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Conserved domains on  [gi|116008302|ref|NP_610441|]
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uncharacterized protein Dmel_CG8170, 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 ...
612-846 6.55e-84

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: 267.99  E-value: 6.55e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302 612 IVGGDDAGFGSFPWQAYIRIGSSR--CGGSLISRRHVVTAGHCVARATPRQVHVTLGDYVINSAVEPlpAYTFGVRRIDV 689
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRhfCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGG--GQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302 690 HPyfKFTPQADRFDISVLTLERTVHFMPHIAPICLPEKNEDFL-GKFGWAAGWGALNPGSRLrPKTLQAVDVPVIENRIC 768
Cdd:cd00190   79 HP--NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPaGTTCTVSGWGRTSEGGPL-PDVLQEVNVPIVSNAEC 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116008302 769 ERWHRQNGinvVIYQEMLCAGYRNGGKDSCQGDSGGPLMHDKNGRWYLIGVVSAGYSCASRGQPGIYHSVSKTVDWVS 846
Cdd:cd00190  156 KRAYSYGG---TITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
612-846 6.55e-84

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: 267.99  E-value: 6.55e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302 612 IVGGDDAGFGSFPWQAYIRIGSSR--CGGSLISRRHVVTAGHCVARATPRQVHVTLGDYVINSAVEPlpAYTFGVRRIDV 689
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRhfCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGG--GQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302 690 HPyfKFTPQADRFDISVLTLERTVHFMPHIAPICLPEKNEDFL-GKFGWAAGWGALNPGSRLrPKTLQAVDVPVIENRIC 768
Cdd:cd00190   79 HP--NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPaGTTCTVSGWGRTSEGGPL-PDVLQEVNVPIVSNAEC 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116008302 769 ERWHRQNGinvVIYQEMLCAGYRNGGKDSCQGDSGGPLMHDKNGRWYLIGVVSAGYSCASRGQPGIYHSVSKTVDWVS 846
Cdd:cd00190  156 KRAYSYGG---TITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
611-845 5.90e-80

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: 257.22  E-value: 5.90e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302   611 RIVGGDDAGFGSFPWQAYIRIGSSR--CGGSLISRRHVVTAGHCVARATPRQVHVTLGDYVINSavePLPAYTFGVRRID 688
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRhfCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSS---GEEGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302   689 VHPyfKFTPQADRFDISVLTLERTVHFMPHIAPICLPEKNEDF-LGKFGWAAGWGALNPGSRLRPKTLQAVDVPVIENRI 767
Cdd:smart00020  78 IHP--NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVpAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116008302   768 CERWHRQNGinvVIYQEMLCAGYRNGGKDSCQGDSGGPLMHdKNGRWYLIGVVSAGYSCASRGQPGIYHSVSKTVDWV 845
Cdd:smart00020 156 CRRAYSGGG---AITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
607-850 1.11e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 203.73  E-value: 1.11e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302 607 TAQRRIVGGDDAGFGSFPWQAYIRI----GSSRCGGSLISRRHVVTAGHCVARATPRQVHVTLGDYVINSAveplPAYTF 682
Cdd:COG5640   26 DAAPAIVGGTPATVGEYPWMVALQSsngpSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTS----GGTVV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302 683 GVRRIDVHPyfKFTPQADRFDISVLTLERTVhfmPHIAPICLPEKNEDF-LGKFGWAAGWGALNPGSRLRPKTLQAVDVP 761
Cdd:COG5640  102 KVARIVVHP--DYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAaPGTPATVAGWGRTSEGPGSQSGTLRKADVP 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302 762 VIENRICERWHRQNGinvviyQEMLCAGYRNGGKDSCQGDSGGPLMHDKNGRWYLIGVVSAGYSCASRGQPGIYHSVSKT 841
Cdd:COG5640  177 VVSDATCAAYGGFDG------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAY 250

                 ....*....
gi 116008302 842 VDWVSYVVG 850
Cdd:COG5640  251 RDWIKSTAG 259
Trypsin pfam00089
Trypsin;
612-845 1.23e-55

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 191.12  E-value: 1.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302  612 IVGGDDAGFGSFPWQA--YIRIGSSRCGGSLISRRHVVTAGHCVARatPRQVHVTLGDYVINSAVEPLPayTFGVRRIDV 689
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVslQLSSGKHFCGGSLISENWVLTAAHCVSG--ASDVKVVLGAHNIVLREGGEQ--KFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302  690 HPyfKFTPQADRFDISVLTLERTVHFMPHIAPICLPEKNEDF-LGKFGWAAGWGalNPGSRLRPKTLQAVDVPVIENRIC 768
Cdd:pfam00089  77 HP--NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLpVGTTCTVSGWG--NTKTLGPSDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116008302  769 ERWHrqngiNVVIYQEMLCAGYrnGGKDSCQGDSGGPLMHDKNgrwYLIGVVSAGYSCASRGQPGIYHSVSKTVDWV 845
Cdd:pfam00089 153 RSAY-----GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
612-846 6.55e-84

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: 267.99  E-value: 6.55e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302 612 IVGGDDAGFGSFPWQAYIRIGSSR--CGGSLISRRHVVTAGHCVARATPRQVHVTLGDYVINSAVEPlpAYTFGVRRIDV 689
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRhfCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGG--GQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302 690 HPyfKFTPQADRFDISVLTLERTVHFMPHIAPICLPEKNEDFL-GKFGWAAGWGALNPGSRLrPKTLQAVDVPVIENRIC 768
Cdd:cd00190   79 HP--NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPaGTTCTVSGWGRTSEGGPL-PDVLQEVNVPIVSNAEC 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116008302 769 ERWHRQNGinvVIYQEMLCAGYRNGGKDSCQGDSGGPLMHDKNGRWYLIGVVSAGYSCASRGQPGIYHSVSKTVDWVS 846
Cdd:cd00190  156 KRAYSYGG---TITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
611-845 5.90e-80

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: 257.22  E-value: 5.90e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302   611 RIVGGDDAGFGSFPWQAYIRIGSSR--CGGSLISRRHVVTAGHCVARATPRQVHVTLGDYVINSavePLPAYTFGVRRID 688
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRhfCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSS---GEEGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302   689 VHPyfKFTPQADRFDISVLTLERTVHFMPHIAPICLPEKNEDF-LGKFGWAAGWGALNPGSRLRPKTLQAVDVPVIENRI 767
Cdd:smart00020  78 IHP--NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVpAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116008302   768 CERWHRQNGinvVIYQEMLCAGYRNGGKDSCQGDSGGPLMHdKNGRWYLIGVVSAGYSCASRGQPGIYHSVSKTVDWV 845
Cdd:smart00020 156 CRRAYSGGG---AITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
607-850 1.11e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 203.73  E-value: 1.11e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302 607 TAQRRIVGGDDAGFGSFPWQAYIRI----GSSRCGGSLISRRHVVTAGHCVARATPRQVHVTLGDYVINSAveplPAYTF 682
Cdd:COG5640   26 DAAPAIVGGTPATVGEYPWMVALQSsngpSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTS----GGTVV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302 683 GVRRIDVHPyfKFTPQADRFDISVLTLERTVhfmPHIAPICLPEKNEDF-LGKFGWAAGWGALNPGSRLRPKTLQAVDVP 761
Cdd:COG5640  102 KVARIVVHP--DYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAaPGTPATVAGWGRTSEGPGSQSGTLRKADVP 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302 762 VIENRICERWHRQNGinvviyQEMLCAGYRNGGKDSCQGDSGGPLMHDKNGRWYLIGVVSAGYSCASRGQPGIYHSVSKT 841
Cdd:COG5640  177 VVSDATCAAYGGFDG------GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAY 250

                 ....*....
gi 116008302 842 VDWVSYVVG 850
Cdd:COG5640  251 RDWIKSTAG 259
Trypsin pfam00089
Trypsin;
612-845 1.23e-55

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 191.12  E-value: 1.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302  612 IVGGDDAGFGSFPWQA--YIRIGSSRCGGSLISRRHVVTAGHCVARatPRQVHVTLGDYVINSAVEPLPayTFGVRRIDV 689
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVslQLSSGKHFCGGSLISENWVLTAAHCVSG--ASDVKVVLGAHNIVLREGGEQ--KFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302  690 HPyfKFTPQADRFDISVLTLERTVHFMPHIAPICLPEKNEDF-LGKFGWAAGWGalNPGSRLRPKTLQAVDVPVIENRIC 768
Cdd:pfam00089  77 HP--NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLpVGTTCTVSGWG--NTKTLGPSDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116008302  769 ERWHrqngiNVVIYQEMLCAGYrnGGKDSCQGDSGGPLMHDKNgrwYLIGVVSAGYSCASRGQPGIYHSVSKTVDWV 845
Cdd:pfam00089 153 RSAY-----GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
632-832 3.88e-14

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 71.63  E-value: 3.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302 632 GSSRCGGSLISRRHVVTAGHCV----ARATPRQVHVTLGdyvinsaVEPLPAYTFGVRRIDVHPYFkFTPQADRFDISVL 707
Cdd:COG3591   10 GGGVCTGTLIGPNLVLTAGHCVydgaGGGWATNIVFVPG-------YNGGPYGTATATRFRVPPGW-VASGDAGYDYALL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008302 708 TLERTVHfmPHIAPICLPEKNEDFLGKFGWAAGWgalnPGSRLRPKTLQAVdvpvienriCERWHRQNgiNVVIYQemlC 787
Cdd:COG3591   82 RLDEPLG--DTTGWLGLAFNDAPLAGEPVTIIGY----PGDRPKDLSLDCS---------GRVTGVQG--NRLSYD---C 141
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 116008302 788 agyrnggkDSCQGDSGGPLMHDKNGRWYLIGVVSAGY-SCASRGQP 832
Cdd:COG3591  142 --------DTTGGSSGSPVLDDSDGGGRVVGVHSAGGaDRANTGVR 179
 
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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