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Conserved domains on  [gi|665394870|ref|NP_651175|]
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uncharacterized protein Dmel_CG10232 [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 ...
260-506 4.01e-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: 197.50  E-value: 4.01e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870 260 GTAARPNEYPWMAMLIYENRRLstmtnNCSGSLINKRYVLTAAHCVVKDKMVNTdlvlrRVRLGEHDITTNpdcDFTGnc 339
Cdd:cd00190    4 GSEAKIGSFPWQVSLQYTGGRH-----FCGGSLISPRWVLTAAHCVYSSAPSNY-----TVRLGSHDLSSN---EGGG-- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870 340 aapfVEIGIEYFNVHEQYfNTSRFESDIALVRLQTPVRYTHEILPICVP-KDPIPLHNHPLQIAGWGYTKNR-EYSQVLL 417
Cdd:cd00190   69 ----QVIKVKKVIVHPNY-NPSTYDNDIALLKLKRPVTLSDNVRPICLPsSGYNLPAGTTCTVSGWGRTSEGgPLPDVLQ 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870 418 HNTVY-------ENRYYCQDKISffrnESQICASG-IRGEDSCEGDSGGPLMLTLNNDYqdivYLAGIVSYGSeNCGD-R 488
Cdd:cd00190  144 EVNVPivsnaecKRAYSYGGTIT----DNMLCAGGlEGGKDACQGDSGGPLVCNDNGRG----VLVGIVSWGS-GCARpN 214
                        250
                 ....*....|....*...
gi 665394870 489 KPGVYTKTGAFFSWIKAN 506
Cdd:cd00190  215 YPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
260-506 4.01e-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: 197.50  E-value: 4.01e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870 260 GTAARPNEYPWMAMLIYENRRLstmtnNCSGSLINKRYVLTAAHCVVKDKMVNTdlvlrRVRLGEHDITTNpdcDFTGnc 339
Cdd:cd00190    4 GSEAKIGSFPWQVSLQYTGGRH-----FCGGSLISPRWVLTAAHCVYSSAPSNY-----TVRLGSHDLSSN---EGGG-- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870 340 aapfVEIGIEYFNVHEQYfNTSRFESDIALVRLQTPVRYTHEILPICVP-KDPIPLHNHPLQIAGWGYTKNR-EYSQVLL 417
Cdd:cd00190   69 ----QVIKVKKVIVHPNY-NPSTYDNDIALLKLKRPVTLSDNVRPICLPsSGYNLPAGTTCTVSGWGRTSEGgPLPDVLQ 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870 418 HNTVY-------ENRYYCQDKISffrnESQICASG-IRGEDSCEGDSGGPLMLTLNNDYqdivYLAGIVSYGSeNCGD-R 488
Cdd:cd00190  144 EVNVPivsnaecKRAYSYGGTIT----DNMLCAGGlEGGKDACQGDSGGPLVCNDNGRG----VLVGIVSWGS-GCARpN 214
                        250
                 ....*....|....*...
gi 665394870 489 KPGVYTKTGAFFSWIKAN 506
Cdd:cd00190  215 YPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
260-503 1.00e-57

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: 191.35  E-value: 1.00e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870   260 GTAARPNEYPWMAMLIYENRRLStmtnnCSGSLINKRYVLTAAHCVVKDKMVNTdlvlrRVRLGEHDITTNPDcdftgnc 339
Cdd:smart00020   5 GSEANIGSFPWQVSLQYGGGRHF-----CGGSLISPRWVLTAAHCVRGSDPSNI-----RVRLGSHDLSSGEE------- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870   340 aapFVEIGIEYFNVHEQYfNTSRFESDIALVRLQTPVRYTHEILPICVP-KDPIPLHNHPLQIAGWGYTKNRE--YSQVL 416
Cdd:smart00020  68 ---GQVIKVSKVIIHPNY-NPSTYDNDIALLKLKEPVTLSDNVRPICLPsSNYNVPAGTTCTVSGWGRTSEGAgsLPDTL 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870   417 LHNTVY-------ENRYYCQDKIsffrNESQICASG-IRGEDSCEGDSGGPLMLTLNndyqdIVYLAGIVSYGSeNCGD- 487
Cdd:smart00020 144 QEVNVPivsnatcRRAYSGGGAI----TDNMLCAGGlEGGKDACQGDSGGPLVCNDG-----RWVLVGIVSWGS-GCARp 213
                          250
                   ....*....|....*.
gi 665394870   488 RKPGVYTKTGAFFSWI 503
Cdd:smart00020 214 GKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
260-505 6.37e-51

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 174.45  E-value: 6.37e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870 260 GTAARPNEYPWMAMLIYENrrlSTMTNNCSGSLINKRYVLTAAHCVVKDKmvNTDLvlrRVRLGEHDITTNPDcdftgnc 339
Cdd:COG5640   34 GTPATVGEYPWMVALQSSN---GPSGQFCGGTLIAPRWVLTAAHCVDGDG--PSDL---RVVIGSTDLSTSGG------- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870 340 aapfVEIGIEYFNVHEQYfNTSRFESDIALVRLQTPVrytHEILPICVPKDPIPLH-NHPLQIAGWGYTKN--REYSQVL 416
Cdd:COG5640   99 ----TVVKVARIVVHPDY-DPATPGNDIALLKLATPV---PGVAPAPLATSADAAApGTPATVAGWGRTSEgpGSQSGTL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870 417 LH-NTVYENRYYCQDkISFFRNESQICASGIRGE-DSCEGDSGGPLMLTLNNDYQdivyLAGIVSYGSENCGDRKPGVYT 494
Cdd:COG5640  171 RKaDVPVVSDATCAA-YGGFDGGTMLCAGYPEGGkDACQGDSGGPLVVKDGGGWV----LVGVVSWGGGPCAAGYPGVYT 245
                        250
                 ....*....|.
gi 665394870 495 KTGAFFSWIKA 505
Cdd:COG5640  246 RVSAYRDWIKS 256
Trypsin pfam00089
Trypsin;
260-503 4.19e-48

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 165.69  E-value: 4.19e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870  260 GTAARPNEYPWMAMLIYENRRLStmtnnCSGSLINKRYVLTAAHCVVKDKMVntdlvlrRVRLGEHDITTNPdcdftgnc 339
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQLSSGKHF-----CGGSLISENWVLTAAHCVSGASDV-------KVVLGAHNIVLRE-------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870  340 aAPFVEIGIEYFNVHEQYfNTSRFESDIALVRLQTPVRYTHEILPICVP-KDPIPLHNHPLQIAGWGYTKNREYSQVLLH 418
Cdd:pfam00089  64 -GGEQKFDVEKIIVHPNY-NPDTLDNDIALLKLESPVTLGDTVRPICLPdASSDLPVGTTCTVSGWGNTKTLGPSDTLQE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870  419 NTV--YENRyYCQDKISFFRNESQICAsGIRGEDSCEGDSGGPLMltlNNDyqdiVYLAGIVSYGsENCGD-RKPGVYTK 495
Cdd:pfam00089 142 VTVpvVSRE-TCRSAYGGTVTDTMICA-GAGGKDACQGDSGGPLV---CSD----GELIGIVSWG-YGCASgNYPGVYTP 211

                  ....*...
gi 665394870  496 TGAFFSWI 503
Cdd:pfam00089 212 VSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
260-506 4.01e-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: 197.50  E-value: 4.01e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870 260 GTAARPNEYPWMAMLIYENRRLstmtnNCSGSLINKRYVLTAAHCVVKDKMVNTdlvlrRVRLGEHDITTNpdcDFTGnc 339
Cdd:cd00190    4 GSEAKIGSFPWQVSLQYTGGRH-----FCGGSLISPRWVLTAAHCVYSSAPSNY-----TVRLGSHDLSSN---EGGG-- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870 340 aapfVEIGIEYFNVHEQYfNTSRFESDIALVRLQTPVRYTHEILPICVP-KDPIPLHNHPLQIAGWGYTKNR-EYSQVLL 417
Cdd:cd00190   69 ----QVIKVKKVIVHPNY-NPSTYDNDIALLKLKRPVTLSDNVRPICLPsSGYNLPAGTTCTVSGWGRTSEGgPLPDVLQ 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870 418 HNTVY-------ENRYYCQDKISffrnESQICASG-IRGEDSCEGDSGGPLMLTLNNDYqdivYLAGIVSYGSeNCGD-R 488
Cdd:cd00190  144 EVNVPivsnaecKRAYSYGGTIT----DNMLCAGGlEGGKDACQGDSGGPLVCNDNGRG----VLVGIVSWGS-GCARpN 214
                        250
                 ....*....|....*...
gi 665394870 489 KPGVYTKTGAFFSWIKAN 506
Cdd:cd00190  215 YPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
260-503 1.00e-57

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: 191.35  E-value: 1.00e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870   260 GTAARPNEYPWMAMLIYENRRLStmtnnCSGSLINKRYVLTAAHCVVKDKMVNTdlvlrRVRLGEHDITTNPDcdftgnc 339
Cdd:smart00020   5 GSEANIGSFPWQVSLQYGGGRHF-----CGGSLISPRWVLTAAHCVRGSDPSNI-----RVRLGSHDLSSGEE------- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870   340 aapFVEIGIEYFNVHEQYfNTSRFESDIALVRLQTPVRYTHEILPICVP-KDPIPLHNHPLQIAGWGYTKNRE--YSQVL 416
Cdd:smart00020  68 ---GQVIKVSKVIIHPNY-NPSTYDNDIALLKLKEPVTLSDNVRPICLPsSNYNVPAGTTCTVSGWGRTSEGAgsLPDTL 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870   417 LHNTVY-------ENRYYCQDKIsffrNESQICASG-IRGEDSCEGDSGGPLMLTLNndyqdIVYLAGIVSYGSeNCGD- 487
Cdd:smart00020 144 QEVNVPivsnatcRRAYSGGGAI----TDNMLCAGGlEGGKDACQGDSGGPLVCNDG-----RWVLVGIVSWGS-GCARp 213
                          250
                   ....*....|....*.
gi 665394870   488 RKPGVYTKTGAFFSWI 503
Cdd:smart00020 214 GKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
260-505 6.37e-51

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 174.45  E-value: 6.37e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870 260 GTAARPNEYPWMAMLIYENrrlSTMTNNCSGSLINKRYVLTAAHCVVKDKmvNTDLvlrRVRLGEHDITTNPDcdftgnc 339
Cdd:COG5640   34 GTPATVGEYPWMVALQSSN---GPSGQFCGGTLIAPRWVLTAAHCVDGDG--PSDL---RVVIGSTDLSTSGG------- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870 340 aapfVEIGIEYFNVHEQYfNTSRFESDIALVRLQTPVrytHEILPICVPKDPIPLH-NHPLQIAGWGYTKN--REYSQVL 416
Cdd:COG5640   99 ----TVVKVARIVVHPDY-DPATPGNDIALLKLATPV---PGVAPAPLATSADAAApGTPATVAGWGRTSEgpGSQSGTL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870 417 LH-NTVYENRYYCQDkISFFRNESQICASGIRGE-DSCEGDSGGPLMLTLNNDYQdivyLAGIVSYGSENCGDRKPGVYT 494
Cdd:COG5640  171 RKaDVPVVSDATCAA-YGGFDGGTMLCAGYPEGGkDACQGDSGGPLVVKDGGGWV----LVGVVSWGGGPCAAGYPGVYT 245
                        250
                 ....*....|.
gi 665394870 495 KTGAFFSWIKA 505
Cdd:COG5640  246 RVSAYRDWIKS 256
Trypsin pfam00089
Trypsin;
260-503 4.19e-48

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 165.69  E-value: 4.19e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870  260 GTAARPNEYPWMAMLIYENRRLStmtnnCSGSLINKRYVLTAAHCVVKDKMVntdlvlrRVRLGEHDITTNPdcdftgnc 339
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQLSSGKHF-----CGGSLISENWVLTAAHCVSGASDV-------KVVLGAHNIVLRE-------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870  340 aAPFVEIGIEYFNVHEQYfNTSRFESDIALVRLQTPVRYTHEILPICVP-KDPIPLHNHPLQIAGWGYTKNREYSQVLLH 418
Cdd:pfam00089  64 -GGEQKFDVEKIIVHPNY-NPDTLDNDIALLKLESPVTLGDTVRPICLPdASSDLPVGTTCTVSGWGNTKTLGPSDTLQE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870  419 NTV--YENRyYCQDKISFFRNESQICAsGIRGEDSCEGDSGGPLMltlNNDyqdiVYLAGIVSYGsENCGD-RKPGVYTK 495
Cdd:pfam00089 142 VTVpvVSRE-TCRSAYGGTVTDTMICA-GAGGKDACQGDSGGPLV---CSD----GELIGIVSWG-YGCASgNYPGVYTP 211

                  ....*...
gi 665394870  496 TGAFFSWI 503
Cdd:pfam00089 212 VSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
288-505 6.12e-17

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 78.95  E-value: 6.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870 288 CSGSLINKRYVLTAAHCvVKDKMVNTDLVLRRVRLGEHDittnpdcdftgncaAPFVEIGIEYFNVHEQYFNTSRFESDI 367
Cdd:COG3591   14 CTGTLIGPNLVLTAGHC-VYDGAGGGWATNIVFVPGYNG--------------GPYGTATATRFRVPPGWVASGDAGYDY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870 368 ALVRLQTPVRYTHEILPIcvPKDPIPLHNHPLQIAGWGYTKNREYSQvllhntvyenryYCQDKISFFRNESQI--Casg 445
Cdd:COG3591   79 ALLRLDEPLGDTTGWLGL--AFNDAPLAGEPVTIIGYPGDRPKDLSL------------DCSGRVTGVQGNRLSydC--- 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394870 446 irgeDSCEGDSGGPLMLTLNNDYqdivYLAGIVSYGSENCGDRkpGVYTKTgAFFSWIKA 505
Cdd:COG3591  142 ----DTTGGSSGSPVLDDSDGGG----RVVGVHSAGGADRANT--GVRLTS-AIVAALRA 190
 
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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