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Conserved domains on  [gi|281364300|ref|NP_608722|]
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uncharacterized protein Dmel_CG3117 [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 ...
95-329 4.07e-62

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: 197.88  E-value: 4.07e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300  95 GDQTKPNQFPWVTALF-AKGSYLGGGSLITPGLVLTAAHILAGLSPNDIMVRAGEWDLSSSEKlnPPMDRQVIKIMEHEA 173
Cdd:cd00190    4 GSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEG--GGQVIKVKKVIVHPN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300 174 FNYSSGANDLALLFLDSPFELRANIQTIRLPIPDKTF-DRRICTVAGWGmRSSTDVDIQTIQQKVDLPVVESSKCQRqlr 252
Cdd:cd00190   82 YNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLpAGTTCTVSGWG-RTSEGGPLPDVLQEVNVPIVSNAECKR--- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300 253 ltKMGSNYQLPASLMCAGGEE-GRDVC---SlfGGfALFCsldDDPNRYEQAGIVSFGVGCGQANVPTTFTHVSKFMEWI 328
Cdd:cd00190  158 --AYSYGGTITDNMLCAGGLEgGKDACqgdS--GG-PLVC---NDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229

                 .
gi 281364300 329 N 329
Cdd:cd00190  230 Q 230
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
95-329 4.07e-62

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: 197.88  E-value: 4.07e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300  95 GDQTKPNQFPWVTALF-AKGSYLGGGSLITPGLVLTAAHILAGLSPNDIMVRAGEWDLSSSEKlnPPMDRQVIKIMEHEA 173
Cdd:cd00190    4 GSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEG--GGQVIKVKKVIVHPN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300 174 FNYSSGANDLALLFLDSPFELRANIQTIRLPIPDKTF-DRRICTVAGWGmRSSTDVDIQTIQQKVDLPVVESSKCQRqlr 252
Cdd:cd00190   82 YNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLpAGTTCTVSGWG-RTSEGGPLPDVLQEVNVPIVSNAECKR--- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300 253 ltKMGSNYQLPASLMCAGGEE-GRDVC---SlfGGfALFCsldDDPNRYEQAGIVSFGVGCGQANVPTTFTHVSKFMEWI 328
Cdd:cd00190  158 --AYSYGGTITDNMLCAGGLEgGKDACqgdS--GG-PLVC---NDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229

                 .
gi 281364300 329 N 329
Cdd:cd00190  230 Q 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
95-328 2.42e-59

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: 190.97  E-value: 2.42e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300    95 GDQTKPNQFPWVTAL-FAKGSYLGGGSLITPGLVLTAAHILAGLSPNDIMVRAGEWDLSSSEklnPPMDRQVIKIMEHEA 173
Cdd:smart00020   5 GSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGE---EGQVIKVSKVIIHPN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300   174 FNYSSGANDLALLFLDSPFELRANIQTIRLPIPDKTF-DRRICTVAGWGMRSSTDVDIQTIQQKVDLPVVESSKCQRqlr 252
Cdd:smart00020  82 YNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVpAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR--- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300   253 ltKMGSNYQLPASLMCAGGEE-GRDVC---SlfGGfALFCSLdddpNRYEQAGIVSFGVGCGQANVPTTFTHVSKFMEWI 328
Cdd:smart00020 159 --AYSGGGAITDNMLCAGGLEgGKDACqgdS--GG-PLVCND----GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
86-332 2.05e-42

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 147.87  E-value: 2.05e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300  86 ALDGSPQVF-GDQTKPNQFPWVTALFAKGSYLG---GGSLITPGLVLTAAHILAGLSPNDIMVRAGEWDLSSSeklnPPM 161
Cdd:COG5640   24 AADAAPAIVgGTPATVGEYPWMVALQSSNGPSGqfcGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTS----GGT 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300 162 DRQVIKIMEHEAFNYSSGANDLALLFLDSPFelrANIQTIRL------PIPDKTFdrricTVAGWGMRSSTDVDIQTIQQ 235
Cdd:COG5640  100 VVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLatsadaAAPGTPA-----TVAGWGRTSEGPGSQSGTLR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300 236 KVDLPVVESSKCQRQLRLtkmgsnyqLPASLMCAGGEEG-RDVC---SlfGGFALFcsldDDPNRYEQAGIVSFGVGCGQ 311
Cdd:COG5640  172 KADVPVVSDATCAAYGGF--------DGGTMLCAGYPEGgKDACqgdS--GGPLVV----KDGGGWVLVGVVSWGGGPCA 237
                        250       260
                 ....*....|....*....|.
gi 281364300 312 ANVPTTFTHVSKFMEWINPHL 332
Cdd:COG5640  238 AGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
93-328 5.03e-42

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 145.66  E-value: 5.03e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300   93 VFGDQTKPNQFPWVTALFAKGSYLG-GGSLITPGLVLTAAHILAGlsPNDIMVRAGEWDLSSSEKlnPPMDRQVIKIMEH 171
Cdd:pfam00089   2 VGGDEAQPGSFPWQVSLQLSSGKHFcGGSLISENWVLTAAHCVSG--ASDVKVVLGAHNIVLREG--GEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300  172 EAFNYSSGANDLALLFLDSPFELRANIQTIRLPIPDKTF-DRRICTVAGWGmRSSTDVDIQTIQQkVDLPVVESSKCQRQ 250
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLpVGTTCTVSGWG-NTKTLGPSDTLQE-VTVPVVSRETCRSA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300  251 LRLTkmgsnyqLPASLMCAGGEeGRDVC---SlfGGfALFCSLDddpnryEQAGIVSFGVGCGQANVPTTFTHVSKFMEW 327
Cdd:pfam00089 156 YGGT-------VTDTMICAGAG-GKDACqgdS--GG-PLVCSDG------ELIGIVSWGYGCASGNYPGVYTPVSSYLDW 218

                  .
gi 281364300  328 I 328
Cdd:pfam00089 219 I 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
95-329 4.07e-62

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: 197.88  E-value: 4.07e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300  95 GDQTKPNQFPWVTALF-AKGSYLGGGSLITPGLVLTAAHILAGLSPNDIMVRAGEWDLSSSEKlnPPMDRQVIKIMEHEA 173
Cdd:cd00190    4 GSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEG--GGQVIKVKKVIVHPN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300 174 FNYSSGANDLALLFLDSPFELRANIQTIRLPIPDKTF-DRRICTVAGWGmRSSTDVDIQTIQQKVDLPVVESSKCQRqlr 252
Cdd:cd00190   82 YNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLpAGTTCTVSGWG-RTSEGGPLPDVLQEVNVPIVSNAECKR--- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300 253 ltKMGSNYQLPASLMCAGGEE-GRDVC---SlfGGfALFCsldDDPNRYEQAGIVSFGVGCGQANVPTTFTHVSKFMEWI 328
Cdd:cd00190  158 --AYSYGGTITDNMLCAGGLEgGKDACqgdS--GG-PLVC---NDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229

                 .
gi 281364300 329 N 329
Cdd:cd00190  230 Q 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
95-328 2.42e-59

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: 190.97  E-value: 2.42e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300    95 GDQTKPNQFPWVTAL-FAKGSYLGGGSLITPGLVLTAAHILAGLSPNDIMVRAGEWDLSSSEklnPPMDRQVIKIMEHEA 173
Cdd:smart00020   5 GSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGE---EGQVIKVSKVIIHPN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300   174 FNYSSGANDLALLFLDSPFELRANIQTIRLPIPDKTF-DRRICTVAGWGMRSSTDVDIQTIQQKVDLPVVESSKCQRqlr 252
Cdd:smart00020  82 YNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVpAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR--- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300   253 ltKMGSNYQLPASLMCAGGEE-GRDVC---SlfGGfALFCSLdddpNRYEQAGIVSFGVGCGQANVPTTFTHVSKFMEWI 328
Cdd:smart00020 159 --AYSGGGAITDNMLCAGGLEgGKDACqgdS--GG-PLVCND----GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
86-332 2.05e-42

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 147.87  E-value: 2.05e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300  86 ALDGSPQVF-GDQTKPNQFPWVTALFAKGSYLG---GGSLITPGLVLTAAHILAGLSPNDIMVRAGEWDLSSSeklnPPM 161
Cdd:COG5640   24 AADAAPAIVgGTPATVGEYPWMVALQSSNGPSGqfcGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTS----GGT 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300 162 DRQVIKIMEHEAFNYSSGANDLALLFLDSPFelrANIQTIRL------PIPDKTFdrricTVAGWGMRSSTDVDIQTIQQ 235
Cdd:COG5640  100 VVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLatsadaAAPGTPA-----TVAGWGRTSEGPGSQSGTLR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300 236 KVDLPVVESSKCQRQLRLtkmgsnyqLPASLMCAGGEEG-RDVC---SlfGGFALFcsldDDPNRYEQAGIVSFGVGCGQ 311
Cdd:COG5640  172 KADVPVVSDATCAAYGGF--------DGGTMLCAGYPEGgKDACqgdS--GGPLVV----KDGGGWVLVGVVSWGGGPCA 237
                        250       260
                 ....*....|....*....|.
gi 281364300 312 ANVPTTFTHVSKFMEWINPHL 332
Cdd:COG5640  238 AGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
93-328 5.03e-42

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 145.66  E-value: 5.03e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300   93 VFGDQTKPNQFPWVTALFAKGSYLG-GGSLITPGLVLTAAHILAGlsPNDIMVRAGEWDLSSSEKlnPPMDRQVIKIMEH 171
Cdd:pfam00089   2 VGGDEAQPGSFPWQVSLQLSSGKHFcGGSLISENWVLTAAHCVSG--ASDVKVVLGAHNIVLREG--GEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300  172 EAFNYSSGANDLALLFLDSPFELRANIQTIRLPIPDKTF-DRRICTVAGWGmRSSTDVDIQTIQQkVDLPVVESSKCQRQ 250
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLpVGTTCTVSGWG-NTKTLGPSDTLQE-VTVPVVSRETCRSA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300  251 LRLTkmgsnyqLPASLMCAGGEeGRDVC---SlfGGfALFCSLDddpnryEQAGIVSFGVGCGQANVPTTFTHVSKFMEW 327
Cdd:pfam00089 156 YGGT-------VTDTMICAGAG-GKDACqgdS--GG-PLVCSDG------ELIGIVSWGYGCASGNYPGVYTPVSSYLDW 218

                  .
gi 281364300  328 I 328
Cdd:pfam00089 219 I 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
113-221 2.29e-03

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 38.50  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364300 113 GSYLGGGSLITPGLVLTAAHIL----AGLSPNDIMVRAGEWDlssseklNPPMDRQVIKIMEHEAF-NYSSGANDLALLF 187
Cdd:COG3591   10 GGGVCTGTLIGPNLVLTAGHCVydgaGGGWATNIVFVPGYNG-------GPYGTATATRFRVPPGWvASGDAGYDYALLR 82
                         90       100       110
                 ....*....|....*....|....*....|....
gi 281364300 188 LDSPfeLRANIQTIRLPIPDKTFDRRICTVAGWG 221
Cdd:COG3591   83 LDEP--LGDTTGWLGLAFNDAPLAGEPVTIIGYP 114
 
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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