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Conserved domains on  [gi|281360421|ref|NP_610438|]
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uncharacterized protein Dmel_CG8172, isoform E [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 ...
300-539 8.43e-96

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: 291.10  E-value: 8.43e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421 300 IVGGHSTGFGSHPWQVALIKSGfltRKLSCGGALISNRWVITAAHCVASTPNSNMKIRLGEWDVRGQEErlNHEEYGIER 379
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTG---GRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEG--GGQVIKVKK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421 380 KEVHPHYNPADFVNDVALIRLDRNVVYKQHIIPVCLPPSTTKLT-GKMATVAGWGRTRHGqSTVPSVLQEVDVEVISNDR 458
Cdd:cd00190   76 VIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPaGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421 459 CQRWFRAAGRreaIHDVFLCAGYKDGGRDSCQGDSGGPLTLTMDGRKTLIGLVSWGIGCGREHLPGVYTNIQRFVPWINK 538
Cdd:cd00190  155 CKRAYSYGGT---ITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231

                 .
gi 281360421 539 V 539
Cdd:cd00190  232 T 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
300-539 8.43e-96

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: 291.10  E-value: 8.43e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421 300 IVGGHSTGFGSHPWQVALIKSGfltRKLSCGGALISNRWVITAAHCVASTPNSNMKIRLGEWDVRGQEErlNHEEYGIER 379
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTG---GRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEG--GGQVIKVKK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421 380 KEVHPHYNPADFVNDVALIRLDRNVVYKQHIIPVCLPPSTTKLT-GKMATVAGWGRTRHGqSTVPSVLQEVDVEVISNDR 458
Cdd:cd00190   76 VIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPaGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421 459 CQRWFRAAGRreaIHDVFLCAGYKDGGRDSCQGDSGGPLTLTMDGRKTLIGLVSWGIGCGREHLPGVYTNIQRFVPWINK 538
Cdd:cd00190  155 CKRAYSYGGT---ITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231

                 .
gi 281360421 539 V 539
Cdd:cd00190  232 T 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
299-536 1.57e-93

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: 284.96  E-value: 1.57e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421   299 RIVGGHSTGFGSHPWQVALIKSGFltrKLSCGGALISNRWVITAAHCVASTPNSNMKIRLGEWDVRGQEERlnhEEYGIE 378
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGG---RHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEG---QVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421   379 RKEVHPHYNPADFVNDVALIRLDRNVVYKQHIIPVCLPPSTTKL-TGKMATVAGWGRTRHGQSTVPSVLQEVDVEVISND 457
Cdd:smart00020  75 KVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVpAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281360421   458 RCQrwfRAAGRREAIHDVFLCAGYKDGGRDSCQGDSGGPLtLTMDGRKTLIGLVSWGIGCGREHLPGVYTNIQRFVPWI 536
Cdd:smart00020 155 TCR---RAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPL-VCNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
289-541 7.69e-75

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 238.01  E-value: 7.69e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421 289 GCGEVYTRSNRIVGGHSTGFGSHPWQVALIKSGFlTRKLSCGGALISNRWVITAAHCVASTPNSNMKIRLGEWDVRGQEE 368
Cdd:COG5640   20 AAAPAADAAPAIVGGTPATVGEYPWMVALQSSNG-PSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421 369 rlnhEEYGIERKEVHPHYNPADFVNDVALIRLDRNVVYKQhiiPVCLPPSTTKL-TGKMATVAGWGRTRHGQSTVPSVLQ 447
Cdd:COG5640   99 ----TVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAaPGTPATVAGWGRTSEGPGSQSGTLR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421 448 EVDVEVISNDRCQRWFRAAGRREaihdvfLCAGYKDGGRDSCQGDSGGPLTLTMDGRKTLIGLVSWGIGCGREHLPGVYT 527
Cdd:COG5640  172 KADVPVVSDATCAAYGGFDGGTM------LCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYT 245
                        250
                 ....*....|....
gi 281360421 528 NIQRFVPWINKVMA 541
Cdd:COG5640  246 RVSAYRDWIKSTAG 259
Trypsin pfam00089
Trypsin;
300-536 4.18e-66

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 213.84  E-value: 4.18e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421  300 IVGGHSTGFGSHPWQVALIKSGfltRKLSCGGALISNRWVITAAHCVASTpnSNMKIRLGEWDVRGQEERLNHeeYGIER 379
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSS---GKHFCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLREGGEQK--FDVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421  380 KEVHPHYNPADFVNDVALIRLDRNVVYKQHIIPVCLPPSTTKLT-GKMATVAGWGRTRHGQStvPSVLQEVDVEVISNDR 458
Cdd:pfam00089  74 IIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPvGTTCTVSGWGNTKTLGP--SDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281360421  459 CQRWFRAAgrreaIHDVFLCAGYkdGGRDSCQGDSGGPLtltMDGRKTLIGLVSWGIGCGREHLPGVYTNIQRFVPWI 536
Cdd:pfam00089 152 CRSAYGGT-----VTDTMICAGA--GGKDACQGDSGGPL---VCSDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
300-539 8.43e-96

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: 291.10  E-value: 8.43e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421 300 IVGGHSTGFGSHPWQVALIKSGfltRKLSCGGALISNRWVITAAHCVASTPNSNMKIRLGEWDVRGQEErlNHEEYGIER 379
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTG---GRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEG--GGQVIKVKK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421 380 KEVHPHYNPADFVNDVALIRLDRNVVYKQHIIPVCLPPSTTKLT-GKMATVAGWGRTRHGqSTVPSVLQEVDVEVISNDR 458
Cdd:cd00190   76 VIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPaGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421 459 CQRWFRAAGRreaIHDVFLCAGYKDGGRDSCQGDSGGPLTLTMDGRKTLIGLVSWGIGCGREHLPGVYTNIQRFVPWINK 538
Cdd:cd00190  155 CKRAYSYGGT---ITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231

                 .
gi 281360421 539 V 539
Cdd:cd00190  232 T 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
299-536 1.57e-93

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: 284.96  E-value: 1.57e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421   299 RIVGGHSTGFGSHPWQVALIKSGFltrKLSCGGALISNRWVITAAHCVASTPNSNMKIRLGEWDVRGQEERlnhEEYGIE 378
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGG---RHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEG---QVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421   379 RKEVHPHYNPADFVNDVALIRLDRNVVYKQHIIPVCLPPSTTKL-TGKMATVAGWGRTRHGQSTVPSVLQEVDVEVISND 457
Cdd:smart00020  75 KVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVpAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281360421   458 RCQrwfRAAGRREAIHDVFLCAGYKDGGRDSCQGDSGGPLtLTMDGRKTLIGLVSWGIGCGREHLPGVYTNIQRFVPWI 536
Cdd:smart00020 155 TCR---RAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPL-VCNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
289-541 7.69e-75

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 238.01  E-value: 7.69e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421 289 GCGEVYTRSNRIVGGHSTGFGSHPWQVALIKSGFlTRKLSCGGALISNRWVITAAHCVASTPNSNMKIRLGEWDVRGQEE 368
Cdd:COG5640   20 AAAPAADAAPAIVGGTPATVGEYPWMVALQSSNG-PSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421 369 rlnhEEYGIERKEVHPHYNPADFVNDVALIRLDRNVVYKQhiiPVCLPPSTTKL-TGKMATVAGWGRTRHGQSTVPSVLQ 447
Cdd:COG5640   99 ----TVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAaPGTPATVAGWGRTSEGPGSQSGTLR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421 448 EVDVEVISNDRCQRWFRAAGRREaihdvfLCAGYKDGGRDSCQGDSGGPLTLTMDGRKTLIGLVSWGIGCGREHLPGVYT 527
Cdd:COG5640  172 KADVPVVSDATCAAYGGFDGGTM------LCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYT 245
                        250
                 ....*....|....
gi 281360421 528 NIQRFVPWINKVMA 541
Cdd:COG5640  246 RVSAYRDWIKSTAG 259
Trypsin pfam00089
Trypsin;
300-536 4.18e-66

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 213.84  E-value: 4.18e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421  300 IVGGHSTGFGSHPWQVALIKSGfltRKLSCGGALISNRWVITAAHCVASTpnSNMKIRLGEWDVRGQEERLNHeeYGIER 379
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSS---GKHFCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLREGGEQK--FDVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421  380 KEVHPHYNPADFVNDVALIRLDRNVVYKQHIIPVCLPPSTTKLT-GKMATVAGWGRTRHGQStvPSVLQEVDVEVISNDR 458
Cdd:pfam00089  74 IIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPvGTTCTVSGWGNTKTLGP--SDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281360421  459 CQRWFRAAgrreaIHDVFLCAGYkdGGRDSCQGDSGGPLtltMDGRKTLIGLVSWGIGCGREHLPGVYTNIQRFVPWI 536
Cdd:pfam00089 152 CRSAYGGT-----VTDTMICAGA--GGKDACQGDSGGPL---VCSDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
328-514 2.53e-12

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 65.85  E-value: 2.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421 328 SCGGALISNRWVITAAHCVASTPN----SNMKIRLGEWDVRgqeerlnHEEYGIERKEVHPHY-NPADFVNDVALIRLDR 402
Cdd:COG3591   13 VCTGTLIGPNLVLTAGHCVYDGAGggwaTNIVFVPGYNGGP-------YGTATATRFRVPPGWvASGDAGYDYALLRLDE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360421 403 NVVYKQHIIPvcLPPSTTKLTGKMATVAGWGRTRHGQSTVpsvlqevdvevisndRCQRWFRAAGRREAIHDvflCagyk 482
Cdd:COG3591   86 PLGDTTGWLG--LAFNDAPLAGEPVTIIGYPGDRPKDLSL---------------DCSGRVTGVQGNRLSYD---C---- 141
                        170       180       190
                 ....*....|....*....|....*....|..
gi 281360421 483 dggrDSCQGDSGGPLTLTMDGRKTLIGLVSWG 514
Cdd:COG3591  142 ----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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