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Conserved domains on  [gi|19922714|ref|NP_611611|]
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tracheal-prostasin [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 ...
127-356 2.25e-103

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: 304.20  E-value: 2.25e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714 127 IVGGQETEVHQYPWVAMLLYG-GRFYCAASLLNDQFLLTASHCVYGFRKERISVRLLEHDRKMSHMQKIDRKVAEVITHP 205
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714 206 KYNARNYDNDIAIIKLDEPVEFNEVLHPVCMPTPGRSFK-GENGIVTGWGALKVGGPTSDTLQEVQVPILSQDECRK-SR 283
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPaGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRaYS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922714 284 YGNKITDNMLCGGYDEGGKDSCQGDSGGPLhiVASGTREHQIAGVVSWGEGCAKAGYPGVYARVNRYGTWIKN 356
Cdd:cd00190 161 YGGTITDNMLCAGGLEGGKDACQGDSGGPL--VCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
127-356 2.25e-103

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: 304.20  E-value: 2.25e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714 127 IVGGQETEVHQYPWVAMLLYG-GRFYCAASLLNDQFLLTASHCVYGFRKERISVRLLEHDRKMSHMQKIDRKVAEVITHP 205
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714 206 KYNARNYDNDIAIIKLDEPVEFNEVLHPVCMPTPGRSFK-GENGIVTGWGALKVGGPTSDTLQEVQVPILSQDECRK-SR 283
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPaGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRaYS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922714 284 YGNKITDNMLCGGYDEGGKDSCQGDSGGPLhiVASGTREHQIAGVVSWGEGCAKAGYPGVYARVNRYGTWIKN 356
Cdd:cd00190 161 YGGTITDNMLCAGGLEGGKDACQGDSGGPL--VCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
126-354 1.49e-99

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: 294.59  E-value: 1.49e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714    126 RIVGGQETEVHQYPWVAMLLY-GGRFYCAASLLNDQFLLTASHCVYGFRKERISVRLLEHDRKmSHMQKIDRKVAEVITH 204
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714    205 PKYNARNYDNDIAIIKLDEPVEFNEVLHPVCMPTPGRSFK-GENGIVTGWGALK-VGGPTSDTLQEVQVPILSQDECRKS 282
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPaGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922714    283 RYGN-KITDNMLCGGYDEGGKDSCQGDSGGPLhivASGTREHQIAGVVSWGEGCAKAGYPGVYARVNRYGTWI 354
Cdd:smart00020 160 YSGGgAITDNMLCAGGLEGGKDACQGDSGGPL---VCNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
118-355 1.05e-75

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 234.93  E-value: 1.05e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714 118 CGIANIQKRIVGGQETEVHQYPWVAMLLYGG---RFYCAASLLNDQFLLTASHCVYGFRKERISVRLLEHDRKMSHMQKi 194
Cdd:COG5640  22 APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTV- 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714 195 dRKVAEVITHPKYNARNYDNDIAIIKLDEPVEFNEvlhPVCMPTPGRSFK-GENGIVTGWGALKVG-GPTSDTLQEVQVP 272
Cdd:COG5640 101 -VKVARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAApGTPATVAGWGRTSEGpGSQSGTLRKADVP 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714 273 ILSQDECRksRYGNKITDNMLCGGYDEGGKDSCQGDSGGPLhIVASGTREHQIaGVVSWGEGCAKAGYPGVYARVNRYGT 352
Cdd:COG5640 177 VVSDATCA--AYGGFDGGTMLCAGYPEGGKDACQGDSGGPL-VVKDGGGWVLV-GVVSWGGGPCAAGYPGVYTRVSAYRD 252

                ...
gi 19922714 353 WIK 355
Cdd:COG5640 253 WIK 255
Trypsin pfam00089
Trypsin;
127-354 6.44e-75

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 231.18  E-value: 6.44e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714   127 IVGGQETEVHQYPWVAMLLYGGRFY-CAASLLNDQFLLTASHCVYGfrKERISVRLLEHDRKMSHMQKIDRKVAEVITHP 205
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSG--ASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714   206 KYNARNYDNDIAIIKLDEPVEFNEVLHPVCMPTPGRSFK-GENGIVTGWGALKVGGPtSDTLQEVQVPILSQDECRkSRY 284
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPvGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCR-SAY 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714   285 GNKITDNMLCGGYdeGGKDSCQGDSGGPLhiVASGtreHQIAGVVSWGEGCAKAGYPGVYARVNRYGTWI 354
Cdd:pfam00089 157 GGTVTDTMICAGA--GGKDACQGDSGGPL--VCSD---GELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
127-356 2.25e-103

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: 304.20  E-value: 2.25e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714 127 IVGGQETEVHQYPWVAMLLYG-GRFYCAASLLNDQFLLTASHCVYGFRKERISVRLLEHDRKMSHMQKIDRKVAEVITHP 205
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714 206 KYNARNYDNDIAIIKLDEPVEFNEVLHPVCMPTPGRSFK-GENGIVTGWGALKVGGPTSDTLQEVQVPILSQDECRK-SR 283
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPaGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRaYS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922714 284 YGNKITDNMLCGGYDEGGKDSCQGDSGGPLhiVASGTREHQIAGVVSWGEGCAKAGYPGVYARVNRYGTWIKN 356
Cdd:cd00190 161 YGGTITDNMLCAGGLEGGKDACQGDSGGPL--VCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
126-354 1.49e-99

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: 294.59  E-value: 1.49e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714    126 RIVGGQETEVHQYPWVAMLLY-GGRFYCAASLLNDQFLLTASHCVYGFRKERISVRLLEHDRKmSHMQKIDRKVAEVITH 204
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714    205 PKYNARNYDNDIAIIKLDEPVEFNEVLHPVCMPTPGRSFK-GENGIVTGWGALK-VGGPTSDTLQEVQVPILSQDECRKS 282
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPaGTTCTVSGWGRTSeGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922714    283 RYGN-KITDNMLCGGYDEGGKDSCQGDSGGPLhivASGTREHQIAGVVSWGEGCAKAGYPGVYARVNRYGTWI 354
Cdd:smart00020 160 YSGGgAITDNMLCAGGLEGGKDACQGDSGGPL---VCNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
118-355 1.05e-75

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 234.93  E-value: 1.05e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714 118 CGIANIQKRIVGGQETEVHQYPWVAMLLYGG---RFYCAASLLNDQFLLTASHCVYGFRKERISVRLLEHDRKMSHMQKi 194
Cdd:COG5640  22 APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTV- 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714 195 dRKVAEVITHPKYNARNYDNDIAIIKLDEPVEFNEvlhPVCMPTPGRSFK-GENGIVTGWGALKVG-GPTSDTLQEVQVP 272
Cdd:COG5640 101 -VKVARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAApGTPATVAGWGRTSEGpGSQSGTLRKADVP 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714 273 ILSQDECRksRYGNKITDNMLCGGYDEGGKDSCQGDSGGPLhIVASGTREHQIaGVVSWGEGCAKAGYPGVYARVNRYGT 352
Cdd:COG5640 177 VVSDATCA--AYGGFDGGTMLCAGYPEGGKDACQGDSGGPL-VVKDGGGWVLV-GVVSWGGGPCAAGYPGVYTRVSAYRD 252

                ...
gi 19922714 353 WIK 355
Cdd:COG5640 253 WIK 255
Trypsin pfam00089
Trypsin;
127-354 6.44e-75

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 231.18  E-value: 6.44e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714   127 IVGGQETEVHQYPWVAMLLYGGRFY-CAASLLNDQFLLTASHCVYGfrKERISVRLLEHDRKMSHMQKIDRKVAEVITHP 205
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSG--ASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714   206 KYNARNYDNDIAIIKLDEPVEFNEVLHPVCMPTPGRSFK-GENGIVTGWGALKVGGPtSDTLQEVQVPILSQDECRkSRY 284
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPvGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCR-SAY 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714   285 GNKITDNMLCGGYdeGGKDSCQGDSGGPLhiVASGtreHQIAGVVSWGEGCAKAGYPGVYARVNRYGTWI 354
Cdd:pfam00089 157 GGTVTDTMICAGA--GGKDACQGDSGGPL--VCSD---GELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
141-354 4.36e-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: 4.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714 141 VAMLLYGGRFYCAASLLNDQFLLTASHCVYGFRKERISVRL-----LEHDRKMSHmqkidrKVAEVITHPKY-NARNYDN 214
Cdd:COG3591   3 GRLETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIvfvpgYNGGPYGTA------TATRFRVPPGWvASGDAGY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922714 215 DIAIIKLDEPVEfnEVLHPVCMPTPGRSFKGENGIVTGWGAlkvGGPTSDTLQEvqvpilsqdECR-KSRYGNKITdnML 293
Cdd:COG3591  77 DYALLRLDEPLG--DTTGWLGLAFNDAPLAGEPVTIIGYPG---DRPKDLSLDC---------SGRvTGVQGNRLS--YD 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922714 294 CggydeggkDSCQGDSGGPlhIVASGTREHQIAGVVSWG-EGCAKAGYPGVYARVNRYGTWI 354
Cdd:COG3591 141 C--------DTTGGSSGSP--VLDDSDGGGRVVGVHSAGgADRANTGVRLTSAIVAALRAWA 192
 
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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