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Conserved domains on  [gi|119616067|gb|EAW95661|]
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chymotrypsinogen B2 [Homo sapiens]

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 ...
34-259 6.12e-103

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: 298.81  E-value: 6.12e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067  34 IVNGEDAVPGSWPWQVSLQDKTGFHFCGGSLISEDWVVTAAHC---GVRTSDVVVAGEFDQGSDEENIQVLKIAKVFKNP 110
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCvysSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067 111 KFSILTVNNDITLLKLATPARFSQTVSAVCLPSADDDFPAGTLCATTGWGKTKYNANkTPDKLQQAALPLLSNAECKK-- 188
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNAECKRay 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119616067 189 SWGRRITDVMICAGAS--GVSSCMGDSGGPLVCQKDGAWTLVGIVSWGSRTCSTTTPAVYARVTKLIPWVQKI 259
Cdd:cd00190  160 SYGGTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
34-259 6.12e-103

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: 298.81  E-value: 6.12e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067  34 IVNGEDAVPGSWPWQVSLQDKTGFHFCGGSLISEDWVVTAAHC---GVRTSDVVVAGEFDQGSDEENIQVLKIAKVFKNP 110
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCvysSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067 111 KFSILTVNNDITLLKLATPARFSQTVSAVCLPSADDDFPAGTLCATTGWGKTKYNANkTPDKLQQAALPLLSNAECKK-- 188
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNAECKRay 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119616067 189 SWGRRITDVMICAGAS--GVSSCMGDSGGPLVCQKDGAWTLVGIVSWGSRTCSTTTPAVYARVTKLIPWVQKI 259
Cdd:cd00190  160 SYGGTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
33-256 9.21e-101

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: 293.04  E-value: 9.21e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067    33 RIVNGEDAVPGSWPWQVSLQDKTGFHFCGGSLISEDWVVTAAHC---GVRTSDVVVAGEFDQGSDEENiQVLKIAKVFKN 109
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCvrgSDPSNIRVRLGSHDLSSGEEG-QVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067   110 PKFSILTVNNDITLLKLATPARFSQTVSAVCLPSADDDFPAGTLCATTGWGKTKYNANKTPDKLQQAALPLLSNAECKKS 189
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119616067   190 WGRR--ITDVMICAGAS--GVSSCMGDSGGPLVCQkDGAWTLVGIVSWGSRTCSTTTPAVYARVTKLIPWV 256
Cdd:smart00020 160 YSGGgaITDNMLCAGGLegGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
34-256 3.03e-86

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 256.22  E-value: 3.03e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067   34 IVNGEDAVPGSWPWQVSLQDKTGFHFCGGSLISEDWVVTAAHCGVRTSDV-VVAGEFDQGSDEENIQVLKIAKVFKNPKF 112
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVkVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067  113 SILTVNNDITLLKLATPARFSQTVSAVCLPSADDDFPAGTLCATTGWGKTKynANKTPDKLQQAALPLLSNAECKKSWGR 192
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTK--TLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119616067  193 RITDVMICAGASGVSSCMGDSGGPLVCqKDGawTLVGIVSWGSRTCSTTTPAVYARVTKLIPWV 256
Cdd:pfam00089 159 TVTDTMICAGAGGKDACQGDSGGPLVC-SDG--ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-263 9.33e-75

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 228.38  E-value: 9.33e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067   1 MASLWLLSCFSLVGAAF---GCGVPAIHPvlsglsRIVNGEDAVPGSWPWQVSLQDKTGF--HFCGGSLISEDWVVTAAH 75
Cdd:COG5640    1 MRRRRLLAALAAAALALalaAAPAADAAP------AIVGGTPATVGEYPWMVALQSSNGPsgQFCGGTLIAPRWVLTAAH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067  76 C--GVRTSDV-VVAGEFDQGSDEEniQVLKIAKVFKNPKFSILTVNNDITLLKLATPARFSQTVSavcLPSADDDFPAGT 152
Cdd:COG5640   75 CvdGDGPSDLrVVIGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067 153 LCATTGWGKTKYNANKTPDKLQQAALPLLSNAECKkSWGRRITDVMICAGAS--GVSSCMGDSGGPLVCQKDGAWTLVGI 230
Cdd:COG5640  150 PATVAGWGRTSEGPGSQSGTLRKADVPVVSDATCA-AYGGFDGGTMLCAGYPegGKDACQGDSGGPLVVKDGGGWVLVGV 228
                        250       260       270
                 ....*....|....*....|....*....|...
gi 119616067 231 VSWGSRTCSTTTPAVYARVTKLIPWVQKILAAN 263
Cdd:COG5640  229 VSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
34-259 6.12e-103

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: 298.81  E-value: 6.12e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067  34 IVNGEDAVPGSWPWQVSLQDKTGFHFCGGSLISEDWVVTAAHC---GVRTSDVVVAGEFDQGSDEENIQVLKIAKVFKNP 110
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCvysSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067 111 KFSILTVNNDITLLKLATPARFSQTVSAVCLPSADDDFPAGTLCATTGWGKTKYNANkTPDKLQQAALPLLSNAECKK-- 188
Cdd:cd00190   81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNAECKRay 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119616067 189 SWGRRITDVMICAGAS--GVSSCMGDSGGPLVCQKDGAWTLVGIVSWGSRTCSTTTPAVYARVTKLIPWVQKI 259
Cdd:cd00190  160 SYGGTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
33-256 9.21e-101

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: 293.04  E-value: 9.21e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067    33 RIVNGEDAVPGSWPWQVSLQDKTGFHFCGGSLISEDWVVTAAHC---GVRTSDVVVAGEFDQGSDEENiQVLKIAKVFKN 109
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCvrgSDPSNIRVRLGSHDLSSGEEG-QVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067   110 PKFSILTVNNDITLLKLATPARFSQTVSAVCLPSADDDFPAGTLCATTGWGKTKYNANKTPDKLQQAALPLLSNAECKKS 189
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119616067   190 WGRR--ITDVMICAGAS--GVSSCMGDSGGPLVCQkDGAWTLVGIVSWGSRTCSTTTPAVYARVTKLIPWV 256
Cdd:smart00020 160 YSGGgaITDNMLCAGGLegGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
34-256 3.03e-86

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 256.22  E-value: 3.03e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067   34 IVNGEDAVPGSWPWQVSLQDKTGFHFCGGSLISEDWVVTAAHCGVRTSDV-VVAGEFDQGSDEENIQVLKIAKVFKNPKF 112
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVkVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067  113 SILTVNNDITLLKLATPARFSQTVSAVCLPSADDDFPAGTLCATTGWGKTKynANKTPDKLQQAALPLLSNAECKKSWGR 192
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTK--TLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119616067  193 RITDVMICAGASGVSSCMGDSGGPLVCqKDGawTLVGIVSWGSRTCSTTTPAVYARVTKLIPWV 256
Cdd:pfam00089 159 TVTDTMICAGAGGKDACQGDSGGPLVC-SDG--ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-263 9.33e-75

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 228.38  E-value: 9.33e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067   1 MASLWLLSCFSLVGAAF---GCGVPAIHPvlsglsRIVNGEDAVPGSWPWQVSLQDKTGF--HFCGGSLISEDWVVTAAH 75
Cdd:COG5640    1 MRRRRLLAALAAAALALalaAAPAADAAP------AIVGGTPATVGEYPWMVALQSSNGPsgQFCGGTLIAPRWVLTAAH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067  76 C--GVRTSDV-VVAGEFDQGSDEEniQVLKIAKVFKNPKFSILTVNNDITLLKLATPARFSQTVSavcLPSADDDFPAGT 152
Cdd:COG5640   75 CvdGDGPSDLrVVIGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067 153 LCATTGWGKTKYNANKTPDKLQQAALPLLSNAECKkSWGRRITDVMICAGAS--GVSSCMGDSGGPLVCQKDGAWTLVGI 230
Cdd:COG5640  150 PATVAGWGRTSEGPGSQSGTLRKADVPVVSDATCA-AYGGFDGGTMLCAGYPegGKDACQGDSGGPLVVKDGGGWVLVGV 228
                        250       260       270
                 ....*....|....*....|....*....|...
gi 119616067 231 VSWGSRTCSTTTPAVYARVTKLIPWVQKILAAN 263
Cdd:COG5640  229 VSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
51-253 6.11e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 57.38  E-value: 6.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067  51 LQDKTGFHFCGGSLISEDWVVTAAHC-------GVRTSDVVVAGEFDQGSDEENIQVLKIAKVFKNPKfsilTVNNDITL 123
Cdd:COG3591    5 LETDGGGGVCTGTLIGPNLVLTAGHCvydgaggGWATNIVFVPGYNGGPYGTATATRFRVPPGWVASG----DAGYDYAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119616067 124 LKLATPARFSQTVSAVclpSADDDFPAGTLCATTGWGKTKynanktPDKLQQAalpllSNAECKKSWGRRItdVMICAGA 203
Cdd:COG3591   81 LRLDEPLGDTTGWLGL---AFNDAPLAGEPVTIIGYPGDR------PKDLSLD-----CSGRVTGVQGNRL--SYDCDTT 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 119616067 204 SgvsscmGDSGGPLVCQKDGAWTLVGIVSWGSRTCSTTTPAVYARVTKLI 253
Cdd:COG3591  145 G------GSSGSPVLDDSDGGGRVVGVHSAGGADRANTGVRLTSAIVAAL 188
 
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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