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Conserved domains on  [gi|1624698660|ref|NP_650177|]
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uncharacterized protein Dmel_CG10041 [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 ...
49-264 1.82e-38

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: 135.10  E-value: 1.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698660  49 RYPYIVSIgenLKGYYKHLCVGVILSNEFVLSAAHCIQTNPTKQLYVAGGADSLNSRKQT--RFFVVERRWHPQFRVLG- 125
Cdd:cd00190    11 SFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGgqVIKVKKVIVHPNYNPSTy 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698660 126 GNDIAVLRIYPKFPLDDvRFRSINFAGKPQR-DSGTQASLVGWGRVGVGKI--RKLQEMPFLTMENDECQQSHR-FVFLK 201
Cdd:cd00190    88 DNDIALLKLKRPVTLSD-NVRPICLPSSGYNlPAGTTCTVSGWGRTSEGGPlpDVLQEVNVPIVSNAECKRAYSyGGTIT 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1624698660 202 PLDICAMHLKGPRGPCDGDSGAPLM--NVAKEKLYGLLSYGRkAC-TPLKPYAFTRINAYSSWIQE 264
Cdd:cd00190   167 DNMLCAGGLEGGKDACQGDSGGPLVcnDNGRGVLVGIVSWGS-GCaRPNYPGVYTRVSSYLDWIQK 231
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
49-264 1.82e-38

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: 135.10  E-value: 1.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698660  49 RYPYIVSIgenLKGYYKHLCVGVILSNEFVLSAAHCIQTNPTKQLYVAGGADSLNSRKQT--RFFVVERRWHPQFRVLG- 125
Cdd:cd00190    11 SFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGgqVIKVKKVIVHPNYNPSTy 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698660 126 GNDIAVLRIYPKFPLDDvRFRSINFAGKPQR-DSGTQASLVGWGRVGVGKI--RKLQEMPFLTMENDECQQSHR-FVFLK 201
Cdd:cd00190    88 DNDIALLKLKRPVTLSD-NVRPICLPSSGYNlPAGTTCTVSGWGRTSEGGPlpDVLQEVNVPIVSNAECKRAYSyGGTIT 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1624698660 202 PLDICAMHLKGPRGPCDGDSGAPLM--NVAKEKLYGLLSYGRkAC-TPLKPYAFTRINAYSSWIQE 264
Cdd:cd00190   167 DNMLCAGGLEGGKDACQGDSGGPLVcnDNGRGVLVGIVSWGS-GCaRPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
49-262 3.77e-37

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: 131.65  E-value: 3.77e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698660   49 RYPYIVSIgenLKGYYKHLCVGVILSNEFVLSAAHCIQTNPTKQLYVAGGADSLNSR-KQTRFFVVERRWHPQF-RVLGG 126
Cdd:smart00020  12 SFPWQVSL---QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGeEGQVIKVSKVIIHPNYnPSTYD 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698660  127 NDIAVLRIYPKFPLDDvRFRSINFAGKPQRDS-GTQASLVGWGRVGVGKI---RKLQEMPFLTMENDECQQSHRFVF-LK 201
Cdd:smart00020  89 NDIALLKLKEPVTLSD-NVRPICLPSSNYNVPaGTTCTVSGWGRTSEGAGslpDTLQEVNVPIVSNATCRRAYSGGGaIT 167
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1624698660  202 PLDICAMHLKGPRGPCDGDSGAPLM-NVAKEKLYGLLSYGRKACTPLKPYAFTRINAYSSWI 262
Cdd:smart00020 168 DNMLCAGGLEGGKDACQGDSGGPLVcNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
50-270 2.66e-36

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 130.15  E-value: 2.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698660  50 YPYIVSIgENLKGYYKHLCVGVILSNEFVLSAAHCIQTNPTKQLYVAGGADSLNSRKQTRFFVVERRWHPQFR-VLGGND 128
Cdd:COG5640    42 YPWMVAL-QSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTVVKVARIVVHPDYDpATPGND 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698660 129 IAVLRIypKFPLDDVRFRSINfAGKPQRDSGTQASLVGWGRV--GVGKI-RKLQEMPFLTMENDECQQSHRFVFlkPLDI 205
Cdd:COG5640   121 IALLKL--ATPVPGVAPAPLA-TSADAAAPGTPATVAGWGRTseGPGSQsGTLRKADVPVVSDATCAAYGGFDG--GTML 195
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624698660 206 CAMHLKGPRGPCDGDSGAPLMNVA--KEKLYGLLSYGRKACTPLKPYAFTRINAYSSWIQESMDSMA 270
Cdd:COG5640   196 CAGYPEGGKDACQGDSGGPLVVKDggGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 262
Trypsin pfam00089
Trypsin;
50-262 2.09e-27

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 105.60  E-value: 2.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698660  50 YPYIVSIgeNLKGYyKHLCVGVILSNEFVLSAAHCIQTNPTKQLYVagGADSLNSRKQTRFFV-VER-RWHPQFRVLG-G 126
Cdd:pfam00089  12 FPWQVSL--QLSSG-KHFCGGSLISENWVLTAAHCVSGASDVKVVL--GAHNIVLREGGEQKFdVEKiIVHPNYNPDTlD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698660 127 NDIAVLRIYPKFPLDDvrfrSINFAGKPQRDS----GTQASLVGWGRVG-VGKIRKLQEMPFLTMENDECQQSHRFVfLK 201
Cdd:pfam00089  87 NDIALLKLESPVTLGD----TVRPICLPDASSdlpvGTTCTVSGWGNTKtLGPSDTLQEVTVPVVSRETCRSAYGGT-VT 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1624698660 202 PLDICAmhLKGPRGPCDGDSGAPLMNvAKEKLYGLLSYGRKACTPLKPYAFTRINAYSSWI 262
Cdd:pfam00089 162 DTMICA--GAGGKDACQGDSGGPLVC-SDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
49-264 1.82e-38

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: 135.10  E-value: 1.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698660  49 RYPYIVSIgenLKGYYKHLCVGVILSNEFVLSAAHCIQTNPTKQLYVAGGADSLNSRKQT--RFFVVERRWHPQFRVLG- 125
Cdd:cd00190    11 SFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGgqVIKVKKVIVHPNYNPSTy 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698660 126 GNDIAVLRIYPKFPLDDvRFRSINFAGKPQR-DSGTQASLVGWGRVGVGKI--RKLQEMPFLTMENDECQQSHR-FVFLK 201
Cdd:cd00190    88 DNDIALLKLKRPVTLSD-NVRPICLPSSGYNlPAGTTCTVSGWGRTSEGGPlpDVLQEVNVPIVSNAECKRAYSyGGTIT 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1624698660 202 PLDICAMHLKGPRGPCDGDSGAPLM--NVAKEKLYGLLSYGRkAC-TPLKPYAFTRINAYSSWIQE 264
Cdd:cd00190   167 DNMLCAGGLEGGKDACQGDSGGPLVcnDNGRGVLVGIVSWGS-GCaRPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
49-262 3.77e-37

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: 131.65  E-value: 3.77e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698660   49 RYPYIVSIgenLKGYYKHLCVGVILSNEFVLSAAHCIQTNPTKQLYVAGGADSLNSR-KQTRFFVVERRWHPQF-RVLGG 126
Cdd:smart00020  12 SFPWQVSL---QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGeEGQVIKVSKVIIHPNYnPSTYD 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698660  127 NDIAVLRIYPKFPLDDvRFRSINFAGKPQRDS-GTQASLVGWGRVGVGKI---RKLQEMPFLTMENDECQQSHRFVF-LK 201
Cdd:smart00020  89 NDIALLKLKEPVTLSD-NVRPICLPSSNYNVPaGTTCTVSGWGRTSEGAGslpDTLQEVNVPIVSNATCRRAYSGGGaIT 167
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1624698660  202 PLDICAMHLKGPRGPCDGDSGAPLM-NVAKEKLYGLLSYGRKACTPLKPYAFTRINAYSSWI 262
Cdd:smart00020 168 DNMLCAGGLEGGKDACQGDSGGPLVcNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
50-270 2.66e-36

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 130.15  E-value: 2.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698660  50 YPYIVSIgENLKGYYKHLCVGVILSNEFVLSAAHCIQTNPTKQLYVAGGADSLNSRKQTRFFVVERRWHPQFR-VLGGND 128
Cdd:COG5640    42 YPWMVAL-QSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTVVKVARIVVHPDYDpATPGND 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698660 129 IAVLRIypKFPLDDVRFRSINfAGKPQRDSGTQASLVGWGRV--GVGKI-RKLQEMPFLTMENDECQQSHRFVFlkPLDI 205
Cdd:COG5640   121 IALLKL--ATPVPGVAPAPLA-TSADAAAPGTPATVAGWGRTseGPGSQsGTLRKADVPVVSDATCAAYGGFDG--GTML 195
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624698660 206 CAMHLKGPRGPCDGDSGAPLMNVA--KEKLYGLLSYGRKACTPLKPYAFTRINAYSSWIQESMDSMA 270
Cdd:COG5640   196 CAGYPEGGKDACQGDSGGPLVVKDggGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 262
Trypsin pfam00089
Trypsin;
50-262 2.09e-27

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 105.60  E-value: 2.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698660  50 YPYIVSIgeNLKGYyKHLCVGVILSNEFVLSAAHCIQTNPTKQLYVagGADSLNSRKQTRFFV-VER-RWHPQFRVLG-G 126
Cdd:pfam00089  12 FPWQVSL--QLSSG-KHFCGGSLISENWVLTAAHCVSGASDVKVVL--GAHNIVLREGGEQKFdVEKiIVHPNYNPDTlD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624698660 127 NDIAVLRIYPKFPLDDvrfrSINFAGKPQRDS----GTQASLVGWGRVG-VGKIRKLQEMPFLTMENDECQQSHRFVfLK 201
Cdd:pfam00089  87 NDIALLKLESPVTLGD----TVRPICLPDASSdlpvGTTCTVSGWGNTKtLGPSDTLQEVTVPVVSRETCRSAYGGT-VT 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1624698660 202 PLDICAmhLKGPRGPCDGDSGAPLMNvAKEKLYGLLSYGRKACTPLKPYAFTRINAYSSWI 262
Cdd:pfam00089 162 DTMICA--GAGGKDACQGDSGGPLVC-SDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
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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