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Conserved domains on  [gi|45550494|ref|NP_611716|]
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uncharacterized protein Dmel_CG13527, 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 ...
43-266 1.46e-44

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: 150.89  E-value: 1.46e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494  43 YVVSIRsrtpnkYFGDNHYCGGGLLSNQWVITAAHCVMGQSKIMYKarwllVVAGSpHRLRYTPGKSVCSPVSSLYVPKN 122
Cdd:cd00190  14 WQVSLQ------YTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYT-----VRLGS-HDLSSNEGGGQVIKVKKVIVHPN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494 123 FTMHNTFN-MALMKLQEKMPSNDpRIGFLHLP--KEAPKIGIRHTVLGWGRMYFGGPLAVHIYQVDVVLMDNAVCKTYFR 199
Cdd:cd00190  82 YNPSTYDNdIALLKLKRPVTLSD-NVRPICLPssGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45550494 200 HYG---DGMMCAGNNNWTIDAepCSGDIGSPLLSGK----VVVGIVAYPIGCGCTNIPSVYTDVFSGLRWIRHT 266
Cdd:cd00190 161 YGGtitDNMLCAGGLEGGKDA--CQGDSGGPLVCNDngrgVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
43-266 1.46e-44

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: 150.89  E-value: 1.46e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494  43 YVVSIRsrtpnkYFGDNHYCGGGLLSNQWVITAAHCVMGQSKIMYKarwllVVAGSpHRLRYTPGKSVCSPVSSLYVPKN 122
Cdd:cd00190  14 WQVSLQ------YTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYT-----VRLGS-HDLSSNEGGGQVIKVKKVIVHPN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494 123 FTMHNTFN-MALMKLQEKMPSNDpRIGFLHLP--KEAPKIGIRHTVLGWGRMYFGGPLAVHIYQVDVVLMDNAVCKTYFR 199
Cdd:cd00190  82 YNPSTYDNdIALLKLKRPVTLSD-NVRPICLPssGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45550494 200 HYG---DGMMCAGNNNWTIDAepCSGDIGSPLLSGK----VVVGIVAYPIGCGCTNIPSVYTDVFSGLRWIRHT 266
Cdd:cd00190 161 YGGtitDNMLCAGGLEGGKDA--CQGDSGGPLVCNDngrgVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
43-263 7.46e-42

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: 143.97  E-value: 7.46e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494     43 YVVSIRsrtpnkYFGDNHYCGGGLLSNQWVITAAHCVMGQSKIMYKarwllVVAGSPHRLRYTPGKSVcsPVSSLYVPKN 122
Cdd:smart00020  15 WQVSLQ------YGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIR-----VRLGSHDLSSGEEGQVI--KVSKVIIHPN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494    123 FTMHNTFNM-ALMKLQEKMPSNDpRIGFLHLP--KEAPKIGIRHTVLGWGRMYFG-GPLAVHIYQVDVVLMDNAVCKTYF 198
Cdd:smart00020  82 YNPSTYDNDiALLKLKEPVTLSD-NVRPICLPssNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45550494    199 RHYG---DGMMCAGNNNWTIDAepCSGDIGSPLLSGK---VVVGIVAYPIGCGCTNIPSVYTDVFSGLRWI 263
Cdd:smart00020 161 SGGGaitDNMLCAGGLEGGKDA--CQGDSGGPLVCNDgrwVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
58-267 5.23e-37

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 132.08  E-value: 5.23e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494  58 DNHYCGGGLLSNQWVITAAHCVMGQSKIMYKarwllVVAGSpHRLRYTPGKSVcsPVSSLYVPKNFTMHNTFN-MALMKL 136
Cdd:COG5640  55 SGQFCGGTLIAPRWVLTAAHCVDGDGPSDLR-----VVIGS-TDLSTSGGTVV--KVARIVVHPDYDPATPGNdIALLKL 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494 137 QEKMPSNDPrigfLHLP--KEAPKIGIRHTVLGWGRMYFG-GPLAVHIYQVDVVLMDNAVCKTYFRHYGDGMMCAGNNNW 213
Cdd:COG5640 127 ATPVPGVAP----APLAtsADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVSDATCAAYGGFDGGTMLCAGYPEG 202
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 45550494 214 TIDAepCSGDIGSPLL----SGKVVVGIVAYPIGCGCTNIPSVYTDVFSGLRWIRHTA 267
Cdd:COG5640 203 GKDA--CQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
54-263 1.79e-32

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 119.08  E-value: 1.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494    54 KYFGDNHYCGGGLLSNQWVITAAHCVMGQSKIMykarwllVVAGSpHRLRYTPGKSVCSPVSSLYVPKNFTMHNTFN-MA 132
Cdd:pfam00089  19 QLSSGKHFCGGSLISENWVLTAAHCVSGASDVK-------VVLGA-HNIVLREGGEQKFDVEKIIVHPNYNPDTLDNdIA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494   133 LMKLQEKMPSNDpRIGFLHLPKEAPKIGIRHT--VLGWGRMYFGGPlAVHIYQVDVVLMDNAVCKTYFRHY-GDGMMCAG 209
Cdd:pfam00089  91 LLKLESPVTLGD-TVRPICLPDASSDLPVGTTctVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAYGGTvTDTMICAG 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 45550494   210 nnnwTIDAEPCSGDIGSPLL-SGKVVVGIVAYPIGCGCTNIPSVYTDVFSGLRWI 263
Cdd:pfam00089 169 ----AGGKDACQGDSGGPLVcSDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
43-266 1.46e-44

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: 150.89  E-value: 1.46e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494  43 YVVSIRsrtpnkYFGDNHYCGGGLLSNQWVITAAHCVMGQSKIMYKarwllVVAGSpHRLRYTPGKSVCSPVSSLYVPKN 122
Cdd:cd00190  14 WQVSLQ------YTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYT-----VRLGS-HDLSSNEGGGQVIKVKKVIVHPN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494 123 FTMHNTFN-MALMKLQEKMPSNDpRIGFLHLP--KEAPKIGIRHTVLGWGRMYFGGPLAVHIYQVDVVLMDNAVCKTYFR 199
Cdd:cd00190  82 YNPSTYDNdIALLKLKRPVTLSD-NVRPICLPssGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45550494 200 HYG---DGMMCAGNNNWTIDAepCSGDIGSPLLSGK----VVVGIVAYPIGCGCTNIPSVYTDVFSGLRWIRHT 266
Cdd:cd00190 161 YGGtitDNMLCAGGLEGGKDA--CQGDSGGPLVCNDngrgVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
43-263 7.46e-42

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: 143.97  E-value: 7.46e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494     43 YVVSIRsrtpnkYFGDNHYCGGGLLSNQWVITAAHCVMGQSKIMYKarwllVVAGSPHRLRYTPGKSVcsPVSSLYVPKN 122
Cdd:smart00020  15 WQVSLQ------YGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIR-----VRLGSHDLSSGEEGQVI--KVSKVIIHPN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494    123 FTMHNTFNM-ALMKLQEKMPSNDpRIGFLHLP--KEAPKIGIRHTVLGWGRMYFG-GPLAVHIYQVDVVLMDNAVCKTYF 198
Cdd:smart00020  82 YNPSTYDNDiALLKLKEPVTLSD-NVRPICLPssNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45550494    199 RHYG---DGMMCAGNNNWTIDAepCSGDIGSPLLSGK---VVVGIVAYPIGCGCTNIPSVYTDVFSGLRWI 263
Cdd:smart00020 161 SGGGaitDNMLCAGGLEGGKDA--CQGDSGGPLVCNDgrwVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
58-267 5.23e-37

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 132.08  E-value: 5.23e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494  58 DNHYCGGGLLSNQWVITAAHCVMGQSKIMYKarwllVVAGSpHRLRYTPGKSVcsPVSSLYVPKNFTMHNTFN-MALMKL 136
Cdd:COG5640  55 SGQFCGGTLIAPRWVLTAAHCVDGDGPSDLR-----VVIGS-TDLSTSGGTVV--KVARIVVHPDYDPATPGNdIALLKL 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494 137 QEKMPSNDPrigfLHLP--KEAPKIGIRHTVLGWGRMYFG-GPLAVHIYQVDVVLMDNAVCKTYFRHYGDGMMCAGNNNW 213
Cdd:COG5640 127 ATPVPGVAP----APLAtsADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVSDATCAAYGGFDGGTMLCAGYPEG 202
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 45550494 214 TIDAepCSGDIGSPLL----SGKVVVGIVAYPIGCGCTNIPSVYTDVFSGLRWIRHTA 267
Cdd:COG5640 203 GKDA--CQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
54-263 1.79e-32

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 119.08  E-value: 1.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494    54 KYFGDNHYCGGGLLSNQWVITAAHCVMGQSKIMykarwllVVAGSpHRLRYTPGKSVCSPVSSLYVPKNFTMHNTFN-MA 132
Cdd:pfam00089  19 QLSSGKHFCGGSLISENWVLTAAHCVSGASDVK-------VVLGA-HNIVLREGGEQKFDVEKIIVHPNYNPDTLDNdIA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494   133 LMKLQEKMPSNDpRIGFLHLPKEAPKIGIRHT--VLGWGRMYFGGPlAVHIYQVDVVLMDNAVCKTYFRHY-GDGMMCAG 209
Cdd:pfam00089  91 LLKLESPVTLGD-TVRPICLPDASSDLPVGTTctVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAYGGTvTDTMICAG 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 45550494   210 nnnwTIDAEPCSGDIGSPLL-SGKVVVGIVAYPIGCGCTNIPSVYTDVFSGLRWI 263
Cdd:pfam00089 169 ----AGGKDACQGDSGGPLVcSDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
57-261 5.86e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 45.82  E-value: 5.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494  57 GDNHYCGGGLLSNQWVITAAHCVMGQSKIMYkARWLLVVAGsphrlrYTPGKSVCSPVSSLYVPKNFTMHNTFN--MALM 134
Cdd:COG3591   9 GGGGVCTGTLIGPNLVLTAGHCVYDGAGGGW-ATNIVFVPG------YNGGPYGTATATRFRVPPGWVASGDAGydYALL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550494 135 KLQEKMPsndPRIGFLHL-PKEAPKIGIRHTVLGWGRmyfGGPLAVHIYQVDVVLMdnavcktyfrhygdgmmcAGNNNW 213
Cdd:COG3591  82 RLDEPLG---DTTGWLGLaFNDAPLAGEPVTIIGYPG---DRPKDLSLDCSGRVTG------------------VQGNRL 137
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 45550494 214 TIDAEPCSGDIGSPLLS----GKVVVGIVAYpIGCGCTNI-PSVYTDVFSGLR 261
Cdd:COG3591 138 SYDCDTTGGSSGSPVLDdsdgGGRVVGVHSA-GGADRANTgVRLTSAIVAALR 189
 
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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