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Conserved domains on  [gi|85725034|ref|NP_001033953|]
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uncharacterized protein Dmel_CG4927 [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 ...
105-358 4.03e-67

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: 211.37  E-value: 4.03e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034 105 IVGGAKAAGREFPFMALLgQRGKNSSQidwdCGAIIIHPKFVLTAAHCLEtsetkeqrldpNYDGPKYVVRLGELDYNST 184
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSL-QYTGGRHF----CGGSLISPRWVLTAAHCVY-----------SSAPSNYTVRLGSHDLSSN 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034 185 tdDAQPQDFRVLNYVVHPAYgeddDTGSRKNDIAVVELEMEATFSEYVAPACLPLDGGNEQL--QVAAAGWGATSESGHA 262
Cdd:cd00190  65 --EGGGQVIKVKKVIVHPNY----NPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAgtTCTVSGWGRTSEGGPL 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034 263 SSHLLKVSLDRYDVAECSQRLEHKIDV-RTQLCAGSRSTSADTCYGDSGGPVFVQHPiysCLKQVIGITSYGLVCGVQGL 341
Cdd:cd00190 139 PDVLQEVNVPIVSNAECKRAYSYGGTItDNMLCAGGLEGGKDACQGDSGGPLVCNDN---GRGVLVGIVSWGSGCARPNY 215
                       250
                ....*....|....*..
gi 85725034 342 PSVYTKVHLYTDWIENI 358
Cdd:cd00190 216 PGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
105-358 4.03e-67

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: 211.37  E-value: 4.03e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034 105 IVGGAKAAGREFPFMALLgQRGKNSSQidwdCGAIIIHPKFVLTAAHCLEtsetkeqrldpNYDGPKYVVRLGELDYNST 184
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSL-QYTGGRHF----CGGSLISPRWVLTAAHCVY-----------SSAPSNYTVRLGSHDLSSN 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034 185 tdDAQPQDFRVLNYVVHPAYgeddDTGSRKNDIAVVELEMEATFSEYVAPACLPLDGGNEQL--QVAAAGWGATSESGHA 262
Cdd:cd00190  65 --EGGGQVIKVKKVIVHPNY----NPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAgtTCTVSGWGRTSEGGPL 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034 263 SSHLLKVSLDRYDVAECSQRLEHKIDV-RTQLCAGSRSTSADTCYGDSGGPVFVQHPiysCLKQVIGITSYGLVCGVQGL 341
Cdd:cd00190 139 PDVLQEVNVPIVSNAECKRAYSYGGTItDNMLCAGGLEGGKDACQGDSGGPLVCNDN---GRGVLVGIVSWGSGCARPNY 215
                       250
                ....*....|....*..
gi 85725034 342 PSVYTKVHLYTDWIENI 358
Cdd:cd00190 216 PGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
105-355 7.10e-64

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: 202.91  E-value: 7.10e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034    105 IVGGAKAAGREFPFMALLGQRGKNSSqidwdCGAIIIHPKFVLTAAHCLEtsetkeqrldpNYDGPKYVVRLGELDYNST 184
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGRHF-----CGGSLISPRWVLTAAHCVR-----------GSDPSNIRVRLGSHDLSSG 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034    185 TDDaqpQDFRVLNYVVHPAYgeDDDTGSrkNDIAVVELEMEATFSEYVAPACLPLDGGN--EQLQVAAAGWGATSESGHA 262
Cdd:smart00020  66 EEG---QVIKVSKVIIHPNY--NPSTYD--NDIALLKLKEPVTLSDNVRPICLPSSNYNvpAGTTCTVSGWGRTSEGAGS 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034    263 -SSHLLKVSLDRYDVAECSQRLEHKIDVR-TQLCAGSRSTSADTCYGDSGGPVFVQHPIYsclkQVIGITSYGLVCGVQG 340
Cdd:smart00020 139 lPDTLQEVNVPIVSNATCRRAYSGGGAITdNMLCAGGLEGGKDACQGDSGGPLVCNDGRW----VLVGIVSWGSGCARPG 214
                          250
                   ....*....|....*
gi 85725034    341 LPSVYTKVHLYTDWI 355
Cdd:smart00020 215 KPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
105-355 1.71e-52

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 173.40  E-value: 1.71e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034   105 IVGGAKAAGREFPFMALLgqrgkNSSQIDWDCGAIIIHPKFVLTAAHCLetsetkeqrldpnYDGPKYVVRLGEldYNST 184
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSL-----QLSSGKHFCGGSLISENWVLTAAHCV-------------SGASDVKVVLGA--HNIV 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034   185 TDDAQPQDFRVLNYVVHPAYGEDDDTgsrkNDIAVVELEMEATFSEYVAPACLPLDGGNEQLQ--VAAAGWGATSESGHa 262
Cdd:pfam00089  61 LREGGEQKFDVEKIIVHPNYNPDTLD----NDIALLKLESPVTLGDTVRPICLPDASSDLPVGttCTVSGWGNTKTLGP- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034   263 SSHLLKVSLDRYDVAECSQRLEHKIdVRTQLCAGSrsTSADTCYGDSGGPVFvqhpiysCLKQ-VIGITSYGLVCGVQGL 341
Cdd:pfam00089 136 SDTLQEVTVPVVSRETCRSAYGGTV-TDTMICAGA--GGKDACQGDSGGPLV-------CSDGeLIGIVSWGYGCASGNY 205
                         250
                  ....*....|....
gi 85725034   342 PSVYTKVHLYTDWI 355
Cdd:pfam00089 206 PGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
102-356 2.25e-52

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 174.45  E-value: 2.25e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034 102 TPFIVGGAKAAGREFPFMALLGQRGKNSSQIdwdCGAIIIHPKFVLTAAHCLEtsetkeqrldpNYDGPKYVVRLGELDY 181
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNGPSGQF---CGGTLIAPRWVLTAAHCVD-----------GDGPSDLRVVIGSTDL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034 182 NSTtddaQPQDFRVLNYVVHPAYgeddDTGSRKNDIAVVELEMEATFSEYVAPAcLPLDGGNEQLQVAAAGWGATSE-SG 260
Cdd:COG5640  94 STS----GGTVVKVARIVVHPDY----DPATPGNDIALLKLATPVPGVAPAPLA-TSADAAAPGTPATVAGWGRTSEgPG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034 261 HASSHLLKVSLDRYDVAECSQRLEhkIDVRTQLCAGSRSTSADTCYGDSGGPVFVQhpiYSCLKQVIGITSYGLVCGVQG 340
Cdd:COG5640 165 SQSGTLRKADVPVVSDATCAAYGG--FDGGTMLCAGYPEGGKDACQGDSGGPLVVK---DGGGWVLVGVVSWGGGPCAAG 239
                       250
                ....*....|....*.
gi 85725034 341 LPSVYTKVHLYTDWIE 356
Cdd:COG5640 240 YPGVYTRVSAYRDWIK 255
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
105-358 4.03e-67

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: 211.37  E-value: 4.03e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034 105 IVGGAKAAGREFPFMALLgQRGKNSSQidwdCGAIIIHPKFVLTAAHCLEtsetkeqrldpNYDGPKYVVRLGELDYNST 184
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSL-QYTGGRHF----CGGSLISPRWVLTAAHCVY-----------SSAPSNYTVRLGSHDLSSN 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034 185 tdDAQPQDFRVLNYVVHPAYgeddDTGSRKNDIAVVELEMEATFSEYVAPACLPLDGGNEQL--QVAAAGWGATSESGHA 262
Cdd:cd00190  65 --EGGGQVIKVKKVIVHPNY----NPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAgtTCTVSGWGRTSEGGPL 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034 263 SSHLLKVSLDRYDVAECSQRLEHKIDV-RTQLCAGSRSTSADTCYGDSGGPVFVQHPiysCLKQVIGITSYGLVCGVQGL 341
Cdd:cd00190 139 PDVLQEVNVPIVSNAECKRAYSYGGTItDNMLCAGGLEGGKDACQGDSGGPLVCNDN---GRGVLVGIVSWGSGCARPNY 215
                       250
                ....*....|....*..
gi 85725034 342 PSVYTKVHLYTDWIENI 358
Cdd:cd00190 216 PGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
105-355 7.10e-64

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: 202.91  E-value: 7.10e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034    105 IVGGAKAAGREFPFMALLGQRGKNSSqidwdCGAIIIHPKFVLTAAHCLEtsetkeqrldpNYDGPKYVVRLGELDYNST 184
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGRHF-----CGGSLISPRWVLTAAHCVR-----------GSDPSNIRVRLGSHDLSSG 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034    185 TDDaqpQDFRVLNYVVHPAYgeDDDTGSrkNDIAVVELEMEATFSEYVAPACLPLDGGN--EQLQVAAAGWGATSESGHA 262
Cdd:smart00020  66 EEG---QVIKVSKVIIHPNY--NPSTYD--NDIALLKLKEPVTLSDNVRPICLPSSNYNvpAGTTCTVSGWGRTSEGAGS 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034    263 -SSHLLKVSLDRYDVAECSQRLEHKIDVR-TQLCAGSRSTSADTCYGDSGGPVFVQHPIYsclkQVIGITSYGLVCGVQG 340
Cdd:smart00020 139 lPDTLQEVNVPIVSNATCRRAYSGGGAITdNMLCAGGLEGGKDACQGDSGGPLVCNDGRW----VLVGIVSWGSGCARPG 214
                          250
                   ....*....|....*
gi 85725034    341 LPSVYTKVHLYTDWI 355
Cdd:smart00020 215 KPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
105-355 1.71e-52

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 173.40  E-value: 1.71e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034   105 IVGGAKAAGREFPFMALLgqrgkNSSQIDWDCGAIIIHPKFVLTAAHCLetsetkeqrldpnYDGPKYVVRLGEldYNST 184
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSL-----QLSSGKHFCGGSLISENWVLTAAHCV-------------SGASDVKVVLGA--HNIV 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034   185 TDDAQPQDFRVLNYVVHPAYGEDDDTgsrkNDIAVVELEMEATFSEYVAPACLPLDGGNEQLQ--VAAAGWGATSESGHa 262
Cdd:pfam00089  61 LREGGEQKFDVEKIIVHPNYNPDTLD----NDIALLKLESPVTLGDTVRPICLPDASSDLPVGttCTVSGWGNTKTLGP- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034   263 SSHLLKVSLDRYDVAECSQRLEHKIdVRTQLCAGSrsTSADTCYGDSGGPVFvqhpiysCLKQ-VIGITSYGLVCGVQGL 341
Cdd:pfam00089 136 SDTLQEVTVPVVSRETCRSAYGGTV-TDTMICAGA--GGKDACQGDSGGPLV-------CSDGeLIGIVSWGYGCASGNY 205
                         250
                  ....*....|....
gi 85725034   342 PSVYTKVHLYTDWI 355
Cdd:pfam00089 206 PGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
102-356 2.25e-52

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 174.45  E-value: 2.25e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034 102 TPFIVGGAKAAGREFPFMALLGQRGKNSSQIdwdCGAIIIHPKFVLTAAHCLEtsetkeqrldpNYDGPKYVVRLGELDY 181
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNGPSGQF---CGGTLIAPRWVLTAAHCVD-----------GDGPSDLRVVIGSTDL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034 182 NSTtddaQPQDFRVLNYVVHPAYgeddDTGSRKNDIAVVELEMEATFSEYVAPAcLPLDGGNEQLQVAAAGWGATSE-SG 260
Cdd:COG5640  94 STS----GGTVVKVARIVVHPDY----DPATPGNDIALLKLATPVPGVAPAPLA-TSADAAAPGTPATVAGWGRTSEgPG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034 261 HASSHLLKVSLDRYDVAECSQRLEhkIDVRTQLCAGSRSTSADTCYGDSGGPVFVQhpiYSCLKQVIGITSYGLVCGVQG 340
Cdd:COG5640 165 SQSGTLRKADVPVVSDATCAAYGG--FDGGTMLCAGYPEGGKDACQGDSGGPLVVK---DGGGWVLVGVVSWGGGPCAAG 239
                       250
                ....*....|....*.
gi 85725034 341 LPSVYTKVHLYTDWIE 356
Cdd:COG5640 240 YPGVYTRVSAYRDWIK 255
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
136-333 5.05e-12

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 64.31  E-value: 5.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034 136 CGAIIIHPKFVLTAAHCLETSETKEQRLD----PNYDGPKYVVrlgeldynsttddaqpqdFRVLNYVVHPAYgedDDTG 211
Cdd:COG3591  14 CTGTLIGPNLVLTAGHCVYDGAGGGWATNivfvPGYNGGPYGT------------------ATATRFRVPPGW---VASG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85725034 212 SRKNDIAVVELEmeATFSEYVAPacLPLDGGNEqlqvAAAGWGATSeSGHASSHLLKVSLDRYD--VAECSQRLEHkidv 289
Cdd:COG3591  73 DAGYDYALLRLD--EPLGDTTGW--LGLAFNDA----PLAGEPVTI-IGYPGDRPKDLSLDCSGrvTGVQGNRLSY---- 139
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 85725034 290 rtqlcagsrstSADTCYGDSGGPVFVQhpiYSCLKQVIGITSYG 333
Cdd:COG3591 140 -----------DCDTTGGSSGSPVLDD---SDGGGRVVGVHSAG 169
 
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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