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Conserved domains on  [gi|1783383267|ref|NP_001182326|]
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chymotrypsin-like elastase family member 3B precursor [Macaca mulatta]

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 ...
28-265 1.22e-93

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: 275.31  E-value: 1.22e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267  28 VVNGEDAVPYSWPWQVSLQYeknGSFHHTCGGSLIAPDWVVTAGHCISSSL--TYQVVLGDYNLAVKEGPEQVIPINSgd 105
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKK-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267 106 LFVHPLWNrlCVACGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNETPCYITGWGRLYTNGPLPDKLQRALLPVVDYE 185
Cdd:cd00190    76 VIVHPNYN--PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267 186 HCSKWNWWGSTVKKTMVCAGGDI--RSGCNGDSGGPLNCpTDDGGWQVHGVTSFVSsfGCNTQRKPTVFTRVSAFIDWIE 263
Cdd:cd00190   154 ECKRAYSYGGTITDNMLCAGGLEggKDACQGDSGGPLVC-NDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQ 230

                  ..
gi 1783383267 264 ET 265
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 ...
28-265 1.22e-93

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: 275.31  E-value: 1.22e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267  28 VVNGEDAVPYSWPWQVSLQYeknGSFHHTCGGSLIAPDWVVTAGHCISSSL--TYQVVLGDYNLAVKEGPEQVIPINSgd 105
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKK-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267 106 LFVHPLWNrlCVACGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNETPCYITGWGRLYTNGPLPDKLQRALLPVVDYE 185
Cdd:cd00190    76 VIVHPNYN--PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267 186 HCSKWNWWGSTVKKTMVCAGGDI--RSGCNGDSGGPLNCpTDDGGWQVHGVTSFVSsfGCNTQRKPTVFTRVSAFIDWIE 263
Cdd:cd00190   154 ECKRAYSYGGTITDNMLCAGGLEggKDACQGDSGGPLVC-NDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQ 230

                  ..
gi 1783383267 264 ET 265
Cdd:cd00190   231 KT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
27-262 2.41e-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: 261.84  E-value: 2.41e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267   27 RVVNGEDAVPYSWPWQVSLQYeknGSFHHTCGGSLIAPDWVVTAGHCISSSL--TYQVVLGDYNLaVKEGPEQVIPINSg 104
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRGSDpsNIRVRLGSHDL-SSGEEGQVIKVSK- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267  105 dLFVHPLWNrlCVACGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNETPCYITGWGRL-YTNGPLPDKLQRALLPVVD 183
Cdd:smart00020  76 -VIIHPNYN--PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267  184 YEHCSKWNWWGSTVKKTMVCAGGDI--RSGCNGDSGGPLNCptDDGGWQVHGVTSFVSsfGCNTQRKPTVFTRVSAFIDW 261
Cdd:smart00020 153 NATCRRAYSGGGAITDNMLCAGGLEggKDACQGDSGGPLVC--NDGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDW 228

                   .
gi 1783383267  262 I 262
Cdd:smart00020 229 I 229
Trypsin pfam00089
Trypsin;
28-262 6.25e-78

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 235.03  E-value: 6.25e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267  28 VVNGEDAVPYSWPWQVSLQYeknGSFHHTCGGSLIAPDWVVTAGHCISSSLTYQVVLGDYNLAVKEGPEQVIPINsgDLF 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVE--KII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267 108 VHPLWNRLCVacGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNETPCYITGWGRLYTNGPlPDKLQRALLPVVDYEHC 187
Cdd:pfam00089  76 VHPNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1783383267 188 SkwNWWGSTVKKTMVCAGGDIRSGCNGDSGGPLNCptddGGWQVHGVTSFvsSFGCNTQRKPTVFTRVSAFIDWI 262
Cdd:pfam00089 153 R--SAYGGTVTDTMICAGAGGKDACQGDSGGPLVC----SDGELIGIVSW--GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
18-268 1.28e-62

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 197.56  E-value: 1.28e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267  18 GQPSSHPSSRVVNGEDAVPYSWPWQVSLQYEkNGSFHHTCGGSLIAPDWVVTAGHCISSSL--TYQVVLGDYNLAVKEGp 95
Cdd:COG5640    21 AAPAADAAPAIVGGTPATVGEYPWMVALQSS-NGPSGQFCGGTLIAPRWVLTAAHCVDGDGpsDLRVVIGSTDLSTSGG- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267  96 eQVIPINsgDLFVHPLWNRlcVACGNDIALIKLSRSAqlgDAVQLASLPPAGDILPNETPCYITGWGRLYTN-GPLPDKL 174
Cdd:COG5640    99 -TVVKVA--RIVVHPDYDP--ATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267 175 QRALLPVVDYEHCskwNWWGSTVKKTMVCAGGD--IRSGCNGDSGGPL--NcptDDGGWQVHGVTSFVSSfGCNTQrKPT 250
Cdd:COG5640   171 RKADVPVVSDATC---AAYGGFDGGTMLCAGYPegGKDACQGDSGGPLvvK---DGGGWVLVGVVSWGGG-PCAAG-YPG 242
                         250
                  ....*....|....*...
gi 1783383267 251 VFTRVSAFIDWIEETIAS 268
Cdd:COG5640   243 VYTRVSAYRDWIKSTAGG 260
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
28-265 1.22e-93

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: 275.31  E-value: 1.22e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267  28 VVNGEDAVPYSWPWQVSLQYeknGSFHHTCGGSLIAPDWVVTAGHCISSSL--TYQVVLGDYNLAVKEGPEQVIPINSgd 105
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYSSApsNYTVRLGSHDLSSNEGGGQVIKVKK-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267 106 LFVHPLWNrlCVACGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNETPCYITGWGRLYTNGPLPDKLQRALLPVVDYE 185
Cdd:cd00190    76 VIVHPNYN--PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267 186 HCSKWNWWGSTVKKTMVCAGGDI--RSGCNGDSGGPLNCpTDDGGWQVHGVTSFVSsfGCNTQRKPTVFTRVSAFIDWIE 263
Cdd:cd00190   154 ECKRAYSYGGTITDNMLCAGGLEggKDACQGDSGGPLVC-NDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQ 230

                  ..
gi 1783383267 264 ET 265
Cdd:cd00190   231 KT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
27-262 2.41e-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: 261.84  E-value: 2.41e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267   27 RVVNGEDAVPYSWPWQVSLQYeknGSFHHTCGGSLIAPDWVVTAGHCISSSL--TYQVVLGDYNLaVKEGPEQVIPINSg 104
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRGSDpsNIRVRLGSHDL-SSGEEGQVIKVSK- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267  105 dLFVHPLWNrlCVACGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNETPCYITGWGRL-YTNGPLPDKLQRALLPVVD 183
Cdd:smart00020  76 -VIIHPNYN--PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267  184 YEHCSKWNWWGSTVKKTMVCAGGDI--RSGCNGDSGGPLNCptDDGGWQVHGVTSFVSsfGCNTQRKPTVFTRVSAFIDW 261
Cdd:smart00020 153 NATCRRAYSGGGAITDNMLCAGGLEggKDACQGDSGGPLVC--NDGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDW 228

                   .
gi 1783383267  262 I 262
Cdd:smart00020 229 I 229
Trypsin pfam00089
Trypsin;
28-262 6.25e-78

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 235.03  E-value: 6.25e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267  28 VVNGEDAVPYSWPWQVSLQYeknGSFHHTCGGSLIAPDWVVTAGHCISSSLTYQVVLGDYNLAVKEGPEQVIPINsgDLF 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVE--KII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267 108 VHPLWNRLCVacGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNETPCYITGWGRLYTNGPlPDKLQRALLPVVDYEHC 187
Cdd:pfam00089  76 VHPNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1783383267 188 SkwNWWGSTVKKTMVCAGGDIRSGCNGDSGGPLNCptddGGWQVHGVTSFvsSFGCNTQRKPTVFTRVSAFIDWI 262
Cdd:pfam00089 153 R--SAYGGTVTDTMICAGAGGKDACQGDSGGPLVC----SDGELIGIVSW--GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
18-268 1.28e-62

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 197.56  E-value: 1.28e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267  18 GQPSSHPSSRVVNGEDAVPYSWPWQVSLQYEkNGSFHHTCGGSLIAPDWVVTAGHCISSSL--TYQVVLGDYNLAVKEGp 95
Cdd:COG5640    21 AAPAADAAPAIVGGTPATVGEYPWMVALQSS-NGPSGQFCGGTLIAPRWVLTAAHCVDGDGpsDLRVVIGSTDLSTSGG- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267  96 eQVIPINsgDLFVHPLWNRlcVACGNDIALIKLSRSAqlgDAVQLASLPPAGDILPNETPCYITGWGRLYTN-GPLPDKL 174
Cdd:COG5640    99 -TVVKVA--RIVVHPDYDP--ATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267 175 QRALLPVVDYEHCskwNWWGSTVKKTMVCAGGD--IRSGCNGDSGGPL--NcptDDGGWQVHGVTSFVSSfGCNTQrKPT 250
Cdd:COG5640   171 RKADVPVVSDATC---AAYGGFDGGTMLCAGYPegGKDACQGDSGGPLvvK---DGGGWVLVGVVSWGGG-PCAAG-YPG 242
                         250
                  ....*....|....*...
gi 1783383267 251 VFTRVSAFIDWIEETIAS 268
Cdd:COG5640   243 VYTRVSAYRDWIKSTAGG 260
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
55-268 2.62e-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: 2.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267  55 HTCGGSLIAPDWVVTAGHCISSSLT------YQVVLGdYNLAvKEGPEQVIpinsgDLFVHPLWnRLCVACGNDIALIKL 128
Cdd:COG3591    12 GVCTGTLIGPNLVLTAGHCVYDGAGggwatnIVFVPG-YNGG-PYGTATAT-----RFRVPPGW-VASGDAGYDYALLRL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783383267 129 SRSaqLGDAVQLASLPPAGDILPNEtPCYITGWGRlytngplpDKLQRALLpvvdYEHCSKWNWWGSTVkkTMVCaggdi 208
Cdd:COG3591    84 DEP--LGDTTGWLGLAFNDAPLAGE-PVTIIGYPG--------DRPKDLSL----DCSGRVTGVQGNRL--SYDC----- 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1783383267 209 rSGCNGDSGGP-LNcpTDDGGWQVHGVTSFVSSFGCNTqrkptvFTRV-SAFIDWIEETIAS 268
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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