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Conserved domains on  [gi|85816275|ref|NP_995714|]
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uncharacterized protein Dmel_CG18636 [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 ...
45-278 5.00e-55

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: 179.78  E-value: 5.00e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275  45 IINGHTAKYNSSPWMVFLHSTTDMFVCGGSLITDKLVLTAAHCFI--ANQHLVARLGEYERTRSEEctgyycnFREEHMV 122
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSSNEG-------GGQVIKV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275 123 DAGFKHKLYDPNTHANDIAILRLSKSVVYRDNIRPICVVWDHRWrhyLDKIDLLTATGWGKTQ-MESDSDALQTLDIRRQ 201
Cdd:cd00190  74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN---LPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275 202 PPDVCAK--FIGQTIAGNQFCAG--NWDSNLCNGDSGGPLgaviTHKNTQRFVQVGIASYtNRNCQKAS---VFTDVLSH 274
Cdd:cd00190 151 SNAECKRaySYGGTITDNMLCAGglEGGKDACQGDSGGPL----VCNDNGRGVLVGIVSW-GSGCARPNypgVYTRVSSY 225

                ....
gi 85816275 275 AEFI 278
Cdd:cd00190 226 LDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
45-278 5.00e-55

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: 179.78  E-value: 5.00e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275  45 IINGHTAKYNSSPWMVFLHSTTDMFVCGGSLITDKLVLTAAHCFI--ANQHLVARLGEYERTRSEEctgyycnFREEHMV 122
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSSNEG-------GGQVIKV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275 123 DAGFKHKLYDPNTHANDIAILRLSKSVVYRDNIRPICVVWDHRWrhyLDKIDLLTATGWGKTQ-MESDSDALQTLDIRRQ 201
Cdd:cd00190  74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN---LPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275 202 PPDVCAK--FIGQTIAGNQFCAG--NWDSNLCNGDSGGPLgaviTHKNTQRFVQVGIASYtNRNCQKAS---VFTDVLSH 274
Cdd:cd00190 151 SNAECKRaySYGGTITDNMLCAGglEGGKDACQGDSGGPL----VCNDNGRGVLVGIVSW-GSGCARPNypgVYTRVSSY 225

                ....
gi 85816275 275 AEFI 278
Cdd:cd00190 226 LDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
44-278 2.63e-54

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: 177.87  E-value: 2.63e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275     44 RIINGHTAKYNSSPWMVFLHSTTDMFVCGGSLITDKLVLTAAHCFI--ANQHLVARLGEYERTRSEECtgyycnfrEEHM 121
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRgsDPSNIRVRLGSHDLSSGEEG--------QVIK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275    122 VDAGFKHKLYDPNTHANDIAILRLSKSVVYRDNIRPICVVWDhrwRHYLDKIDLLTATGWGKTQMESD--SDALQTLDIR 199
Cdd:smart00020  73 VSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSS---NYNVPAGTTCTVSGWGRTSEGAGslPDTLQEVNVP 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275    200 RQPPDVCAK--FIGQTIAGNQFCAG--NWDSNLCNGDSGGPLgavITHKNtqRFVQVGIASYtNRNCQKAS---VFTDVL 272
Cdd:smart00020 150 IVSNATCRRaySGGGAITDNMLCAGglEGGKDACQGDSGGPL---VCNDG--RWVLVGIVSW-GSGCARPGkpgVYTRVS 223

                   ....*.
gi 85816275    273 SHAEFI 278
Cdd:smart00020 224 SYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
44-278 1.15e-44

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 154.04  E-value: 1.15e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275  44 RIINGHTAKYNSSPWMVFLHST--TDMFVCGGSLITDKLVLTAAHCF--IANQHLVARLGEYERTRSEectgyycnfREE 119
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVdgDGPSDLRVVIGSTDLSTSG---------GTV 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275 120 HMVDAGFKHKLYDPNTHANDIAILRLSKSVvyrDNIRPICVVwdhRWRHYLDKIDLLTATGWGKTQMESD--SDALQTLD 197
Cdd:COG5640 101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLA---TSADAAAPGTPATVAGWGRTSEGPGsqSGTLRKAD 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275 198 IRRQPPDVCAKFiGQTIAGNQFCAGNWDSNL--CNGDSGGPLgaviTHKNTQRFVQVGIASYTNRNC--QKASVFTDVLS 273
Cdd:COG5640 175 VPVVSDATCAAY-GGFDGGTMLCAGYPEGGKdaCQGDSGGPL----VVKDGGGWVLVGVVSWGGGPCaaGYPGVYTRVSA 249

                ....*
gi 85816275 274 HAEFI 278
Cdd:COG5640 250 YRDWI 254
Trypsin pfam00089
Trypsin;
45-278 2.75e-44

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 151.83  E-value: 2.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275    45 IINGHTAKYNSSPWMVFLHSTTDMFVCGGSLITDKLVLTAAHCFIANQHLVARLGEYERTRSEECTGYYcnfreehMVDA 124
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKF-------DVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275   125 GFKHKLYDPNTHANDIAILRLSKSVVYRDNIRPICvvwdhrWRHYLDKI---DLLTATGWGKTQMESDSDALQTLDIRRQ 201
Cdd:pfam00089  74 IIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPIC------LPDASSDLpvgTTCTVSGWGNTKTLGPSDTLQEVTVPVV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275   202 PPDVCAKFIGQTIAGNQFCAGNWDSNLCNGDSGGPLgavITHKNTqrfvQVGIASYtNRNCQKA---SVFTDVLSHAEFI 278
Cdd:pfam00089 148 SRETCRSAYGGTVTDTMICAGAGGKDACQGDSGGPL---VCSDGE----LIGIVSW-GYGCASGnypGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
45-278 5.00e-55

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: 179.78  E-value: 5.00e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275  45 IINGHTAKYNSSPWMVFLHSTTDMFVCGGSLITDKLVLTAAHCFI--ANQHLVARLGEYERTRSEEctgyycnFREEHMV 122
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSSNEG-------GGQVIKV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275 123 DAGFKHKLYDPNTHANDIAILRLSKSVVYRDNIRPICVVWDHRWrhyLDKIDLLTATGWGKTQ-MESDSDALQTLDIRRQ 201
Cdd:cd00190  74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYN---LPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275 202 PPDVCAK--FIGQTIAGNQFCAG--NWDSNLCNGDSGGPLgaviTHKNTQRFVQVGIASYtNRNCQKAS---VFTDVLSH 274
Cdd:cd00190 151 SNAECKRaySYGGTITDNMLCAGglEGGKDACQGDSGGPL----VCNDNGRGVLVGIVSW-GSGCARPNypgVYTRVSSY 225

                ....
gi 85816275 275 AEFI 278
Cdd:cd00190 226 LDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
44-278 2.63e-54

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: 177.87  E-value: 2.63e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275     44 RIINGHTAKYNSSPWMVFLHSTTDMFVCGGSLITDKLVLTAAHCFI--ANQHLVARLGEYERTRSEECtgyycnfrEEHM 121
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRgsDPSNIRVRLGSHDLSSGEEG--------QVIK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275    122 VDAGFKHKLYDPNTHANDIAILRLSKSVVYRDNIRPICVVWDhrwRHYLDKIDLLTATGWGKTQMESD--SDALQTLDIR 199
Cdd:smart00020  73 VSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSS---NYNVPAGTTCTVSGWGRTSEGAGslPDTLQEVNVP 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275    200 RQPPDVCAK--FIGQTIAGNQFCAG--NWDSNLCNGDSGGPLgavITHKNtqRFVQVGIASYtNRNCQKAS---VFTDVL 272
Cdd:smart00020 150 IVSNATCRRaySGGGAITDNMLCAGglEGGKDACQGDSGGPL---VCNDG--RWVLVGIVSW-GSGCARPGkpgVYTRVS 223

                   ....*.
gi 85816275    273 SHAEFI 278
Cdd:smart00020 224 SYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
44-278 1.15e-44

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 154.04  E-value: 1.15e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275  44 RIINGHTAKYNSSPWMVFLHST--TDMFVCGGSLITDKLVLTAAHCF--IANQHLVARLGEYERTRSEectgyycnfREE 119
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVdgDGPSDLRVVIGSTDLSTSG---------GTV 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275 120 HMVDAGFKHKLYDPNTHANDIAILRLSKSVvyrDNIRPICVVwdhRWRHYLDKIDLLTATGWGKTQMESD--SDALQTLD 197
Cdd:COG5640 101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLA---TSADAAAPGTPATVAGWGRTSEGPGsqSGTLRKAD 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275 198 IRRQPPDVCAKFiGQTIAGNQFCAGNWDSNL--CNGDSGGPLgaviTHKNTQRFVQVGIASYTNRNC--QKASVFTDVLS 273
Cdd:COG5640 175 VPVVSDATCAAY-GGFDGGTMLCAGYPEGGKdaCQGDSGGPL----VVKDGGGWVLVGVVSWGGGPCaaGYPGVYTRVSA 249

                ....*
gi 85816275 274 HAEFI 278
Cdd:COG5640 250 YRDWI 254
Trypsin pfam00089
Trypsin;
45-278 2.75e-44

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 151.83  E-value: 2.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275    45 IINGHTAKYNSSPWMVFLHSTTDMFVCGGSLITDKLVLTAAHCFIANQHLVARLGEYERTRSEECTGYYcnfreehMVDA 124
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKF-------DVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275   125 GFKHKLYDPNTHANDIAILRLSKSVVYRDNIRPICvvwdhrWRHYLDKI---DLLTATGWGKTQMESDSDALQTLDIRRQ 201
Cdd:pfam00089  74 IIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPIC------LPDASSDLpvgTTCTVSGWGNTKTLGPSDTLQEVTVPVV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85816275   202 PPDVCAKFIGQTIAGNQFCAGNWDSNLCNGDSGGPLgavITHKNTqrfvQVGIASYtNRNCQKA---SVFTDVLSHAEFI 278
Cdd:pfam00089 148 SRETCRSAYGGTVTDTMICAGAGGKDACQGDSGGPL---VCSDGE----LIGIVSW-GYGCASGnypGVYTPVSSYLDWI 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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