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Conserved domains on  [gi|24645302|ref|NP_649880|]
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uncharacterized protein Dmel_CG12951 [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 ...
30-260 1.11e-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: 222.15  E-value: 1.11e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302  30 VVNGTDSSVLKYPFVVSLRSYDGSHSCGGSIISKHFVMTAAHCTNGRPADTLSIQFGVTNISAMGPN--VVGIKKIIQHE 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGgqVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302 108 DFDPTRQNaNDISLLMVEEPFEFDGvSVAPVELPALAFAVPqsdAGVEGVLIGWGLNDTYGSVQDTLQEVSLKIYSDEEC 187
Cdd:cd00190  81 NYNPSTYD-NDIALLKLKRPVTLSD-NVRPICLPSSGYNLP---AGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24645302 188 TSRH-NGQTDPKYHICGGVDEGGKGQCSGDSGGPLIYN----GQQVGIVSWSIKpCTVAPYPGVYCKVSQYVDWIKSN 260
Cdd:cd00190 156 KRAYsYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
30-260 1.11e-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: 222.15  E-value: 1.11e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302  30 VVNGTDSSVLKYPFVVSLRSYDGSHSCGGSIISKHFVMTAAHCTNGRPADTLSIQFGVTNISAMGPN--VVGIKKIIQHE 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGgqVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302 108 DFDPTRQNaNDISLLMVEEPFEFDGvSVAPVELPALAFAVPqsdAGVEGVLIGWGLNDTYGSVQDTLQEVSLKIYSDEEC 187
Cdd:cd00190  81 NYNPSTYD-NDIALLKLKRPVTLSD-NVRPICLPSSGYNLP---AGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24645302 188 TSRH-NGQTDPKYHICGGVDEGGKGQCSGDSGGPLIYN----GQQVGIVSWSIKpCTVAPYPGVYCKVSQYVDWIKSN 260
Cdd:cd00190 156 KRAYsYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
29-257 3.67e-72

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: 220.63  E-value: 3.67e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302     29 RVVNGTDSSVLKYPFVVSLRSYDGSHSCGGSIISKHFVMTAAHCTNGRPADTLSIQFGVTNISAMGPN-VVGIKKIIQHE 107
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGqVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302    108 DFDPTRQNaNDISLLMVEEPFEFDGvSVAPVELPALAFAVPqsdAGVEGVLIGWG-LNDTYGSVQDTLQEVSLKIYSDEE 186
Cdd:smart00020  81 NYNPSTYD-NDIALLKLKEPVTLSD-NVRPICLPSSNYNVP---AGTTCTVSGWGrTSEGAGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24645302    187 CTSRHNGQ-TDPKYHICGGVDEGGKGQCSGDSGGPLIYN---GQQVGIVSWSIkPCTVAPYPGVYCKVSQYVDWI 257
Cdd:smart00020 156 CRRAYSGGgAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
7-259 9.27e-69

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 212.97  E-value: 9.27e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302   7 LSLSLIVILAVTTVGQAAPsisRVVNGTDSSVLKYPFVVSLRSYDG--SHSCGGSIISKHFVMTAAHCTNGRPADTLSIQ 84
Cdd:COG5640  11 AAAALALALAAAPAADAAP---AIVGGTPATVGEYPWMVALQSSNGpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302  85 FGVTNISAMGPNVVGIKKIIQHEDFDPTRQNaNDISLLMVEEPFEfdgvSVAPVELPAlafAVPQSDAGVEGVLIGWGL- 163
Cdd:COG5640  88 IGSTDLSTSGGTVVKVARIVVHPDYDPATPG-NDIALLKLATPVP----GVAPAPLAT---SADAAAPGTPATVAGWGRt 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302 164 NDTYGSVQDTLQEVSLKIYSDEECTSrhNGQTDPKYHICGGVDEGGKGQCSGDSGGPLIY----NGQQVGIVSWSIKPCt 239
Cdd:COG5640 160 SEGPGSQSGTLRKADVPVVSDATCAA--YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVkdggGWVLVGVVSWGGGPC- 236
                       250       260
                ....*....|....*....|
gi 24645302 240 VAPYPGVYCKVSQYVDWIKS 259
Cdd:COG5640 237 AAGYPGVYTRVSAYRDWIKS 256
Trypsin pfam00089
Trypsin;
30-257 6.01e-51

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 166.08  E-value: 6.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302    30 VVNGTDSSVLKYPFVVSLRSYDGSHSCGGSIISKHFVMTAAHCTNGRPADTLSiqFGVTNISAM--GPNVVGIKKIIQHE 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVV--LGAHNIVLRegGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302   108 DFDPTRQNaNDISLLMVEEPFEFdGVSVAPVELPALAFAVPqsdAGVEGVLIGWGLNDTYGSVqDTLQEVSLKIYSDEEC 187
Cdd:pfam00089  79 NYNPDTLD-NDIALLKLESPVTL-GDTVRPICLPDASSDLP---VGTTCTVSGWGNTKTLGPS-DTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24645302   188 TSRHNGQTDPKYhICggVDEGGKGQCSGDSGGPLIYNGQQV-GIVSWsIKPCTVAPYPGVYCKVSQYVDWI 257
Cdd:pfam00089 153 RSAYGGTVTDTM-IC--AGAGGKDACQGDSGGPLVCSDGELiGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
30-260 1.11e-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: 222.15  E-value: 1.11e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302  30 VVNGTDSSVLKYPFVVSLRSYDGSHSCGGSIISKHFVMTAAHCTNGRPADTLSIQFGVTNISAMGPN--VVGIKKIIQHE 107
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGgqVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302 108 DFDPTRQNaNDISLLMVEEPFEFDGvSVAPVELPALAFAVPqsdAGVEGVLIGWGLNDTYGSVQDTLQEVSLKIYSDEEC 187
Cdd:cd00190  81 NYNPSTYD-NDIALLKLKRPVTLSD-NVRPICLPSSGYNLP---AGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24645302 188 TSRH-NGQTDPKYHICGGVDEGGKGQCSGDSGGPLIYN----GQQVGIVSWSIKpCTVAPYPGVYCKVSQYVDWIKSN 260
Cdd:cd00190 156 KRAYsYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
29-257 3.67e-72

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: 220.63  E-value: 3.67e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302     29 RVVNGTDSSVLKYPFVVSLRSYDGSHSCGGSIISKHFVMTAAHCTNGRPADTLSIQFGVTNISAMGPN-VVGIKKIIQHE 107
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGqVIKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302    108 DFDPTRQNaNDISLLMVEEPFEFDGvSVAPVELPALAFAVPqsdAGVEGVLIGWG-LNDTYGSVQDTLQEVSLKIYSDEE 186
Cdd:smart00020  81 NYNPSTYD-NDIALLKLKEPVTLSD-NVRPICLPSSNYNVP---AGTTCTVSGWGrTSEGAGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24645302    187 CTSRHNGQ-TDPKYHICGGVDEGGKGQCSGDSGGPLIYN---GQQVGIVSWSIkPCTVAPYPGVYCKVSQYVDWI 257
Cdd:smart00020 156 CRRAYSGGgAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
7-259 9.27e-69

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 212.97  E-value: 9.27e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302   7 LSLSLIVILAVTTVGQAAPsisRVVNGTDSSVLKYPFVVSLRSYDG--SHSCGGSIISKHFVMTAAHCTNGRPADTLSIQ 84
Cdd:COG5640  11 AAAALALALAAAPAADAAP---AIVGGTPATVGEYPWMVALQSSNGpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302  85 FGVTNISAMGPNVVGIKKIIQHEDFDPTRQNaNDISLLMVEEPFEfdgvSVAPVELPAlafAVPQSDAGVEGVLIGWGL- 163
Cdd:COG5640  88 IGSTDLSTSGGTVVKVARIVVHPDYDPATPG-NDIALLKLATPVP----GVAPAPLAT---SADAAAPGTPATVAGWGRt 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302 164 NDTYGSVQDTLQEVSLKIYSDEECTSrhNGQTDPKYHICGGVDEGGKGQCSGDSGGPLIY----NGQQVGIVSWSIKPCt 239
Cdd:COG5640 160 SEGPGSQSGTLRKADVPVVSDATCAA--YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVkdggGWVLVGVVSWGGGPC- 236
                       250       260
                ....*....|....*....|
gi 24645302 240 VAPYPGVYCKVSQYVDWIKS 259
Cdd:COG5640 237 AAGYPGVYTRVSAYRDWIKS 256
Trypsin pfam00089
Trypsin;
30-257 6.01e-51

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 166.08  E-value: 6.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302    30 VVNGTDSSVLKYPFVVSLRSYDGSHSCGGSIISKHFVMTAAHCTNGRPADTLSiqFGVTNISAM--GPNVVGIKKIIQHE 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVV--LGAHNIVLRegGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302   108 DFDPTRQNaNDISLLMVEEPFEFdGVSVAPVELPALAFAVPqsdAGVEGVLIGWGLNDTYGSVqDTLQEVSLKIYSDEEC 187
Cdd:pfam00089  79 NYNPDTLD-NDIALLKLESPVTL-GDTVRPICLPDASSDLP---VGTTCTVSGWGNTKTLGPS-DTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24645302   188 TSRHNGQTDPKYhICggVDEGGKGQCSGDSGGPLIYNGQQV-GIVSWsIKPCTVAPYPGVYCKVSQYVDWI 257
Cdd:pfam00089 153 RSAYGGTVTDTM-IC--AGAGGKDACQGDSGGPLVCSDGELiGIVSW-GYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
44-238 6.27e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 48.52  E-value: 6.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302  44 VVSLRSYDGSHSCGGSIISKHFVMTAAHC----TNGRPADTLSIQFGVTNisamGPN-VVGIKKIIQHEDFDPTRQNAND 118
Cdd:COG3591   2 VGRLETDGGGGVCTGTLIGPNLVLTAGHCvydgAGGGWATNIVFVPGYNG----GPYgTATATRFRVPPGWVASGDAGYD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645302 119 ISLLMVEEPFefdGVSVAPVELPALAFAVPQSDAGVegvlIGWGLNDTYgsvqdtlqevslKIYSDEECTSRhNGQTDPK 198
Cdd:COG3591  78 YALLRLDEPL---GDTTGWLGLAFNDAPLAGEPVTI----IGYPGDRPK------------DLSLDCSGRVT-GVQGNRL 137
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 24645302 199 YHICGGvdeggkgqCSGDSGGPLIYN----GQQVGIVSWSIKPC 238
Cdd:COG3591 138 SYDCDT--------TGGSSGSPVLDDsdggGRVVGVHSAGGADR 173
 
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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