVANNWVLTAAHCISNS 80
Cdd:COG5640   1 MRRRRLLAALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQS-SNGPSGQFCGGTLIAPRWVLTAAHCVDGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803   81 R--TYRVLLGRHSLSTSEsGSLaVQVSKLVVHEKWNAQklSNGNDIALVKLASPValtSKIQTACLPPAGTILPNNYPCY 158
Cdd:COG5640  80 GpsDLRVVIGSTDLSTSG-GTV-VKVARIVVHPDYDPA--TPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPAT 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803  159 VTGWGRLQTN-GATPDVLQQGRLLVVDYATCSSaswWGSSVKTNMVCAGG-DGVTSSCNGDSGGPLnCQASNGQWQVHGI 236
Cdd:COG5640 153 VAGWGRTSEGpGSQSGTLRKADVPVVSDATCAA---YGGFDGGTMLCAGYpEGGKDACQGDSGGPL-VVKDGGGWVLVGV 228
                       250       260       270
                ....*....|....*....|....*....|....*
gi 6978803  237 VSFGSTlGCnYPRKPSVFTRVSNYIDWINSVIAKN 271
Cdd:COG5640 229 VSWGGG-PC-AAGYPGVYTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
58-242 3.01e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 58.15  E-value: 3.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803   58 HTCGGSLVANNWVLTAAHCISNSRT------YRVLLGRHSlstseSGSLAVQVSKLVVHEKWnAQKLSNGNDIALVKLAS 131
Cdd:COG3591  12 GVCTGTLIGPNLVLTAGHCVYDGAGggwatnIVFVPGYNG-----GPYGTATATRFRVPPGW-VASGDAGYDYALLRLDE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978803  132 PVALTskiqTACLPPAGTILP-NNYPCYVTGWGrlqtnGATPDVLQQgrllvvdYATCSSASWWGSSVKTNmvcaggdgv 210
Cdd:COG3591  86 PLGDT----TGWLGLAFNDAPlAGEPVTIIGYP-----GDRPKDLSL-------DCSGRVTGVQGNRLSYD--------- 140
                       170       180       190
                ....*....|....*....|....*....|..
gi 6978803  211 TSSCNGDSGGPLnCQASNGQWQVHGIVSFGST 242
Cdd:COG3591 141 CDTTGGSSGSPV-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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