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Conserved domains on  [gi|1653962449|ref|NP_056933|]
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chymotrypsin-like elastase family member 2B preproprotein [Homo sapiens]

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 ...
31-265 9.17e-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: 278.39  E-value: 9.17e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449  31 GGEEARPNSWPWQVSLQYSSngqWYHTCGGSLIANSWVLTAAHCISSSGI--YRVMLGQHNLYVAESGSLAVSVSKIVVH 108
Cdd:cd00190     3 GGSEAKIGSFPWQVSLQYTG---GRHFCGGSLISPRWVLTAAHCVYSSAPsnYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449 109 KDWNSDqvSKGNDIALLKLANPVSLTDKIQLACLPPAGTILPNNYPCYVTGWGRLQTNGALPDDLKQGQLLVVDYATCSS 188
Cdd:cd00190    80 PNYNPS--TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1653962449 189 SGWWGSTVKTNMICAGG-DGVICTCNGDSGGPLNCQaSDGRWEVHGIgslTS-VLGCNYYYKPSIFTRVSNYNDWINSV 265
Cdd:cd00190   158 AYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCN-DNGRGVLVGI---VSwGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
31-265 9.17e-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: 278.39  E-value: 9.17e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449  31 GGEEARPNSWPWQVSLQYSSngqWYHTCGGSLIANSWVLTAAHCISSSGI--YRVMLGQHNLYVAESGSLAVSVSKIVVH 108
Cdd:cd00190     3 GGSEAKIGSFPWQVSLQYTG---GRHFCGGSLISPRWVLTAAHCVYSSAPsnYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449 109 KDWNSDqvSKGNDIALLKLANPVSLTDKIQLACLPPAGTILPNNYPCYVTGWGRLQTNGALPDDLKQGQLLVVDYATCSS 188
Cdd:cd00190    80 PNYNPS--TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1653962449 189 SGWWGSTVKTNMICAGG-DGVICTCNGDSGGPLNCQaSDGRWEVHGIgslTS-VLGCNYYYKPSIFTRVSNYNDWINSV 265
Cdd:cd00190   158 AYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCN-DNGRGVLVGI---VSwGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
28-262 1.72e-88

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: 262.23  E-value: 1.72e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449   28 RMLGGEEARPNSWPWQVSLQYSSngqWYHTCGGSLIANSWVLTAAHCISSSGI--YRVMLGQHNLYVAESGsLAVSVSKI 105
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG---GRHFCGGSLISPRWVLTAAHCVRGSDPsnIRVRLGSHDLSSGEEG-QVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449  106 VVHKDWNSDqvSKGNDIALLKLANPVSLTDKIQLACLPPAGTILPNNYPCYVTGWGRLQ-TNGALPDDLKQGQLLVVDYA 184
Cdd:smart00020  77 IIHPNYNPS--TYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449  185 TCSSSGWWGSTVKTNMICAGG-DGVICTCNGDSGGPLNCQasDGRWEVHGIgslTS-VLGCNYYYKPSIFTRVSNYNDWI 262
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCN--DGRWVLVGI---VSwGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
31-262 8.36e-74

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 224.63  E-value: 8.36e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449  31 GGEEARPNSWPWQVSLQYSSNGqwyHTCGGSLIANSWVLTAAHCISSSGIYRVMLGQHNLYVAESGSLAVSVSKIVVHKD 110
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLQLSSGK---HFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449 111 WNSDqvSKGNDIALLKLANPVSLTDKIQLACLPPAGTILPNNYPCYVTGWGRLQTNGaLPDDLKQGQLLVVDYATCSSSg 190
Cdd:pfam00089  80 YNPD--TLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSA- 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1653962449 191 wWGSTVKTNMICAGGDGViCTCNGDSGGPLNCqaSDGrwEVHGIgsLTSVLGCNYYYKPSIFTRVSNYNDWI 262
Cdd:pfam00089 156 -YGGTVTDTMICAGAGGK-DACQGDSGGPLVC--SDG--ELIGI--VSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-269 2.90e-62

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 196.79  E-value: 2.90e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449   1 MIRTLLLSTLVAGALSCGVST-YAPDMS-RMLGGEEARPNSWPWQVSLQySSNGQWYHTCGGSLIANSWVLTAAHCISSS 78
Cdd:COG5640     1 MRRRRLLAALAAAALALALAAaPAADAApAIVGGTPATVGEYPWMVALQ-SSNGPSGQFCGGTLIAPRWVLTAAHCVDGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449  79 GI--YRVMLGQHNLyvAESGSLAVSVSKIVVHKDWNSdqVSKGNDIALLKLANPVsltDKIQLACLPPAGTILPNNYPCY 156
Cdd:COG5640    80 GPsdLRVVIGSTDL--STSGGTVVKVARIVVHPDYDP--ATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPAT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449 157 VTGWGRLQTN-GALPDDLKQGQLLVVDYATCSSsgwWGSTVKTNMICAGG-DGVICTCNGDSGGPLnCQASDGRWEVHGI 234
Cdd:COG5640   153 VAGWGRTSEGpGSQSGTLRKADVPVVSDATCAA---YGGFDGGTMLCAGYpEGGKDACQGDSGGPL-VVKDGGGWVLVGV 228
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1653962449 235 GSlTSVLGCNYYYkPSIFTRVSNYNDWINSVIANN 269
Cdd:COG5640   229 VS-WGGGPCAAGY-PGVYTRVSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
31-265 9.17e-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: 278.39  E-value: 9.17e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449  31 GGEEARPNSWPWQVSLQYSSngqWYHTCGGSLIANSWVLTAAHCISSSGI--YRVMLGQHNLYVAESGSLAVSVSKIVVH 108
Cdd:cd00190     3 GGSEAKIGSFPWQVSLQYTG---GRHFCGGSLISPRWVLTAAHCVYSSAPsnYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449 109 KDWNSDqvSKGNDIALLKLANPVSLTDKIQLACLPPAGTILPNNYPCYVTGWGRLQTNGALPDDLKQGQLLVVDYATCSS 188
Cdd:cd00190    80 PNYNPS--TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1653962449 189 SGWWGSTVKTNMICAGG-DGVICTCNGDSGGPLNCQaSDGRWEVHGIgslTS-VLGCNYYYKPSIFTRVSNYNDWINSV 265
Cdd:cd00190   158 AYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCN-DNGRGVLVGI---VSwGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
28-262 1.72e-88

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: 262.23  E-value: 1.72e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449   28 RMLGGEEARPNSWPWQVSLQYSSngqWYHTCGGSLIANSWVLTAAHCISSSGI--YRVMLGQHNLYVAESGsLAVSVSKI 105
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG---GRHFCGGSLISPRWVLTAAHCVRGSDPsnIRVRLGSHDLSSGEEG-QVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449  106 VVHKDWNSDqvSKGNDIALLKLANPVSLTDKIQLACLPPAGTILPNNYPCYVTGWGRLQ-TNGALPDDLKQGQLLVVDYA 184
Cdd:smart00020  77 IIHPNYNPS--TYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449  185 TCSSSGWWGSTVKTNMICAGG-DGVICTCNGDSGGPLNCQasDGRWEVHGIgslTS-VLGCNYYYKPSIFTRVSNYNDWI 262
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCN--DGRWVLVGI---VSwGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
31-262 8.36e-74

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 224.63  E-value: 8.36e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449  31 GGEEARPNSWPWQVSLQYSSNGqwyHTCGGSLIANSWVLTAAHCISSSGIYRVMLGQHNLYVAESGSLAVSVSKIVVHKD 110
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLQLSSGK---HFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449 111 WNSDqvSKGNDIALLKLANPVSLTDKIQLACLPPAGTILPNNYPCYVTGWGRLQTNGaLPDDLKQGQLLVVDYATCSSSg 190
Cdd:pfam00089  80 YNPD--TLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSA- 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1653962449 191 wWGSTVKTNMICAGGDGViCTCNGDSGGPLNCqaSDGrwEVHGIgsLTSVLGCNYYYKPSIFTRVSNYNDWI 262
Cdd:pfam00089 156 -YGGTVTDTMICAGAGGK-DACQGDSGGPLVC--SDG--ELIGI--VSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-269 2.90e-62

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 196.79  E-value: 2.90e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449   1 MIRTLLLSTLVAGALSCGVST-YAPDMS-RMLGGEEARPNSWPWQVSLQySSNGQWYHTCGGSLIANSWVLTAAHCISSS 78
Cdd:COG5640     1 MRRRRLLAALAAAALALALAAaPAADAApAIVGGTPATVGEYPWMVALQ-SSNGPSGQFCGGTLIAPRWVLTAAHCVDGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449  79 GI--YRVMLGQHNLyvAESGSLAVSVSKIVVHKDWNSdqVSKGNDIALLKLANPVsltDKIQLACLPPAGTILPNNYPCY 156
Cdd:COG5640    80 GPsdLRVVIGSTDL--STSGGTVVKVARIVVHPDYDP--ATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPAT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449 157 VTGWGRLQTN-GALPDDLKQGQLLVVDYATCSSsgwWGSTVKTNMICAGG-DGVICTCNGDSGGPLnCQASDGRWEVHGI 234
Cdd:COG5640   153 VAGWGRTSEGpGSQSGTLRKADVPVVSDATCAA---YGGFDGGTMLCAGYpEGGKDACQGDSGGPL-VVKDGGGWVLVGV 228
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1653962449 235 GSlTSVLGCNYYYkPSIFTRVSNYNDWINSVIANN 269
Cdd:COG5640   229 VS-WGGGPCAAGY-PGVYTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
56-234 3.03e-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: 3.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449  56 HTCGGSLIANSWVLTAAHCISSSG------IYRVMLGQHNlyvaeSGSLAVSVSKIVVHKDWNSDQvSKGNDIALLKLAN 129
Cdd:COG3591    12 GVCTGTLIGPNLVLTAGHCVYDGAgggwatNIVFVPGYNG-----GPYGTATATRFRVPPGWVASG-DAGYDYALLRLDE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653962449 130 PVSLTdkiqLACLPPAGTILP-NNYPCYVTGWGRlqtngalpDDLKQGQLlvvdYATCSSSGWWGSTVKTNmiCAggdgv 208
Cdd:COG3591    86 PLGDT----TGWLGLAFNDAPlAGEPVTIIGYPG--------DRPKDLSL----DCSGRVTGVQGNRLSYD--CD----- 142
                         170       180
                  ....*....|....*....|....*.
gi 1653962449 209 icTCNGDSGGPLnCQASDGRWEVHGI 234
Cdd:COG3591   143 --TTGGSSGSPV-LDDSDGGGRVVGV 165
 
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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