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Conserved domains on  [gi|10835849|pdb|1FNI|A]
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Chain A, TRYPSIN

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 2.22e-109

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: 313.44  E-value: 2.22e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A        1 IVGGYTCAANSIPYQVSL--NSGSHFCGGSLINSQWVVSAAHCY----KSRIQVRLGEHNIDVLEGNEQFINAAKIITHP 74
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCVyssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A       75 NFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRS--CAAAGTECLISGWGNTkSSGSSYPSLLQCLKAPVLSNSSCKSSY 152
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1FNI_A      153 --PGQITGNMICVGFLQGGKDSCQGDSGGPVVCN----GQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQT 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 2.22e-109

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: 313.44  E-value: 2.22e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A        1 IVGGYTCAANSIPYQVSL--NSGSHFCGGSLINSQWVVSAAHCY----KSRIQVRLGEHNIDVLEGNEQFINAAKIITHP 74
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCVyssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A       75 NFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRS--CAAAGTECLISGWGNTkSSGSSYPSLLQCLKAPVLSNSSCKSSY 152
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1FNI_A      153 --PGQITGNMICVGFLQGGKDSCQGDSGGPVVCN----GQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQT 219
Cdd:cd00190 160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-216 2.42e-107

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: 308.07  E-value: 2.42e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A           1 IVGGYTCAANSIPYQVSL--NSGSHFCGGSLINSQWVVSAAHC----YKSRIQVRLGEHNIDVlEGNEQFINAAKIITHP 74
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLqyGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSS-GEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A          75 NFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRS--CAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSNSSCKSSY 152
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1FNI_A         153 PGQ--ITGNMICVGFLQGGKDSCQGDSGGPVVCN---GQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWI 216
Cdd:smart00020 161 SGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-216 1.16e-91

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 268.16  E-value: 1.16e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A          1 IVGGYTCAANSIPYQVSLN--SGSHFCGGSLINSQWVVSAAHCYKSR--IQVRLGEHNIDVLEGNEQFINAAKIITHPNF 76
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlsSGKHFCGGSLISENWVLTAAHCVSGAsdVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A         77 NGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCA--AAGTECLISGWGNTKSSGssYPSLLQCLKAPVLSNSSCKSSYPG 154
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
1FNI_A        155 QITGNMICVGFlqGGKDSCQGDSGGPVVCNGQ-LQGIVSWGYGCAQKNKPGVYTKVCNYVNWI 216
Cdd:pfam00089 159 TVTDTMICAGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-223 3.23e-71

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 217.59  E-value: 3.23e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A        1 IVGGYTCAANSIPYQVSLNS----GSHFCGGSLINSQWVVSAAHCY----KSRIQVRLGEHNIDVLEGneQFINAAKIIT 72
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSsngpSGQFCGGTLIAPRWVLTAAHCVdgdgPSDLRVVIGSTDLSTSGG--TVVKVARIVV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A       73 HPNFNGNTLDNDIMLIKLSSPATlnsRVATVSLPRS--CAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSNSSCkS 150
Cdd:COG5640 109 HPDYDPATPGNDIALLKLATPVP---GVAPAPLATSadAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATC-A 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1FNI_A      151 SYPGQITGNMICVGFLQGGKDSCQGDSGGPVV----CNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN 223
Cdd:COG5640 185 AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-219 2.22e-109

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: 313.44  E-value: 2.22e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A        1 IVGGYTCAANSIPYQVSL--NSGSHFCGGSLINSQWVVSAAHCY----KSRIQVRLGEHNIDVLEGNEQFINAAKIITHP 74
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqyTGGRHFCGGSLISPRWVLTAAHCVyssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A       75 NFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRS--CAAAGTECLISGWGNTkSSGSSYPSLLQCLKAPVLSNSSCKSSY 152
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRT-SEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1FNI_A      153 --PGQITGNMICVGFLQGGKDSCQGDSGGPVVCN----GQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQT 219
Cdd:cd00190 160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-216 2.42e-107

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: 308.07  E-value: 2.42e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A           1 IVGGYTCAANSIPYQVSL--NSGSHFCGGSLINSQWVVSAAHC----YKSRIQVRLGEHNIDVlEGNEQFINAAKIITHP 74
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLqyGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSS-GEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A          75 NFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRS--CAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSNSSCKSSY 152
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1FNI_A         153 PGQ--ITGNMICVGFLQGGKDSCQGDSGGPVVCN---GQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWI 216
Cdd:smart00020 161 SGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-216 1.16e-91

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 268.16  E-value: 1.16e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A          1 IVGGYTCAANSIPYQVSLN--SGSHFCGGSLINSQWVVSAAHCYKSR--IQVRLGEHNIDVLEGNEQFINAAKIITHPNF 76
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlsSGKHFCGGSLISENWVLTAAHCVSGAsdVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A         77 NGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCA--AAGTECLISGWGNTKSSGssYPSLLQCLKAPVLSNSSCKSSYPG 154
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
1FNI_A        155 QITGNMICVGFlqGGKDSCQGDSGGPVVCNGQ-LQGIVSWGYGCAQKNKPGVYTKVCNYVNWI 216
Cdd:pfam00089 159 TVTDTMICAGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-223 3.23e-71

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 217.59  E-value: 3.23e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A        1 IVGGYTCAANSIPYQVSLNS----GSHFCGGSLINSQWVVSAAHCY----KSRIQVRLGEHNIDVLEGneQFINAAKIIT 72
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSsngpSGQFCGGTLIAPRWVLTAAHCVdgdgPSDLRVVIGSTDLSTSGG--TVVKVARIVV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A       73 HPNFNGNTLDNDIMLIKLSSPATlnsRVATVSLPRS--CAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSNSSCkS 150
Cdd:COG5640 109 HPDYDPATPGNDIALLKLATPVP---GVAPAPLATSadAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATC-A 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1FNI_A      151 SYPGQITGNMICVGFLQGGKDSCQGDSGGPVV----CNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN 223
Cdd:COG5640 185 AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
15-196 9.55e-08

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 50.45  E-value: 9.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A       15 QVSLNSGSHFCGGSLINSQWVVSAAHC--------YKSRIQVRLGEHNidvleGNEQFINAAKIITHPNFNGNTLDN-DI 85
Cdd:COG3591   4 RLETDGGGGVCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGDAGyDY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FNI_A       86 MLIKLSSPATLNSRVATVSLPRScAAAGTECLISGWGNTKSSGSSypslLQClkapvlsnsSCKSSYPGQitgnmicvGF 165
Cdd:COG3591  79 ALLRLDEPLGDTTGWLGLAFNDA-PLAGEPVTIIGYPGDRPKDLS----LDC---------SGRVTGVQG--------NR 136
                       170       180       190
                ....*....|....*....|....*....|....*
1FNI_A      166 LQGGKDSCQGDSGGPVV----CNGQLQGIVSWGYG 196
Cdd:COG3591 137 LSYDCDTTGGSSGSPVLddsdGGGRVVGVHSAGGA 171
 
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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