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Conserved domains on  [gi|47086795|ref|NP_997783|]
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chymotrypsinogen B precursor [Danio rerio]

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 ...
34-259 3.30e-96

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: 281.86  E-value: 3.30e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795  34 IVNGEEARPHSWPWQVSLQDSTGFHFCGGSLINENWVVTAAHCNVR---TSHRVILGEHDRSSNAEAIQTIAVGKSIKHP 110
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSsapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795 111 NYNSFTINNDILLIKLATPAKINTHVSPVCLAETNDNFPGGMKCVTSGWGLTRYNAPDTpALLQQAALPLLTNDDCKRYW 190
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP-DVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47086795 191 GTN--ITDLMICAGAS--GVSSCMGDSGGPLVCENNRVWTLVGIVSWGSSTCSTSTPAVYARVTKLRAWVDQT 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 3.30e-96

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: 281.86  E-value: 3.30e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795  34 IVNGEEARPHSWPWQVSLQDSTGFHFCGGSLINENWVVTAAHCNVR---TSHRVILGEHDRSSNAEAIQTIAVGKSIKHP 110
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSsapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795 111 NYNSFTINNDILLIKLATPAKINTHVSPVCLAETNDNFPGGMKCVTSGWGLTRYNAPDTpALLQQAALPLLTNDDCKRYW 190
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP-DVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47086795 191 GTN--ITDLMICAGAS--GVSSCMGDSGGPLVCENNRVWTLVGIVSWGSSTCSTSTPAVYARVTKLRAWVDQT 259
Cdd:cd00190 160 SYGgtITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
33-256 6.40e-96

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: 281.10  E-value: 6.40e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795     33 RIVNGEEARPHSWPWQVSLQDSTGFHFCGGSLINENWVVTAAHC---NVRTSHRVILGEHDRSSNaEAIQTIAVGKSIKH 109
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCvrgSDPSNIRVRLGSHDLSSG-EEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795    110 PNYNSFTINNDILLIKLATPAKINTHVSPVCLAETNDNFPGGMKCVTSGWGLTRYNAPDTPALLQQAALPLLTNDDCKRY 189
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47086795    190 WGTN--ITDLMICAGAS--GVSSCMGDSGGPLVCENNRvWTLVGIVSWGSSTCSTSTPAVYARVTKLRAWV 256
Cdd:smart00020 160 YSGGgaITDNMLCAGGLegGKDACQGDSGGPLVCNDGR-WVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
34-256 3.34e-78

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 235.41  E-value: 3.34e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795    34 IVNGEEARPHSWPWQVSLQDSTGFHFCGGSLINENWVVTAAHCnVRTSH--RVILGEHDRSSNAEAIQTIAVGKSIKHPN 111
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHC-VSGASdvKVVLGAHNIVLREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795   112 YNSFTINNDILLIKLATPAKINTHVSPVCLAETNDNFPGGMKCVTSGWGLTRYNAPDTpaLLQQAALPLLTNDDCKRYWG 191
Cdd:pfam00089  80 YNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSD--TLQEVTVPVVSRETCRSAYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47086795   192 TNITDLMICAGASGVSSCMGDSGGPLVCENNrvwTLVGIVSWGSSTCSTSTPAVYARVTKLRAWV 256
Cdd:pfam00089 158 GTVTDTMICAGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-263 2.56e-67

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 209.51  E-value: 2.56e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795   1 MAFLWILSCLAffGAAYGCGIPAIPPVVTGyARIVNGEEARPHSWPWQVSLQDSTGF--HFCGGSLINENWVVTAAHC-- 76
Cdd:COG5640   1 MRRRRLLAALA--AAALALALAAAPAADAA-PAIVGGTPATVGEYPWMVALQSSNGPsgQFCGGTLIAPRWVLTAAHCvd 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795  77 -NVRTSHRVILGEHDRSSNAEaiQTIAVGKSIKHPNYNSFTINNDILLIKLATPAkinTHVSPVCLAETNDNFPGGMKCV 155
Cdd:COG5640  78 gDGPSDLRVVIGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPAT 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795 156 TSGWGLTRYNAPDTPALLQQAALPLLTNDDCKRYWGtNITDLMICAGAS--GVSSCMGDSGGPLVCENNRVWTLVGIVSW 233
Cdd:COG5640 153 VAGWGRTSEGPGSQSGTLRKADVPVVSDATCAAYGG-FDGGTMLCAGYPegGKDACQGDSGGPLVVKDGGGWVLVGVVSW 231
                       250       260       270
                ....*....|....*....|....*....|
gi 47086795 234 GSSTCSTSTPAVYARVTKLRAWVDQTIASN 263
Cdd:COG5640 232 GGGPCAAGYPGVYTRVSAYRDWIKSTAGGL 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 3.30e-96

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: 281.86  E-value: 3.30e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795  34 IVNGEEARPHSWPWQVSLQDSTGFHFCGGSLINENWVVTAAHCNVR---TSHRVILGEHDRSSNAEAIQTIAVGKSIKHP 110
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSsapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795 111 NYNSFTINNDILLIKLATPAKINTHVSPVCLAETNDNFPGGMKCVTSGWGLTRYNAPDTpALLQQAALPLLTNDDCKRYW 190
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP-DVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47086795 191 GTN--ITDLMICAGAS--GVSSCMGDSGGPLVCENNRVWTLVGIVSWGSSTCSTSTPAVYARVTKLRAWVDQT 259
Cdd:cd00190 160 SYGgtITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
33-256 6.40e-96

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: 281.10  E-value: 6.40e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795     33 RIVNGEEARPHSWPWQVSLQDSTGFHFCGGSLINENWVVTAAHC---NVRTSHRVILGEHDRSSNaEAIQTIAVGKSIKH 109
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCvrgSDPSNIRVRLGSHDLSSG-EEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795    110 PNYNSFTINNDILLIKLATPAKINTHVSPVCLAETNDNFPGGMKCVTSGWGLTRYNAPDTPALLQQAALPLLTNDDCKRY 189
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47086795    190 WGTN--ITDLMICAGAS--GVSSCMGDSGGPLVCENNRvWTLVGIVSWGSSTCSTSTPAVYARVTKLRAWV 256
Cdd:smart00020 160 YSGGgaITDNMLCAGGLegGKDACQGDSGGPLVCNDGR-WVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
34-256 3.34e-78

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 235.41  E-value: 3.34e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795    34 IVNGEEARPHSWPWQVSLQDSTGFHFCGGSLINENWVVTAAHCnVRTSH--RVILGEHDRSSNAEAIQTIAVGKSIKHPN 111
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHC-VSGASdvKVVLGAHNIVLREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795   112 YNSFTINNDILLIKLATPAKINTHVSPVCLAETNDNFPGGMKCVTSGWGLTRYNAPDTpaLLQQAALPLLTNDDCKRYWG 191
Cdd:pfam00089  80 YNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSD--TLQEVTVPVVSRETCRSAYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47086795   192 TNITDLMICAGASGVSSCMGDSGGPLVCENNrvwTLVGIVSWGSSTCSTSTPAVYARVTKLRAWV 256
Cdd:pfam00089 158 GTVTDTMICAGAGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-263 2.56e-67

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 209.51  E-value: 2.56e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795   1 MAFLWILSCLAffGAAYGCGIPAIPPVVTGyARIVNGEEARPHSWPWQVSLQDSTGF--HFCGGSLINENWVVTAAHC-- 76
Cdd:COG5640   1 MRRRRLLAALA--AAALALALAAAPAADAA-PAIVGGTPATVGEYPWMVALQSSNGPsgQFCGGTLIAPRWVLTAAHCvd 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795  77 -NVRTSHRVILGEHDRSSNAEaiQTIAVGKSIKHPNYNSFTINNDILLIKLATPAkinTHVSPVCLAETNDNFPGGMKCV 155
Cdd:COG5640  78 gDGPSDLRVVIGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPAT 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795 156 TSGWGLTRYNAPDTPALLQQAALPLLTNDDCKRYWGtNITDLMICAGAS--GVSSCMGDSGGPLVCENNRVWTLVGIVSW 233
Cdd:COG5640 153 VAGWGRTSEGPGSQSGTLRKADVPVVSDATCAAYGG-FDGGTMLCAGYPegGKDACQGDSGGPLVVKDGGGWVLVGVVSW 231
                       250       260       270
                ....*....|....*....|....*....|
gi 47086795 234 GSSTCSTSTPAVYARVTKLRAWVDQTIASN 263
Cdd:COG5640 232 GGGPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
51-258 1.43e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 56.22  E-value: 1.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795  51 LQDSTGFHFCGGSLINENWVVTAAHC-------NVRTSHRVILGEHDRSSNAEAIQTIAVgksikHPNY-NSFTINNDIL 122
Cdd:COG3591   5 LETDGGGGVCTGTLIGPNLVLTAGHCvydgaggGWATNIVFVPGYNGGPYGTATATRFRV-----PPGWvASGDAGYDYA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795 123 LIKLATPakINTHVSPVCLAeTNDNFPGGMKCVTSGWGLTRYNAPDtpallqqaalpllTNDDCkRYWGTNITDLMICAG 202
Cdd:COG3591  80 LLRLDEP--LGDTTGWLGLA-FNDAPLAGEPVTIIGYPGDRPKDLS-------------LDCSG-RVTGVQGNRLSYDCD 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 47086795 203 ASGvsscmGDSGGPLVCENNRVWTLVGIVSWGSSTCS-TSTPAVYARVTKLRAWVDQ 258
Cdd:COG3591 143 TTG-----GSSGSPVLDDSDGGGRVVGVHSAGGADRAnTGVRLTSAIVAALRAWASA 194
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
45-158 9.28e-05

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 40.99  E-value: 9.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086795    45 WPWQVSLQdSTGFHFCGGSLINENWVVTAAHC----NVRTSH-RVILGEHDRSSNAEAIQTIAVGKSIKHPNYNSftinn 119
Cdd:pfam09342   1 WPWIAKVY-LDGNMICSGVLIDASWVIVSGSClrdtNLRHQYiSVVLGGAKTLKSIEGPYEQIVRVDCRHDIPES----- 74
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 47086795   120 DILLIKLATPAKINTHVSPVCLAETNDNFPGGMKCVTSG 158
Cdd:pfam09342  75 EISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
 
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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