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Conserved domains on  [gi|7766893]
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Chain A, PROTEIN (TRYPSIN)

Protein Classification

serine protease( domain architecture ID 10076129)

serine protease such as human cathepsin G with trypsin- and chymotrypsin-like specificity; also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity

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 8.29e-106

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: 304.20  E-value: 8.29e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893    1 IVGGYTCGANTVPYQVSL--NSGYHFCGGSLINSQWVVSAAHCY----KSGIQVRLGEDNINVVEGNEQFISASKSIVHP 74
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCVyssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893   75 SYNSNTLNNDIMLIKLKSAASLNSRVASISLPTS--CASAGTQCLISGWGNTKSSGtSYPDVLKCLKAPILSDSSCKSAY 152
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7766893  153 --PGQITSNMFCAGYLEGGKDSCQGDSGGPVVC----SGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQT 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 8.29e-106

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: 304.20  E-value: 8.29e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893    1 IVGGYTCGANTVPYQVSL--NSGYHFCGGSLINSQWVVSAAHCY----KSGIQVRLGEDNINVVEGNEQFISASKSIVHP 74
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCVyssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893   75 SYNSNTLNNDIMLIKLKSAASLNSRVASISLPTS--CASAGTQCLISGWGNTKSSGtSYPDVLKCLKAPILSDSSCKSAY 152
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7766893  153 --PGQITSNMFCAGYLEGGKDSCQGDSGGPVVC----SGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQT 219
Cdd:cd00190 160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-216 1.21e-104

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 [Multi-domain]  Cd Length: 229  Bit Score: 301.13  E-value: 1.21e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893       1 IVGGYTCGANTVPYQVSL--NSGYHFCGGSLINSQWVVSAAHC----YKSGIQVRLGEDNINVvEGNEQFISASKSIVHP 74
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLqyGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSS-GEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893      75 SYNSNTLNNDIMLIKLKSAASLNSRVASISLPTS--CASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAY 152
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7766893     153 PGQ--ITSNMFCAGYLEGGKDSCQGDSGGPVVCSGK---LQGIVSWGSGCAQKNKPGVYTKVCNYVSWI 216
Cdd:smart00020 161 SGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-216 1.67e-86

Trypsin;


Pssm-ID: 395042 [Multi-domain]  Cd Length: 219  Bit Score: 255.06  E-value: 1.67e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893      1 IVGGYTCGANTVPYQVSLN--SGYHFCGGSLINSQWVVSAAHCYKSG--IQVRLGEDNINVVEGNEQFISASKSIVHPSY 76
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlsSGKHFCGGSLISENWVLTAAHCVSGAsdVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893     77 NSNTLNNDIMLIKLKSAASLNSRVASISLPTSCAS--AGTQCLISGWGNTKSSGtsYPDVLKCLKAPILSDSSCKSAYPG 154
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDlpVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7766893    155 QITSNMFCAGYleGGKDSCQGDSGGPVVCS-GKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWI 216
Cdd:pfam00089 159 TVTDTMICAGA--GGKDACQGDSGGPLVCSdGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-216 6.44e-28

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 109.20  E-value: 6.44e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893    1 IVGGYTCGANTVPYQVSL------NSGYHFCGGSLINSQWVVSAAHC-YKSGIQVrlGEDNINVVEGNE----QFISASK 69
Cdd:COG5640  33 IIGGSNANAGEYPSLVALvdrisdYVSGTFCGGSKLGGRYVLTAAHCaDASSPIS--SDVNRVVVDLNDssqaERGHVRT 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893   70 SIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCA----SAGTQCLISGWGNTKSS----GTSYPDVLKCLKAP 141
Cdd:COG5640 111 IYVHEFYSPGNLGNDIAVLELARAASLPRVKITSFDASDTFlnsvTTVSPMTNGTFGVTTPSdvprSSPKGTILHEVAVL 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893  142 ILSDSSCKSAYPGQITSNM------FCAGYLegGKDSCQGDSGGPVV---CSGKLQ-GIVSWG-SGCAQKNKPGVYTKVC 210
Cdd:COG5640 191 FVPLSTCAQYKGCANASDGatgltgFCAGRP--PKDACQGDSGGPIFhkgEEGRVQrGVVSWGdGGCGGTLIPGVYTNVS 268

                ....*.
gi 7766893  211 NYVSWI 216
Cdd:COG5640 269 NYQDWI 274
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-219 8.29e-106

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: 304.20  E-value: 8.29e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893    1 IVGGYTCGANTVPYQVSL--NSGYHFCGGSLINSQWVVSAAHCY----KSGIQVRLGEDNINVVEGNEQFISASKSIVHP 74
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCVyssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893   75 SYNSNTLNNDIMLIKLKSAASLNSRVASISLPTS--CASAGTQCLISGWGNTKSSGtSYPDVLKCLKAPILSDSSCKSAY 152
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7766893  153 --PGQITSNMFCAGYLEGGKDSCQGDSGGPVVC----SGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQT 219
Cdd:cd00190 160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-216 1.21e-104

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 [Multi-domain]  Cd Length: 229  Bit Score: 301.13  E-value: 1.21e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893       1 IVGGYTCGANTVPYQVSL--NSGYHFCGGSLINSQWVVSAAHC----YKSGIQVRLGEDNINVvEGNEQFISASKSIVHP 74
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLqyGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSS-GEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893      75 SYNSNTLNNDIMLIKLKSAASLNSRVASISLPTS--CASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAY 152
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7766893     153 PGQ--ITSNMFCAGYLEGGKDSCQGDSGGPVVCSGK---LQGIVSWGSGCAQKNKPGVYTKVCNYVSWI 216
Cdd:smart00020 161 SGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-216 1.67e-86

Trypsin;


Pssm-ID: 395042 [Multi-domain]  Cd Length: 219  Bit Score: 255.06  E-value: 1.67e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893      1 IVGGYTCGANTVPYQVSLN--SGYHFCGGSLINSQWVVSAAHCYKSG--IQVRLGEDNINVVEGNEQFISASKSIVHPSY 76
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlsSGKHFCGGSLISENWVLTAAHCVSGAsdVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893     77 NSNTLNNDIMLIKLKSAASLNSRVASISLPTSCAS--AGTQCLISGWGNTKSSGtsYPDVLKCLKAPILSDSSCKSAYPG 154
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDlpVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7766893    155 QITSNMFCAGYleGGKDSCQGDSGGPVVCS-GKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWI 216
Cdd:pfam00089 159 TVTDTMICAGA--GGKDACQGDSGGPLVCSdGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-216 6.44e-28

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 109.20  E-value: 6.44e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893    1 IVGGYTCGANTVPYQVSL------NSGYHFCGGSLINSQWVVSAAHC-YKSGIQVrlGEDNINVVEGNE----QFISASK 69
Cdd:COG5640  33 IIGGSNANAGEYPSLVALvdrisdYVSGTFCGGSKLGGRYVLTAAHCaDASSPIS--SDVNRVVVDLNDssqaERGHVRT 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893   70 SIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCA----SAGTQCLISGWGNTKSS----GTSYPDVLKCLKAP 141
Cdd:COG5640 111 IYVHEFYSPGNLGNDIAVLELARAASLPRVKITSFDASDTFlnsvTTVSPMTNGTFGVTTPSdvprSSPKGTILHEVAVL 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7766893  142 ILSDSSCKSAYPGQITSNM------FCAGYLegGKDSCQGDSGGPVV---CSGKLQ-GIVSWG-SGCAQKNKPGVYTKVC 210
Cdd:COG5640 191 FVPLSTCAQYKGCANASDGatgltgFCAGRP--PKDACQGDSGGPIFhkgEEGRVQrGVVSWGdGGCGGTLIPGVYTNVS 268

                ....*.
gi 7766893  211 NYVSWI 216
Cdd:COG5640 269 NYQDWI 274
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
174-209 9.98e-03

alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and similar proteins; This family represents the catalytic domain of alpha-lytic protease (alpha-LP) and its closely-related homologs. Alpha-lytic protease (EC 3.4.21.12; also called alpha-lytic endopeptidase), originally isolated from the myxobacterium Lysobacter enzymogenes, belongs to the MEROPS peptidase family S1, subfamily S1E (streptogrisin A subfamily). It is synthesized as a pro-enzyme, thus having two domains; the N-terminal pro-domain acts as a foldase, required transiently for the correct folding of the protease domain, and also acts as a potent inhibitor of the mature enzyme, while the C-terminal domain catalyzes the cleavage of peptide bonds. Members of the alpha-lytic protease subfamily include Nocardiopsis alba protease (NAPase), a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis, streptogrisins (SPG-A, SPG-B, SPG-C, and SPG-D), and Thermobifida fusca protease A (TFPA). These serine proteases have characteristic kinetic stability, exhibited by their extremely slow unfolding kinetics. The active site, characteristic of serine proteases, contains the catalytic triad consisting of serine acting as a nucleophile, aspartate as an electrophile, and histidine as a base, all required for activity. This model represents the C-terminal catalytic domain of alpha-lytic proteases.


Pssm-ID: 411050  Cd Length: 188  Bit Score: 35.74  E-value: 9.98e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 7766893  174 QGDSGGPVVCSGKLQGIVSWGSG-CAQKNKPGVYTKV 209
Cdd:cd21112 144 PGDSGGPVFSGTQALGITSGGSGnCGSGGGTSYFQPV 180
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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