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Conserved domains on  [gi|10835459|pdb|1EQ9|A]
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Chain A, CHYMOTRYPSIN

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 ...
1-219 6.30e-81

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: 241.41  E-value: 6.30e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A        1 IVGGKDAPVGKYPYQVSLRLS-GSHRCGASILDNNNVLTAAHCVDGlSNLNRLKVHVGTNYLSE---SGDVYDVEDAVVN 76
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSnegGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A       77 KNYDDFLLRNDVALVHLTNPIKFNDLVQPIKLSTNDEDLESN-PCTLTGWGSTRLGGNTPNALQEIELIVHPQKQCERDQ 155
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGtTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1EQ9_A      156 W---RVIDSHICTLTKR-GEGACHGDSGGPLVAN----GAQIGIVSFGSPCAL-GEPDVYTRVSSFVSWINAN 219
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 ...
1-219 6.30e-81

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: 241.41  E-value: 6.30e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A        1 IVGGKDAPVGKYPYQVSLRLS-GSHRCGASILDNNNVLTAAHCVDGlSNLNRLKVHVGTNYLSE---SGDVYDVEDAVVN 76
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSnegGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A       77 KNYDDFLLRNDVALVHLTNPIKFNDLVQPIKLSTNDEDLESN-PCTLTGWGSTRLGGNTPNALQEIELIVHPQKQCERDQ 155
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGtTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1EQ9_A      156 W---RVIDSHICTLTKR-GEGACHGDSGGPLVAN----GAQIGIVSFGSPCAL-GEPDVYTRVSSFVSWINAN 219
Cdd:cd00190 160 SyggTITDNMLCAGGLEgGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARpNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-216 7.53e-76

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: 228.33  E-value: 7.53e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A           1 IVGGKDAPVGKYPYQVSLRLSG-SHRCGASILDNNNVLTAAHCVDGlSNLNRLKVHVGTNYLSESGD--VYDVEDAVVNK 77
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSSGEEgqVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A          78 NYDDFLLRNDVALVHLTNPIKFNDLVQPIKLSTNDEDLESN-PCTLTGWGSTRLG-GNTPNALQEIELIVHPQKQCERDQ 155
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGtTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1EQ9_A         156 WRVI---DSHICTLT-KRGEGACHGDSGGPLVANGA---QIGIVSFGSPCALGE-PDVYTRVSSFVSWI 216
Cdd:smart00020 161 SGGGaitDNMLCAGGlEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGCARPGkPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-222 9.45e-64

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 198.72  E-value: 9.45e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A        1 IVGGKDAPVGKYPYQVSLRLSG---SHRCGASILDNNNVLTAAHCVDGLSNlNRLKVHVGTNYLSES-GDVYDVEDAVVN 76
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGP-SDLRVVIGSTDLSTSgGTVVKVARIVVH 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A       77 KNYDDFLLRNDVALVHLTNPIkfnDLVQPIKLSTNDEDLESN-PCTLTGWGSTRLG-GNTPNALQEIELIVHPQKQCERD 154
Cdd:COG5640 110 PDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGtPATVAGWGRTSEGpGSQSGTLRKADVPVVSDATCAAY 186
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1EQ9_A      155 QWRVIDSHICTLTKRGE-GACHGDSGGPLVA----NGAQIGIVSFG-SPCALGEPDVYTRVSSFVSWINANLKK 222
Cdd:COG5640 187 GGFDGGTMLCAGYPEGGkDACQGDSGGPLVVkdggGWVLVGVVSWGgGPCAAGYPGVYTRVSAYRDWIKSTAGG 260
Trypsin pfam00089
Trypsin;
1-216 6.69e-58

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 182.26  E-value: 6.69e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A          1 IVGGKDAPVGKYPYQVSLRL-SGSHRCGASILDNNNVLTAAHCVDGLSNLnrlKVHVGTNYLS---ESGDVYDVEDAVVN 76
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDV---KVVLGAHNIVlreGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A         77 KNYDDFLLRNDVALVHLTNPIKFNDLVQPIKLSTNDEDLESN-PCTLTGWGSTRLGGnTPNALQEIELIVHPQKQCERD- 154
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGtTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSAy 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
1EQ9_A        155 QWRVIDSHICTLTKrGEGACHGDSGGPLVA-NGAQIGIVSFGSPCALGE-PDVYTRVSSFVSWI 216
Cdd:pfam00089 157 GGTVTDTMICAGAG-GKDACQGDSGGPLVCsDGELIGIVSWGYGCASGNyPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-219 6.30e-81

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: 241.41  E-value: 6.30e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A        1 IVGGKDAPVGKYPYQVSLRLS-GSHRCGASILDNNNVLTAAHCVDGlSNLNRLKVHVGTNYLSE---SGDVYDVEDAVVN 76
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSnegGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A       77 KNYDDFLLRNDVALVHLTNPIKFNDLVQPIKLSTNDEDLESN-PCTLTGWGSTRLGGNTPNALQEIELIVHPQKQCERDQ 155
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGtTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1EQ9_A      156 W---RVIDSHICTLTKR-GEGACHGDSGGPLVAN----GAQIGIVSFGSPCAL-GEPDVYTRVSSFVSWINAN 219
Cdd:cd00190 160 SyggTITDNMLCAGGLEgGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARpNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-216 7.53e-76

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: 228.33  E-value: 7.53e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A           1 IVGGKDAPVGKYPYQVSLRLSG-SHRCGASILDNNNVLTAAHCVDGlSNLNRLKVHVGTNYLSESGD--VYDVEDAVVNK 77
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSSGEEgqVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A          78 NYDDFLLRNDVALVHLTNPIKFNDLVQPIKLSTNDEDLESN-PCTLTGWGSTRLG-GNTPNALQEIELIVHPQKQCERDQ 155
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGtTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1EQ9_A         156 WRVI---DSHICTLT-KRGEGACHGDSGGPLVANGA---QIGIVSFGSPCALGE-PDVYTRVSSFVSWI 216
Cdd:smart00020 161 SGGGaitDNMLCAGGlEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGCARPGkPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-222 9.45e-64

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 198.72  E-value: 9.45e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A        1 IVGGKDAPVGKYPYQVSLRLSG---SHRCGASILDNNNVLTAAHCVDGLSNlNRLKVHVGTNYLSES-GDVYDVEDAVVN 76
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGP-SDLRVVIGSTDLSTSgGTVVKVARIVVH 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A       77 KNYDDFLLRNDVALVHLTNPIkfnDLVQPIKLSTNDEDLESN-PCTLTGWGSTRLG-GNTPNALQEIELIVHPQKQCERD 154
Cdd:COG5640 110 PDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGtPATVAGWGRTSEGpGSQSGTLRKADVPVVSDATCAAY 186
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1EQ9_A      155 QWRVIDSHICTLTKRGE-GACHGDSGGPLVA----NGAQIGIVSFG-SPCALGEPDVYTRVSSFVSWINANLKK 222
Cdd:COG5640 187 GGFDGGTMLCAGYPEGGkDACQGDSGGPLVVkdggGWVLVGVVSWGgGPCAAGYPGVYTRVSAYRDWIKSTAGG 260
Trypsin pfam00089
Trypsin;
1-216 6.69e-58

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 182.26  E-value: 6.69e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A          1 IVGGKDAPVGKYPYQVSLRL-SGSHRCGASILDNNNVLTAAHCVDGLSNLnrlKVHVGTNYLS---ESGDVYDVEDAVVN 76
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDV---KVVLGAHNIVlreGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A         77 KNYDDFLLRNDVALVHLTNPIKFNDLVQPIKLSTNDEDLESN-PCTLTGWGSTRLGGnTPNALQEIELIVHPQKQCERD- 154
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGtTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSAy 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
1EQ9_A        155 QWRVIDSHICTLTKrGEGACHGDSGGPLVA-NGAQIGIVSFGSPCALGE-PDVYTRVSSFVSWI 216
Cdd:pfam00089 157 GGTVTDTMICAGAG-GKDACQGDSGGPLVCsDGELIGIVSWGYGCASGNyPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
21-221 1.15e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 58.53  E-value: 1.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A       21 SGSHRCGASILDNNNVLTAAHCVDGLSNLNRL-KVHVGTNYLSESGDVYDVEDAVVNKNYD-DFLLRNDVALVHLTNPIk 98
Cdd:COG3591   9 GGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWAtNIVFVPGYNGGPYGTATATRFRVPPGWVaSGDAGYDYALLRLDEPL- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EQ9_A       99 fNDLVQPIKLSTNDEDLESNPCTLTGWGSTRLGGNTpnalqeieliVHPQKQCERDQWRVIdSHICTltkrgegACHGDS 178
Cdd:COG3591  88 -GDTTGWLGLAFNDAPLAGEPVTIIGYPGDRPKDLS----------LDCSGRVTGVQGNRL-SYDCD-------TTGGSS 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
1EQ9_A      179 GGPLVAN----GAQIGIVSFGSpcalgePDVYTRVSSFVSWINANLK 221
Cdd:COG3591 149 GSPVLDDsdggGRVVGVHSAGG------ADRANTGVRLTSAIVAALR 189
 
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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