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Conserved domains on  [gi|24581083|ref|NP_722787|]
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uncharacterized protein Dmel_CG17242, 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 ...
24-235 2.88e-47

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: 156.28  E-value: 2.88e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083  24 IEQAPWQASVQIND-KHHCGGVIYSEDIILTIAECVRKARLEFISVRVGSA---QENAGGTVLKVEKMRLQ---VLGLRP 96
Cdd:cd00190   9 IGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHdlsSNEGGGQVIKVKKVIVHpnyNPSTYD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083  97 SDVAILQLRSPLYLDGGIRAIPLAT--IPLVPGTNASVSGWGQLSAMNPSSEVLLRVDVKIQDQLMCAtNLALKGRLMSV 174
Cdd:cd00190  89 NDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK-RAYSYGGTITD 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581083 175 GEICAAPAGEIPYACQGFVGGPLVANNR----LYGILSWQSACDVLNKSSVYANIAMFKVWIEST 235
Cdd:cd00190 168 NMLCAGGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
24-235 2.88e-47

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: 156.28  E-value: 2.88e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083  24 IEQAPWQASVQIND-KHHCGGVIYSEDIILTIAECVRKARLEFISVRVGSA---QENAGGTVLKVEKMRLQ---VLGLRP 96
Cdd:cd00190   9 IGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHdlsSNEGGGQVIKVKKVIVHpnyNPSTYD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083  97 SDVAILQLRSPLYLDGGIRAIPLAT--IPLVPGTNASVSGWGQLSAMNPSSEVLLRVDVKIQDQLMCAtNLALKGRLMSV 174
Cdd:cd00190  89 NDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK-RAYSYGGTITD 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581083 175 GEICAAPAGEIPYACQGFVGGPLVANNR----LYGILSWQSACDVLNKSSVYANIAMFKVWIEST 235
Cdd:cd00190 168 NMLCAGGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-232 2.90e-44

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: 148.59  E-value: 2.90e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083     24 IEQAPWQASVQIND-KHHCGGVIYSEDIILTIAECVRKARLEFISVRVGS--AQENAGGTVLKVEKMRLQ---VLGLRPS 97
Cdd:smart00020  10 IGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGShdLSSGEEGQVIKVSKVIIHpnyNPSTYDN 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083     98 DVAILQLRSPLYLDGGIRAIPLAT--IPLVPGTNASVSGWGQLSAMNPS-SEVLLRVDVKIQDQLMCATNLALKGRLMSv 174
Cdd:smart00020  90 DIALLKLKEPVTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATCRRAYSGGGAITD- 168
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581083    175 GEICAAPAGEIPYACQGFVGGPLVANNR---LYGILSWQSACDVLNKSSVYANIAMFKVWI 232
Cdd:smart00020 169 NMLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-236 2.08e-34

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 123.99  E-value: 2.08e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083   1 MLLKGILLLVSIAQIAADFKSIG-----IEQAPWQASVQIND---KHHCGGVIYSEDIILTIAECVRKARLEFISVRVGS 72
Cdd:COG5640  11 AAAALALALAAAPAADAAPAIVGgtpatVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGS 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083  73 A-QENAGGTVLKVEKMRLQ---VLGLRPSDVAILQLRSPLyldGGIRAIPLAT--IPLVPGTNASVSGWGQLSA-MNPSS 145
Cdd:COG5640  91 TdLSTSGGTVVKVARIVVHpdyDPATPGNDIALLKLATPV---PGVAPAPLATsaDAAAPGTPATVAGWGRTSEgPGSQS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083 146 EVLLRVDVKIQDQLMCATNLALKGRLMsvgeICAAPAGEIPYACQGFVGGPLVANN----RLYGILSW-QSACDVlNKSS 220
Cdd:COG5640 168 GTLRKADVPVVSDATCAAYGGFDGGTM----LCAGYPEGGKDACQGDSGGPLVVKDgggwVLVGVVSWgGGPCAA-GYPG 242
                       250
                ....*....|....*.
gi 24581083 221 VYANIAMFKVWIESTV 236
Cdd:COG5640 243 VYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
26-232 2.96e-32

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 117.16  E-value: 2.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083    26 QAPWQASVQINDKHH-CGGVIYSEDIILTIAECVRKARleFISVRVG--SAQENAGG----TVLKVEKMRLQVLGLRPSD 98
Cdd:pfam00089  11 SFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGAS--DVKVVLGahNIVLREGGeqkfDVEKIIVHPNYNPDTLDND 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083    99 VAILQLRSPLYLDGGIRAIPLATI--PLVPGTNASVSGWGQLSAMNPSsEVLLRVDVKIQDQLMCATNLalkGRLMSVGE 176
Cdd:pfam00089  89 IALLKLESPVTLGDTVRPICLPDAssDLPVGTTCTVSGWGNTKTLGPS-DTLQEVTVPVVSRETCRSAY---GGTVTDTM 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581083   177 ICAAPAGEipYACQGFVGGPLVANNR-LYGILSWQSACDVLNKSSVYANIAMFKVWI 232
Cdd:pfam00089 165 ICAGAGGK--DACQGDSGGPLVCSDGeLIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
24-235 2.88e-47

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: 156.28  E-value: 2.88e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083  24 IEQAPWQASVQIND-KHHCGGVIYSEDIILTIAECVRKARLEFISVRVGSA---QENAGGTVLKVEKMRLQ---VLGLRP 96
Cdd:cd00190   9 IGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHdlsSNEGGGQVIKVKKVIVHpnyNPSTYD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083  97 SDVAILQLRSPLYLDGGIRAIPLAT--IPLVPGTNASVSGWGQLSAMNPSSEVLLRVDVKIQDQLMCAtNLALKGRLMSV 174
Cdd:cd00190  89 NDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK-RAYSYGGTITD 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581083 175 GEICAAPAGEIPYACQGFVGGPLVANNR----LYGILSWQSACDVLNKSSVYANIAMFKVWIEST 235
Cdd:cd00190 168 NMLCAGGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-232 2.90e-44

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: 148.59  E-value: 2.90e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083     24 IEQAPWQASVQIND-KHHCGGVIYSEDIILTIAECVRKARLEFISVRVGS--AQENAGGTVLKVEKMRLQ---VLGLRPS 97
Cdd:smart00020  10 IGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGShdLSSGEEGQVIKVSKVIIHpnyNPSTYDN 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083     98 DVAILQLRSPLYLDGGIRAIPLAT--IPLVPGTNASVSGWGQLSAMNPS-SEVLLRVDVKIQDQLMCATNLALKGRLMSv 174
Cdd:smart00020  90 DIALLKLKEPVTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVSNATCRRAYSGGGAITD- 168
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581083    175 GEICAAPAGEIPYACQGFVGGPLVANNR---LYGILSWQSACDVLNKSSVYANIAMFKVWI 232
Cdd:smart00020 169 NMLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-236 2.08e-34

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 123.99  E-value: 2.08e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083   1 MLLKGILLLVSIAQIAADFKSIG-----IEQAPWQASVQIND---KHHCGGVIYSEDIILTIAECVRKARLEFISVRVGS 72
Cdd:COG5640  11 AAAALALALAAAPAADAAPAIVGgtpatVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGS 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083  73 A-QENAGGTVLKVEKMRLQ---VLGLRPSDVAILQLRSPLyldGGIRAIPLAT--IPLVPGTNASVSGWGQLSA-MNPSS 145
Cdd:COG5640  91 TdLSTSGGTVVKVARIVVHpdyDPATPGNDIALLKLATPV---PGVAPAPLATsaDAAAPGTPATVAGWGRTSEgPGSQS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083 146 EVLLRVDVKIQDQLMCATNLALKGRLMsvgeICAAPAGEIPYACQGFVGGPLVANN----RLYGILSW-QSACDVlNKSS 220
Cdd:COG5640 168 GTLRKADVPVVSDATCAAYGGFDGGTM----LCAGYPEGGKDACQGDSGGPLVVKDgggwVLVGVVSWgGGPCAA-GYPG 242
                       250
                ....*....|....*.
gi 24581083 221 VYANIAMFKVWIESTV 236
Cdd:COG5640 243 VYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
26-232 2.96e-32

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 117.16  E-value: 2.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083    26 QAPWQASVQINDKHH-CGGVIYSEDIILTIAECVRKARleFISVRVG--SAQENAGG----TVLKVEKMRLQVLGLRPSD 98
Cdd:pfam00089  11 SFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGAS--DVKVVLGahNIVLREGGeqkfDVEKIIVHPNYNPDTLDND 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581083    99 VAILQLRSPLYLDGGIRAIPLATI--PLVPGTNASVSGWGQLSAMNPSsEVLLRVDVKIQDQLMCATNLalkGRLMSVGE 176
Cdd:pfam00089  89 IALLKLESPVTLGDTVRPICLPDAssDLPVGTTCTVSGWGNTKTLGPS-DTLQEVTVPVVSRETCRSAY---GGTVTDTM 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581083   177 ICAAPAGEipYACQGFVGGPLVANNR-LYGILSWQSACDVLNKSSVYANIAMFKVWI 232
Cdd:pfam00089 165 ICAGAGGK--DACQGDSGGPLVCSDGeLIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
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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