NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24649918|ref|NP_733078|]
View 

uncharacterized protein Dmel_CG11836, isoform B [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 ...
1-215 1.11e-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: 266.06  E-value: 1.11e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918   1 MARIVY-DGKFHCGGSLLTKDYVLSAAHCVKKLRKSKIRVIFGDHDQEiTSESQAIQRAVTAVIKHKSFDPDTYNNDIAL 79
Cdd:cd00190  15 QVSLQYtGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLS-SNEGGGQVIKVKKVIVHPNYNPSTYDNDIAL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918  80 LRLRKPISFSKIIKPICLPRYNYD-PAGRIGTVVGWGRTSEGGELPSIVNQVKVPIMSITECRNQRYKSTRITSSMLCAG 158
Cdd:cd00190  94 LKLKRPVTLSDNVRPICLPSSGYNlPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYSYGGTITDNMLCAG 173
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24649918 159 --RPSMDSCQGDSGGPLLLSNGVKYFIVGIVSWGVGCGREGYPGVYSRVSKFIPWIKSN 215
Cdd:cd00190 174 glEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-215 1.11e-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: 266.06  E-value: 1.11e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918   1 MARIVY-DGKFHCGGSLLTKDYVLSAAHCVKKLRKSKIRVIFGDHDQEiTSESQAIQRAVTAVIKHKSFDPDTYNNDIAL 79
Cdd:cd00190  15 QVSLQYtGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLS-SNEGGGQVIKVKKVIVHPNYNPSTYDNDIAL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918  80 LRLRKPISFSKIIKPICLPRYNYD-PAGRIGTVVGWGRTSEGGELPSIVNQVKVPIMSITECRNQRYKSTRITSSMLCAG 158
Cdd:cd00190  94 LKLKRPVTLSDNVRPICLPSSGYNlPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYSYGGTITDNMLCAG 173
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24649918 159 --RPSMDSCQGDSGGPLLLSNGVKYFIVGIVSWGVGCGREGYPGVYSRVSKFIPWIKSN 215
Cdd:cd00190 174 glEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-212 4.54e-87

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: 256.84  E-value: 4.54e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918      1 MARIVY-DGKFHCGGSLLTKDYVLSAAHCVKKLRKSKIRVIFGDHDQEITSESQAIQraVTAVIKHKSFDPDTYNNDIAL 79
Cdd:smart00020  16 QVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVIK--VSKVIIHPNYNPSTYDNDIAL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918     80 LRLRKPISFSKIIKPICLPRYNYD-PAGRIGTVVGWGRTSEG-GELPSIVNQVKVPIMSITECRNQRYKSTRITSSMLCA 157
Cdd:smart00020  94 LKLKEPVTLSDNVRPICLPSSNYNvPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRAYSGGGAITDNMLCA 173
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24649918    158 G--RPSMDSCQGDSGGPLLLSNGVkYFIVGIVSWGVGCGREGYPGVYSRVSKFIPWI 212
Cdd:smart00020 174 GglEGGKDACQGDSGGPLVCNDGR-WVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-214 4.57e-69

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 212.20  E-value: 4.57e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918   1 MARIVYDG---KFHCGGSLLTKDYVLSAAHCVKKLRKSKIRVIFGDHDQeitSESQAIQRAVTAVIKHKSFDPDTYNNDI 77
Cdd:COG5640  45 MVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDL---STSGGTVVKVARIVVHPDYDPATPGNDI 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918  78 ALLRLRKPISFskiIKPICLPRYNYDPA-GRIGTVVGWGRTSEG-GELPSIVNQVKVPIMSITECRNQrykSTRITSSML 155
Cdd:COG5640 122 ALLKLATPVPG---VAPAPLATSADAAApGTPATVAGWGRTSEGpGSQSGTLRKADVPVVSDATCAAY---GGFDGGTML 195
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24649918 156 CAGRPS--MDSCQGDSGGPLLLSNGVKYFIVGIVSWGVGCGREGYPGVYSRVSKFIPWIKS 214
Cdd:COG5640 196 CAGYPEggKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKS 256
Trypsin pfam00089
Trypsin;
1-212 9.35e-66

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 202.29  E-value: 9.35e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918     1 MARIVYDGKFH-CGGSLLTKDYVLSAAHCVKklRKSKIRVIFGDHDQEITSESQAIqRAVTAVIKHKSFDPDTYNNDIAL 79
Cdd:pfam00089  15 QVSLQLSSGKHfCGGSLISENWVLTAAHCVS--GASDVKVVLGAHNIVLREGGEQK-FDVEKIIVHPNYNPDTLDNDIAL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918    80 LRLRKPISFSKIIKPICLPRYNYD-PAGRIGTVVGWGRTSEGGeLPSIVNQVKVPIMSITECRnqRYKSTRITSSMLCAG 158
Cdd:pfam00089  92 LKLESPVTLGDTVRPICLPDASSDlPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCR--SAYGGTVTDTMICAG 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 24649918   159 RPSMDSCQGDSGGPLLLSNGvkyFIVGIVSWGVGCGREGYPGVYSRVSKFIPWI 212
Cdd:pfam00089 169 AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-215 1.11e-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: 266.06  E-value: 1.11e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918   1 MARIVY-DGKFHCGGSLLTKDYVLSAAHCVKKLRKSKIRVIFGDHDQEiTSESQAIQRAVTAVIKHKSFDPDTYNNDIAL 79
Cdd:cd00190  15 QVSLQYtGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLS-SNEGGGQVIKVKKVIVHPNYNPSTYDNDIAL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918  80 LRLRKPISFSKIIKPICLPRYNYD-PAGRIGTVVGWGRTSEGGELPSIVNQVKVPIMSITECRNQRYKSTRITSSMLCAG 158
Cdd:cd00190  94 LKLKRPVTLSDNVRPICLPSSGYNlPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYSYGGTITDNMLCAG 173
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24649918 159 --RPSMDSCQGDSGGPLLLSNGVKYFIVGIVSWGVGCGREGYPGVYSRVSKFIPWIKSN 215
Cdd:cd00190 174 glEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-212 4.54e-87

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: 256.84  E-value: 4.54e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918      1 MARIVY-DGKFHCGGSLLTKDYVLSAAHCVKKLRKSKIRVIFGDHDQEITSESQAIQraVTAVIKHKSFDPDTYNNDIAL 79
Cdd:smart00020  16 QVSLQYgGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVIK--VSKVIIHPNYNPSTYDNDIAL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918     80 LRLRKPISFSKIIKPICLPRYNYD-PAGRIGTVVGWGRTSEG-GELPSIVNQVKVPIMSITECRNQRYKSTRITSSMLCA 157
Cdd:smart00020  94 LKLKEPVTLSDNVRPICLPSSNYNvPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRAYSGGGAITDNMLCA 173
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24649918    158 G--RPSMDSCQGDSGGPLLLSNGVkYFIVGIVSWGVGCGREGYPGVYSRVSKFIPWI 212
Cdd:smart00020 174 GglEGGKDACQGDSGGPLVCNDGR-WVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-214 4.57e-69

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 212.20  E-value: 4.57e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918   1 MARIVYDG---KFHCGGSLLTKDYVLSAAHCVKKLRKSKIRVIFGDHDQeitSESQAIQRAVTAVIKHKSFDPDTYNNDI 77
Cdd:COG5640  45 MVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDL---STSGGTVVKVARIVVHPDYDPATPGNDI 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918  78 ALLRLRKPISFskiIKPICLPRYNYDPA-GRIGTVVGWGRTSEG-GELPSIVNQVKVPIMSITECRNQrykSTRITSSML 155
Cdd:COG5640 122 ALLKLATPVPG---VAPAPLATSADAAApGTPATVAGWGRTSEGpGSQSGTLRKADVPVVSDATCAAY---GGFDGGTML 195
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24649918 156 CAGRPS--MDSCQGDSGGPLLLSNGVKYFIVGIVSWGVGCGREGYPGVYSRVSKFIPWIKS 214
Cdd:COG5640 196 CAGYPEggKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKS 256
Trypsin pfam00089
Trypsin;
1-212 9.35e-66

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 202.29  E-value: 9.35e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918     1 MARIVYDGKFH-CGGSLLTKDYVLSAAHCVKklRKSKIRVIFGDHDQEITSESQAIqRAVTAVIKHKSFDPDTYNNDIAL 79
Cdd:pfam00089  15 QVSLQLSSGKHfCGGSLISENWVLTAAHCVS--GASDVKVVLGAHNIVLREGGEQK-FDVEKIIVHPNYNPDTLDNDIAL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918    80 LRLRKPISFSKIIKPICLPRYNYD-PAGRIGTVVGWGRTSEGGeLPSIVNQVKVPIMSITECRnqRYKSTRITSSMLCAG 158
Cdd:pfam00089  92 LKLESPVTLGDTVRPICLPDASSDlPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCR--SAYGGTVTDTMICAG 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 24649918   159 RPSMDSCQGDSGGPLLLSNGvkyFIVGIVSWGVGCGREGYPGVYSRVSKFIPWI 212
Cdd:pfam00089 169 AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
2-192 7.56e-13

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 64.70  E-value: 7.56e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918   2 ARIVYDG-KFHCGGSLLTKDYVLSAAHCVK----KLRKSKIRVIFGDHDQEITSESqaiqraVTAVIKHKSFDPDT-YNN 75
Cdd:COG3591   3 GRLETDGgGGVCTGTLIGPNLVLTAGHCVYdgagGGWATNIVFVPGYNGGPYGTAT------ATRFRVPPGWVASGdAGY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918  76 DIALLRLRKPISFSKIIKPIclpRYNYDPA-GRIGTVVGWgrtseGGELPSIVNQVkvpimsiTECRNQRYKSTRItsSM 154
Cdd:COG3591  77 DYALLRLDEPLGDTTGWLGL---AFNDAPLaGEPVTIIGY-----PGDRPKDLSLD-------CSGRVTGVQGNRL--SY 139
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 24649918 155 LCagrpsmDSCQGDSGGPLLLSNGVKYFIVGIVSWGVG 192
Cdd:COG3591 140 DC------DTTGGSSGSPVLDDSDGGGRVVGVHSAGGA 171
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
21-186 4.73e-03

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 36.25  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918    21 YVLSAAHCVKK---LRKSKIRVIFGDHdqeitsesqaiqRAVTAVIKHksFDPDTynnDIALLRLRKPISfskiikPICL 97
Cdd:pfam13365  11 LVLTNAHVVDDaeeAAVELVSVVLADG------------REYPATVVA--RDPDL---DLALLRVSGDGR------GLPP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649918    98 PRYNYDPAGRIGT---VVGWGRtseGGELPSIVNQVkvpIMSITECRNQRYKSTRITSSMLCAGrpsmdscqGDSGGPLL 174
Cdd:pfam13365  68 LPLGDSEPLVGGErvyAVGYPL---GGEKLSLSEGI---VSGVDEGRDGGDDGRVIQTDAALSP--------GSSGGPVF 133
                         170
                  ....*....|..
gi 24649918   175 LSNGVkyfIVGI 186
Cdd:pfam13365 134 DADGR---VVGI 142
 
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