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Conserved domains on  [gi|24581698|ref|NP_608848|]
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uncharacterized protein Dmel_CG3355, 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

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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 ...
76-305 4.75e-104

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: 303.81  E-value: 4.75e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698  76 IVGGQQVRSNKYPWTAQLVKGRHypRLFCGGSLINDRYVLTAAHCVHG-NRDQITIRLLQIDRSSRDP-GIVRKVVQTTV 153
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGG--RHFCGGSLISPRWVLTAAHCVYSsAPSNYTVRLGSHDLSSNEGgGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698 154 HPNYDPNRIVNDVALLKLESPVPLTGNMRPVCLPEANHNF-DGKTAVVAGWGLIKEGGVTSNYLQEVNVPVITNAQCRQT 232
Cdd:cd00190  79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLpAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581698 233 -RYKDKIAEVMLCAGlVQQGGKDACQGDSGGPLIVN-EGRYKLAGVVSFGYGCAQKNAPGVYARVSKFLDWIRKN 305
Cdd:cd00190 159 ySYGGTITDNMLCAG-GLEGGKDACQGDSGGPLVCNdNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
76-305 4.75e-104

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: 303.81  E-value: 4.75e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698  76 IVGGQQVRSNKYPWTAQLVKGRHypRLFCGGSLINDRYVLTAAHCVHG-NRDQITIRLLQIDRSSRDP-GIVRKVVQTTV 153
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGG--RHFCGGSLISPRWVLTAAHCVYSsAPSNYTVRLGSHDLSSNEGgGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698 154 HPNYDPNRIVNDVALLKLESPVPLTGNMRPVCLPEANHNF-DGKTAVVAGWGLIKEGGVTSNYLQEVNVPVITNAQCRQT 232
Cdd:cd00190  79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLpAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581698 233 -RYKDKIAEVMLCAGlVQQGGKDACQGDSGGPLIVN-EGRYKLAGVVSFGYGCAQKNAPGVYARVSKFLDWIRKN 305
Cdd:cd00190 159 ySYGGTITDNMLCAG-GLEGGKDACQGDSGGPLVCNdNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
75-302 1.38e-103

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: 302.29  E-value: 1.38e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698     75 RIVGGQQVRSNKYPWTAQLVkgRHYPRLFCGGSLINDRYVLTAAHCVHG-NRDQITIRLLQIDRSSRDPGIVRKVVQTTV 153
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQ--YGGGRHFCGGSLISPRWVLTAAHCVRGsDPSNIRVRLGSHDLSSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698    154 HPNYDPNRIVNDVALLKLESPVPLTGNMRPVCLPEANHNF-DGKTAVVAGWGLIKEG-GVTSNYLQEVNVPVITNAQCRQ 231
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVpAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581698    232 T-RYKDKIAEVMLCAGlVQQGGKDACQGDSGGPLIVNEGRYKLAGVVSFGYGCAQKNAPGVYARVSKFLDWI 302
Cdd:smart00020 159 AySGGGAITDNMLCAG-GLEGGKDACQGDSGGPLVCNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
75-307 2.44e-83

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 252.26  E-value: 2.44e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698  75 RIVGGQQVRSNKYPWTAQLVKGRHYPRLFCGGSLINDRYVLTAAHCVHGNR-DQITIRLLQIDRSSrDPGIVRKVVQTTV 153
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGpSDLRVVIGSTDLST-SGGTVVKVARIVV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698 154 HPNYDPNRIVNDVALLKLESPVPltgNMRPVCLPEANHNFD-GKTAVVAGWGLIKEG-GVTSNYLQEVNVPVITNAQCRQ 231
Cdd:COG5640 109 HPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAApGTPATVAGWGRTSEGpGSQSGTLRKADVPVVSDATCAA 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581698 232 trYKDKIAEVMLCAGlVQQGGKDACQGDSGGPLIVNE-GRYKLAGVVSFGYGCAQKNAPGVYARVSKFLDWIRKNTA 307
Cdd:COG5640 186 --YGGFDGGTMLCAG-YPEGGKDACQGDSGGPLVVKDgGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAG 259
Trypsin pfam00089
Trypsin;
76-302 3.14e-74

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 227.33  E-value: 3.14e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698    76 IVGGQQVRSNKYPWTAQLVKGRhyPRLFCGGSLINDRYVLTAAHCVHgNRDQITIRLLQIDRSSRDPGI-VRKVVQTTVH 154
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSS--GKHFCGGSLISENWVLTAAHCVS-GASDVKVVLGAHNIVLREGGEqKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698   155 PNYDPNRIVNDVALLKLESPVPLTGNMRPVCLPEANHNF-DGKTAVVAGWGLIKEGGvTSNYLQEVNVPVITNAQCRQtR 233
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLpVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS-A 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581698   234 YKDKIAEVMLCAGLvqqGGKDACQGDSGGPLIVNEGryKLAGVVSFGYGCAQKNAPGVYARVSKFLDWI 302
Cdd:pfam00089 156 YGGTVTDTMICAGA---GGKDACQGDSGGPLVCSDG--ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
76-305 4.75e-104

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: 303.81  E-value: 4.75e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698  76 IVGGQQVRSNKYPWTAQLVKGRHypRLFCGGSLINDRYVLTAAHCVHG-NRDQITIRLLQIDRSSRDP-GIVRKVVQTTV 153
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGG--RHFCGGSLISPRWVLTAAHCVYSsAPSNYTVRLGSHDLSSNEGgGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698 154 HPNYDPNRIVNDVALLKLESPVPLTGNMRPVCLPEANHNF-DGKTAVVAGWGLIKEGGVTSNYLQEVNVPVITNAQCRQT 232
Cdd:cd00190  79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLpAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581698 233 -RYKDKIAEVMLCAGlVQQGGKDACQGDSGGPLIVN-EGRYKLAGVVSFGYGCAQKNAPGVYARVSKFLDWIRKN 305
Cdd:cd00190 159 ySYGGTITDNMLCAG-GLEGGKDACQGDSGGPLVCNdNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
75-302 1.38e-103

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: 302.29  E-value: 1.38e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698     75 RIVGGQQVRSNKYPWTAQLVkgRHYPRLFCGGSLINDRYVLTAAHCVHG-NRDQITIRLLQIDRSSRDPGIVRKVVQTTV 153
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQ--YGGGRHFCGGSLISPRWVLTAAHCVRGsDPSNIRVRLGSHDLSSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698    154 HPNYDPNRIVNDVALLKLESPVPLTGNMRPVCLPEANHNF-DGKTAVVAGWGLIKEG-GVTSNYLQEVNVPVITNAQCRQ 231
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVpAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581698    232 T-RYKDKIAEVMLCAGlVQQGGKDACQGDSGGPLIVNEGRYKLAGVVSFGYGCAQKNAPGVYARVSKFLDWI 302
Cdd:smart00020 159 AySGGGAITDNMLCAG-GLEGGKDACQGDSGGPLVCNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
75-307 2.44e-83

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 252.26  E-value: 2.44e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698  75 RIVGGQQVRSNKYPWTAQLVKGRHYPRLFCGGSLINDRYVLTAAHCVHGNR-DQITIRLLQIDRSSrDPGIVRKVVQTTV 153
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGpSDLRVVIGSTDLST-SGGTVVKVARIVV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698 154 HPNYDPNRIVNDVALLKLESPVPltgNMRPVCLPEANHNFD-GKTAVVAGWGLIKEG-GVTSNYLQEVNVPVITNAQCRQ 231
Cdd:COG5640 109 HPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAApGTPATVAGWGRTSEGpGSQSGTLRKADVPVVSDATCAA 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581698 232 trYKDKIAEVMLCAGlVQQGGKDACQGDSGGPLIVNE-GRYKLAGVVSFGYGCAQKNAPGVYARVSKFLDWIRKNTA 307
Cdd:COG5640 186 --YGGFDGGTMLCAG-YPEGGKDACQGDSGGPLVVKDgGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAG 259
Trypsin pfam00089
Trypsin;
76-302 3.14e-74

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 227.33  E-value: 3.14e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698    76 IVGGQQVRSNKYPWTAQLVKGRhyPRLFCGGSLINDRYVLTAAHCVHgNRDQITIRLLQIDRSSRDPGI-VRKVVQTTVH 154
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSS--GKHFCGGSLISENWVLTAAHCVS-GASDVKVVLGAHNIVLREGGEqKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698   155 PNYDPNRIVNDVALLKLESPVPLTGNMRPVCLPEANHNF-DGKTAVVAGWGLIKEGGvTSNYLQEVNVPVITNAQCRQtR 233
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLpVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRS-A 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581698   234 YKDKIAEVMLCAGLvqqGGKDACQGDSGGPLIVNEGryKLAGVVSFGYGCAQKNAPGVYARVSKFLDWI 302
Cdd:pfam00089 156 YGGTVTDTMICAGA---GGKDACQGDSGGPLVCSDG--ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
103-282 7.14e-14

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 68.93  E-value: 7.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698 103 FCGGSLINDRYVLTAAHCVHGNRDQITIRLLQI--DRSSRDPGIVRkVVQTTVHPNYDPNRIVN-DVALLKLESPVPLTg 179
Cdd:COG3591  13 VCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFvpGYNGGPYGTAT-ATRFRVPPGWVASGDAGyDYALLRLDEPLGDT- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581698 180 nMRPVCLPEANHNFDGKTAVVAGWGlikEGGVTSNYLQEVNvpVITNAQCRQTRYKdkiaevmlCaglvqqggkDACQGD 259
Cdd:COG3591  91 -TGWLGLAFNDAPLAGEPVTIIGYP---GDRPKDLSLDCSG--RVTGVQGNRLSYD--------C---------DTTGGS 147
                       170       180
                ....*....|....*....|....
gi 24581698 260 SGGPLIVNE-GRYKLAGVVSFGYG 282
Cdd:COG3591 148 SGSPVLDDSdGGGRVVGVHSAGGA 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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