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Conserved domains on  [gi|161076432|ref|NP_610437|]
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notopleural, 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

 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 ...
798-1038 1.54e-90

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: 288.79  E-value: 1.54e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432  798 IVGGANAAFGRWPWQISLRQWRTStylHKCGAALLNENWAITAAHCVDNVPPSDLLLRLGEYDLAEEEEpyGYQERRVQI 877
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEG--GGQVIKVKK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432  878 VASHPQFDPRTFEYDLALLRFYEPVIFQPNIIPVCVPDNDENFI-GQTAFVTGWGRLYEDGPLPSVLQEVAVPVINNTIC 956
Cdd:cd00190    76 VIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPaGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432  957 ESMYRSAGYIehiPHIFICAGWKKGGYDSCEGDSGGPMVLQreSDKRFHLGGVISWGIGCAEANQPGVYTRISEFRDWIN 1036
Cdd:cd00190   156 KRAYSYGGTI---TDNMLCAGGLEGGKDACQGDSGGPLVCN--DNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230

                  ..
gi 161076432 1037 QI 1038
Cdd:cd00190   231 KT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
798-1038 1.54e-90

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: 288.79  E-value: 1.54e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432  798 IVGGANAAFGRWPWQISLRQWRTStylHKCGAALLNENWAITAAHCVDNVPPSDLLLRLGEYDLAEEEEpyGYQERRVQI 877
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEG--GGQVIKVKK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432  878 VASHPQFDPRTFEYDLALLRFYEPVIFQPNIIPVCVPDNDENFI-GQTAFVTGWGRLYEDGPLPSVLQEVAVPVINNTIC 956
Cdd:cd00190    76 VIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPaGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432  957 ESMYRSAGYIehiPHIFICAGWKKGGYDSCEGDSGGPMVLQreSDKRFHLGGVISWGIGCAEANQPGVYTRISEFRDWIN 1036
Cdd:cd00190   156 KRAYSYGGTI---TDNMLCAGGLEGGKDACQGDSGGPLVCN--DNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230

                  ..
gi 161076432 1037 QI 1038
Cdd:cd00190   231 KT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
797-1035 2.55e-90

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: 288.04  E-value: 2.55e-90
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432    797 RIVGGANAAFGRWPWQISLRqwrTSTYLHKCGAALLNENWAITAAHCVDNVPPSDLLLRLGEYDLAEEEEPygyQERRVQ 876
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQ---YGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEG---QVIKVS 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432    877 IVASHPQFDPRTFEYDLALLRFYEPVIFQPNIIPVCVPDNDENFI-GQTAFVTGWGRLYED-GPLPSVLQEVAVPVINNT 954
Cdd:smart00020   75 KVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPaGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNA 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432    955 ICESMYrsaGYIEHIPHIFICAGWKKGGYDSCEGDSGGPMVLQresDKRFHLGGVISWGIGCAEANQPGVYTRISEFRDW 1034
Cdd:smart00020  155 TCRRAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN---DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228

                    .
gi 161076432   1035 I 1035
Cdd:smart00020  229 I 229
Trypsin pfam00089
Trypsin;
798-1035 9.77e-64

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 215.00  E-value: 9.77e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432   798 IVGGANAAFGRWPWQISLrQWRTSTylHKCGAALLNENWAITAAHCVDNvpPSDLLLRLGEYDLAEEEEpyGYQERRVQI 877
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSL-QLSSGK--HFCGGSLISENWVLTAAHCVSG--ASDVKVVLGAHNIVLREG--GEQKFDVEK 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432   878 VASHPQFDPRTFEYDLALLRFYEPVIFQPNIIPVCVPDNDENF-IGQTAFVTGWGRLYEDGPlPSVLQEVAVPVINNTIC 956
Cdd:pfam00089   74 IIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLpVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETC 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076432   957 ESMYRsAGYIEHiphiFICAGWkkGGYDSCEGDSGGPMVLqreSDKRFHlgGVISWGIGCAEANQPGVYTRISEFRDWI 1035
Cdd:pfam00089  153 RSAYG-GTVTDT----MICAGA--GGKDACQGDSGGPLVC---SDGELI--GIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
794-1039 1.12e-63

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 216.44  E-value: 1.12e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432  794 PEPRIVGGANAAFGRWPWQISLrQWRTSTYLHKCGAALLNENWAITAAHCVDNVPPSDLLLRLGEYDLAEEEEpygyQER 873
Cdd:COG5640    27 AAPAIVGGTPATVGEYPWMVAL-QSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGG----TVV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432  874 RVQIVASHPQFDPRTFEYDLALLRFYEPVifqPNIIPVCVPD-NDENFIGQTAFVTGWGRLYED-GPLPSVLQEVAVPVI 951
Cdd:COG5640   102 KVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATsADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVV 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432  952 NNTICesmyrsAGYIEHIPHIFICAGWKKGGYDSCEGDSGGPMVLQResDKRFHLGGVISWGIGCAEANQPGVYTRISEF 1031
Cdd:COG5640   179 SDATC------AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKD--GGGWVLVGVVSWGGGPCAAGYPGVYTRVSAY 250

                  ....*...
gi 161076432 1032 RDWINQIL 1039
Cdd:COG5640   251 RDWIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
798-1038 1.54e-90

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: 288.79  E-value: 1.54e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432  798 IVGGANAAFGRWPWQISLRQWRTStylHKCGAALLNENWAITAAHCVDNVPPSDLLLRLGEYDLAEEEEpyGYQERRVQI 877
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEG--GGQVIKVKK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432  878 VASHPQFDPRTFEYDLALLRFYEPVIFQPNIIPVCVPDNDENFI-GQTAFVTGWGRLYEDGPLPSVLQEVAVPVINNTIC 956
Cdd:cd00190    76 VIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPaGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432  957 ESMYRSAGYIehiPHIFICAGWKKGGYDSCEGDSGGPMVLQreSDKRFHLGGVISWGIGCAEANQPGVYTRISEFRDWIN 1036
Cdd:cd00190   156 KRAYSYGGTI---TDNMLCAGGLEGGKDACQGDSGGPLVCN--DNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230

                  ..
gi 161076432 1037 QI 1038
Cdd:cd00190   231 KT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
797-1035 2.55e-90

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: 288.04  E-value: 2.55e-90
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432    797 RIVGGANAAFGRWPWQISLRqwrTSTYLHKCGAALLNENWAITAAHCVDNVPPSDLLLRLGEYDLAEEEEPygyQERRVQ 876
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQ---YGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEG---QVIKVS 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432    877 IVASHPQFDPRTFEYDLALLRFYEPVIFQPNIIPVCVPDNDENFI-GQTAFVTGWGRLYED-GPLPSVLQEVAVPVINNT 954
Cdd:smart00020   75 KVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPaGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNA 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432    955 ICESMYrsaGYIEHIPHIFICAGWKKGGYDSCEGDSGGPMVLQresDKRFHLGGVISWGIGCAEANQPGVYTRISEFRDW 1034
Cdd:smart00020  155 TCRRAY---SGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN---DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228

                    .
gi 161076432   1035 I 1035
Cdd:smart00020  229 I 229
Trypsin pfam00089
Trypsin;
798-1035 9.77e-64

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 215.00  E-value: 9.77e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432   798 IVGGANAAFGRWPWQISLrQWRTSTylHKCGAALLNENWAITAAHCVDNvpPSDLLLRLGEYDLAEEEEpyGYQERRVQI 877
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSL-QLSSGK--HFCGGSLISENWVLTAAHCVSG--ASDVKVVLGAHNIVLREG--GEQKFDVEK 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432   878 VASHPQFDPRTFEYDLALLRFYEPVIFQPNIIPVCVPDNDENF-IGQTAFVTGWGRLYEDGPlPSVLQEVAVPVINNTIC 956
Cdd:pfam00089   74 IIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLpVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETC 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076432   957 ESMYRsAGYIEHiphiFICAGWkkGGYDSCEGDSGGPMVLqreSDKRFHlgGVISWGIGCAEANQPGVYTRISEFRDWI 1035
Cdd:pfam00089  153 RSAYG-GTVTDT----MICAGA--GGKDACQGDSGGPLVC---SDGELI--GIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
794-1039 1.12e-63

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 216.44  E-value: 1.12e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432  794 PEPRIVGGANAAFGRWPWQISLrQWRTSTYLHKCGAALLNENWAITAAHCVDNVPPSDLLLRLGEYDLAEEEEpygyQER 873
Cdd:COG5640    27 AAPAIVGGTPATVGEYPWMVAL-QSSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGG----TVV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432  874 RVQIVASHPQFDPRTFEYDLALLRFYEPVifqPNIIPVCVPD-NDENFIGQTAFVTGWGRLYED-GPLPSVLQEVAVPVI 951
Cdd:COG5640   102 KVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATsADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVV 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432  952 NNTICesmyrsAGYIEHIPHIFICAGWKKGGYDSCEGDSGGPMVLQResDKRFHLGGVISWGIGCAEANQPGVYTRISEF 1031
Cdd:COG5640   179 SDATC------AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKD--GGGWVLVGVVSWGGGPCAAGYPGVYTRVSAY 250

                  ....*...
gi 161076432 1032 RDWINQIL 1039
Cdd:COG5640   251 RDWIKSTA 258
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
827-1040 7.37e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 56.61  E-value: 7.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432  827 CGAALLNENWAITAAHCV----DNVPPSDLLLRLGeYDLAeeeePYGYQerRVQIVASHPQFDPRT-FEYDLALLRFYEP 901
Cdd:COG3591    14 CTGTLIGPNLVLTAGHCVydgaGGGWATNIVFVPG-YNGG----PYGTA--TATRFRVPPGWVASGdAGYDYALLRLDEP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076432  902 VifQPNIIPVCVPDNDENFIGQTAFVTGWGRlyeDGPLPSVLQEVavpvinntiCESMYRSAGYIEHiphifICagwkkg 981
Cdd:COG3591    87 L--GDTTGWLGLAFNDAPLAGEPVTIIGYPG---DRPKDLSLDCS---------GRVTGVQGNRLSY-----DC------ 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 161076432  982 gyDSCEGDSGGPMVlqRESDKRFHLGGVISWGiGCAEANQpGVYTrISEFRDWINQILQ 1040
Cdd:COG3591   142 --DTTGGSSGSPVL--DDSDGGGRVVGVHSAG-GADRANT-GVRL-TSAIVAALRAWAS 193
 
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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