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Conserved domains on  [gi|24581085|ref|NP_608665|]
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uncharacterized protein Dmel_CG4271 [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 ...
19-234 1.13e-52

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: 170.15  E-value: 1.13e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085  19 IYNGVEAKFDFWTFLASVWVS-GYHECGGAVIDSRIVLTAAQCVKNKPVKRITVRVGTPDIYR---GGRIIRVTALVVHE 94
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSnegGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085  95 NY--KNWDNDIALLWLEKPV-LSVRVTKIPLatkePSENEYPSN------AGWGeKLLESYVVTRKLQNGVTKIRPRSMC 165
Cdd:cd00190  81 NYnpSTYDNDIALLKLKRPVtLSDNVRPICL----PSSGYNLPAgttctvSGWG-RTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581085 166 AEELV--EPVGEELLCAFYTEN--DICPGDYGGPLVL----ANKVVGIAVQGHGCGFAVLPSLYTNVFHYLEWIEEN 234
Cdd:cd00190 156 KRAYSygGTITDNMLCAGGLEGgkDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
19-234 1.13e-52

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: 170.15  E-value: 1.13e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085  19 IYNGVEAKFDFWTFLASVWVS-GYHECGGAVIDSRIVLTAAQCVKNKPVKRITVRVGTPDIYR---GGRIIRVTALVVHE 94
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSnegGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085  95 NY--KNWDNDIALLWLEKPV-LSVRVTKIPLatkePSENEYPSN------AGWGeKLLESYVVTRKLQNGVTKIRPRSMC 165
Cdd:cd00190  81 NYnpSTYDNDIALLKLKRPVtLSDNVRPICL----PSSGYNLPAgttctvSGWG-RTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581085 166 AEELV--EPVGEELLCAFYTEN--DICPGDYGGPLVL----ANKVVGIAVQGHGCGFAVLPSLYTNVFHYLEWIEEN 234
Cdd:cd00190 156 KRAYSygGTITDNMLCAGGLEGgkDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
19-231 3.57e-52

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: 168.63  E-value: 3.57e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085     19 IYNGVEAKFDFWTFLASVWVSG-YHECGGAVIDSRIVLTAAQCVKNKPVKRITVRVGTPDIYRGGR--IIRVTALVVHEN 95
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEgqVIKVSKVIIHPN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085     96 Y--KNWDNDIALLWLEKPV-LSVRVTKIPLatkePSENEYPSN------AGWGEKLLESYVVTRKLQNGVTKIRPRSMCA 166
Cdd:smart00020  82 YnpSTYDNDIALLKLKEPVtLSDNVRPICL----PSSNYNVPAgttctvSGWGRTSEGAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581085    167 EELV--EPVGEELLCAFYTEN--DICPGDYGGPLVLANK---VVGIAVQGHGCGFAVLPSLYTNVFHYLEWI 231
Cdd:smart00020 158 RAYSggGAITDNMLCAGGLEGgkDACQGDSGGPLVCNDGrwvLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
19-235 2.63e-42

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 144.41  E-value: 2.63e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085  19 IYNGVEAKFDFWTFLASVWVSG---YHECGGAVIDSRIVLTAAQCVKNKPVKRITVRVGTPDIY-RGGRIIRVTALVVHE 94
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLStSGGTVVKVARIVVHP 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085  95 NYKNW--DNDIALLWLEKPVLSVRVtkIPLATKEPSENEYPSN--AGWGEKLLESYVVTRKLQNGVTKIRPRSMCAeELV 170
Cdd:COG5640 111 DYDPAtpGNDIALLKLATPVPGVAP--APLATSADAAAPGTPAtvAGWGRTSEGPGSQSGTLRKADVPVVSDATCA-AYG 187
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581085 171 EPVGEELLCAFYTE--NDICPGDYGGPLVLAN----KVVGIAVQGHGCGFAVLPSLYTNVFHYLEWIEENA 235
Cdd:COG5640 188 GFDGGTMLCAGYPEggKDACQGDSGGPLVVKDgggwVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
19-231 3.39e-41

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 140.27  E-value: 3.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085    19 IYNGVEAKFDFWTFLASV-WVSGYHECGGAVIDSRIVLTAAQCVKNkpVKRITVRVGTPDIYR---GGRIIRVTALVVHE 94
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVSG--ASDVKVVLGAHNIVLregGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085    95 NY--KNWDNDIALLWLEKPV-LSVRVTKIPLATKEPS--ENEYPSNAGWGekLLESYVVTRKLQNGVTKIRPRSMCAEEL 169
Cdd:pfam00089  79 NYnpDTLDNDIALLKLESPVtLGDTVRPICLPDASSDlpVGTTCTVSGWG--NTKTLGPSDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24581085   170 VEPVGEELLCAFYTENDICPGDYGGPLVLANK-VVGIAVQGHGCGFAVLPSLYTNVFHYLEWI 231
Cdd:pfam00089 157 GGTVTDTMICAGAGGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
19-234 1.13e-52

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: 170.15  E-value: 1.13e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085  19 IYNGVEAKFDFWTFLASVWVS-GYHECGGAVIDSRIVLTAAQCVKNKPVKRITVRVGTPDIYR---GGRIIRVTALVVHE 94
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSnegGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085  95 NY--KNWDNDIALLWLEKPV-LSVRVTKIPLatkePSENEYPSN------AGWGeKLLESYVVTRKLQNGVTKIRPRSMC 165
Cdd:cd00190  81 NYnpSTYDNDIALLKLKRPVtLSDNVRPICL----PSSGYNLPAgttctvSGWG-RTSEGGPLPDVLQEVNVPIVSNAEC 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581085 166 AEELV--EPVGEELLCAFYTEN--DICPGDYGGPLVL----ANKVVGIAVQGHGCGFAVLPSLYTNVFHYLEWIEEN 234
Cdd:cd00190 156 KRAYSygGTITDNMLCAGGLEGgkDACQGDSGGPLVCndngRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
19-231 3.57e-52

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: 168.63  E-value: 3.57e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085     19 IYNGVEAKFDFWTFLASVWVSG-YHECGGAVIDSRIVLTAAQCVKNKPVKRITVRVGTPDIYRGGR--IIRVTALVVHEN 95
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEgqVIKVSKVIIHPN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085     96 Y--KNWDNDIALLWLEKPV-LSVRVTKIPLatkePSENEYPSN------AGWGEKLLESYVVTRKLQNGVTKIRPRSMCA 166
Cdd:smart00020  82 YnpSTYDNDIALLKLKEPVtLSDNVRPICL----PSSNYNVPAgttctvSGWGRTSEGAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581085    167 EELV--EPVGEELLCAFYTEN--DICPGDYGGPLVLANK---VVGIAVQGHGCGFAVLPSLYTNVFHYLEWI 231
Cdd:smart00020 158 RAYSggGAITDNMLCAGGLEGgkDACQGDSGGPLVCNDGrwvLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
19-235 2.63e-42

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 144.41  E-value: 2.63e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085  19 IYNGVEAKFDFWTFLASVWVSG---YHECGGAVIDSRIVLTAAQCVKNKPVKRITVRVGTPDIY-RGGRIIRVTALVVHE 94
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLStSGGTVVKVARIVVHP 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085  95 NYKNW--DNDIALLWLEKPVLSVRVtkIPLATKEPSENEYPSN--AGWGEKLLESYVVTRKLQNGVTKIRPRSMCAeELV 170
Cdd:COG5640 111 DYDPAtpGNDIALLKLATPVPGVAP--APLATSADAAAPGTPAtvAGWGRTSEGPGSQSGTLRKADVPVVSDATCA-AYG 187
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581085 171 EPVGEELLCAFYTE--NDICPGDYGGPLVLAN----KVVGIAVQGHGCGFAVLPSLYTNVFHYLEWIEENA 235
Cdd:COG5640 188 GFDGGTMLCAGYPEggKDACQGDSGGPLVVKDgggwVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
19-231 3.39e-41

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 140.27  E-value: 3.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085    19 IYNGVEAKFDFWTFLASV-WVSGYHECGGAVIDSRIVLTAAQCVKNkpVKRITVRVGTPDIYR---GGRIIRVTALVVHE 94
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVSG--ASDVKVVLGAHNIVLregGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085    95 NY--KNWDNDIALLWLEKPV-LSVRVTKIPLATKEPS--ENEYPSNAGWGekLLESYVVTRKLQNGVTKIRPRSMCAEEL 169
Cdd:pfam00089  79 NYnpDTLDNDIALLKLESPVtLGDTVRPICLPDASSDlpVGTTCTVSGWG--NTKTLGPSDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24581085   170 VEPVGEELLCAFYTENDICPGDYGGPLVLANK-VVGIAVQGHGCGFAVLPSLYTNVFHYLEWI 231
Cdd:pfam00089 157 GGTVTDTMICAGAGGKDACQGDSGGPLVCSDGeLIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
39-211 7.60e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 48.13  E-value: 7.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085  39 SGYHECGGAVIDSRIVLTAAQCVKN----KPVKRITVRVGtpdiYRGGR--IIRVTALVVHENYK---NWDNDIALLWLE 109
Cdd:COG3591   9 GGGGVCTGTLIGPNLVLTAGHCVYDgaggGWATNIVFVPG----YNGGPygTATATRFRVPPGWVasgDAGYDYALLRLD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581085 110 KPvLSVRVTKIPLATKEPSENE-------YPSNagwgekllESYVVTRKLQNGVTKIRPRSMcaeelvepvgeellcafY 182
Cdd:COG3591  85 EP-LGDTTGWLGLAFNDAPLAGepvtiigYPGD--------RPKDLSLDCSGRVTGVQGNRL-----------------S 138
                       170       180       190
                ....*....|....*....|....*....|...
gi 24581085 183 TENDICPGDYGGPLVLA----NKVVGIAVQGHG 211
Cdd:COG3591 139 YDCDTTGGSSGSPVLDDsdggGRVVGVHSAGGA 171
 
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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