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Conserved domains on  [gi|24650929|ref|NP_651662|]
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uncharacterized protein Dmel_CG11842 [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 ...
73-315 1.05e-60

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: 193.26  E-value: 1.05e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929  73 IIGGGPAVPKEFPHAARLghkdENGEVEWFCGGTLISDRHVLTAAHCHYSPQGSVNIARLGDLefDTNNDDADPEDFDVK 152
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSL----QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSH--DLSSNEGGGQVIKVK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929 153 DFTAHPEFSYPAIYNDISVVRLSRPVTFNDYKHPACLPFDDGRL--GTSFIAIGWGQLEIVPRTeNKKLQKVKLYNYGTR 230
Cdd:cd00190  75 KVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLpaGTTCTVSGWGRTSEGGPL-PDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929 231 -CritadRNDELPEGYNATTQLCIGSNEH-KDTCNGDSGGPvLIYHmdYPCMYHVMGITSIGVACDTPDLPAMYTRVHFY 308
Cdd:cd00190 154 eC-----KRAYSYGGTITDNMLCAGGLEGgKDACQGDSGGP-LVCN--DNGRGVLVGIVSWGSGCARPNYPGVYTRVSSY 225

                ....*..
gi 24650929 309 LDWIKQQ 315
Cdd:cd00190 226 LDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
73-315 1.05e-60

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: 193.26  E-value: 1.05e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929  73 IIGGGPAVPKEFPHAARLghkdENGEVEWFCGGTLISDRHVLTAAHCHYSPQGSVNIARLGDLefDTNNDDADPEDFDVK 152
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSL----QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSH--DLSSNEGGGQVIKVK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929 153 DFTAHPEFSYPAIYNDISVVRLSRPVTFNDYKHPACLPFDDGRL--GTSFIAIGWGQLEIVPRTeNKKLQKVKLYNYGTR 230
Cdd:cd00190  75 KVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLpaGTTCTVSGWGRTSEGGPL-PDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929 231 -CritadRNDELPEGYNATTQLCIGSNEH-KDTCNGDSGGPvLIYHmdYPCMYHVMGITSIGVACDTPDLPAMYTRVHFY 308
Cdd:cd00190 154 eC-----KRAYSYGGTITDNMLCAGGLEGgKDACQGDSGGP-LVCN--DNGRGVLVGIVSWGSGCARPNYPGVYTRVSSY 225

                ....*..
gi 24650929 309 LDWIKQQ 315
Cdd:cd00190 226 LDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
73-312 1.47e-58

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: 187.89  E-value: 1.47e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929     73 IIGGGPAVPKEFPHAARLghkdENGEVEWFCGGTLISDRHVLTAAHCHYSPQGSVNIARLGDLefDTNNDDaDPEDFDVK 152
Cdd:smart00020   2 IVGGSEANIGSFPWQVSL----QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSH--DLSSGE-EGQVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929    153 DFTAHPEFSYPAIYNDISVVRLSRPVTFNDYKHPACLPFDDGRL--GTSFIAIGWGQLEIVPRTENKKLQKVKLY----- 225
Cdd:smart00020  75 KVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVpaGTTCTVSGWGRTSEGAGSLPDTLQEVNVPivsna 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929    226 ----NYGTRCRITAdrndelpegynatTQLCIGSNE-HKDTCNGDSGGPvLIYHMDypcMYHVMGITSIGVACDTPDLPA 300
Cdd:smart00020 155 tcrrAYSGGGAITD-------------NMLCAGGLEgGKDACQGDSGGP-LVCNDG---RWVLVGIVSWGSGCARPGKPG 217
                          250
                   ....*....|..
gi 24650929    301 MYTRVHFYLDWI 312
Cdd:smart00020 218 VYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
70-319 3.00e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 188.32  E-value: 3.00e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929  70 APLIIGGGPAVPKEFPHAARLGhkDENGEVEWFCGGTLISDRHVLTAAHCHYSPQGSVNIARLGdlefDTNNDDADPEDF 149
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQ--SSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIG----STDLSTSGGTVV 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929 150 DVKDFTAHPEFSYPAIYNDISVVRLSRPVTfnDYKhPACLP--FDDGRLGTSFIAIGWGQLEIVPRTENKKLQKVKLyny 227
Cdd:COG5640 102 KVARIVVHPDYDPATPGNDIALLKLATPVP--GVA-PAPLAtsADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADV--- 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929 228 gtrcRITADRNDELPEGYNATTQLCIGSNE-HKDTCNGDSGGPVLIyhmDYPCMYHVMGITSIGVACDTPDLPAMYTRVH 306
Cdd:COG5640 176 ----PVVSDATCAAYGGFDGGTMLCAGYPEgGKDACQGDSGGPLVV---KDGGGWVLVGVVSWGGGPCAAGYPGVYTRVS 248
                       250
                ....*....|...
gi 24650929 307 FYLDWIKQQLAKN 319
Cdd:COG5640 249 AYRDWIKSTAGGL 261
Trypsin pfam00089
Trypsin;
73-312 8.48e-47

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 157.22  E-value: 8.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929    73 IIGGGPAVPKEFPHAARLghkdENGEVEWFCGGTLISDRHVLTAAHCHYSPqGSVNIaRLGdlEFDTNNDDADPEDFDVK 152
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSL----QLSSGKHFCGGSLISENWVLTAAHCVSGA-SDVKV-VLG--AHNIVLREGGEQKFDVE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929   153 DFTAHPEFSYPAIYNDISVVRLSRPVTFNDYKHPACLP--FDDGRLGTSFIAIGWGQLEivPRTENKKLQKVKLYNYGT- 229
Cdd:pfam00089  73 KIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPdaSSDLPVGTTCTVSGWGNTK--TLGPSDTLQEVTVPVVSRe 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929   230 RCRITADrndelpeGYNATTQLCIGSNEhKDTCNGDSGGPVLiyhmdypCMYH-VMGITSIGVACDTPDLPAMYTRVHFY 308
Cdd:pfam00089 151 TCRSAYG-------GTVTDTMICAGAGG-KDACQGDSGGPLV-------CSDGeLIGIVSWGYGCASGNYPGVYTPVSSY 215

                  ....
gi 24650929   309 LDWI 312
Cdd:pfam00089 216 LDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
73-315 1.05e-60

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: 193.26  E-value: 1.05e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929  73 IIGGGPAVPKEFPHAARLghkdENGEVEWFCGGTLISDRHVLTAAHCHYSPQGSVNIARLGDLefDTNNDDADPEDFDVK 152
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSL----QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSH--DLSSNEGGGQVIKVK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929 153 DFTAHPEFSYPAIYNDISVVRLSRPVTFNDYKHPACLPFDDGRL--GTSFIAIGWGQLEIVPRTeNKKLQKVKLYNYGTR 230
Cdd:cd00190  75 KVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLpaGTTCTVSGWGRTSEGGPL-PDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929 231 -CritadRNDELPEGYNATTQLCIGSNEH-KDTCNGDSGGPvLIYHmdYPCMYHVMGITSIGVACDTPDLPAMYTRVHFY 308
Cdd:cd00190 154 eC-----KRAYSYGGTITDNMLCAGGLEGgKDACQGDSGGP-LVCN--DNGRGVLVGIVSWGSGCARPNYPGVYTRVSSY 225

                ....*..
gi 24650929 309 LDWIKQQ 315
Cdd:cd00190 226 LDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
73-312 1.47e-58

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: 187.89  E-value: 1.47e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929     73 IIGGGPAVPKEFPHAARLghkdENGEVEWFCGGTLISDRHVLTAAHCHYSPQGSVNIARLGDLefDTNNDDaDPEDFDVK 152
Cdd:smart00020   2 IVGGSEANIGSFPWQVSL----QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSH--DLSSGE-EGQVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929    153 DFTAHPEFSYPAIYNDISVVRLSRPVTFNDYKHPACLPFDDGRL--GTSFIAIGWGQLEIVPRTENKKLQKVKLY----- 225
Cdd:smart00020  75 KVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVpaGTTCTVSGWGRTSEGAGSLPDTLQEVNVPivsna 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929    226 ----NYGTRCRITAdrndelpegynatTQLCIGSNE-HKDTCNGDSGGPvLIYHMDypcMYHVMGITSIGVACDTPDLPA 300
Cdd:smart00020 155 tcrrAYSGGGAITD-------------NMLCAGGLEgGKDACQGDSGGP-LVCNDG---RWVLVGIVSWGSGCARPGKPG 217
                          250
                   ....*....|..
gi 24650929    301 MYTRVHFYLDWI 312
Cdd:smart00020 218 VYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
70-319 3.00e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 188.32  E-value: 3.00e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929  70 APLIIGGGPAVPKEFPHAARLGhkDENGEVEWFCGGTLISDRHVLTAAHCHYSPQGSVNIARLGdlefDTNNDDADPEDF 149
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQ--SSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIG----STDLSTSGGTVV 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929 150 DVKDFTAHPEFSYPAIYNDISVVRLSRPVTfnDYKhPACLP--FDDGRLGTSFIAIGWGQLEIVPRTENKKLQKVKLyny 227
Cdd:COG5640 102 KVARIVVHPDYDPATPGNDIALLKLATPVP--GVA-PAPLAtsADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADV--- 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929 228 gtrcRITADRNDELPEGYNATTQLCIGSNE-HKDTCNGDSGGPVLIyhmDYPCMYHVMGITSIGVACDTPDLPAMYTRVH 306
Cdd:COG5640 176 ----PVVSDATCAAYGGFDGGTMLCAGYPEgGKDACQGDSGGPLVV---KDGGGWVLVGVVSWGGGPCAAGYPGVYTRVS 248
                       250
                ....*....|...
gi 24650929 307 FYLDWIKQQLAKN 319
Cdd:COG5640 249 AYRDWIKSTAGGL 261
Trypsin pfam00089
Trypsin;
73-312 8.48e-47

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 157.22  E-value: 8.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929    73 IIGGGPAVPKEFPHAARLghkdENGEVEWFCGGTLISDRHVLTAAHCHYSPqGSVNIaRLGdlEFDTNNDDADPEDFDVK 152
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSL----QLSSGKHFCGGSLISENWVLTAAHCVSGA-SDVKV-VLG--AHNIVLREGGEQKFDVE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929   153 DFTAHPEFSYPAIYNDISVVRLSRPVTFNDYKHPACLP--FDDGRLGTSFIAIGWGQLEivPRTENKKLQKVKLYNYGT- 229
Cdd:pfam00089  73 KIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPdaSSDLPVGTTCTVSGWGNTK--TLGPSDTLQEVTVPVVSRe 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929   230 RCRITADrndelpeGYNATTQLCIGSNEhKDTCNGDSGGPVLiyhmdypCMYH-VMGITSIGVACDTPDLPAMYTRVHFY 308
Cdd:pfam00089 151 TCRSAYG-------GTVTDTMICAGAGG-KDACQGDSGGPLV-------CSDGeLIGIVSWGYGCASGNYPGVYTPVSSY 215

                  ....
gi 24650929   309 LDWI 312
Cdd:pfam00089 216 LDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
95-292 5.04e-16

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 75.10  E-value: 5.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929  95 ENGEVEWFCGGTLISDRHVLTAAHCHYSPQGSvniARLGDLEFDTNNDDADPEDFDVKDFTAHPEF-SYPAIYNDISVVR 173
Cdd:COG3591   6 ETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGG---GWATNIVFVPGYNGGPYGTATATRFRVPPGWvASGDAGYDYALLR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650929 174 LSRPVTfNDYKHPACLPFDDGRLGTSFIAIGWGQleivprtenkklQKVKLYNYGTRCRITADRNDELpeGYNAttqlci 253
Cdd:COG3591  83 LDEPLG-DTTGWLGLAFNDAPLAGEPVTIIGYPG------------DRPKDLSLDCSGRVTGVQGNRL--SYDC------ 141
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24650929 254 gsnehkDTCNGDSGGPVLIyhmDYPCMYHVMGITSIGVA 292
Cdd:COG3591 142 ------DTTGGSSGSPVLD---DSDGGGRVVGVHSAGGA 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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