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Conserved domains on  [gi|24650931|ref|NP_651663|]
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uncharacterized protein Dmel_CG11843, isoform A [Drosophila melanogaster]

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

 Zoom to residue level

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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 ...
68-312 3.15e-71

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: 220.23  E-value: 3.15e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931  68 IVGGHPAQPREFPHMARLGRRPDpssraDWFCGGVLISERFVLTAAHCLESERGEVNVVRLGELDFDSLDEDaaPRDYMV 147
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGG-----RHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGG--GQVIKV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931 148 AGYIAHPGYEDPQFYHDIGLVKLTEAVVFDLYKHPACLPfqderSSDSFIAV-------GWGSTGLALKPSAQLLKVKLQ 220
Cdd:cd00190  74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLP-----SSGYNLPAgttctvsGWGRTSEGGPLPDVLQEVNVP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931 221 RYGNWVCKKLltrqveEFPRGFDGNNQLCVGSEMA-QDTCNGDSGGPLLMyhrEYPCMYVVVGITSAGLSCGSPGIPGIY 299
Cdd:cd00190 149 IVSNAECKRA------YSYGGTITDNMLCAGGLEGgKDACQGDSGGPLVC---NDNGRGVLVGIVSWGSGCARPNYPGVY 219
                       250
                ....*....|...
gi 24650931 300 TRVYPYLGWIART 312
Cdd:cd00190 220 TRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
68-312 3.15e-71

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: 220.23  E-value: 3.15e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931  68 IVGGHPAQPREFPHMARLGRRPDpssraDWFCGGVLISERFVLTAAHCLESERGEVNVVRLGELDFDSLDEDaaPRDYMV 147
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGG-----RHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGG--GQVIKV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931 148 AGYIAHPGYEDPQFYHDIGLVKLTEAVVFDLYKHPACLPfqderSSDSFIAV-------GWGSTGLALKPSAQLLKVKLQ 220
Cdd:cd00190  74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLP-----SSGYNLPAgttctvsGWGRTSEGGPLPDVLQEVNVP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931 221 RYGNWVCKKLltrqveEFPRGFDGNNQLCVGSEMA-QDTCNGDSGGPLLMyhrEYPCMYVVVGITSAGLSCGSPGIPGIY 299
Cdd:cd00190 149 IVSNAECKRA------YSYGGTITDNMLCAGGLEGgKDACQGDSGGPLVC---NDNGRGVLVGIVSWGSGCARPNYPGVY 219
                       250
                ....*....|...
gi 24650931 300 TRVYPYLGWIART 312
Cdd:cd00190 220 TRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
68-309 5.75e-66

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: 206.76  E-value: 5.75e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931     68 IVGGHPAQPREFPHMARLGRRpdpssRADWFCGGVLISERFVLTAAHCLESERGEVNVVRLGELDFDSLDEDaapRDYMV 147
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYG-----GGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEG---QVIKV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931    148 AGYIAHPGYEDPQFYHDIGLVKLTEAVVFDLYKHPACLPFQDERSSDSFIAV--GWGSTGL-ALKPSAQLLKVKLQRYGN 224
Cdd:smart00020  74 SKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTvsGWGRTSEgAGSLPDTLQEVNVPIVSN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931    225 WVCKKLLtrqveeFPRGFDGNNQLCVG-SEMAQDTCNGDSGGPLLMYHREypcmYVVVGITSAGLSCGSPGIPGIYTRVY 303
Cdd:smart00020 154 ATCRRAY------SGGGAITDNMLCAGgLEGGKDACQGDSGGPLVCNDGR----WVLVGIVSWGSGCARPGKPGVYTRVS 223

                   ....*.
gi 24650931    304 PYLGWI 309
Cdd:smart00020 224 SYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
65-315 6.65e-56

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 182.16  E-value: 6.65e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931  65 TPLIVGGHPAQPREFPHMARLGRRPDPSSradWFCGGVLISERFVLTAAHCLESERGEVNVVRLGELDFDSLDEDAAPrd 144
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNGPSG---QFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTVVK-- 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931 145 ymVAGYIAHPGYEDPQFYHDIGLVKLTEAVvfDLYKhPACLPFQDERSS--DSFIAVGWGSTGLAL-KPSAQLLKVKLQR 221
Cdd:COG5640 103 --VARIVVHPDYDPATPGNDIALLKLATPV--PGVA-PAPLATSADAAApgTPATVAGWGRTSEGPgSQSGTLRKADVPV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931 222 YGNWVCKKlltrqveefPRGFDGNNQLCVGSEMA-QDTCNGDSGGPLLmyhREYPCMYVVVGITSAGLSCGSPGIPGIYT 300
Cdd:COG5640 178 VSDATCAA---------YGGFDGGTMLCAGYPEGgKDACQGDSGGPLV---VKDGGGWVLVGVVSWGGGPCAAGYPGVYT 245
                       250
                ....*....|....*
gi 24650931 301 RVYPYLGWIARTLAT 315
Cdd:COG5640 246 RVSAYRDWIKSTAGG 260
Trypsin pfam00089
Trypsin;
68-309 1.40e-54

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 177.25  E-value: 1.40e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931    68 IVGGHPAQPREFPHMARLGRRpdpssRADWFCGGVLISERFVLTAAHCLeSERGEVNVvRLGELDFDSLDEDAAPRDymV 147
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLS-----SGKHFCGGSLISENWVLTAAHCV-SGASDVKV-VLGAHNIVLREGGEQKFD--V 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931   148 AGYIAHPGYEDPQFYHDIGLVKLTEAVVFDLYKHPACLPFQDERSS--DSFIAVGWGSTGlALKPSAQLLKVKLQRYGNW 225
Cdd:pfam00089  72 EKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPvgTTCTVSGWGNTK-TLGPSDTLQEVTVPVVSRE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931   226 VCKKLLTRQVEEfprgfdgnNQLCVGSEmAQDTCNGDSGGPLLMYHREypcmyvVVGITSAGLSCGSPGIPGIYTRVYPY 305
Cdd:pfam00089 151 TCRSAYGGTVTD--------TMICAGAG-GKDACQGDSGGPLVCSDGE------LIGIVSWGYGCASGNYPGVYTPVSSY 215

                  ....
gi 24650931   306 LGWI 309
Cdd:pfam00089 216 LDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
68-312 3.15e-71

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: 220.23  E-value: 3.15e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931  68 IVGGHPAQPREFPHMARLGRRPDpssraDWFCGGVLISERFVLTAAHCLESERGEVNVVRLGELDFDSLDEDaaPRDYMV 147
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGG-----RHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGG--GQVIKV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931 148 AGYIAHPGYEDPQFYHDIGLVKLTEAVVFDLYKHPACLPfqderSSDSFIAV-------GWGSTGLALKPSAQLLKVKLQ 220
Cdd:cd00190  74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLP-----SSGYNLPAgttctvsGWGRTSEGGPLPDVLQEVNVP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931 221 RYGNWVCKKLltrqveEFPRGFDGNNQLCVGSEMA-QDTCNGDSGGPLLMyhrEYPCMYVVVGITSAGLSCGSPGIPGIY 299
Cdd:cd00190 149 IVSNAECKRA------YSYGGTITDNMLCAGGLEGgKDACQGDSGGPLVC---NDNGRGVLVGIVSWGSGCARPNYPGVY 219
                       250
                ....*....|...
gi 24650931 300 TRVYPYLGWIART 312
Cdd:cd00190 220 TRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
68-309 5.75e-66

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: 206.76  E-value: 5.75e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931     68 IVGGHPAQPREFPHMARLGRRpdpssRADWFCGGVLISERFVLTAAHCLESERGEVNVVRLGELDFDSLDEDaapRDYMV 147
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYG-----GGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEG---QVIKV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931    148 AGYIAHPGYEDPQFYHDIGLVKLTEAVVFDLYKHPACLPFQDERSSDSFIAV--GWGSTGL-ALKPSAQLLKVKLQRYGN 224
Cdd:smart00020  74 SKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTvsGWGRTSEgAGSLPDTLQEVNVPIVSN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931    225 WVCKKLLtrqveeFPRGFDGNNQLCVG-SEMAQDTCNGDSGGPLLMYHREypcmYVVVGITSAGLSCGSPGIPGIYTRVY 303
Cdd:smart00020 154 ATCRRAY------SGGGAITDNMLCAGgLEGGKDACQGDSGGPLVCNDGR----WVLVGIVSWGSGCARPGKPGVYTRVS 223

                   ....*.
gi 24650931    304 PYLGWI 309
Cdd:smart00020 224 SYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
65-315 6.65e-56

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 182.16  E-value: 6.65e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931  65 TPLIVGGHPAQPREFPHMARLGRRPDPSSradWFCGGVLISERFVLTAAHCLESERGEVNVVRLGELDFDSLDEDAAPrd 144
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNGPSG---QFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTVVK-- 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931 145 ymVAGYIAHPGYEDPQFYHDIGLVKLTEAVvfDLYKhPACLPFQDERSS--DSFIAVGWGSTGLAL-KPSAQLLKVKLQR 221
Cdd:COG5640 103 --VARIVVHPDYDPATPGNDIALLKLATPV--PGVA-PAPLATSADAAApgTPATVAGWGRTSEGPgSQSGTLRKADVPV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931 222 YGNWVCKKlltrqveefPRGFDGNNQLCVGSEMA-QDTCNGDSGGPLLmyhREYPCMYVVVGITSAGLSCGSPGIPGIYT 300
Cdd:COG5640 178 VSDATCAA---------YGGFDGGTMLCAGYPEGgKDACQGDSGGPLV---VKDGGGWVLVGVVSWGGGPCAAGYPGVYT 245
                       250
                ....*....|....*
gi 24650931 301 RVYPYLGWIARTLAT 315
Cdd:COG5640 246 RVSAYRDWIKSTAGG 260
Trypsin pfam00089
Trypsin;
68-309 1.40e-54

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 177.25  E-value: 1.40e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931    68 IVGGHPAQPREFPHMARLGRRpdpssRADWFCGGVLISERFVLTAAHCLeSERGEVNVvRLGELDFDSLDEDAAPRDymV 147
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLS-----SGKHFCGGSLISENWVLTAAHCV-SGASDVKV-VLGAHNIVLREGGEQKFD--V 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931   148 AGYIAHPGYEDPQFYHDIGLVKLTEAVVFDLYKHPACLPFQDERSS--DSFIAVGWGSTGlALKPSAQLLKVKLQRYGNW 225
Cdd:pfam00089  72 EKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPvgTTCTVSGWGNTK-TLGPSDTLQEVTVPVVSRE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931   226 VCKKLLTRQVEEfprgfdgnNQLCVGSEmAQDTCNGDSGGPLLMYHREypcmyvVVGITSAGLSCGSPGIPGIYTRVYPY 305
Cdd:pfam00089 151 TCRSAYGGTVTD--------TMICAGAG-GKDACQGDSGGPLVCSDGE------LIGIVSWGYGCASGNYPGVYTPVSSY 215

                  ....
gi 24650931   306 LGWI 309
Cdd:pfam00089 216 LDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
96-311 8.50e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 60.08  E-value: 8.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931  96 DWFCGGVLISERFVLTAAHCLESERGEVNVVRlgeLDFDSLDEDAAPRDYMVAGYIAHPGY-EDPQFYHDIGLVKLTEAV 174
Cdd:COG3591  11 GGVCTGTLIGPNLVLTAGHCVYDGAGGGWATN---IVFVPGYNGGPYGTATATRFRVPPGWvASGDAGYDYALLRLDEPL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650931 175 V-----FDLYKHPACLPfqdersSDSFIAVGWgstglalkPSAQLLKVKLQRYGnwvckKLLTRQveefprgfdgNNQLC 249
Cdd:COG3591  88 GdttgwLGLAFNDAPLA------GEPVTIIGY--------PGDRPKDLSLDCSG-----RVTGVQ----------GNRLS 138
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24650931 250 VGSemaqDTCNGDSGGPLLmyhREYPCMYVVVGITSAGL-SCGSPGIPGIYTRVYPYLGWIAR 311
Cdd:COG3591 139 YDC----DTTGGSSGSPVL---DDSDGGGRVVGVHSAGGaDRANTGVRLTSAIVAALRAWASA 194
 
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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