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Conserved domains on  [gi|157821559|ref|NP_001100162|]
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chymotrypsin-like elastase family member 3B 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 ...
28-265 4.18e-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: 4.18e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559  28 VVNGEDAVPYSWPWQVSLQYekdGSFHHTCGGTLIAPDWVMTAGHCI--STSRTYQVVLGEFERGVEEGPEQVIPVNagD 105
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVysSAPSNYTVRLGSHDLSSNEGGGQVIKVK--K 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559 106 LFVHPKWNSNcvSCGNDIALVKLSRSAQLGDTVQLACLPPAGEILPNGAPCYISGWGRLSTNGPLPDKLQQALLPVVDYA 185
Cdd:cd00190   76 VIVHPNYNPS--TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559 186 HCSKWDWWGFSVKKTMVCAGGDI--QSGCNGDSGGPLNCpAENGTWQVHGVTSFVSslGCNTLKKPTVFTRVSAFNEWIE 263
Cdd:cd00190  154 ECKRAYSYGGTITDNMLCAGGLEggKDACQGDSGGPLVC-NDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQ 230

                 ..
gi 157821559 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 4.18e-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: 4.18e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559  28 VVNGEDAVPYSWPWQVSLQYekdGSFHHTCGGTLIAPDWVMTAGHCI--STSRTYQVVLGEFERGVEEGPEQVIPVNagD 105
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVysSAPSNYTVRLGSHDLSSNEGGGQVIKVK--K 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559 106 LFVHPKWNSNcvSCGNDIALVKLSRSAQLGDTVQLACLPPAGEILPNGAPCYISGWGRLSTNGPLPDKLQQALLPVVDYA 185
Cdd:cd00190   76 VIVHPNYNPS--TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559 186 HCSKWDWWGFSVKKTMVCAGGDI--QSGCNGDSGGPLNCpAENGTWQVHGVTSFVSslGCNTLKKPTVFTRVSAFNEWIE 263
Cdd:cd00190  154 ECKRAYSYGGTITDNMLCAGGLEggKDACQGDSGGPLVC-NDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQ 230

                 ..
gi 157821559 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 2.81e-89

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: 264.15  E-value: 2.81e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559    27 RVVNGEDAVPYSWPWQVSLQYekdGSFHHTCGGTLIAPDWVMTAGHCI--STSRTYQVVLGEFERGVEEgPEQVIPVNag 104
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVrgSDPSNIRVRLGSHDLSSGE-EGQVIKVS-- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559   105 DLFVHPKWNSNcvSCGNDIALVKLSRSAQLGDTVQLACLPPAGEILPNGAPCYISGWGRLS-TNGPLPDKLQQALLPVVD 183
Cdd:smart00020  75 KVIIHPNYNPS--TYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559   184 YAHCSKWDWWGFSVKKTMVCAGGDI--QSGCNGDSGGPLNCpaENGTWQVHGVTSFVSslGCNTLKKPTVFTRVSAFNEW 261
Cdd:smart00020 153 NATCRRAYSGGGAITDNMLCAGGLEggKDACQGDSGGPLVC--NDGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDW 228

                   .
gi 157821559   262 I 262
Cdd:smart00020 229 I 229
Trypsin pfam00089
Trypsin;
28-262 2.16e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.87  E-value: 2.16e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559   28 VVNGEDAVPYSWPWQVSLQYekdGSFHHTCGGTLIAPDWVMTAGHCISTSRTYQVVLGEFERGVEEGPEQVIPVNagDLF 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVE--KII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559  108 VHPKWNSNCVscGNDIALVKLSRSAQLGDTVQLACLPPAGEILPNGAPCYISGWGRLSTNGPlPDKLQQALLPVVDYAHC 187
Cdd:pfam00089  76 VHPNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157821559  188 SKwdWWGFSVKKTMVCAGGDIQSGCNGDSGGPLNCPAEngtwQVHGVTSFvsSLGCNTLKKPTVFTRVSAFNEWI 262
Cdd:pfam00089 153 RS--AYGGTVTDTMICAGAGGKDACQGDSGGPLVCSDG----ELIGIVSW--GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
18-269 6.21e-61

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 193.33  E-value: 6.21e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559  18 GQPSYNPSSRVVNGEDAVPYSWPWQVSLQYEkDGSFHHTCGGTLIAPDWVMTAGHCISTSR--TYQVVLGEFERGVEEGp 95
Cdd:COG5640   21 AAPAADAAPAIVGGTPATVGEYPWMVALQSS-NGPSGQFCGGTLIAPRWVLTAAHCVDGDGpsDLRVVIGSTDLSTSGG- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559  96 eQVIPVNagDLFVHPKWNSNcvSCGNDIALVKLSRSAqlgDTVQLACLPPAGEILPNGAPCYISGWGRLSTN-GPLPDKL 174
Cdd:COG5640   99 -TVVKVA--RIVVHPDYDPA--TPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559 175 QQALLPVVDYAHCSKwdwWGFSVKKTMVCAG---GDIQSgCNGDSGGPL--NcpaENGTWQVHGVTSFVSSlGCNTlKKP 249
Cdd:COG5640  171 RKADVPVVSDATCAA---YGGFDGGTMLCAGypeGGKDA-CQGDSGGPLvvK---DGGGWVLVGVVSWGGG-PCAA-GYP 241
                        250       260
                 ....*....|....*....|
gi 157821559 250 TVFTRVSAFNEWIEETIANN 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 4.18e-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: 4.18e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559  28 VVNGEDAVPYSWPWQVSLQYekdGSFHHTCGGTLIAPDWVMTAGHCI--STSRTYQVVLGEFERGVEEGPEQVIPVNagD 105
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVysSAPSNYTVRLGSHDLSSNEGGGQVIKVK--K 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559 106 LFVHPKWNSNcvSCGNDIALVKLSRSAQLGDTVQLACLPPAGEILPNGAPCYISGWGRLSTNGPLPDKLQQALLPVVDYA 185
Cdd:cd00190   76 VIVHPNYNPS--TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559 186 HCSKWDWWGFSVKKTMVCAGGDI--QSGCNGDSGGPLNCpAENGTWQVHGVTSFVSslGCNTLKKPTVFTRVSAFNEWIE 263
Cdd:cd00190  154 ECKRAYSYGGTITDNMLCAGGLEggKDACQGDSGGPLVC-NDNGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQ 230

                 ..
gi 157821559 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 2.81e-89

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: 264.15  E-value: 2.81e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559    27 RVVNGEDAVPYSWPWQVSLQYekdGSFHHTCGGTLIAPDWVMTAGHCI--STSRTYQVVLGEFERGVEEgPEQVIPVNag 104
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVrgSDPSNIRVRLGSHDLSSGE-EGQVIKVS-- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559   105 DLFVHPKWNSNcvSCGNDIALVKLSRSAQLGDTVQLACLPPAGEILPNGAPCYISGWGRLS-TNGPLPDKLQQALLPVVD 183
Cdd:smart00020  75 KVIIHPNYNPS--TYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559   184 YAHCSKWDWWGFSVKKTMVCAGGDI--QSGCNGDSGGPLNCpaENGTWQVHGVTSFVSslGCNTLKKPTVFTRVSAFNEW 261
Cdd:smart00020 153 NATCRRAYSGGGAITDNMLCAGGLEggKDACQGDSGGPLVC--NDGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDW 228

                   .
gi 157821559   262 I 262
Cdd:smart00020 229 I 229
Trypsin pfam00089
Trypsin;
28-262 2.16e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.87  E-value: 2.16e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559   28 VVNGEDAVPYSWPWQVSLQYekdGSFHHTCGGTLIAPDWVMTAGHCISTSRTYQVVLGEFERGVEEGPEQVIPVNagDLF 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVE--KII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559  108 VHPKWNSNCVscGNDIALVKLSRSAQLGDTVQLACLPPAGEILPNGAPCYISGWGRLSTNGPlPDKLQQALLPVVDYAHC 187
Cdd:pfam00089  76 VHPNYNPDTL--DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157821559  188 SKwdWWGFSVKKTMVCAGGDIQSGCNGDSGGPLNCPAEngtwQVHGVTSFvsSLGCNTLKKPTVFTRVSAFNEWI 262
Cdd:pfam00089 153 RS--AYGGTVTDTMICAGAGGKDACQGDSGGPLVCSDG----ELIGIVSW--GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
18-269 6.21e-61

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 193.33  E-value: 6.21e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559  18 GQPSYNPSSRVVNGEDAVPYSWPWQVSLQYEkDGSFHHTCGGTLIAPDWVMTAGHCISTSR--TYQVVLGEFERGVEEGp 95
Cdd:COG5640   21 AAPAADAAPAIVGGTPATVGEYPWMVALQSS-NGPSGQFCGGTLIAPRWVLTAAHCVDGDGpsDLRVVIGSTDLSTSGG- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559  96 eQVIPVNagDLFVHPKWNSNcvSCGNDIALVKLSRSAqlgDTVQLACLPPAGEILPNGAPCYISGWGRLSTN-GPLPDKL 174
Cdd:COG5640   99 -TVVKVA--RIVVHPDYDPA--TPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559 175 QQALLPVVDYAHCSKwdwWGFSVKKTMVCAG---GDIQSgCNGDSGGPL--NcpaENGTWQVHGVTSFVSSlGCNTlKKP 249
Cdd:COG5640  171 RKADVPVVSDATCAA---YGGFDGGTMLCAGypeGGKDA-CQGDSGGPLvvK---DGGGWVLVGVVSWGGG-PCAA-GYP 241
                        250       260
                 ....*....|....*....|
gi 157821559 250 TVFTRVSAFNEWIEETIANN 269
Cdd:COG5640  242 GVYTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
55-237 5.19e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 60.46  E-value: 5.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559  55 HTCGGTLIAPDWVMTAGHCISTSRTYQVVLG-EFERGVEEGPEQVipVNAGDLFVHPKWNSNCvSCGNDIALVKLSRSaq 133
Cdd:COG3591   12 GVCTGTLIGPNLVLTAGHCVYDGAGGGWATNiVFVPGYNGGPYGT--ATATRFRVPPGWVASG-DAGYDYALLRLDEP-- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559 134 LGDTVqlACLPPAGEILP-NGAPCYISGWGRlstngplpDKLQQALLpvvdYAHCSKWDWwgfsvkktmvcAGGDIQSGC 212
Cdd:COG3591   87 LGDTT--GWLGLAFNDAPlAGEPVTIIGYPG--------DRPKDLSL----DCSGRVTGV-----------QGNRLSYDC 141
                        170       180
                 ....*....|....*....|....*....
gi 157821559 213 N---GDSGGP-LNcpAENGTWQVHGVTSF 237
Cdd:COG3591  142 DttgGSSGSPvLD--DSDGGGRVVGVHSA 168
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
59-220 2.14e-03

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 37.40  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559   59 GTLIAPD-WVMTAGHCISTSRTYQVVLGEF-ERGVEEGPEQVIPVNAgdlfvhpkwnsncvscGNDIALVKLSRSAQLGD 136
Cdd:pfam13365   3 GFVVSSDgLVLTNAHVVDDAEEAAVELVSVvLADGREYPATVVARDP----------------DLDLALLRVSGDGRGLP 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821559  137 TVQLAclppAGEILPNGAPCYISGWgrlstngPLPDKLQQALLPVVdyahCSKWDWWGFSVKKTMVCAGGDIQSGCngdS 216
Cdd:pfam13365  67 PLPLG----DSEPLVGGERVYAVGY-------PLGGEKLSLSEGIV----SGVDEGRDGGDDGRVIQTDAALSPGS---S 128

                  ....
gi 157821559  217 GGPL 220
Cdd:pfam13365 129 GGPV 132
 
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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