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Conserved domains on  [gi|665399683|ref|NP_001286222|]
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uncharacterized protein Dmel_CG8172, isoform G [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

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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 ...
1-186 1.06e-72

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: 219.07  E-value: 1.06e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683   1 MKIRLGEWDVRGQEErlNHEEYGIERKEVHPHYNPADFVNDVALIRLDRNVVYKQHIIPVCLPPSTTKLT-GKMATVAGW 79
Cdd:cd00190   52 YTVRLGSHDLSSNEG--GGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPaGTTCTVSGW 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683  80 GRTRHGqSTVPSVLQEVDVEVISNDRCQRWFRAAGRreaIHDVFLCAGYKDGGRDSCQGDSGGPLTLTMDGRKTLIGLVS 159
Cdd:cd00190  130 GRTSEG-GPLPDVLQEVNVPIVSNAECKRAYSYGGT---ITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVS 205
                        170       180
                 ....*....|....*....|....*..
gi 665399683 160 WGIGCGREHLPGVYTNIQRFVPWINKV 186
Cdd:cd00190  206 WGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-186 1.06e-72

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: 219.07  E-value: 1.06e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683   1 MKIRLGEWDVRGQEErlNHEEYGIERKEVHPHYNPADFVNDVALIRLDRNVVYKQHIIPVCLPPSTTKLT-GKMATVAGW 79
Cdd:cd00190   52 YTVRLGSHDLSSNEG--GGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPaGTTCTVSGW 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683  80 GRTRHGqSTVPSVLQEVDVEVISNDRCQRWFRAAGRreaIHDVFLCAGYKDGGRDSCQGDSGGPLTLTMDGRKTLIGLVS 159
Cdd:cd00190  130 GRTSEG-GPLPDVLQEVNVPIVSNAECKRAYSYGGT---ITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVS 205
                        170       180
                 ....*....|....*....|....*..
gi 665399683 160 WGIGCGREHLPGVYTNIQRFVPWINKV 186
Cdd:cd00190  206 WGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-183 3.97e-69

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: 209.84  E-value: 3.97e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683     1 MKIRLGEWDVRGQEERlnhEEYGIERKEVHPHYNPADFVNDVALIRLDRNVVYKQHIIPVCLPPSTTKL-TGKMATVAGW 79
Cdd:smart00020  53 IRVRLGSHDLSSGEEG---QVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVpAGTTCTVSGW 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683    80 GRTRHGQSTVPSVLQEVDVEVISNDRCQRwfrAAGRREAIHDVFLCAGYKDGGRDSCQGDSGGPLtLTMDGRKTLIGLVS 159
Cdd:smart00020 130 GRTSEGAGSLPDTLQEVNVPIVSNATCRR---AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPL-VCNDGRWVLVGIVS 205
                          170       180
                   ....*....|....*....|....
gi 665399683   160 WGIGCGREHLPGVYTNIQRFVPWI 183
Cdd:smart00020 206 WGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-188 3.07e-54

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 173.30  E-value: 3.07e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683   1 MKIRLGEWDVRGQEErlnhEEYGIERKEVHPHYNPADFVNDVALIRLDRNVVYKQhiiPVCLPPSTTKL-TGKMATVAGW 79
Cdd:COG5640   84 LRVVIGSTDLSTSGG----TVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAaPGTPATVAGW 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683  80 GRTRHGQSTVPSVLQEVDVEVISNDRCQRWFRAAGRREaihdvfLCAGYKDGGRDSCQGDSGGPLTLTMDGRKTLIGLVS 159
Cdd:COG5640  157 GRTSEGPGSQSGTLRKADVPVVSDATCAAYGGFDGGTM------LCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVS 230
                        170       180
                 ....*....|....*....|....*....
gi 665399683 160 WGIGCGREHLPGVYTNIQRFVPWINKVMA 188
Cdd:COG5640  231 WGGGPCAAGYPGVYTRVSAYRDWIKSTAG 259
Trypsin pfam00089
Trypsin;
1-183 4.16e-48

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 156.06  E-value: 4.16e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683    1 MKIRLGEWDVRGQEERLNHeeYGIERKEVHPHYNPADFVNDVALIRLDRNVVYKQHIIPVCLPPSTTKLT-GKMATVAGW 79
Cdd:pfam00089  50 VKVVLGAHNIVLREGGEQK--FDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPvGTTCTVSGW 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683   80 GRTRHGQStvPSVLQEVDVEVISNDRCQRWFRAAgrreaIHDVFLCAGYkdGGRDSCQGDSGGPLtltMDGRKTLIGLVS 159
Cdd:pfam00089 128 GNTKTLGP--SDTLQEVTVPVVSRETCRSAYGGT-----VTDTMICAGA--GGKDACQGDSGGPL---VCSDGELIGIVS 195
                         170       180
                  ....*....|....*....|....
gi 665399683  160 WGIGCGREHLPGVYTNIQRFVPWI 183
Cdd:pfam00089 196 WGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-186 1.06e-72

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: 219.07  E-value: 1.06e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683   1 MKIRLGEWDVRGQEErlNHEEYGIERKEVHPHYNPADFVNDVALIRLDRNVVYKQHIIPVCLPPSTTKLT-GKMATVAGW 79
Cdd:cd00190   52 YTVRLGSHDLSSNEG--GGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPaGTTCTVSGW 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683  80 GRTRHGqSTVPSVLQEVDVEVISNDRCQRWFRAAGRreaIHDVFLCAGYKDGGRDSCQGDSGGPLTLTMDGRKTLIGLVS 159
Cdd:cd00190  130 GRTSEG-GPLPDVLQEVNVPIVSNAECKRAYSYGGT---ITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVS 205
                        170       180
                 ....*....|....*....|....*..
gi 665399683 160 WGIGCGREHLPGVYTNIQRFVPWINKV 186
Cdd:cd00190  206 WGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-183 3.97e-69

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: 209.84  E-value: 3.97e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683     1 MKIRLGEWDVRGQEERlnhEEYGIERKEVHPHYNPADFVNDVALIRLDRNVVYKQHIIPVCLPPSTTKL-TGKMATVAGW 79
Cdd:smart00020  53 IRVRLGSHDLSSGEEG---QVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVpAGTTCTVSGW 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683    80 GRTRHGQSTVPSVLQEVDVEVISNDRCQRwfrAAGRREAIHDVFLCAGYKDGGRDSCQGDSGGPLtLTMDGRKTLIGLVS 159
Cdd:smart00020 130 GRTSEGAGSLPDTLQEVNVPIVSNATCRR---AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPL-VCNDGRWVLVGIVS 205
                          170       180
                   ....*....|....*....|....
gi 665399683   160 WGIGCGREHLPGVYTNIQRFVPWI 183
Cdd:smart00020 206 WGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-188 3.07e-54

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 173.30  E-value: 3.07e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683   1 MKIRLGEWDVRGQEErlnhEEYGIERKEVHPHYNPADFVNDVALIRLDRNVVYKQhiiPVCLPPSTTKL-TGKMATVAGW 79
Cdd:COG5640   84 LRVVIGSTDLSTSGG----TVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAaPGTPATVAGW 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683  80 GRTRHGQSTVPSVLQEVDVEVISNDRCQRWFRAAGRREaihdvfLCAGYKDGGRDSCQGDSGGPLTLTMDGRKTLIGLVS 159
Cdd:COG5640  157 GRTSEGPGSQSGTLRKADVPVVSDATCAAYGGFDGGTM------LCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVS 230
                        170       180
                 ....*....|....*....|....*....
gi 665399683 160 WGIGCGREHLPGVYTNIQRFVPWINKVMA 188
Cdd:COG5640  231 WGGGPCAAGYPGVYTRVSAYRDWIKSTAG 259
Trypsin pfam00089
Trypsin;
1-183 4.16e-48

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 156.06  E-value: 4.16e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683    1 MKIRLGEWDVRGQEERLNHeeYGIERKEVHPHYNPADFVNDVALIRLDRNVVYKQHIIPVCLPPSTTKLT-GKMATVAGW 79
Cdd:pfam00089  50 VKVVLGAHNIVLREGGEQK--FDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPvGTTCTVSGW 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683   80 GRTRHGQStvPSVLQEVDVEVISNDRCQRWFRAAgrreaIHDVFLCAGYkdGGRDSCQGDSGGPLtltMDGRKTLIGLVS 159
Cdd:pfam00089 128 GNTKTLGP--SDTLQEVTVPVVSRETCRSAYGGT-----VTDTMICAGA--GGKDACQGDSGGPL---VCSDGELIGIVS 195
                         170       180
                  ....*....|....*....|....
gi 665399683  160 WGIGCGREHLPGVYTNIQRFVPWI 183
Cdd:pfam00089 196 WGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
29-161 1.54e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 40.82  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399683  29 VHPHY-NPADFVNDVALIRLDRNVVYKQHIIPvcLPPSTTKLTGKMATVAGWGRTRHGQSTVpsvlqevdvevisndRCQ 107
Cdd:COG3591   64 VPPGWvASGDAGYDYALLRLDEPLGDTTGWLG--LAFNDAPLAGEPVTIIGYPGDRPKDLSL---------------DCS 126
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 665399683 108 RWFRAAGRREAIHDvflCagykdggrDSCQGDSGGPLTLTMDGRKTLIGLVSWG 161
Cdd:COG3591  127 GRVTGVQGNRLSYD---C--------DTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
 
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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