NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24650927|ref|NP_651661|]
View 

uncharacterized protein Dmel_CG11841 [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

show extra options »

Show site features     Horizontal zoom: ×

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 ...
72-311 2.07e-56

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: 182.48  E-value: 2.07e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927  72 IVDGTPAEPKEFPFAARLghrkTNNEIKWFCGGTLISNRLVLTAAHCFFSEHGEVNVVRLGELefDTDTDDAEPEDFGVL 151
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSL----QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSH--DLSSNEGGGQVIKVK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927 152 ALKAHPGFENPQLYNDIGIVQLDREVKFNRYKHPACLPfDDGEQHE---SFIAIGWGQKKFAQKESKKLLKVQLQGY-KD 227
Cdd:cd00190  75 KVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLP-SSGYNLPagtTCTVSGWGRTSEGGPLPDVLQEVNVPIVsNA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927 228 RCVSSVDANDELPNgyepkSQLCIG-SRDNKDTCNGDSGGPvLAYHKDlaCMYHVMGITSAGITCSTPDIPSAYTRVHYF 306
Cdd:cd00190 154 ECKRAYSYGGTITD-----NMLCAGgLEGGKDACQGDSGGP-LVCNDN--GRGVLVGIVSWGSGCARPNYPGVYTRVSSY 225

                ....*
gi 24650927 307 LNWIK 311
Cdd:cd00190 226 LDWIQ 230
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
72-311 2.07e-56

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: 182.48  E-value: 2.07e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927  72 IVDGTPAEPKEFPFAARLghrkTNNEIKWFCGGTLISNRLVLTAAHCFFSEHGEVNVVRLGELefDTDTDDAEPEDFGVL 151
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSL----QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSH--DLSSNEGGGQVIKVK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927 152 ALKAHPGFENPQLYNDIGIVQLDREVKFNRYKHPACLPfDDGEQHE---SFIAIGWGQKKFAQKESKKLLKVQLQGY-KD 227
Cdd:cd00190  75 KVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLP-SSGYNLPagtTCTVSGWGRTSEGGPLPDVLQEVNVPIVsNA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927 228 RCVSSVDANDELPNgyepkSQLCIG-SRDNKDTCNGDSGGPvLAYHKDlaCMYHVMGITSAGITCSTPDIPSAYTRVHYF 306
Cdd:cd00190 154 ECKRAYSYGGTITD-----NMLCAGgLEGGKDACQGDSGGP-LVCNDN--GRGVLVGIVSWGSGCARPNYPGVYTRVSSY 225

                ....*
gi 24650927 307 LNWIK 311
Cdd:cd00190 226 LDWIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
72-310 5.68e-53

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: 173.63  E-value: 5.68e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927     72 IVDGTPAEPKEFPFAARLghrkTNNEIKWFCGGTLISNRLVLTAAHCFFSEHGEVNVVRLGELEFDTDTDDaepEDFGVL 151
Cdd:smart00020   2 IVGGSEANIGSFPWQVSL----QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEG---QVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927    152 ALKAHPGFENPQLYNDIGIVQLDREVKFNRYKHPACLP--FDDGEQHESFIAIGWGQKKFAQKE-SKKLLKVQLQGY-KD 227
Cdd:smart00020  75 KVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPssNYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVsNA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927    228 RCVSSVDandelPNGYEPKSQLCIGSRDN-KDTCNGDSGGPvLAYHKDlacMYHVMGITSAGITCSTPDIPSAYTRVHYF 306
Cdd:smart00020 155 TCRRAYS-----GGGAITDNMLCAGGLEGgKDACQGDSGGP-LVCNDG---RWVLVGIVSWGSGCARPGKPGVYTRVSSY 225

                   ....
gi 24650927    307 LNWI 310
Cdd:smart00020 226 LDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
70-311 2.21e-47

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 160.20  E-value: 2.21e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927  70 PLIVDGTPAEPKEFPFAARLGHRktNNEIKWFCGGTLISNRLVLTAAHCFFSEHGEVNVVRLGelefDTDTDDAEPEDFG 149
Cdd:COG5640  29 PAIVGGTPATVGEYPWMVALQSS--NGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIG----STDLSTSGGTVVK 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927 150 VLALKAHPGFENPQLYNDIGIVQLDREVKFNRykhPACLP--FDDGEQHESFIAIGWGQKKFAQKE-SKKLLKVQLQgyk 226
Cdd:COG5640 103 VARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLAtsADAAAPGTPATVAGWGRTSEGPGSqSGTLRKADVP--- 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927 227 drcVSSvDANDELPNGYEPKSQLCIGSRD-NKDTCNGDSGGPVLAyhkDLACMYHVMGITSAGITCSTPDIPSAYTRVHY 305
Cdd:COG5640 177 ---VVS-DATCAAYGGFDGGTMLCAGYPEgGKDACQGDSGGPLVV---KDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSA 249

                ....*.
gi 24650927 306 FLNWIK 311
Cdd:COG5640 250 YRDWIK 255
Trypsin pfam00089
Trypsin;
72-310 6.57e-46

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 154.91  E-value: 6.57e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927    72 IVDGTPAEPKEFPFAARLghrkTNNEIKWFCGGTLISNRLVLTAAHCFfSEHGEVNVvRLGELefDTDTDDAEPEDFGVL 151
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSL----QLSSGKHFCGGSLISENWVLTAAHCV-SGASDVKV-VLGAH--NIVLREGGEQKFDVE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927   152 ALKAHPGFENPQLYNDIGIVQLDREVKFNRYKHPACLP--FDDGEQHESFIAIGWGqKKFAQKESKKLLKVQLQGY-KDR 228
Cdd:pfam00089  73 KIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPdaSSDLPVGTTCTVSGWG-NTKTLGPSDTLQEVTVPVVsRET 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927   229 CVSSVdandelpNGYEPKSQLCIGSRDnKDTCNGDSGGPVLAYHKDLAcmyhvmGITSAGITCSTPDIPSAYTRVHYFLN 308
Cdd:pfam00089 152 CRSAY-------GGTVTDTMICAGAGG-KDACQGDSGGPLVCSDGELI------GIVSWGYGCASGNYPGVYTPVSSYLD 217

                  ..
gi 24650927   309 WI 310
Cdd:pfam00089 218 WI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
72-311 2.07e-56

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: 182.48  E-value: 2.07e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927  72 IVDGTPAEPKEFPFAARLghrkTNNEIKWFCGGTLISNRLVLTAAHCFFSEHGEVNVVRLGELefDTDTDDAEPEDFGVL 151
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSL----QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSH--DLSSNEGGGQVIKVK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927 152 ALKAHPGFENPQLYNDIGIVQLDREVKFNRYKHPACLPfDDGEQHE---SFIAIGWGQKKFAQKESKKLLKVQLQGY-KD 227
Cdd:cd00190  75 KVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLP-SSGYNLPagtTCTVSGWGRTSEGGPLPDVLQEVNVPIVsNA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927 228 RCVSSVDANDELPNgyepkSQLCIG-SRDNKDTCNGDSGGPvLAYHKDlaCMYHVMGITSAGITCSTPDIPSAYTRVHYF 306
Cdd:cd00190 154 ECKRAYSYGGTITD-----NMLCAGgLEGGKDACQGDSGGP-LVCNDN--GRGVLVGIVSWGSGCARPNYPGVYTRVSSY 225

                ....*
gi 24650927 307 LNWIK 311
Cdd:cd00190 226 LDWIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
72-310 5.68e-53

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: 173.63  E-value: 5.68e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927     72 IVDGTPAEPKEFPFAARLghrkTNNEIKWFCGGTLISNRLVLTAAHCFFSEHGEVNVVRLGELEFDTDTDDaepEDFGVL 151
Cdd:smart00020   2 IVGGSEANIGSFPWQVSL----QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEG---QVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927    152 ALKAHPGFENPQLYNDIGIVQLDREVKFNRYKHPACLP--FDDGEQHESFIAIGWGQKKFAQKE-SKKLLKVQLQGY-KD 227
Cdd:smart00020  75 KVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPssNYNVPAGTTCTVSGWGRTSEGAGSlPDTLQEVNVPIVsNA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927    228 RCVSSVDandelPNGYEPKSQLCIGSRDN-KDTCNGDSGGPvLAYHKDlacMYHVMGITSAGITCSTPDIPSAYTRVHYF 306
Cdd:smart00020 155 TCRRAYS-----GGGAITDNMLCAGGLEGgKDACQGDSGGP-LVCNDG---RWVLVGIVSWGSGCARPGKPGVYTRVSSY 225

                   ....
gi 24650927    307 LNWI 310
Cdd:smart00020 226 LDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
70-311 2.21e-47

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 160.20  E-value: 2.21e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927  70 PLIVDGTPAEPKEFPFAARLGHRktNNEIKWFCGGTLISNRLVLTAAHCFFSEHGEVNVVRLGelefDTDTDDAEPEDFG 149
Cdd:COG5640  29 PAIVGGTPATVGEYPWMVALQSS--NGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIG----STDLSTSGGTVVK 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927 150 VLALKAHPGFENPQLYNDIGIVQLDREVKFNRykhPACLP--FDDGEQHESFIAIGWGQKKFAQKE-SKKLLKVQLQgyk 226
Cdd:COG5640 103 VARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLAtsADAAAPGTPATVAGWGRTSEGPGSqSGTLRKADVP--- 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927 227 drcVSSvDANDELPNGYEPKSQLCIGSRD-NKDTCNGDSGGPVLAyhkDLACMYHVMGITSAGITCSTPDIPSAYTRVHY 305
Cdd:COG5640 177 ---VVS-DATCAAYGGFDGGTMLCAGYPEgGKDACQGDSGGPLVV---KDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSA 249

                ....*.
gi 24650927 306 FLNWIK 311
Cdd:COG5640 250 YRDWIK 255
Trypsin pfam00089
Trypsin;
72-310 6.57e-46

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 154.91  E-value: 6.57e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927    72 IVDGTPAEPKEFPFAARLghrkTNNEIKWFCGGTLISNRLVLTAAHCFfSEHGEVNVvRLGELefDTDTDDAEPEDFGVL 151
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSL----QLSSGKHFCGGSLISENWVLTAAHCV-SGASDVKV-VLGAH--NIVLREGGEQKFDVE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927   152 ALKAHPGFENPQLYNDIGIVQLDREVKFNRYKHPACLP--FDDGEQHESFIAIGWGqKKFAQKESKKLLKVQLQGY-KDR 228
Cdd:pfam00089  73 KIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPdaSSDLPVGTTCTVSGWG-NTKTLGPSDTLQEVTVPVVsRET 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927   229 CVSSVdandelpNGYEPKSQLCIGSRDnKDTCNGDSGGPVLAYHKDLAcmyhvmGITSAGITCSTPDIPSAYTRVHYFLN 308
Cdd:pfam00089 152 CRSAY-------GGTVTDTMICAGAGG-KDACQGDSGGPLVCSDGELI------GIVSWGYGCASGNYPGVYTPVSSYLD 217

                  ..
gi 24650927   309 WI 310
Cdd:pfam00089 218 WI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
100-288 4.90e-13

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 66.62  E-value: 4.90e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927 100 WFCGGTLISNRLVLTAAHCFFSEHGEVNVVRlgeLEFDTDTDDAEPEDFGVLALKAHPGFENPQLYN-DIGIVQLDREVk 178
Cdd:COG3591  12 GVCTGTLIGPNLVLTAGHCVYDGAGGGWATN---IVFVPGYNGGPYGTATATRFRVPPGWVASGDAGyDYALLRLDEPL- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650927 179 fnrYKHPACLPFDDGEQH---ESFIAIGWGQ---KKFAQKESKKLLKVQLQGYKDRCvssvdandelpngyepksqlcig 252
Cdd:COG3591  88 ---GDTTGWLGLAFNDAPlagEPVTIIGYPGdrpKDLSLDCSGRVTGVQGNRLSYDC----------------------- 141
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 24650927 253 srdnkDTCNGDSGGPVLAYHkdlACMYHVMGITSAG 288
Cdd:COG3591 142 -----DTTGGSSGSPVLDDS---DGGGRVVGVHSAG 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH