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Conserved domains on  [gi|24658948|ref|NP_648011|]
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uncharacterized protein Dmel_CG6462 [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

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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 ...
77-314 2.08e-67

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: 210.60  E-value: 2.08e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948  77 IAGGELATRGMFPYQVGLVIQLSGadlVKCGGSLITLQFVLTAAHCLTDAIAA--KIYTGATVFADVEDSVEELQVThrD 154
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSAPSnyTVRLGSHDLSSNEGGGQVIKVK--K 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948 155 FIIYPDYLGFGGYSDLALIRLPRKVRTSEQVQPIELAGEfmHQNFLVGKVVTLSGWGYLGDsTDKRTRLLQYLDAEVIDQ 234
Cdd:cd00190  76 VIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSS--GYNLPAGTTCTVSGWGRTSE-GGPLPDVLQEVNVPIVSN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948 235 ERCICYFLPGLVSQRRHLCTDGSN-GRGACNGDSGGPVVYHWRNVSYLIGVTSFGSaeGCEVGG-PTVYTRITAYLPWIR 312
Cdd:cd00190 153 AECKRAYSYGGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS--GCARPNyPGVYTRVSSYLDWIQ 230

                ..
gi 24658948 313 QQ 314
Cdd:cd00190 231 KT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
77-314 2.08e-67

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: 210.60  E-value: 2.08e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948  77 IAGGELATRGMFPYQVGLVIQLSGadlVKCGGSLITLQFVLTAAHCLTDAIAA--KIYTGATVFADVEDSVEELQVThrD 154
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSAPSnyTVRLGSHDLSSNEGGGQVIKVK--K 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948 155 FIIYPDYLGFGGYSDLALIRLPRKVRTSEQVQPIELAGEfmHQNFLVGKVVTLSGWGYLGDsTDKRTRLLQYLDAEVIDQ 234
Cdd:cd00190  76 VIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSS--GYNLPAGTTCTVSGWGRTSE-GGPLPDVLQEVNVPIVSN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948 235 ERCICYFLPGLVSQRRHLCTDGSN-GRGACNGDSGGPVVYHWRNVSYLIGVTSFGSaeGCEVGG-PTVYTRITAYLPWIR 312
Cdd:cd00190 153 AECKRAYSYGGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS--GCARPNyPGVYTRVSSYLDWIQ 230

                ..
gi 24658948 313 QQ 314
Cdd:cd00190 231 KT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
76-311 8.10e-64

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: 201.37  E-value: 8.10e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948     76 RIAGGELATRGMFPYQVGLVIQLSGadlVKCGGSLITLQFVLTAAHCLTDAIAA--KIYTGATvFADVEDSVEELQVThr 153
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR---HFCGGSLISPRWVLTAAHCVRGSDPSniRVRLGSH-DLSSGEEGQVIKVS-- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948    154 DFIIYPDYLGFGGYSDLALIRLPRKVRTSEQVQPIELAGEFmhQNFLVGKVVTLSGWGYLGDSTDKRTRLLQYLDAEVID 233
Cdd:smart00020  75 KVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN--YNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948    234 QERCICYFLPGLVSQRRHLCT-DGSNGRGACNGDSGGPVVYHwRNVSYLIGVTSFGSaeGCEVGG-PTVYTRITAYLPWI 311
Cdd:smart00020 153 NATCRRAYSGGGAITDNMLCAgGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGS--GCARPGkPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
67-316 6.07e-55

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 179.85  E-value: 6.07e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948  67 GNQTAAVRTRIAGGELATRGMFPYQVGLVIQlSGADLVKCGGSLITLQFVLTAAHCLTDAIAAKIytgaTVFADVEDSVE 146
Cdd:COG5640  21 AAPAADAAPAIVGGTPATVGEYPWMVALQSS-NGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDL----RVVIGSTDLST 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948 147 ELQVTHR--DFIIYPDYLGFGGYSDLALIRLPRKVRTseqVQPIELAGEFMHQNflVGKVVTLSGWGYLGDSTDKRTRLL 224
Cdd:COG5640  96 SGGTVVKvaRIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAA--PGTPATVAGWGRTSEGPGSQSGTL 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948 225 QYLDAEVIDQERCICYflPGLVSQRrHLCTDGSNG-RGACNGDSGGPVVYHWRNVSYLIGVTSFGSAeGCEVGGPTVYTR 303
Cdd:COG5640 171 RKADVPVVSDATCAAY--GGFDGGT-MLCAGYPEGgKDACQGDSGGPLVVKDGGGWVLVGVVSWGGG-PCAAGYPGVYTR 246
                       250
                ....*....|...
gi 24658948 304 ITAYLPWIRQQTA 316
Cdd:COG5640 247 VSAYRDWIKSTAG 259
Trypsin pfam00089
Trypsin;
77-311 1.16e-53

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 174.94  E-value: 1.16e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948    77 IAGGELATRGMFPYQVGLviQLSGADLVkCGGSLITLQFVLTAAHCLTDAIAAKIYTGATVFADVEDSVEELQVthRDFI 156
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSL--QLSSGKHF-CGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDV--EKII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948   157 IYPDYLGFGGYSDLALIRLPRKVRTSEQVQPIELAGEFmhQNFLVGKVVTLSGWGYlgDSTDKRTRLLQYLDAEVIDQER 236
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDAS--SDLPVGTTCTVSGWGN--TKTLGPSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24658948   237 CICYFlPGLVSQrRHLCTDGsNGRGACNGDSGGPVVyhwRNVSYLIGVTSFGsaEGCEVGG-PTVYTRITAYLPWI 311
Cdd:pfam00089 152 CRSAY-GGTVTD-TMICAGA-GGKDACQGDSGGPLV---CSDGELIGIVSWG--YGCASGNyPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
77-314 2.08e-67

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: 210.60  E-value: 2.08e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948  77 IAGGELATRGMFPYQVGLVIQLSGadlVKCGGSLITLQFVLTAAHCLTDAIAA--KIYTGATVFADVEDSVEELQVThrD 154
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSSAPSnyTVRLGSHDLSSNEGGGQVIKVK--K 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948 155 FIIYPDYLGFGGYSDLALIRLPRKVRTSEQVQPIELAGEfmHQNFLVGKVVTLSGWGYLGDsTDKRTRLLQYLDAEVIDQ 234
Cdd:cd00190  76 VIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSS--GYNLPAGTTCTVSGWGRTSE-GGPLPDVLQEVNVPIVSN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948 235 ERCICYFLPGLVSQRRHLCTDGSN-GRGACNGDSGGPVVYHWRNVSYLIGVTSFGSaeGCEVGG-PTVYTRITAYLPWIR 312
Cdd:cd00190 153 AECKRAYSYGGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIVSWGS--GCARPNyPGVYTRVSSYLDWIQ 230

                ..
gi 24658948 313 QQ 314
Cdd:cd00190 231 KT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
76-311 8.10e-64

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: 201.37  E-value: 8.10e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948     76 RIAGGELATRGMFPYQVGLVIQLSGadlVKCGGSLITLQFVLTAAHCLTDAIAA--KIYTGATvFADVEDSVEELQVThr 153
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR---HFCGGSLISPRWVLTAAHCVRGSDPSniRVRLGSH-DLSSGEEGQVIKVS-- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948    154 DFIIYPDYLGFGGYSDLALIRLPRKVRTSEQVQPIELAGEFmhQNFLVGKVVTLSGWGYLGDSTDKRTRLLQYLDAEVID 233
Cdd:smart00020  75 KVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN--YNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948    234 QERCICYFLPGLVSQRRHLCT-DGSNGRGACNGDSGGPVVYHwRNVSYLIGVTSFGSaeGCEVGG-PTVYTRITAYLPWI 311
Cdd:smart00020 153 NATCRRAYSGGGAITDNMLCAgGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGS--GCARPGkPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
67-316 6.07e-55

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 179.85  E-value: 6.07e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948  67 GNQTAAVRTRIAGGELATRGMFPYQVGLVIQlSGADLVKCGGSLITLQFVLTAAHCLTDAIAAKIytgaTVFADVEDSVE 146
Cdd:COG5640  21 AAPAADAAPAIVGGTPATVGEYPWMVALQSS-NGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDL----RVVIGSTDLST 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948 147 ELQVTHR--DFIIYPDYLGFGGYSDLALIRLPRKVRTseqVQPIELAGEFMHQNflVGKVVTLSGWGYLGDSTDKRTRLL 224
Cdd:COG5640  96 SGGTVVKvaRIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAA--PGTPATVAGWGRTSEGPGSQSGTL 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948 225 QYLDAEVIDQERCICYflPGLVSQRrHLCTDGSNG-RGACNGDSGGPVVYHWRNVSYLIGVTSFGSAeGCEVGGPTVYTR 303
Cdd:COG5640 171 RKADVPVVSDATCAAY--GGFDGGT-MLCAGYPEGgKDACQGDSGGPLVVKDGGGWVLVGVVSWGGG-PCAAGYPGVYTR 246
                       250
                ....*....|...
gi 24658948 304 ITAYLPWIRQQTA 316
Cdd:COG5640 247 VSAYRDWIKSTAG 259
Trypsin pfam00089
Trypsin;
77-311 1.16e-53

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 174.94  E-value: 1.16e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948    77 IAGGELATRGMFPYQVGLviQLSGADLVkCGGSLITLQFVLTAAHCLTDAIAAKIYTGATVFADVEDSVEELQVthRDFI 156
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSL--QLSSGKHF-CGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDV--EKII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948   157 IYPDYLGFGGYSDLALIRLPRKVRTSEQVQPIELAGEFmhQNFLVGKVVTLSGWGYlgDSTDKRTRLLQYLDAEVIDQER 236
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDAS--SDLPVGTTCTVSGWGN--TKTLGPSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24658948   237 CICYFlPGLVSQrRHLCTDGsNGRGACNGDSGGPVVyhwRNVSYLIGVTSFGsaEGCEVGG-PTVYTRITAYLPWI 311
Cdd:pfam00089 152 CRSAY-GGTVTD-TMICAGA-GGKDACQGDSGGPLV---CSDGELIGIVSWG--YGCASGNyPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
106-308 1.25e-12

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 65.47  E-value: 1.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948 106 CGGSLITLQFVLTAAHCLTDAIAAKIYTGATVFADVEDSVEElQVTHRDFIIYPDYLGFGGYS-DLALIRLPRKVrtSEQ 184
Cdd:COG3591  14 CTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGPYG-TATATRFRVPPGWVASGDAGyDYALLRLDEPL--GDT 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658948 185 VQPIELAGEfmhQNFLVGKVVTLSGWGylGDSTDKRTRllqyldaevidqeRCICYFLPGLVSQRRHLCTdgsngrgACN 264
Cdd:COG3591  91 TGWLGLAFN---DAPLAGEPVTIIGYP--GDRPKDLSL-------------DCSGRVTGVQGNRLSYDCD-------TTG 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 24658948 265 GDSGGPVVYHWRNVSYLIGVTSFGSAeGCEVGGPTVYTRITAYL 308
Cdd:COG3591 146 GSSGSPVLDDSDGGGRVVGVHSAGGA-DRANTGVRLTSAIVAAL 188
 
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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