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Conserved domains on  [gi|24647620|ref|NP_650600|]
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uncharacterized protein Dmel_CG17475, 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 ...
50-269 3.37e-69

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: 214.06  E-value: 3.37e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620  50 VINGEDVQLGEAKYQISLQGMYGGHICGGCIIDERHVLTAAHCVYGYNPTYLRVITGTV---EYEKPDAVYFVEEHWIHC 126
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHdlsSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620 127 NYNSPDYHNDIALIRLNDTIKFNEYTQPAELPT--APVANGTQLLLTGWGSTELWGDTPDILQKAYLTHVVYSTCQEIMN 204
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24647620 205 NDPSNGPCHICTLT-TGGQGACHGDSGGPLTHN----GVLYGLVNWGYPCAL-GVPDSHANVYYYLEWIRS 269
Cdd:cd00190 161 YGGTITDNMLCAGGlEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARpNYPGVYTRVSSYLDWIQK 231
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
50-269 3.37e-69

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: 214.06  E-value: 3.37e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620  50 VINGEDVQLGEAKYQISLQGMYGGHICGGCIIDERHVLTAAHCVYGYNPTYLRVITGTV---EYEKPDAVYFVEEHWIHC 126
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHdlsSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620 127 NYNSPDYHNDIALIRLNDTIKFNEYTQPAELPT--APVANGTQLLLTGWGSTELWGDTPDILQKAYLTHVVYSTCQEIMN 204
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24647620 205 NDPSNGPCHICTLT-TGGQGACHGDSGGPLTHN----GVLYGLVNWGYPCAL-GVPDSHANVYYYLEWIRS 269
Cdd:cd00190 161 YGGTITDNMLCAGGlEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARpNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
49-267 1.58e-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: 207.15  E-value: 1.58e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620     49 RVINGEDVQLGEAKYQISLQGMYGGHICGGCIIDERHVLTAAHCVYGYNPTYLRVITGT--VEYEKPDAVYFVEEHWIHC 126
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGShdLSSGEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620    127 NYNSPDYHNDIALIRLNDTIKFNEYTQPAELPTA--PVANGTQLLLTGWGSTELW-GDTPDILQKAYLTHVVYSTCQEIM 203
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24647620    204 NNDPSNGPCHICTLT-TGGQGACHGDSGGPLTHN---GVLYGLVNWGYPCAL-GVPDSHANVYYYLEWI 267
Cdd:smart00020 161 SGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARpGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
47-274 2.33e-57

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 184.85  E-value: 2.33e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620  47 QNRVINGEDVQLGEAKYQISLQGMYG--GHICGGCIIDERHVLTAAHCVYGYNPTYLRVITGTVEYEKPDA-VYFVEEHW 123
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNGpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGtVVKVARIV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620 124 IHCNYNSPDYHNDIALIRLNDTIKFNeytQPAELPTAP--VANGTQLLLTGWGST-ELWGDTPDILQKAYLTHVVYSTCQ 200
Cdd:COG5640 108 VHPDYDPATPGNDIALLKLATPVPGV---APAPLATSAdaAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVVSDATCA 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620 201 EIMNNDPSNgpcHICT-LTTGGQGACHGDSGGPLTH----NGVLYGLVNWGY-PCALGVPDSHANVYYYLEWIRSMISGP 274
Cdd:COG5640 185 AYGGFDGGT---MLCAgYPEGGKDACQGDSGGPLVVkdggGWVLVGVVSWGGgPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
Trypsin pfam00089
Trypsin;
50-267 7.92e-52

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 169.16  E-value: 7.92e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620    50 VINGEDVQLGEAKYQISLQGMYGGHICGGCIIDERHVLTAAHCVYGYNPTYLRVITGTVEYEKPDAVYF-VEEHWIHCNY 128
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFdVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620   129 NSPDYHNDIALIRLNDTIKFNEYTQPAELPTA--PVANGTQLLLTGWGSTELwGDTPDILQKAYLTHVVYSTCQEIMNND 206
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDAssDLPVGTTCTVSGWGNTKT-LGPSDTLQEVTVPVVSRETCRSAYGGT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24647620   207 PSNGpcHICTlTTGGQGACHGDSGGPL-THNGVLYGLVNWGYPCALG-VPDSHANVYYYLEWI 267
Cdd:pfam00089 160 VTDT--MICA-GAGGKDACQGDSGGPLvCSDGELIGIVSWGYGCASGnYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
50-269 3.37e-69

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: 214.06  E-value: 3.37e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620  50 VINGEDVQLGEAKYQISLQGMYGGHICGGCIIDERHVLTAAHCVYGYNPTYLRVITGTV---EYEKPDAVYFVEEHWIHC 126
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHdlsSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620 127 NYNSPDYHNDIALIRLNDTIKFNEYTQPAELPT--APVANGTQLLLTGWGSTELWGDTPDILQKAYLTHVVYSTCQEIMN 204
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24647620 205 NDPSNGPCHICTLT-TGGQGACHGDSGGPLTHN----GVLYGLVNWGYPCAL-GVPDSHANVYYYLEWIRS 269
Cdd:cd00190 161 YGGTITDNMLCAGGlEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARpNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
49-267 1.58e-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: 207.15  E-value: 1.58e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620     49 RVINGEDVQLGEAKYQISLQGMYGGHICGGCIIDERHVLTAAHCVYGYNPTYLRVITGT--VEYEKPDAVYFVEEHWIHC 126
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGShdLSSGEEGQVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620    127 NYNSPDYHNDIALIRLNDTIKFNEYTQPAELPTA--PVANGTQLLLTGWGSTELW-GDTPDILQKAYLTHVVYSTCQEIM 203
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24647620    204 NNDPSNGPCHICTLT-TGGQGACHGDSGGPLTHN---GVLYGLVNWGYPCAL-GVPDSHANVYYYLEWI 267
Cdd:smart00020 161 SGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARpGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
47-274 2.33e-57

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 184.85  E-value: 2.33e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620  47 QNRVINGEDVQLGEAKYQISLQGMYG--GHICGGCIIDERHVLTAAHCVYGYNPTYLRVITGTVEYEKPDA-VYFVEEHW 123
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNGpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGtVVKVARIV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620 124 IHCNYNSPDYHNDIALIRLNDTIKFNeytQPAELPTAP--VANGTQLLLTGWGST-ELWGDTPDILQKAYLTHVVYSTCQ 200
Cdd:COG5640 108 VHPDYDPATPGNDIALLKLATPVPGV---APAPLATSAdaAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVVSDATCA 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620 201 EIMNNDPSNgpcHICT-LTTGGQGACHGDSGGPLTH----NGVLYGLVNWGY-PCALGVPDSHANVYYYLEWIRSMISGP 274
Cdd:COG5640 185 AYGGFDGGT---MLCAgYPEGGKDACQGDSGGPLVVkdggGWVLVGVVSWGGgPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
Trypsin pfam00089
Trypsin;
50-267 7.92e-52

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 169.16  E-value: 7.92e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620    50 VINGEDVQLGEAKYQISLQGMYGGHICGGCIIDERHVLTAAHCVYGYNPTYLRVITGTVEYEKPDAVYF-VEEHWIHCNY 128
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFdVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620   129 NSPDYHNDIALIRLNDTIKFNEYTQPAELPTA--PVANGTQLLLTGWGSTELwGDTPDILQKAYLTHVVYSTCQEIMNND 206
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDAssDLPVGTTCTVSGWGNTKT-LGPSDTLQEVTVPVVSRETCRSAYGGT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24647620   207 PSNGpcHICTlTTGGQGACHGDSGGPL-THNGVLYGLVNWGYPCALG-VPDSHANVYYYLEWI 267
Cdd:pfam00089 160 VTDT--MICA-GAGGKDACQGDSGGPLvCSDGELIGIVSWGYGCASGnYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
72-248 1.22e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 62.39  E-value: 1.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620  72 GGHICGGCIIDERHVLTAAHCVY----GYNPTYLRVITGtveYEK-PDAVYFVEEHWIHCNY-NSPDYHNDIALIRLNDT 145
Cdd:COG3591  10 GGGVCTGTLIGPNLVLTAGHCVYdgagGGWATNIVFVPG---YNGgPYGTATATRFRVPPGWvASGDAGYDYALLRLDEP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647620 146 IkfNEYTQPAEL-PTAPVANGTQLLLTGWGstelwGDTPDILqkaylthVVYSTCQeiMNNDPSNGPCHICTlttggqgA 224
Cdd:COG3591  87 L--GDTTGWLGLaFNDAPLAGEPVTIIGYP-----GDRPKDL-------SLDCSGR--VTGVQGNRLSYDCD-------T 143
                       170       180
                ....*....|....*....|....*...
gi 24647620 225 CHGDSGGPL----THNGVLYGLVNWGYP 248
Cdd:COG3591 144 TGGSSGSPVlddsDGGGRVVGVHSAGGA 171
 
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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