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Conserved domains on  [gi|6978667|ref|NP_037224|]
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chymase 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 ...
22-243 5.69e-66

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: 204.43  E-value: 5.69e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667   22 IIGGTECIPHSRPYMAYLEIVTSDNYlsaCSGFLIRRNFVLTAAHC----AGRSITVLLGAHNKTYKEDTWQKLEVEKQF 97
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHF---CGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667   98 IHPNYDKRLVLHDIMLLKLKEKAKLTLGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPASDTLQEVKMRLQEPQSCKH 177
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6978667  178 FTSFQ---HKSQLCVGNPKKMQNVYKGDSGGPLLC----AGIAQGIASYVHPNAKP--PAVFTRISHYRPWINKI 243
Cdd:cd00190 158 AYSYGgtiTDNMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
22-243 5.69e-66

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: 204.43  E-value: 5.69e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667   22 IIGGTECIPHSRPYMAYLEIVTSDNYlsaCSGFLIRRNFVLTAAHC----AGRSITVLLGAHNKTYKEDTWQKLEVEKQF 97
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHF---CGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667   98 IHPNYDKRLVLHDIMLLKLKEKAKLTLGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPASDTLQEVKMRLQEPQSCKH 177
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6978667  178 FTSFQ---HKSQLCVGNPKKMQNVYKGDSGGPLLC----AGIAQGIASYVHPNAKP--PAVFTRISHYRPWINKI 243
Cdd:cd00190 158 AYSYGgtiTDNMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
21-240 2.61e-61

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: 192.12  E-value: 2.61e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667      21 EIIGGTECIPHSRPYMAYLEIVTSDNYlsaCSGFLIRRNFVLTAAHC----AGRSITVLLGAHNKTYKEDTwQKLEVEKQ 96
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHF---CGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEEG-QVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667      97 FIHPNYDKRLVLHDIMLLKLKEKAKLTLGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPA-SDTLQEVKMRLQEPQSC 175
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6978667     176 KHFTSFQHK---SQLCVGNPKKMQNVYKGDSGGPLLC---AGIAQGIASYVHPNAKP--PAVFTRISHYRPWI 240
Cdd:smart00020 157 RRAYSGGGAitdNMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
22-240 1.12e-52

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 169.93  E-value: 1.12e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667     22 IIGGTECIPHSRPYMAYLEIVTSdnyLSACSGFLIRRNFVLTAAHCA--GRSITVLLGAHNKTYKEDTWQKLEVEKQFIH 99
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSG---KHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667    100 PNYDKRLVLHDIMLLKLKEKAKLTLGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPaSDTLQEVKMRLQEPQSCKHFT 179
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6978667    180 SFQH-KSQLCVGNPKKMQNvyKGDSGGPLLCA-GIAQGIASYVHPNAKP--PAVFTRISHYRPWI 240
Cdd:pfam00089 157 GGTVtDTMICAGAGGKDAC--QGDSGGPLVCSdGELIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
16-247 5.99e-41

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 140.94  E-value: 5.99e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667   16 STKAGEIIGGTECIPHSRPYMAYLEIVTSDNYLSaCSGFLIRRNFVLTAAHC----AGRSITVLLGAHNKTykEDTWQKL 91
Cdd:COG5640  25 ADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQF-CGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLS--TSGGTVV 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667   92 EVEKQFIHPNYDKRLVLHDI--------MLlklkekakltlGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPA-SDTL 162
Cdd:COG5640 102 KVARIVVHPDYDPATPGNDIallklatpVP-----------GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSqSGTL 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667  163 QEVKMRLQEPQSCKHFTSFQHKSQLCVGNPKKMQNVYKGDSGGPLL--CAGIAQ--GIASYVHPNAKP--PAVFTRISHY 236
Cdd:COG5640 171 RKADVPVVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkDGGGWVlvGVVSWGGGPCAAgyPGVYTRVSAY 250
                       250
                ....*....|.
gi 6978667  237 RPWINKILREN 247
Cdd:COG5640 251 RDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
22-243 5.69e-66

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: 204.43  E-value: 5.69e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667   22 IIGGTECIPHSRPYMAYLEIVTSDNYlsaCSGFLIRRNFVLTAAHC----AGRSITVLLGAHNKTYKEDTWQKLEVEKQF 97
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHF---CGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667   98 IHPNYDKRLVLHDIMLLKLKEKAKLTLGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPASDTLQEVKMRLQEPQSCKH 177
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6978667  178 FTSFQ---HKSQLCVGNPKKMQNVYKGDSGGPLLC----AGIAQGIASYVHPNAKP--PAVFTRISHYRPWINKI 243
Cdd:cd00190 158 AYSYGgtiTDNMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
21-240 2.61e-61

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: 192.12  E-value: 2.61e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667      21 EIIGGTECIPHSRPYMAYLEIVTSDNYlsaCSGFLIRRNFVLTAAHC----AGRSITVLLGAHNKTYKEDTwQKLEVEKQ 96
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHF---CGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEEG-QVIKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667      97 FIHPNYDKRLVLHDIMLLKLKEKAKLTLGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPA-SDTLQEVKMRLQEPQSC 175
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6978667     176 KHFTSFQHK---SQLCVGNPKKMQNVYKGDSGGPLLC---AGIAQGIASYVHPNAKP--PAVFTRISHYRPWI 240
Cdd:smart00020 157 RRAYSGGGAitdNMLCAGGLEGGKDACQGDSGGPLVCndgRWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
22-240 1.12e-52

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 169.93  E-value: 1.12e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667     22 IIGGTECIPHSRPYMAYLEIVTSdnyLSACSGFLIRRNFVLTAAHCA--GRSITVLLGAHNKTYKEDTWQKLEVEKQFIH 99
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSG---KHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667    100 PNYDKRLVLHDIMLLKLKEKAKLTLGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPaSDTLQEVKMRLQEPQSCKHFT 179
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6978667    180 SFQH-KSQLCVGNPKKMQNvyKGDSGGPLLCA-GIAQGIASYVHPNAKP--PAVFTRISHYRPWI 240
Cdd:pfam00089 157 GGTVtDTMICAGAGGKDAC--QGDSGGPLVCSdGELIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
16-247 5.99e-41

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 140.94  E-value: 5.99e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667   16 STKAGEIIGGTECIPHSRPYMAYLEIVTSDNYLSaCSGFLIRRNFVLTAAHC----AGRSITVLLGAHNKTykEDTWQKL 91
Cdd:COG5640  25 ADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQF-CGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLS--TSGGTVV 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667   92 EVEKQFIHPNYDKRLVLHDI--------MLlklkekakltlGVGTLPLSANFNFIPPGRMCRAVGWGRTNVNEPA-SDTL 162
Cdd:COG5640 102 KVARIVVHPDYDPATPGNDIallklatpVP-----------GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSqSGTL 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978667  163 QEVKMRLQEPQSCKHFTSFQHKSQLCVGNPKKMQNVYKGDSGGPLL--CAGIAQ--GIASYVHPNAKP--PAVFTRISHY 236
Cdd:COG5640 171 RKADVPVVSDATCAAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkDGGGWVlvGVVSWGGGPCAAgyPGVYTRVSAY 250
                       250
                ....*....|.
gi 6978667  237 RPWINKILREN 247
Cdd:COG5640 251 RDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
42-103 1.57e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 47.36  E-value: 1.57e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6978667   42 VTSDNYLSACSGFLIRRNFVLTAAHC--------AGRSITVLLGAHNKTYKEDTWQKLEVEKQFIH---PNYD 103
Cdd:COG3591   5 LETDGGGGVCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNGGPYGTATATRFRVPPGWVAsgdAGYD 77
 
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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