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Conserved domains on  [gi|1218242563|ref|XP_001663061|]
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trypsin-1 [Aedes aegypti]

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 ...
26-265 3.69e-88

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: 261.44  E-value: 3.69e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563  26 IVGGDEAEAHEFPYQISLQWNFNdgqtetMHFCGASVLNENFVLTAAHCKTaYSNTGFIEVVAAEHDVAVAEGSEQRRLV 105
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGG------RHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQVIKV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563 106 AEFIVHEDYQGGVSPDDIAVIRVDKPFELNDKVKAVKLPKQLEQF-DGD-VTLSGWGSVSTTVFpdYPDKLRKVVLPLVD 183
Cdd:cd00190    74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLpAGTtCTVSGWGRTSEGGP--LPDVLQEVNVPIVS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563 184 YEQCNALWDNDSALAKSNVCAGPIDGSKSACSADSGGPLVKQSGEDVIQVGVVSWGaVPCGSPRRPTVFAGVSHYVDWIE 263
Cdd:cd00190   152 NAECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWG-SGCARPNYPGVYTRVSSYLDWIQ 230

                  ..
gi 1218242563 264 QQ 265
Cdd:cd00190   231 KT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
26-265 3.69e-88

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: 261.44  E-value: 3.69e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563  26 IVGGDEAEAHEFPYQISLQWNFNdgqtetMHFCGASVLNENFVLTAAHCKTaYSNTGFIEVVAAEHDVAVAEGSEQRRLV 105
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGG------RHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQVIKV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563 106 AEFIVHEDYQGGVSPDDIAVIRVDKPFELNDKVKAVKLPKQLEQF-DGD-VTLSGWGSVSTTVFpdYPDKLRKVVLPLVD 183
Cdd:cd00190    74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLpAGTtCTVSGWGRTSEGGP--LPDVLQEVNVPIVS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563 184 YEQCNALWDNDSALAKSNVCAGPIDGSKSACSADSGGPLVKQSGEDVIQVGVVSWGaVPCGSPRRPTVFAGVSHYVDWIE 263
Cdd:cd00190   152 NAECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWG-SGCARPNYPGVYTRVSSYLDWIQ 230

                  ..
gi 1218242563 264 QQ 265
Cdd:cd00190   231 KT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
25-262 1.26e-82

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: 247.21  E-value: 1.26e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563   25 KIVGGDEAEAHEFPYQISLQWNFNDgqtetmHFCGASVLNENFVLTAAHCKTaYSNTGFIEVVAAEHDVAVaEGSEQRRL 104
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR------HFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSS-GEEGQVIK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563  105 VAEFIVHEDYQGGVSPDDIAVIRVDKPFELNDKVKAVKLPKQLEQF-DGD-VTLSGWGSVSTTVfPDYPDKLRKVVLPLV 182
Cdd:smart00020  73 VSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVpAGTtCTVSGWGRTSEGA-GSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563  183 DYEQCNALWDNDSALAKSNVCAGPIDGSKSACSADSGGPLVKQSGEdVIQVGVVSWGaVPCGSPRRPTVFAGVSHYVDWI 262
Cdd:smart00020 152 SNATCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR-WVLVGIVSWG-SGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-268 2.51e-69

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 214.51  E-value: 2.51e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563   1 MAFKLTVAFLLVASLALASSRATHKIVGGDEAEAHEFPYQISLQwnFNDGQTEtmHFCGASVLNENFVLTAAHCKTAYSN 80
Cdd:COG5640     6 LLAALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQ--SSNGPSG--QFCGGTLIAPRWVLTAAHCVDGDGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563  81 TGfIEVVAAEHDVAVAEGseQRRLVAEFIVHEDYQGGVSPDDIAVIRVDKPFelnDKVKAVKLPKQLEQFD-GD-VTLSG 158
Cdd:COG5640    82 SD-LRVVIGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAApGTpATVAG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563 159 WGSVSTTVfPDYPDKLRKVVLPLVDYEQCNALWDNDSAlakSNVCAGPIDGSKSACSADSGGPLVKQSGEDVIQVGVVSW 238
Cdd:COG5640   156 WGRTSEGP-GSQSGTLRKADVPVVSDATCAAYGGFDGG---TMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSW 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 1218242563 239 GAVPCGsPRRPTVFAGVSHYVDWIEQQLRA 268
Cdd:COG5640   232 GGGPCA-AGYPGVYTRVSAYRDWIKSTAGG 260
Trypsin pfam00089
Trypsin;
26-262 1.14e-62

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 196.12  E-value: 1.14e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563  26 IVGGDEAEAHEFPYQISLQWnfndgqTETMHFCGASVLNENFVLTAAHCktaYSNTGFIEVVAAEHDVAVAEGSEQRRLV 105
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL------SSGKHFCGGSLISENWVLTAAHC---VSGASDVKVVLGAHNIVLREGGEQKFDV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563 106 AEFIVHEDYQGGVSPDDIAVIRVDKPFELNDKVKAVKLPKQLEQF-DGD-VTLSGWGSVSTTvfpDYPDKLRKVVLPLVD 183
Cdd:pfam00089  72 EKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLpVGTtCTVSGWGNTKTL---GPSDTLQEVTVPVVS 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1218242563 184 YEQCNALWDNDsaLAKSNVCAGPidGSKSACSADSGGPLVKqsgEDVIQVGVVSWGaVPCGSPRRPTVFAGVSHYVDWI 262
Cdd:pfam00089 149 RETCRSAYGGT--VTDTMICAGA--GGKDACQGDSGGPLVC---SDGELIGIVSWG-YGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
26-265 3.69e-88

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: 261.44  E-value: 3.69e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563  26 IVGGDEAEAHEFPYQISLQWNFNdgqtetMHFCGASVLNENFVLTAAHCKTaYSNTGFIEVVAAEHDVAVAEGSEQRRLV 105
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGG------RHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQVIKV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563 106 AEFIVHEDYQGGVSPDDIAVIRVDKPFELNDKVKAVKLPKQLEQF-DGD-VTLSGWGSVSTTVFpdYPDKLRKVVLPLVD 183
Cdd:cd00190    74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLpAGTtCTVSGWGRTSEGGP--LPDVLQEVNVPIVS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563 184 YEQCNALWDNDSALAKSNVCAGPIDGSKSACSADSGGPLVKQSGEDVIQVGVVSWGaVPCGSPRRPTVFAGVSHYVDWIE 263
Cdd:cd00190   152 NAECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWG-SGCARPNYPGVYTRVSSYLDWIQ 230

                  ..
gi 1218242563 264 QQ 265
Cdd:cd00190   231 KT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
25-262 1.26e-82

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: 247.21  E-value: 1.26e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563   25 KIVGGDEAEAHEFPYQISLQWNFNDgqtetmHFCGASVLNENFVLTAAHCKTaYSNTGFIEVVAAEHDVAVaEGSEQRRL 104
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR------HFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSS-GEEGQVIK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563  105 VAEFIVHEDYQGGVSPDDIAVIRVDKPFELNDKVKAVKLPKQLEQF-DGD-VTLSGWGSVSTTVfPDYPDKLRKVVLPLV 182
Cdd:smart00020  73 VSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVpAGTtCTVSGWGRTSEGA-GSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563  183 DYEQCNALWDNDSALAKSNVCAGPIDGSKSACSADSGGPLVKQSGEdVIQVGVVSWGaVPCGSPRRPTVFAGVSHYVDWI 262
Cdd:smart00020 152 SNATCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR-WVLVGIVSWG-SGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-268 2.51e-69

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 214.51  E-value: 2.51e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563   1 MAFKLTVAFLLVASLALASSRATHKIVGGDEAEAHEFPYQISLQwnFNDGQTEtmHFCGASVLNENFVLTAAHCKTAYSN 80
Cdd:COG5640     6 LLAALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQ--SSNGPSG--QFCGGTLIAPRWVLTAAHCVDGDGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563  81 TGfIEVVAAEHDVAVAEGseQRRLVAEFIVHEDYQGGVSPDDIAVIRVDKPFelnDKVKAVKLPKQLEQFD-GD-VTLSG 158
Cdd:COG5640    82 SD-LRVVIGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAApGTpATVAG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563 159 WGSVSTTVfPDYPDKLRKVVLPLVDYEQCNALWDNDSAlakSNVCAGPIDGSKSACSADSGGPLVKQSGEDVIQVGVVSW 238
Cdd:COG5640   156 WGRTSEGP-GSQSGTLRKADVPVVSDATCAAYGGFDGG---TMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSW 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 1218242563 239 GAVPCGsPRRPTVFAGVSHYVDWIEQQLRA 268
Cdd:COG5640   232 GGGPCA-AGYPGVYTRVSAYRDWIKSTAGG 260
Trypsin pfam00089
Trypsin;
26-262 1.14e-62

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 196.12  E-value: 1.14e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563  26 IVGGDEAEAHEFPYQISLQWnfndgqTETMHFCGASVLNENFVLTAAHCktaYSNTGFIEVVAAEHDVAVAEGSEQRRLV 105
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL------SSGKHFCGGSLISENWVLTAAHC---VSGASDVKVVLGAHNIVLREGGEQKFDV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563 106 AEFIVHEDYQGGVSPDDIAVIRVDKPFELNDKVKAVKLPKQLEQF-DGD-VTLSGWGSVSTTvfpDYPDKLRKVVLPLVD 183
Cdd:pfam00089  72 EKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLpVGTtCTVSGWGNTKTL---GPSDTLQEVTVPVVS 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1218242563 184 YEQCNALWDNDsaLAKSNVCAGPidGSKSACSADSGGPLVKqsgEDVIQVGVVSWGaVPCGSPRRPTVFAGVSHYVDWI 262
Cdd:pfam00089 149 RETCRSAYGGT--VTDTMICAGA--GGKDACQGDSGGPLVC---SDGELIGIVSWG-YGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
56-244 4.07e-08

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 51.99  E-value: 4.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563  56 HFCGASVLNENFVLTAAHCKTAYSNTGF---IEVVAAEHDvavaeGSEQRRLVAEFIVHEDY-QGGVSPDDIAVIRVDKP 131
Cdd:COG3591    12 GVCTGTLIGPNLVLTAGHCVYDGAGGGWatnIVFVPGYNG-----GPYGTATATRFRVPPGWvASGDAGYDYALLRLDEP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218242563 132 feLNDKVKAVKLPKQLEQFDGD-VTLSGwgsvsttvfpdYP-DKLRKVVLplvdYEQCNALWDNDSALA-KSNVCAGpid 208
Cdd:COG3591    87 --LGDTTGWLGLAFNDAPLAGEpVTIIG-----------YPgDRPKDLSL----DCSGRVTGVQGNRLSyDCDTTGG--- 146
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1218242563 209 gsksacsaDSGGPLVKQSGEDVIQVGVVSWGAVPCG 244
Cdd:COG3591   147 --------SSGSPVLDDSDGGGRVVGVHSAGGADRA 174
 
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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