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Conserved domains on  [gi|386769824|ref|NP_001097175|]
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uncharacterized protein Dmel_CG34171, isoform B [Drosophila melanogaster]

Protein Classification

serine protease family protein( domain architecture ID 229414)

trypsin-like serine protease family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
38-263 8.69e-33

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.


The actual alignment was detected with superfamily member cd00190:

Pssm-ID: 473915 [Multi-domain]  Cd Length: 232  Bit Score: 120.46  E-value: 8.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824  38 YLVSLRTRkyihtpGDNHFCTGVILTNRHVLTSAHCITDKNgvmmsPKRIVVALCASLFKTPESEEFVVDIHNMIIHPYY 117
Cdd:cd00190   14 WQVSLQYT------GGRHFCGGSLISPRWVLTAAHCVYSSA-----PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824 118 HRNQ-HNDIAIIKLKRYVKLdGHHLAPVVL--GNSSLEVGNDCKTIGgiFGvrRQRFGSFHSMLL--VNVELRPFDEClk 192
Cdd:cd00190   83 NPSTyDNDIALLKLKRPVTL-SDNVRPICLpsSGYNLPAGTTCTVSG--WG--RTSEGGPLPDVLqeVNVPIVSNAEC-- 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769824 193 vKKSLMAARPENEDLICVKSTEKQM--CTTDFGGPLFCD----GQLYGIALGSINCSSPD-PVFFSDVSFYNSWVTKI 263
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 ...
38-263 8.69e-33

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: 120.46  E-value: 8.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824  38 YLVSLRTRkyihtpGDNHFCTGVILTNRHVLTSAHCITDKNgvmmsPKRIVVALCASLFKTPESEEFVVDIHNMIIHPYY 117
Cdd:cd00190   14 WQVSLQYT------GGRHFCGGSLISPRWVLTAAHCVYSSA-----PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824 118 HRNQ-HNDIAIIKLKRYVKLdGHHLAPVVL--GNSSLEVGNDCKTIGgiFGvrRQRFGSFHSMLL--VNVELRPFDEClk 192
Cdd:cd00190   83 NPSTyDNDIALLKLKRPVTL-SDNVRPICLpsSGYNLPAGTTCTVSG--WG--RTSEGGPLPDVLqeVNVPIVSNAEC-- 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769824 193 vKKSLMAARPENEDLICVKSTEKQM--CTTDFGGPLFCD----GQLYGIALGSINCSSPD-PVFFSDVSFYNSWVTKI 263
Cdd:cd00190  156 -KRAYSYGGTITDNMLCAGGLEGGKdaCQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
38-260 7.79e-31

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: 115.08  E-value: 7.79e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824    38 YLVSLRTRkyihtpGDNHFCTGVILTNRHVLTSAHCITDKNgvmmsPKRIVVALcASLFKTPESEEFVVDIHNMIIHP-Y 116
Cdd:smart00020  15 WQVSLQYG------GGRHFCGGSLISPRWVLTAAHCVRGSD-----PSNIRVRL-GSHDLSSGEEGQVIKVSKVIIHPnY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824   117 YHRNQHNDIAIIKLKRYVKLdGHHLAPVVL--GNSSLEVGNDCKTIGgiFGVRRQRFGSFHSMLL-VNVELRPFDECLKV 193
Cdd:smart00020  83 NPSTYDNDIALLKLKEPVTL-SDNVRPICLpsSNYNVPAGTTCTVSG--WGRTSEGAGSLPDTLQeVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769824   194 KKslmAARPENEDLICVKSTEKQM--CTTDFGGPLFCD---GQLYGIALGSINCSSPD-PVFFSDVSFYNSWV 260
Cdd:smart00020 160 YS---GGGAITDNMLCAGGLEGGKdaCQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
29-260 1.94e-30

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 113.69  E-value: 1.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824   29 EPTYSHLSSYLVSLRTRkyihtpGDNHFCTGVILTNRHVLTSAHCITDkngvmmsPKRIVVALCASLFKTPESEEFVVDI 108
Cdd:pfam00089   5 DEAQPGSFPWQVSLQLS------SGKHFCGGSLISENWVLTAAHCVSG-------ASDVKVVLGAHNIVLREGGEQKFDV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824  109 HNMIIHPYY-HRNQHNDIAIIKLKRYVKLdGHHLAPVVLG--NSSLEVGNDCKTIGgiFGvRRQRFGSFHSMLLVNVELR 185
Cdd:pfam00089  72 EKIIVHPNYnPDTLDNDIALLKLESPVTL-GDTVRPICLPdaSSDLPVGTTCTVSG--WG-NTKTLGPSDTLQEVTVPVV 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769824  186 PFDECLKVKKslmaaRPENEDLICVKSTEKQMCTTDFGGPLFC-DGQLYGIALGSINCSSPD-PVFFSDVSFYNSWV 260
Cdd:pfam00089 148 SRETCRSAYG-----GTVTDTMICAGAGGKDACQGDSGGPLVCsDGELIGIVSWGYGCASGNyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
53-268 8.74e-21

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 88.94  E-value: 8.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824  53 DNHFCTGVILTNRHVLTSAHCITDKngvmmSPKRI-VVALCASLFKTPESEEFVVDIhnmIIHPYYHRNQ-HNDIAIIKL 130
Cdd:COG5640   55 SGQFCGGTLIAPRWVLTAAHCVDGD-----GPSDLrVVIGSTDLSTSGGTVVKVARI---VVHPDYDPATpGNDIALLKL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824 131 KRYVKLdghhLAPVVLGNSSL--EVGNDCKTIGgiFGVRRQRFGSFHSMLL-VNVELRPFDEClkvkKSLMAARPENEdl 207
Cdd:COG5640  127 ATPVPG----VAPAPLATSADaaAPGTPATVAG--WGRTSEGPGSQSGTLRkADVPVVSDATC----AAYGGFDGGTM-- 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769824 208 ICVKSTE--KQMCTTDFGGPLF----CDGQLYGIA-LGSINCSSPDPVFFSDVSFYNSWVTKIISEAV 268
Cdd:COG5640  195 LCAGYPEggKDACQGDSGGPLVvkdgGGWVLVGVVsWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
38-263 8.69e-33

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: 120.46  E-value: 8.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824  38 YLVSLRTRkyihtpGDNHFCTGVILTNRHVLTSAHCITDKNgvmmsPKRIVVALCASLFKTPESEEFVVDIHNMIIHPYY 117
Cdd:cd00190   14 WQVSLQYT------GGRHFCGGSLISPRWVLTAAHCVYSSA-----PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824 118 HRNQ-HNDIAIIKLKRYVKLdGHHLAPVVL--GNSSLEVGNDCKTIGgiFGvrRQRFGSFHSMLL--VNVELRPFDEClk 192
Cdd:cd00190   83 NPSTyDNDIALLKLKRPVTL-SDNVRPICLpsSGYNLPAGTTCTVSG--WG--RTSEGGPLPDVLqeVNVPIVSNAEC-- 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769824 193 vKKSLMAARPENEDLICVKSTEKQM--CTTDFGGPLFCD----GQLYGIALGSINCSSPD-PVFFSDVSFYNSWVTKI 263
Cdd:cd00190  156 -KRAYSYGGTITDNMLCAGGLEGGKdaCQGDSGGPLVCNdngrGVLVGIVSWGSGCARPNyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
38-260 7.79e-31

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: 115.08  E-value: 7.79e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824    38 YLVSLRTRkyihtpGDNHFCTGVILTNRHVLTSAHCITDKNgvmmsPKRIVVALcASLFKTPESEEFVVDIHNMIIHP-Y 116
Cdd:smart00020  15 WQVSLQYG------GGRHFCGGSLISPRWVLTAAHCVRGSD-----PSNIRVRL-GSHDLSSGEEGQVIKVSKVIIHPnY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824   117 YHRNQHNDIAIIKLKRYVKLdGHHLAPVVL--GNSSLEVGNDCKTIGgiFGVRRQRFGSFHSMLL-VNVELRPFDECLKV 193
Cdd:smart00020  83 NPSTYDNDIALLKLKEPVTL-SDNVRPICLpsSNYNVPAGTTCTVSG--WGRTSEGAGSLPDTLQeVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769824   194 KKslmAARPENEDLICVKSTEKQM--CTTDFGGPLFCD---GQLYGIALGSINCSSPD-PVFFSDVSFYNSWV 260
Cdd:smart00020 160 YS---GGGAITDNMLCAGGLEGGKdaCQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
29-260 1.94e-30

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 113.69  E-value: 1.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824   29 EPTYSHLSSYLVSLRTRkyihtpGDNHFCTGVILTNRHVLTSAHCITDkngvmmsPKRIVVALCASLFKTPESEEFVVDI 108
Cdd:pfam00089   5 DEAQPGSFPWQVSLQLS------SGKHFCGGSLISENWVLTAAHCVSG-------ASDVKVVLGAHNIVLREGGEQKFDV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824  109 HNMIIHPYY-HRNQHNDIAIIKLKRYVKLdGHHLAPVVLG--NSSLEVGNDCKTIGgiFGvRRQRFGSFHSMLLVNVELR 185
Cdd:pfam00089  72 EKIIVHPNYnPDTLDNDIALLKLESPVTL-GDTVRPICLPdaSSDLPVGTTCTVSG--WG-NTKTLGPSDTLQEVTVPVV 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769824  186 PFDECLKVKKslmaaRPENEDLICVKSTEKQMCTTDFGGPLFC-DGQLYGIALGSINCSSPD-PVFFSDVSFYNSWV 260
Cdd:pfam00089 148 SRETCRSAYG-----GTVTDTMICAGAGGKDACQGDSGGPLVCsDGELIGIVSWGYGCASGNyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
53-268 8.74e-21

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 88.94  E-value: 8.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824  53 DNHFCTGVILTNRHVLTSAHCITDKngvmmSPKRI-VVALCASLFKTPESEEFVVDIhnmIIHPYYHRNQ-HNDIAIIKL 130
Cdd:COG5640   55 SGQFCGGTLIAPRWVLTAAHCVDGD-----GPSDLrVVIGSTDLSTSGGTVVKVARI---VVHPDYDPATpGNDIALLKL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824 131 KRYVKLdghhLAPVVLGNSSL--EVGNDCKTIGgiFGVRRQRFGSFHSMLL-VNVELRPFDEClkvkKSLMAARPENEdl 207
Cdd:COG5640  127 ATPVPG----VAPAPLATSADaaAPGTPATVAG--WGRTSEGPGSQSGTLRkADVPVVSDATC----AAYGGFDGGTM-- 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769824 208 ICVKSTE--KQMCTTDFGGPLF----CDGQLYGIA-LGSINCSSPDPVFFSDVSFYNSWVTKIISEAV 268
Cdd:COG5640  195 LCAGYPEggKDACQGDSGGPLVvkdgGGWVLVGVVsWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
50-132 2.27e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 44.28  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824  50 TPGDNHFCTGVILTNRHVLTSAHCITD-KNGVMMSPKRIVVALCASLFKTPESEEFVVdihnmiiHPYYHR--NQHNDIA 126
Cdd:COG3591    7 TDGGGGVCTGTLIGPNLVLTAGHCVYDgAGGGWATNIVFVPGYNGGPYGTATATRFRV-------PPGWVAsgDAGYDYA 79

                 ....*.
gi 386769824 127 IIKLKR 132
Cdd:COG3591   80 LLRLDE 85
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
58-161 1.98e-03

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 37.79  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769824   58 TGVILTNRHVLTSAHcitdkngvmmspkriVVALCASLFKTPESEEFVVDIhnmiihpyYHRNQHNDIAIIKlkryVKLD 137
Cdd:pfam13365   9 DGLVLTNAHVVDDAE---------------EAAVELVSVVLADGREYPATV--------VARDPDLDLALLR----VSGD 61
                          90       100
                  ....*....|....*....|....*
gi 386769824  138 GHHLAPVVLGNSS-LEVGNDCKTIG 161
Cdd:pfam13365  62 GRGLPPLPLGDSEpLVGGERVYAVG 86
 
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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