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Conserved domains on  [gi|76443665|ref|NP_001029047|]
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chymotrypsin-C 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

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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 ...
30-265 1.01e-94

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: 278.01  E-value: 1.01e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665  30 VVGGEDAVPNSWPWQVSLQYlrdDTWRHTCGGSLITTSHVLTAAHCIN--TNLTYRVGLGKYNLTVEDEEGSVYaEVDTI 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSSNEGGGQVI-KVKKV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665 108 YVHEKWNRLLLWNDIAIIKLAEPVELSDTIQVACIPEQDSLLPGDYPCYVTGWGRLWTNGPIAEVLQQGLQPIVNHTTCS 187
Cdd:cd00190  77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 76443665 188 RLDWWFIKVRETMVCAGG-DGVISACNGDSGGPLNCPVeDGLWQVHGIVSFGSsrGCNTYKKPVVFTRVSAYIDWIKEK 265
Cdd:cd00190 157 RAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
30-265 1.01e-94

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: 278.01  E-value: 1.01e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665  30 VVGGEDAVPNSWPWQVSLQYlrdDTWRHTCGGSLITTSHVLTAAHCIN--TNLTYRVGLGKYNLTVEDEEGSVYaEVDTI 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSSNEGGGQVI-KVKKV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665 108 YVHEKWNRLLLWNDIAIIKLAEPVELSDTIQVACIPEQDSLLPGDYPCYVTGWGRLWTNGPIAEVLQQGLQPIVNHTTCS 187
Cdd:cd00190  77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 76443665 188 RLDWWFIKVRETMVCAGG-DGVISACNGDSGGPLNCPVeDGLWQVHGIVSFGSsrGCNTYKKPVVFTRVSAYIDWIKEK 265
Cdd:cd00190 157 RAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
29-262 7.25e-94

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: 276.10  E-value: 7.25e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665     29 RVVGGEDAVPNSWPWQVSLQYlrdDTWRHTCGGSLITTSHVLTAAHCIN--TNLTYRVGLGKYNLTVEDEEgsVYAEVDT 106
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRgsDPSNIRVRLGSHDLSSGEEG--QVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665    107 IYVHEKWNRLLLWNDIAIIKLAEPVELSDTIQVACIPEQDSLLPGDYPCYVTGWGRL-WTNGPIAEVLQQGLQPIVNHTT 185
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 76443665    186 CSRLDWWFIKVRETMVCAGG-DGVISACNGDSGGPLNCpvEDGLWQVHGIVSFGSsrGCNTYKKPVVFTRVSAYIDWI 262
Cdd:smart00020 156 CRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVC--NDGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
30-262 3.87e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 223.09  E-value: 3.87e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665    30 VVGGEDAVPNSWPWQVSLQYlrdDTWRHTCGGSLITTSHVLTAAHCINTNLTYRVGLGKYNLTVeDEEGSVYAEVDTIYV 109
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVL-REGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665   110 HEKWNRLLLWNDIAIIKLAEPVELSDTIQVACIPEQDSLLPGDYPCYVTGWGRLWTNGPiAEVLQQGLQPIVNHTTCSRl 189
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRS- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 76443665   190 dWWFIKVRETMVCAGGDGViSACNGDSGGPLNCPVEdglwQVHGIVSFGssRGCNTYKKPVVFTRVSAYIDWI 262
Cdd:pfam00089 155 -AYGGTVTDTMICAGAGGK-DACQGDSGGPLVCSDG----ELIGIVSWG--YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
2-266 1.10e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 189.86  E-value: 1.10e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665   2 LGITVLAAILACASSCGDPTFPpnlSARVVGGEDAVPNSWPWQVSLQYlRDDTWRHTCGGSLITTSHVLTAAHCIN--TN 79
Cdd:COG5640   6 LLAALAAAALALALAAAPAADA---APAIVGGTPATVGEYPWMVALQS-SNGPSGQFCGGTLIAPRWVLTAAHCVDgdGP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665  80 LTYRVGLGKYNLTveDEEGSVyAEVDTIYVHEKWNRLLLWNDIAIIKLAEPVELSDTIQVAciPEQDSLLPGDyPCYVTG 159
Cdd:COG5640  82 SDLRVVIGSTDLS--TSGGTV-VKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAPLA--TSADAAAPGT-PATVAG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665 160 WGRLWTN-GPIAEVLQQGLQPIVNHTTCSRLDWWfikVRETMVCAGG-DGVISACNGDSGGPLncpV--EDGLWQVHGIV 235
Cdd:COG5640 156 WGRTSEGpGSQSGTLRKADVPVVSDATCAAYGGF---DGGTMLCAGYpEGGKDACQGDSGGPL---VvkDGGGWVLVGVV 229
                       250       260       270
                ....*....|....*....|....*....|.
gi 76443665 236 SFGSSrGCNTyKKPVVFTRVSAYIDWIKEKI 266
Cdd:COG5640 230 SWGGG-PCAA-GYPGVYTRVSAYRDWIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
30-265 1.01e-94

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: 278.01  E-value: 1.01e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665  30 VVGGEDAVPNSWPWQVSLQYlrdDTWRHTCGGSLITTSHVLTAAHCIN--TNLTYRVGLGKYNLTVEDEEGSVYaEVDTI 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSSNEGGGQVI-KVKKV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665 108 YVHEKWNRLLLWNDIAIIKLAEPVELSDTIQVACIPEQDSLLPGDYPCYVTGWGRLWTNGPIAEVLQQGLQPIVNHTTCS 187
Cdd:cd00190  77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 76443665 188 RLDWWFIKVRETMVCAGG-DGVISACNGDSGGPLNCPVeDGLWQVHGIVSFGSsrGCNTYKKPVVFTRVSAYIDWIKEK 265
Cdd:cd00190 157 RAYSYGGTITDNMLCAGGlEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWGS--GCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
29-262 7.25e-94

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: 276.10  E-value: 7.25e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665     29 RVVGGEDAVPNSWPWQVSLQYlrdDTWRHTCGGSLITTSHVLTAAHCIN--TNLTYRVGLGKYNLTVEDEEgsVYAEVDT 106
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRgsDPSNIRVRLGSHDLSSGEEG--QVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665    107 IYVHEKWNRLLLWNDIAIIKLAEPVELSDTIQVACIPEQDSLLPGDYPCYVTGWGRL-WTNGPIAEVLQQGLQPIVNHTT 185
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 76443665    186 CSRLDWWFIKVRETMVCAGG-DGVISACNGDSGGPLNCpvEDGLWQVHGIVSFGSsrGCNTYKKPVVFTRVSAYIDWI 262
Cdd:smart00020 156 CRRAYSGGGAITDNMLCAGGlEGGKDACQGDSGGPLVC--NDGRWVLVGIVSWGS--GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
30-262 3.87e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 223.09  E-value: 3.87e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665    30 VVGGEDAVPNSWPWQVSLQYlrdDTWRHTCGGSLITTSHVLTAAHCINTNLTYRVGLGKYNLTVeDEEGSVYAEVDTIYV 109
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVL-REGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665   110 HEKWNRLLLWNDIAIIKLAEPVELSDTIQVACIPEQDSLLPGDYPCYVTGWGRLWTNGPiAEVLQQGLQPIVNHTTCSRl 189
Cdd:pfam00089  77 HPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRS- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 76443665   190 dWWFIKVRETMVCAGGDGViSACNGDSGGPLNCPVEdglwQVHGIVSFGssRGCNTYKKPVVFTRVSAYIDWI 262
Cdd:pfam00089 155 -AYGGTVTDTMICAGAGGK-DACQGDSGGPLVCSDG----ELIGIVSWG--YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
2-266 1.10e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 189.86  E-value: 1.10e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665   2 LGITVLAAILACASSCGDPTFPpnlSARVVGGEDAVPNSWPWQVSLQYlRDDTWRHTCGGSLITTSHVLTAAHCIN--TN 79
Cdd:COG5640   6 LLAALAAAALALALAAAPAADA---APAIVGGTPATVGEYPWMVALQS-SNGPSGQFCGGTLIAPRWVLTAAHCVDgdGP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665  80 LTYRVGLGKYNLTveDEEGSVyAEVDTIYVHEKWNRLLLWNDIAIIKLAEPVELSDTIQVAciPEQDSLLPGDyPCYVTG 159
Cdd:COG5640  82 SDLRVVIGSTDLS--TSGGTV-VKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAPLA--TSADAAAPGT-PATVAG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665 160 WGRLWTN-GPIAEVLQQGLQPIVNHTTCSRLDWWfikVRETMVCAGG-DGVISACNGDSGGPLncpV--EDGLWQVHGIV 235
Cdd:COG5640 156 WGRTSEGpGSQSGTLRKADVPVVSDATCAAYGGF---DGGTMLCAGYpEGGKDACQGDSGGPL---VvkDGGGWVLVGVV 229
                       250       260       270
                ....*....|....*....|....*....|.
gi 76443665 236 SFGSSrGCNTyKKPVVFTRVSAYIDWIKEKI 266
Cdd:COG5640 230 SWGGG-PCAA-GYPGVYTRVSAYRDWIKSTA 258
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
49-245 6.91e-08

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 51.60  E-value: 6.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665  49 YLRDDTWRHTCGGSLITTSHVLTAAHCIN--------TNLTYRVGlgkYNLTVEDEEGSVYAEVDTIYVHEKWNRLllwn 120
Cdd:COG3591   4 RLETDGGGGVCTGTLIGPNLVLTAGHCVYdgagggwaTNIVFVPG---YNGGPYGTATATRFRVPPGWVASGDAGY---- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76443665 121 DIAIIKLAEPveLSDTIQVACIPEQDSLLPGDyPCYVTGWGR-------LWTNGPIAEVLQQGLqpivnHTTCsrldwwf 193
Cdd:COG3591  77 DYALLRLDEP--LGDTTGWLGLAFNDAPLAGE-PVTIIGYPGdrpkdlsLDCSGRVTGVQGNRL-----SYDC------- 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 76443665 194 ikvretmvcaggdgviSACNGDSGGP-LNcpVEDGLWQVHGIVSFGSSRGCNT 245
Cdd:COG3591 142 ----------------DTTGGSSGSPvLD--DSDGGGRVVGVHSAGGADRANT 176
 
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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