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Conserved domains on  [gi|317373457|sp|P08861|]
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RecName: Full=Chymotrypsin-like elastase family member 3B; AltName: Full=Elastase IIIB; AltName: Full=Elastase-3B; AltName: Full=Protease E; Flags: Precursor

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 ...
29-266 3.88e-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: 279.16  E-value: 3.88e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457  29 VVNGEDAVPYSWPWQVSLQYeksGSFYHTCGGSLIAPDWVVTAGHCISSS--RTYQVVLGEYDRAVKEGPEQVIPINSgd 106
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKK-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457 107 LFVHPLWNRScvACGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNETPCYITGWGRLYTNGPLPDKLQEALLPVVDYE 186
Cdd:cd00190   76 VIVHPNYNPS--TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457 187 HCSRWNWWGSSVKKTMVCAGGDI--RSGCNGDSGGPLNCPTeDGGWQVHGVTSFVSafGCNTRRKPTVFTRVSAFIDWIE 264
Cdd:cd00190  154 ECKRAYSYGGTITDNMLCAGGLEggKDACQGDSGGPLVCND-NGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQ 230

                 ..
gi 317373457 265 ET 266
Cdd:cd00190  231 KT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
29-266 3.88e-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: 279.16  E-value: 3.88e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457  29 VVNGEDAVPYSWPWQVSLQYeksGSFYHTCGGSLIAPDWVVTAGHCISSS--RTYQVVLGEYDRAVKEGPEQVIPINSgd 106
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKK-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457 107 LFVHPLWNRScvACGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNETPCYITGWGRLYTNGPLPDKLQEALLPVVDYE 186
Cdd:cd00190   76 VIVHPNYNPS--TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457 187 HCSRWNWWGSSVKKTMVCAGGDI--RSGCNGDSGGPLNCPTeDGGWQVHGVTSFVSafGCNTRRKPTVFTRVSAFIDWIE 264
Cdd:cd00190  154 ECKRAYSYGGTITDNMLCAGGLEggKDACQGDSGGPLVCND-NGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQ 230

                 ..
gi 317373457 265 ET 266
Cdd:cd00190  231 KT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
28-263 3.66e-90

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: 3.66e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457    28 RVVNGEDAVPYSWPWQVSLQYeksGSFYHTCGGSLIAPDWVVTAGHCISSS--RTYQVVLGEYDRaVKEGPEQVIPINSg 105
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDL-SSGEEGQVIKVSK- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457   106 dLFVHPLWNRScvACGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNETPCYITGWGRL-YTNGPLPDKLQEALLPVVD 184
Cdd:smart00020  76 -VIIHPNYNPS--TYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457   185 YEHCSRWNWWGSSVKKTMVCAGGDI--RSGCNGDSGGPLNCptEDGGWQVHGVTSFVSafGCNTRRKPTVFTRVSAFIDW 262
Cdd:smart00020 153 NATCRRAYSGGGAITDNMLCAGGLEggKDACQGDSGGPLVC--NDGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDW 228

                   .
gi 317373457   263 I 263
Cdd:smart00020 229 I 229
Trypsin pfam00089
Trypsin;
29-263 5.64e-80

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 240.42  E-value: 5.64e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457   29 VVNGEDAVPYSWPWQVSLQYeksGSFYHTCGGSLIAPDWVVTAGHCISSSRTYQVVLGEYDRAVKEGPEQVIPINsgDLF 108
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVE--KII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457  109 VHPLWNRSCVacGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNETPCYITGWGRLYTNGPlPDKLQEALLPVVDYEHC 188
Cdd:pfam00089  76 VHPNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 317373457  189 SRwnWWGSSVKKTMVCAGGDIRSGCNGDSGGPLNCPTEdggwQVHGVTSFVsaFGCNTRRKPTVFTRVSAFIDWI 263
Cdd:pfam00089 153 RS--AYGGTVTDTMICAGAGGKDACQGDSGGPLVCSDG----ELIGIVSWG--YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
19-269 5.06e-63

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 198.72  E-value: 5.06e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457  19 GPPSSRPSSRVVNGEDAVPYSWPWQVSLQYEkSGSFYHTCGGSLIAPDWVVTAGHCISSSR--TYQVVLGEYDRAVKEGp 96
Cdd:COG5640   21 AAPAADAAPAIVGGTPATVGEYPWMVALQSS-NGPSGQFCGGTLIAPRWVLTAAHCVDGDGpsDLRVVIGSTDLSTSGG- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457  97 eQVIPINsgDLFVHPLWNRScvACGNDIALIKLSRSAqlgDAVQLASLPPAGDILPNETPCYITGWGRLYTN-GPLPDKL 175
Cdd:COG5640   99 -TVVKVA--RIVVHPDYDPA--TPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457 176 QEALLPVVDYEHCSRwnwWGSSVKKTMVCAGGD--IRSGCNGDSGGPLNCPTeDGGWQVHGVTSFVSAfGCNTrRKPTVF 253
Cdd:COG5640  171 RKADVPVVSDATCAA---YGGFDGGTMLCAGYPegGKDACQGDSGGPLVVKD-GGGWVLVGVVSWGGG-PCAA-GYPGVY 244
                        250
                 ....*....|....*.
gi 317373457 254 TRVSAFIDWIEETIAS 269
Cdd:COG5640  245 TRVSAYRDWIKSTAGG 260
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
29-266 3.88e-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: 279.16  E-value: 3.88e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457  29 VVNGEDAVPYSWPWQVSLQYeksGSFYHTCGGSLIAPDWVVTAGHCISSS--RTYQVVLGEYDRAVKEGPEQVIPINSgd 106
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSapSNYTVRLGSHDLSSNEGGGQVIKVKK-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457 107 LFVHPLWNRScvACGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNETPCYITGWGRLYTNGPLPDKLQEALLPVVDYE 186
Cdd:cd00190   76 VIVHPNYNPS--TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457 187 HCSRWNWWGSSVKKTMVCAGGDI--RSGCNGDSGGPLNCPTeDGGWQVHGVTSFVSafGCNTRRKPTVFTRVSAFIDWIE 264
Cdd:cd00190  154 ECKRAYSYGGTITDNMLCAGGLEggKDACQGDSGGPLVCND-NGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQ 230

                 ..
gi 317373457 265 ET 266
Cdd:cd00190  231 KT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
28-263 3.66e-90

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: 3.66e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457    28 RVVNGEDAVPYSWPWQVSLQYeksGSFYHTCGGSLIAPDWVVTAGHCISSS--RTYQVVLGEYDRaVKEGPEQVIPINSg 105
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRGSdpSNIRVRLGSHDL-SSGEEGQVIKVSK- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457   106 dLFVHPLWNRScvACGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNETPCYITGWGRL-YTNGPLPDKLQEALLPVVD 184
Cdd:smart00020  76 -VIIHPNYNPS--TYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457   185 YEHCSRWNWWGSSVKKTMVCAGGDI--RSGCNGDSGGPLNCptEDGGWQVHGVTSFVSafGCNTRRKPTVFTRVSAFIDW 262
Cdd:smart00020 153 NATCRRAYSGGGAITDNMLCAGGLEggKDACQGDSGGPLVC--NDGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDW 228

                   .
gi 317373457   263 I 263
Cdd:smart00020 229 I 229
Trypsin pfam00089
Trypsin;
29-263 5.64e-80

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 240.42  E-value: 5.64e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457   29 VVNGEDAVPYSWPWQVSLQYeksGSFYHTCGGSLIAPDWVVTAGHCISSSRTYQVVLGEYDRAVKEGPEQVIPINsgDLF 108
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVE--KII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457  109 VHPLWNRSCVacGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNETPCYITGWGRLYTNGPlPDKLQEALLPVVDYEHC 188
Cdd:pfam00089  76 VHPNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 317373457  189 SRwnWWGSSVKKTMVCAGGDIRSGCNGDSGGPLNCPTEdggwQVHGVTSFVsaFGCNTRRKPTVFTRVSAFIDWI 263
Cdd:pfam00089 153 RS--AYGGTVTDTMICAGAGGKDACQGDSGGPLVCSDG----ELIGIVSWG--YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
19-269 5.06e-63

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 198.72  E-value: 5.06e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457  19 GPPSSRPSSRVVNGEDAVPYSWPWQVSLQYEkSGSFYHTCGGSLIAPDWVVTAGHCISSSR--TYQVVLGEYDRAVKEGp 96
Cdd:COG5640   21 AAPAADAAPAIVGGTPATVGEYPWMVALQSS-NGPSGQFCGGTLIAPRWVLTAAHCVDGDGpsDLRVVIGSTDLSTSGG- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457  97 eQVIPINsgDLFVHPLWNRScvACGNDIALIKLSRSAqlgDAVQLASLPPAGDILPNETPCYITGWGRLYTN-GPLPDKL 175
Cdd:COG5640   99 -TVVKVA--RIVVHPDYDPA--TPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457 176 QEALLPVVDYEHCSRwnwWGSSVKKTMVCAGGD--IRSGCNGDSGGPLNCPTeDGGWQVHGVTSFVSAfGCNTrRKPTVF 253
Cdd:COG5640  171 RKADVPVVSDATCAA---YGGFDGGTMLCAGYPegGKDACQGDSGGPLVVKD-GGGWVLVGVVSWGGG-PCAA-GYPGVY 244
                        250
                 ....*....|....*.
gi 317373457 254 TRVSAFIDWIEETIAS 269
Cdd:COG5640  245 TRVSAYRDWIKSTAGG 260
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
56-269 9.74e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 59.69  E-value: 9.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457  56 HTCGGSLIAPDWVVTAGHCISSSRT------YQVVLGeYDRAvKEGPEQVIpinsgDLFVHPLWNRSCvACGNDIALIKL 129
Cdd:COG3591   12 GVCTGTLIGPNLVLTAGHCVYDGAGggwatnIVFVPG-YNGG-PYGTATAT-----RFRVPPGWVASG-DAGYDYALLRL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373457 130 SRSaqLGDAVQLASLPPAGDILPNEtPCYITGWGRlytngplpDKLQEALLpvvdYEHCSRWNWWGSSVkkTMVCaggdi 209
Cdd:COG3591   84 DEP--LGDTTGWLGLAFNDAPLAGE-PVTIIGYPG--------DRPKDLSL----DCSGRVTGVQGNRL--SYDC----- 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 317373457 210 rSGCNGDSGGP-LNcpTEDGGWQVHGVTSFVSAFGCNTrrkptvFTRV-SAFIDWIEETIAS 269
Cdd:COG3591  142 -DTTGGSSGSPvLD--DSDGGGRVVGVHSAGGADRANT------GVRLtSAIVAALRAWASA 194
 
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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