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Conserved domains on  [gi|665395327|ref|NP_001287578|]
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uncharacterized protein Dmel_CG11843, isoform B [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 665395327  68 IVGGHPAQPREFPHMARLGRRPDpssraDWFCGGVLISERFVLTAAHCLESERGEVNVVRLGELDFDSLDEDaaPRDYMV 147
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGG-----RHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGG--GQVIKV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327 148 AGYIAHPGYEDPQFYHDIGLVKLTEAVVFDLYKHPACLPfqderSSDSFIAV-------GWGSTGLALKPSAQLLKVKLQ 220
Cdd:cd00190   74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLP-----SSGYNLPAgttctvsGWGRTSEGGPLPDVLQEVNVP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327 221 RYGNWVCKKLltrqveEFPRGFDGNNQLCVGSEMA-QDTCNGDSGGPLLMyhrEYPCMYVVVGITSAGLSCGSPGIPGIY 299
Cdd:cd00190  149 IVSNAECKRA------YSYGGTITDNMLCAGGLEGgKDACQGDSGGPLVC---NDNGRGVLVGIVSWGSGCARPNYPGVY 219
                        250
                 ....*....|...
gi 665395327 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 665395327  68 IVGGHPAQPREFPHMARLGRRPDpssraDWFCGGVLISERFVLTAAHCLESERGEVNVVRLGELDFDSLDEDaaPRDYMV 147
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGG-----RHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGG--GQVIKV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327 148 AGYIAHPGYEDPQFYHDIGLVKLTEAVVFDLYKHPACLPfqderSSDSFIAV-------GWGSTGLALKPSAQLLKVKLQ 220
Cdd:cd00190   74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLP-----SSGYNLPAgttctvsGWGRTSEGGPLPDVLQEVNVP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327 221 RYGNWVCKKLltrqveEFPRGFDGNNQLCVGSEMA-QDTCNGDSGGPLLMyhrEYPCMYVVVGITSAGLSCGSPGIPGIY 299
Cdd:cd00190  149 IVSNAECKRA------YSYGGTITDNMLCAGGLEGgKDACQGDSGGPLVC---NDNGRGVLVGIVSWGSGCARPNYPGVY 219
                        250
                 ....*....|...
gi 665395327 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 665395327    68 IVGGHPAQPREFPHMARLGRRpdpssRADWFCGGVLISERFVLTAAHCLESERGEVNVVRLGELDFDSLDEDaapRDYMV 147
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYG-----GGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEG---QVIKV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327   148 AGYIAHPGYEDPQFYHDIGLVKLTEAVVFDLYKHPACLPFQDERSSDSFIAV--GWGSTGL-ALKPSAQLLKVKLQRYGN 224
Cdd:smart00020  74 SKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTvsGWGRTSEgAGSLPDTLQEVNVPIVSN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327   225 WVCKKLLtrqveeFPRGFDGNNQLCVG-SEMAQDTCNGDSGGPLLMYHREypcmYVVVGITSAGLSCGSPGIPGIYTRVY 303
Cdd:smart00020 154 ATCRRAY------SGGGAITDNMLCAGgLEGGKDACQGDSGGPLVCNDGR----WVLVGIVSWGSGCARPGKPGVYTRVS 223

                   ....*.
gi 665395327   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 665395327  65 TPLIVGGHPAQPREFPHMARLGRRPDPSSradWFCGGVLISERFVLTAAHCLESERGEVNVVRLGELDFDSLDEDAAPrd 144
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSSNGPSG---QFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTVVK-- 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327 145 ymVAGYIAHPGYEDPQFYHDIGLVKLTEAVvfDLYKhPACLPFQDERSS--DSFIAVGWGSTGLAL-KPSAQLLKVKLQR 221
Cdd:COG5640  103 --VARIVVHPDYDPATPGNDIALLKLATPV--PGVA-PAPLATSADAAApgTPATVAGWGRTSEGPgSQSGTLRKADVPV 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327 222 YGNWVCKKlltrqveefPRGFDGNNQLCVGSEMA-QDTCNGDSGGPLLmyhREYPCMYVVVGITSAGLSCGSPGIPGIYT 300
Cdd:COG5640  178 VSDATCAA---------YGGFDGGTMLCAGYPEGgKDACQGDSGGPLV---VKDGGGWVLVGVVSWGGGPCAAGYPGVYT 245
                        250
                 ....*....|....*
gi 665395327 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 665395327   68 IVGGHPAQPREFPHMARLGRRpdpssRADWFCGGVLISERFVLTAAHCLeSERGEVNVvRLGELDFDSLDEDAAPRDymV 147
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLS-----SGKHFCGGSLISENWVLTAAHCV-SGASDVKV-VLGAHNIVLREGGEQKFD--V 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327  148 AGYIAHPGYEDPQFYHDIGLVKLTEAVVFDLYKHPACLPFQDERSS--DSFIAVGWGSTGlALKPSAQLLKVKLQRYGNW 225
Cdd:pfam00089  72 EKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPvgTTCTVSGWGNTK-TLGPSDTLQEVTVPVVSRE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327  226 VCKKLLTRQVEEfprgfdgnNQLCVGSEmAQDTCNGDSGGPLLMYHREypcmyvVVGITSAGLSCGSPGIPGIYTRVYPY 305
Cdd:pfam00089 151 TCRSAYGGTVTD--------TMICAGAG-GKDACQGDSGGPLVCSDGE------LIGIVSWGYGCASGNYPGVYTPVSSY 215

                  ....
gi 665395327  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 665395327  68 IVGGHPAQPREFPHMARLGRRPDpssraDWFCGGVLISERFVLTAAHCLESERGEVNVVRLGELDFDSLDEDaaPRDYMV 147
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGG-----RHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGG--GQVIKV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327 148 AGYIAHPGYEDPQFYHDIGLVKLTEAVVFDLYKHPACLPfqderSSDSFIAV-------GWGSTGLALKPSAQLLKVKLQ 220
Cdd:cd00190   74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLP-----SSGYNLPAgttctvsGWGRTSEGGPLPDVLQEVNVP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327 221 RYGNWVCKKLltrqveEFPRGFDGNNQLCVGSEMA-QDTCNGDSGGPLLMyhrEYPCMYVVVGITSAGLSCGSPGIPGIY 299
Cdd:cd00190  149 IVSNAECKRA------YSYGGTITDNMLCAGGLEGgKDACQGDSGGPLVC---NDNGRGVLVGIVSWGSGCARPNYPGVY 219
                        250
                 ....*....|...
gi 665395327 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 665395327    68 IVGGHPAQPREFPHMARLGRRpdpssRADWFCGGVLISERFVLTAAHCLESERGEVNVVRLGELDFDSLDEDaapRDYMV 147
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYG-----GGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEG---QVIKV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327   148 AGYIAHPGYEDPQFYHDIGLVKLTEAVVFDLYKHPACLPFQDERSSDSFIAV--GWGSTGL-ALKPSAQLLKVKLQRYGN 224
Cdd:smart00020  74 SKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTvsGWGRTSEgAGSLPDTLQEVNVPIVSN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327   225 WVCKKLLtrqveeFPRGFDGNNQLCVG-SEMAQDTCNGDSGGPLLMYHREypcmYVVVGITSAGLSCGSPGIPGIYTRVY 303
Cdd:smart00020 154 ATCRRAY------SGGGAITDNMLCAGgLEGGKDACQGDSGGPLVCNDGR----WVLVGIVSWGSGCARPGKPGVYTRVS 223

                   ....*.
gi 665395327   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 665395327  65 TPLIVGGHPAQPREFPHMARLGRRPDPSSradWFCGGVLISERFVLTAAHCLESERGEVNVVRLGELDFDSLDEDAAPrd 144
Cdd:COG5640   28 APAIVGGTPATVGEYPWMVALQSSNGPSG---QFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTVVK-- 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327 145 ymVAGYIAHPGYEDPQFYHDIGLVKLTEAVvfDLYKhPACLPFQDERSS--DSFIAVGWGSTGLAL-KPSAQLLKVKLQR 221
Cdd:COG5640  103 --VARIVVHPDYDPATPGNDIALLKLATPV--PGVA-PAPLATSADAAApgTPATVAGWGRTSEGPgSQSGTLRKADVPV 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327 222 YGNWVCKKlltrqveefPRGFDGNNQLCVGSEMA-QDTCNGDSGGPLLmyhREYPCMYVVVGITSAGLSCGSPGIPGIYT 300
Cdd:COG5640  178 VSDATCAA---------YGGFDGGTMLCAGYPEGgKDACQGDSGGPLV---VKDGGGWVLVGVVSWGGGPCAAGYPGVYT 245
                        250
                 ....*....|....*
gi 665395327 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 665395327   68 IVGGHPAQPREFPHMARLGRRpdpssRADWFCGGVLISERFVLTAAHCLeSERGEVNVvRLGELDFDSLDEDAAPRDymV 147
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLS-----SGKHFCGGSLISENWVLTAAHCV-SGASDVKV-VLGAHNIVLREGGEQKFD--V 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327  148 AGYIAHPGYEDPQFYHDIGLVKLTEAVVFDLYKHPACLPFQDERSS--DSFIAVGWGSTGlALKPSAQLLKVKLQRYGNW 225
Cdd:pfam00089  72 EKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPvgTTCTVSGWGNTK-TLGPSDTLQEVTVPVVSRE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327  226 VCKKLLTRQVEEfprgfdgnNQLCVGSEmAQDTCNGDSGGPLLMYHREypcmyvVVGITSAGLSCGSPGIPGIYTRVYPY 305
Cdd:pfam00089 151 TCRSAYGGTVTD--------TMICAGAG-GKDACQGDSGGPLVCSDGE------LIGIVSWGYGCASGNYPGVYTPVSSY 215

                  ....
gi 665395327  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 665395327  96 DWFCGGVLISERFVLTAAHCLESERGEVNVVRlgeLDFDSLDEDAAPRDYMVAGYIAHPGY-EDPQFYHDIGLVKLTEAV 174
Cdd:COG3591   11 GGVCTGTLIGPNLVLTAGHCVYDGAGGGWATN---IVFVPGYNGGPYGTATATRFRVPPGWvASGDAGYDYALLRLDEPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665395327 175 V-----FDLYKHPACLPfqdersSDSFIAVGWgstglalkPSAQLLKVKLQRYGnwvckKLLTRQveefprgfdgNNQLC 249
Cdd:COG3591   88 GdttgwLGLAFNDAPLA------GEPVTIIGY--------PGDRPKDLSLDCSG-----RVTGVQ----------GNRLS 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665395327 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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