NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24652706|ref|NP_524904|]
View 

betaTrypsin, isoform A [Drosophila melanogaster]

Protein Classification

S1 family serine peptidase( domain architecture ID 12184331)

S1 family trypsin-like serine peptidase such as snake venom serine proteases and trypsin, which preferentially cleaves peptide bonds after arginine and lysine residues

CATH:  2.40.10.10
EC:  3.4.-.-
Gene Ontology:  GO:0008236|GO:0006508
MEROPS:  S1
SCOP:  3000114

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
30-249 5.11e-67

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: 207.15  E-value: 5.11e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706     30 RIVGGTATTISSFPWQISLQRSG-SHSCGGSIYSARVIVTAAHCLQSVSASSLQIRAGSSYWSSGG--VVAKVSSFKNHE 106
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEegQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706    107 GYNANTMVNDIAVLHLSSSLSFSSTIKAIGLASSN--PANGAAASVSGWGTESSGSSSIPSQLRYVNVNIVSQSRCSSSs 184
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA- 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706    185 YGYGNQIKSSMICAFAS--GKDSCQGDSGGPLVSGGVLVGVV---SWGYGCAAANYPGVYADVAALRSWV 249
Cdd:smart00020 160 YSGGGAITDNMLCAGGLegGKDACQGDSGGPLVCNDGRWVLVgivSWGSGCARPGKPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
30-249 5.11e-67

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: 207.15  E-value: 5.11e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706     30 RIVGGTATTISSFPWQISLQRSG-SHSCGGSIYSARVIVTAAHCLQSVSASSLQIRAGSSYWSSGG--VVAKVSSFKNHE 106
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEegQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706    107 GYNANTMVNDIAVLHLSSSLSFSSTIKAIGLASSN--PANGAAASVSGWGTESSGSSSIPSQLRYVNVNIVSQSRCSSSs 184
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA- 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706    185 YGYGNQIKSSMICAFAS--GKDSCQGDSGGPLVSGGVLVGVV---SWGYGCAAANYPGVYADVAALRSWV 249
Cdd:smart00020 160 YSGGGAITDNMLCAGGLegGKDACQGDSGGPLVCNDGRWVLVgivSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
31-252 4.41e-64

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: 199.81  E-value: 4.41e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706  31 IVGGTATTISSFPWQISLQRS-GSHSCGGSIYSARVIVTAAHCLQSVSASSLQIRAGSSYWSS---GGVVAKVSSFKNHE 106
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSnegGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706 107 GYNANTMVNDIAVLHLSSSLSFSSTIKAIGLASSN--PANGAAASVSGWGTESSGSSSIPsQLRYVNVNIVSQSRCSSSs 184
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWGRTSEGGPLPD-VLQEVNVPIVSNAECKRA- 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24652706 185 YGYGNQIKSSMICAFAS--GKDSCQGDSGGPLVSGGVLVGVVS----WGYGCAAANYPGVYADVAALRSWVINN 252
Cdd:cd00190 159 YSYGGTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVgivsWGSGCARPNYPGVYTRVSSYLDWIQKT 232
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-249 1.08e-51

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 169.06  E-value: 1.08e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706   1 MLKFLILLSAVACALGGTIPEGLLPQLDGRIVGGTATTISSFPWQISLQRSG---SHSCGGSIYSARVIVTAAHCLQSVS 77
Cdd:COG5640   1 MRRRRLLAALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706  78 ASSLQIRAGS-SYWSSGGVVAKVSSFKNHEGYNANTMVNDIAVLHLSSSLSFSSTIKaIGLASSNPANGAAASVSGWGTE 156
Cdd:COG5640  81 PSDLRVVIGStDLSTSGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP-LATSADAAAPGTPATVAGWGRT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706 157 SSGSSSIPSQLRYVNVNIVSQSRCSsssyGYGNQIKSSMICA--FASGKDSCQGDSGGPLVSGGVLVGV----VSWGYGC 230
Cdd:COG5640 160 SEGPGSQSGTLRKADVPVVSDATCA----AYGGFDGGTMLCAgyPEGGKDACQGDSGGPLVVKDGGGWVlvgvVSWGGGP 235
                       250
                ....*....|....*....
gi 24652706 231 AAANYPGVYADVAALRSWV 249
Cdd:COG5640 236 CAAGYPGVYTRVSAYRDWI 254
Trypsin pfam00089
Trypsin;
31-249 5.91e-45

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 150.29  E-value: 5.91e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706    31 IVGGTATTISSFPWQISLQ-RSGSHSCGGSIYSARVIVTAAHCLqsVSASSLQIRAGS---SYWSSGGVVAKVSSFKNHE 106
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCV--SGASDVKVVLGAhniVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706   107 GYNANTMVNDIAVLHLSSSLSFSSTIKAIGLA--SSNPANGAAASVSGWGTesSGSSSIPSQLRYVNVNIVSQSRCSSSs 184
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPdaSSDLPVGTTCTVSGWGN--TKTLGPSDTLQEVTVPVVSRETCRSA- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24652706   185 ygYGNQIKSSMICAFASGKDSCQGDSGGPLVSGGVLVG-VVSWGYGCAAANYPGVYADVAALRSWV 249
Cdd:pfam00089 156 --YGGTVTDTMICAGAGGKDACQGDSGGPLVCSDGELIgIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
30-249 5.11e-67

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: 207.15  E-value: 5.11e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706     30 RIVGGTATTISSFPWQISLQRSG-SHSCGGSIYSARVIVTAAHCLQSVSASSLQIRAGSSYWSSGG--VVAKVSSFKNHE 106
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEegQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706    107 GYNANTMVNDIAVLHLSSSLSFSSTIKAIGLASSN--PANGAAASVSGWGTESSGSSSIPSQLRYVNVNIVSQSRCSSSs 184
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA- 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706    185 YGYGNQIKSSMICAFAS--GKDSCQGDSGGPLVSGGVLVGVV---SWGYGCAAANYPGVYADVAALRSWV 249
Cdd:smart00020 160 YSGGGAITDNMLCAGGLegGKDACQGDSGGPLVCNDGRWVLVgivSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
31-252 4.41e-64

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: 199.81  E-value: 4.41e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706  31 IVGGTATTISSFPWQISLQRS-GSHSCGGSIYSARVIVTAAHCLQSVSASSLQIRAGSSYWSS---GGVVAKVSSFKNHE 106
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSnegGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706 107 GYNANTMVNDIAVLHLSSSLSFSSTIKAIGLASSN--PANGAAASVSGWGTESSGSSSIPsQLRYVNVNIVSQSRCSSSs 184
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWGRTSEGGPLPD-VLQEVNVPIVSNAECKRA- 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24652706 185 YGYGNQIKSSMICAFAS--GKDSCQGDSGGPLVSGGVLVGVVS----WGYGCAAANYPGVYADVAALRSWVINN 252
Cdd:cd00190 159 YSYGGTITDNMLCAGGLegGKDACQGDSGGPLVCNDNGRGVLVgivsWGSGCARPNYPGVYTRVSSYLDWIQKT 232
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-249 1.08e-51

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 169.06  E-value: 1.08e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706   1 MLKFLILLSAVACALGGTIPEGLLPQLDGRIVGGTATTISSFPWQISLQRSG---SHSCGGSIYSARVIVTAAHCLQSVS 77
Cdd:COG5640   1 MRRRRLLAALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706  78 ASSLQIRAGS-SYWSSGGVVAKVSSFKNHEGYNANTMVNDIAVLHLSSSLSFSSTIKaIGLASSNPANGAAASVSGWGTE 156
Cdd:COG5640  81 PSDLRVVIGStDLSTSGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP-LATSADAAAPGTPATVAGWGRT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706 157 SSGSSSIPSQLRYVNVNIVSQSRCSsssyGYGNQIKSSMICA--FASGKDSCQGDSGGPLVSGGVLVGV----VSWGYGC 230
Cdd:COG5640 160 SEGPGSQSGTLRKADVPVVSDATCA----AYGGFDGGTMLCAgyPEGGKDACQGDSGGPLVVKDGGGWVlvgvVSWGGGP 235
                       250
                ....*....|....*....
gi 24652706 231 AAANYPGVYADVAALRSWV 249
Cdd:COG5640 236 CAAGYPGVYTRVSAYRDWI 254
Trypsin pfam00089
Trypsin;
31-249 5.91e-45

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 150.29  E-value: 5.91e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706    31 IVGGTATTISSFPWQISLQ-RSGSHSCGGSIYSARVIVTAAHCLqsVSASSLQIRAGS---SYWSSGGVVAKVSSFKNHE 106
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCV--SGASDVKVVLGAhniVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652706   107 GYNANTMVNDIAVLHLSSSLSFSSTIKAIGLA--SSNPANGAAASVSGWGTesSGSSSIPSQLRYVNVNIVSQSRCSSSs 184
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPdaSSDLPVGTTCTVSGWGN--TKTLGPSDTLQEVTVPVVSRETCRSA- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24652706   185 ygYGNQIKSSMICAFASGKDSCQGDSGGPLVSGGVLVG-VVSWGYGCAAANYPGVYADVAALRSWV 249
Cdd:pfam00089 156 --YGGTVTDTMICAGAGGKDACQGDSGGPLVCSDGELIgIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
51-119 9.33e-03

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 36.19  E-value: 9.33e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24652706  51 SGSHSCGGSIYSARVIVTAAHCLQSVS----ASSLQIRAGssYWSSGGVVAKVSSFKNHEGYNANTMVN-DIAV 119
Cdd:COG3591   9 GGGGVCTGTLIGPNLVLTAGHCVYDGAgggwATNIVFVPG--YNGGPYGTATATRFRVPPGWVASGDAGyDYAL 80
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH