NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|13385916|ref|NP_080695|]
View 

chymotrypsin-like elastase family member 3B precursor [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

show extra options »

Show site features     Horizontal zoom: ×

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 6.27e-98

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: 286.48  E-value: 6.27e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916  28 VVNGEEAVPHSWPWQVSLQYekdGSFHHTCGGSLITPDWVLTAGHCI--STSRTYQVVLGEHERGVEEGQEQVIPINagD 105
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVysSAPSNYTVRLGSHDLSSNEGGGQVIKVK--K 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916 106 LFVHPKWNSmcVSCGNDIALVKLSRSAQLGDAVQLACLPPAGEILPNGAPCYISGWGRLSTNGPLPDKLQQALLPVVDYE 185
Cdd:cd00190  76 VIVHPNYNP--STYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916 186 HCSRWNWWGLSVKTTMVCAGGDI--QSGCNGDSGGPLNCpADNGTWQVHGVTSFVSslGCNTLRKPTVFTRVSAFIDWIE 263
Cdd:cd00190 154 ECKRAYSYGGTITDNMLCAGGLEggKDACQGDSGGPLVC-NDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQ 230

                ..
gi 13385916 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 6.27e-98

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: 286.48  E-value: 6.27e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916  28 VVNGEEAVPHSWPWQVSLQYekdGSFHHTCGGSLITPDWVLTAGHCI--STSRTYQVVLGEHERGVEEGQEQVIPINagD 105
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVysSAPSNYTVRLGSHDLSSNEGGGQVIKVK--K 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916 106 LFVHPKWNSmcVSCGNDIALVKLSRSAQLGDAVQLACLPPAGEILPNGAPCYISGWGRLSTNGPLPDKLQQALLPVVDYE 185
Cdd:cd00190  76 VIVHPNYNP--STYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916 186 HCSRWNWWGLSVKTTMVCAGGDI--QSGCNGDSGGPLNCpADNGTWQVHGVTSFVSslGCNTLRKPTVFTRVSAFIDWIE 263
Cdd:cd00190 154 ECKRAYSYGGTITDNMLCAGGLEggKDACQGDSGGPLVC-NDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQ 230

                ..
gi 13385916 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 1.00e-91

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: 270.70  E-value: 1.00e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916     27 RVVNGEEAVPHSWPWQVSLQYekdGSFHHTCGGSLITPDWVLTAGHCI--STSRTYQVVLGEHERGVEEGQeQVIPINag 104
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVrgSDPSNIRVRLGSHDLSSGEEG-QVIKVS-- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916    105 DLFVHPKWNSMcvSCGNDIALVKLSRSAQLGDAVQLACLPPAGEILPNGAPCYISGWGRLS-TNGPLPDKLQQALLPVVD 183
Cdd:smart00020  75 KVIIHPNYNPS--TYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916    184 YEHCSRWNWWGLSVKTTMVCAGGDI--QSGCNGDSGGPLNCpaDNGTWQVHGVTSFVSslGCNTLRKPTVFTRVSAFIDW 261
Cdd:smart00020 153 NATCRRAYSGGGAITDNMLCAGGLEggKDACQGDSGGPLVC--NDGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDW 228

                   .
gi 13385916    262 I 262
Cdd:smart00020 229 I 229
Trypsin pfam00089
Trypsin;
28-262 1.22e-79

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 239.65  E-value: 1.22e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916    28 VVNGEEAVPHSWPWQVSLQYekdGSFHHTCGGSLITPDWVLTAGHCISTSRTYQVVLGEHERGVEEGQEQVIPINagDLF 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVE--KII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916   108 VHPKWNSMCVscGNDIALVKLSRSAQLGDAVQLACLPPAGEILPNGAPCYISGWGRLSTNGPlPDKLQQALLPVVDYEHC 187
Cdd:pfam00089  76 VHPNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13385916   188 SRwnWWGLSVKTTMVCAGGDIQSGCNGDSGGPLNCpaDNGTwqVHGVTSFvsSLGCNTLRKPTVFTRVSAFIDWI 262
Cdd:pfam00089 153 RS--AYGGTVTDTMICAGAGGKDACQGDSGGPLVC--SDGE--LIGIVSW--GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
18-269 2.60e-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: 2.60e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916  18 GQPSHNPSSRVVNGEEAVPHSWPWQVSLQYEkDGSFHHTCGGSLITPDWVLTAGHCISTSR--TYQVVLGEHERGVEEGQ 95
Cdd:COG5640  21 AAPAADAAPAIVGGTPATVGEYPWMVALQSS-NGPSGQFCGGTLIAPRWVLTAAHCVDGDGpsDLRVVIGSTDLSTSGGT 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916  96 EqvipINAGDLFVHPKWNSmcVSCGNDIALVKLSRSAqlgDAVQLACLPPAGEILPNGAPCYISGWGRLSTN-GPLPDKL 174
Cdd:COG5640 100 V----VKVARIVVHPDYDP--ATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTL 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916 175 QQALLPVVDYEHCSRwnwWGLSVKTTMVCAG---GDIQSgCNGDSGGPL--NcpaDNGTWQVHGVTSFVSSlGCNTlRKP 249
Cdd:COG5640 171 RKADVPVVSDATCAA---YGGFDGGTMLCAGypeGGKDA-CQGDSGGPLvvK---DGGGWVLVGVVSWGGG-PCAA-GYP 241
                       250       260
                ....*....|....*....|
gi 13385916 250 TVFTRVSAFIDWIEETIANN 269
Cdd:COG5640 242 GVYTRVSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
28-265 6.27e-98

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: 286.48  E-value: 6.27e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916  28 VVNGEEAVPHSWPWQVSLQYekdGSFHHTCGGSLITPDWVLTAGHCI--STSRTYQVVLGEHERGVEEGQEQVIPINagD 105
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVysSAPSNYTVRLGSHDLSSNEGGGQVIKVK--K 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916 106 LFVHPKWNSmcVSCGNDIALVKLSRSAQLGDAVQLACLPPAGEILPNGAPCYISGWGRLSTNGPLPDKLQQALLPVVDYE 185
Cdd:cd00190  76 VIVHPNYNP--STYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916 186 HCSRWNWWGLSVKTTMVCAGGDI--QSGCNGDSGGPLNCpADNGTWQVHGVTSFVSslGCNTLRKPTVFTRVSAFIDWIE 263
Cdd:cd00190 154 ECKRAYSYGGTITDNMLCAGGLEggKDACQGDSGGPLVC-NDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQ 230

                ..
gi 13385916 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 1.00e-91

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: 270.70  E-value: 1.00e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916     27 RVVNGEEAVPHSWPWQVSLQYekdGSFHHTCGGSLITPDWVLTAGHCI--STSRTYQVVLGEHERGVEEGQeQVIPINag 104
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVrgSDPSNIRVRLGSHDLSSGEEG-QVIKVS-- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916    105 DLFVHPKWNSMcvSCGNDIALVKLSRSAQLGDAVQLACLPPAGEILPNGAPCYISGWGRLS-TNGPLPDKLQQALLPVVD 183
Cdd:smart00020  75 KVIIHPNYNPS--TYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916    184 YEHCSRWNWWGLSVKTTMVCAGGDI--QSGCNGDSGGPLNCpaDNGTWQVHGVTSFVSslGCNTLRKPTVFTRVSAFIDW 261
Cdd:smart00020 153 NATCRRAYSGGGAITDNMLCAGGLEggKDACQGDSGGPLVC--NDGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDW 228

                   .
gi 13385916    262 I 262
Cdd:smart00020 229 I 229
Trypsin pfam00089
Trypsin;
28-262 1.22e-79

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 239.65  E-value: 1.22e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916    28 VVNGEEAVPHSWPWQVSLQYekdGSFHHTCGGSLITPDWVLTAGHCISTSRTYQVVLGEHERGVEEGQEQVIPINagDLF 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVE--KII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916   108 VHPKWNSMCVscGNDIALVKLSRSAQLGDAVQLACLPPAGEILPNGAPCYISGWGRLSTNGPlPDKLQQALLPVVDYEHC 187
Cdd:pfam00089  76 VHPNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13385916   188 SRwnWWGLSVKTTMVCAGGDIQSGCNGDSGGPLNCpaDNGTwqVHGVTSFvsSLGCNTLRKPTVFTRVSAFIDWI 262
Cdd:pfam00089 153 RS--AYGGTVTDTMICAGAGGKDACQGDSGGPLVC--SDGE--LIGIVSW--GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
18-269 2.60e-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: 2.60e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916  18 GQPSHNPSSRVVNGEEAVPHSWPWQVSLQYEkDGSFHHTCGGSLITPDWVLTAGHCISTSR--TYQVVLGEHERGVEEGQ 95
Cdd:COG5640  21 AAPAADAAPAIVGGTPATVGEYPWMVALQSS-NGPSGQFCGGTLIAPRWVLTAAHCVDGDGpsDLRVVIGSTDLSTSGGT 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916  96 EqvipINAGDLFVHPKWNSmcVSCGNDIALVKLSRSAqlgDAVQLACLPPAGEILPNGAPCYISGWGRLSTN-GPLPDKL 174
Cdd:COG5640 100 V----VKVARIVVHPDYDP--ATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTL 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916 175 QQALLPVVDYEHCSRwnwWGLSVKTTMVCAG---GDIQSgCNGDSGGPL--NcpaDNGTWQVHGVTSFVSSlGCNTlRKP 249
Cdd:COG5640 171 RKADVPVVSDATCAA---YGGFDGGTMLCAGypeGGKDA-CQGDSGGPLvvK---DGGGWVLVGVVSWGGG-PCAA-GYP 241
                       250       260
                ....*....|....*....|
gi 13385916 250 TVFTRVSAFIDWIEETIANN 269
Cdd:COG5640 242 GVYTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
55-268 1.20e-08

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 53.53  E-value: 1.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916  55 HTCGGSLITPDWVLTAGHCISTSRT------YQVVLGEHERgvEEGQEQVIpinagDLFVHPKWNSMCvSCGNDIALVKL 128
Cdd:COG3591  12 GVCTGTLIGPNLVLTAGHCVYDGAGggwatnIVFVPGYNGG--PYGTATAT-----RFRVPPGWVASG-DAGYDYALLRL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385916 129 SRSaqLGDAVqlACLPPAGEILP-NGAPCYISGWGRlstngplpDKLQQALLpvvdYEHCSRWNWwglsvkttmvcAGGD 207
Cdd:COG3591  84 DEP--LGDTT--GWLGLAFNDAPlAGEPVTIIGYPG--------DRPKDLSL----DCSGRVTGV-----------QGNR 136
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13385916 208 IQSGCN---GDSGGP-LNcpADNGTWQVHGVTSFVSSLGCNTlrkptvFTRV-SAFIDWIEETIAN 268
Cdd:COG3591 137 LSYDCDttgGSSGSPvLD--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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH