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Conserved domains on  [gi|281364084|ref|NP_001163264|]
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uncharacterized protein Dmel_CG30414, 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

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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 ...
41-290 9.72e-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: 177.47  E-value: 9.72e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084  41 ITGG--ADAGLFsnPWMVKV---LGEKLCGGSLITSRFVLTAAHCIVSthmrvrlgeyktrfpgkdcsrCVPKSYklrRI 115
Cdd:cd00190    1 IVGGseAKIGSF--PWQVSLqytGGRHFCGGSLISPRWVLTAAHCVYS---------------------SAPSNY---TV 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084 116 RLGEYDTRFPGkdccvPKSYELAVDRKILHADYNLN-LDNDIGLLRMKSFVQYSDYVRPICL------LVEGHMAEspif 188
Cdd:cd00190   55 RLGSHDLSSNE-----GGGQVIKVKKVIVHPNYNPStYDNDIALLKLKRPVTLSDNVRPICLpssgynLPAGTTCT---- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084 189 nITGWGVTND-GTPSRRLQRATVYNTDLHFCRSKFTKQ--VDESQICAAGTNS--DACHGDSGGPLSAQVPfaGSWltFQ 263
Cdd:cd00190  126 -VSGWGRTSEgGPLPDVLQEVNVPIVSNAECKRAYSYGgtITDNMLCAGGLEGgkDACQGDSGGPLVCNDN--GRG--VL 200
                        250       260
                 ....*....|....*....|....*....
gi 281364084 264 YGLVSYGS--AACHSFSVYTNVTHHRDWI 290
Cdd:cd00190  201 VGIVSWGSgcARPNYPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
41-290 9.72e-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: 177.47  E-value: 9.72e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084  41 ITGG--ADAGLFsnPWMVKV---LGEKLCGGSLITSRFVLTAAHCIVSthmrvrlgeyktrfpgkdcsrCVPKSYklrRI 115
Cdd:cd00190    1 IVGGseAKIGSF--PWQVSLqytGGRHFCGGSLISPRWVLTAAHCVYS---------------------SAPSNY---TV 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084 116 RLGEYDTRFPGkdccvPKSYELAVDRKILHADYNLN-LDNDIGLLRMKSFVQYSDYVRPICL------LVEGHMAEspif 188
Cdd:cd00190   55 RLGSHDLSSNE-----GGGQVIKVKKVIVHPNYNPStYDNDIALLKLKRPVTLSDNVRPICLpssgynLPAGTTCT---- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084 189 nITGWGVTND-GTPSRRLQRATVYNTDLHFCRSKFTKQ--VDESQICAAGTNS--DACHGDSGGPLSAQVPfaGSWltFQ 263
Cdd:cd00190  126 -VSGWGRTSEgGPLPDVLQEVNVPIVSNAECKRAYSYGgtITDNMLCAGGLEGgkDACQGDSGGPLVCNDN--GRG--VL 200
                        250       260
                 ....*....|....*....|....*....
gi 281364084 264 YGLVSYGS--AACHSFSVYTNVTHHRDWI 290
Cdd:cd00190  201 VGIVSWGSgcARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
41-290 2.12e-53

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: 174.02  E-value: 2.12e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084    41 ITGGADAGLFSNPWMVKVL---GEKLCGGSLITSRFVLTAAHCIVSTH---MRVRLGEYktrfpgkdcsrcvpksyklrR 114
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQyggGRHFCGGSLISPRWVLTAAHCVRGSDpsnIRVRLGSH--------------------D 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084   115 IRLGEYDTRFPgkdccvpksyelaVDRKILHADYNL-NLDNDIGLLRMKSFVQYSDYVRPICL------LVEGHMAEspi 187
Cdd:smart00020  62 LSSGEEGQVIK-------------VSKVIIHPNYNPsTYDNDIALLKLKEPVTLSDNVRPICLpssnynVPAGTTCT--- 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084   188 fnITGWGVT--NDGTPSRRLQRATVYNTDLHFCRSKF--TKQVDESQICAAGTN--SDACHGDSGGPLSAQVpfaGSWlt 261
Cdd:smart00020 126 --VSGWGRTseGAGSLPDTLQEVNVPIVSNATCRRAYsgGGAITDNMLCAGGLEggKDACQGDSGGPLVCND---GRW-- 198
                          250       260       270
                   ....*....|....*....|....*....|.
gi 281364084   262 FQYGLVSYGS--AACHSFSVYTNVTHHRDWI 290
Cdd:smart00020 199 VLVGIVSWGSgcARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-294 3.29e-45

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 154.04  E-value: 3.29e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084   1 MK--FIAAGLALLVCSIQLgegapghlldSSCGTTKPEfiPMITGGADAGLFSNPWMVKVLGEK-----LCGGSLITSRF 73
Cdd:COG5640    1 MRrrRLLAALAAAALALAL----------AAAPAADAA--PAIVGGTPATVGEYPWMVALQSSNgpsgqFCGGTLIAPRW 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084  74 VLTAAHCIVS---THMRVRLGEYKTRFPGkdcsrcvpksyklrrirlGEydtrfpgkdccvpksyELAVDRKILHADYNL 150
Cdd:COG5640   69 VLTAAHCVDGdgpSDLRVVIGSTDLSTSG------------------GT----------------VVKVARIVVHPDYDP 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084 151 N-LDNDIGLLRMKSFVqysDYVRPICLLVEGHMAES-PIFNITGWGVT--NDGTPSRRLQRATVYNTDLHFCRSkFTKQV 226
Cdd:COG5640  115 AtPGNDIALLKLATPV---PGVAPAPLATSADAAAPgTPATVAGWGRTseGPGSQSGTLRKADVPVVSDATCAA-YGGFD 190
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281364084 227 DESQICAAGTN--SDACHGDSGGPLSAQVPfaGSWLtfQYGLVSYGSAAC--HSFSVYTNVTHHRDWIVNAI 294
Cdd:COG5640  191 GGTMLCAGYPEggKDACQGDSGGPLVVKDG--GGWV--LVGVVSWGGGPCaaGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
41-290 2.16e-40

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 140.27  E-value: 2.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084   41 ITGGADAGLFSNPWMVKVL---GEKLCGGSLITSRFVLTAAHCIVSTH-MRVRLGEYktrfpgkdcsrcvpksyklrRIR 116
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlssGKHFCGGSLISENWVLTAAHCVSGASdVKVVLGAH--------------------NIV 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084  117 LGEydtrfpgkdccvPKSYELAVDRKILHADYNLN-LDNDIGLLRMKSFVQYSDYVRPICLLVEG--HMAESPIFnITGW 193
Cdd:pfam00089  61 LRE------------GGEQKFDVEKIIVHPNYNPDtLDNDIALLKLESPVTLGDTVRPICLPDASsdLPVGTTCT-VSGW 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084  194 GVTNDGTPSRRLQRATVYNTDLHFCRSKFTKQVDESQICAAGTNSDACHGDSGGPLsaqvpFAGSwlTFQYGLVS--YGS 271
Cdd:pfam00089 128 GNTKTLGPSDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGAGGKDACQGDSGGPL-----VCSD--GELIGIVSwgYGC 200
                         250
                  ....*....|....*....
gi 281364084  272 AACHSFSVYTNVTHHRDWI 290
Cdd:pfam00089 201 ASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
41-290 9.72e-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: 177.47  E-value: 9.72e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084  41 ITGG--ADAGLFsnPWMVKV---LGEKLCGGSLITSRFVLTAAHCIVSthmrvrlgeyktrfpgkdcsrCVPKSYklrRI 115
Cdd:cd00190    1 IVGGseAKIGSF--PWQVSLqytGGRHFCGGSLISPRWVLTAAHCVYS---------------------SAPSNY---TV 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084 116 RLGEYDTRFPGkdccvPKSYELAVDRKILHADYNLN-LDNDIGLLRMKSFVQYSDYVRPICL------LVEGHMAEspif 188
Cdd:cd00190   55 RLGSHDLSSNE-----GGGQVIKVKKVIVHPNYNPStYDNDIALLKLKRPVTLSDNVRPICLpssgynLPAGTTCT---- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084 189 nITGWGVTND-GTPSRRLQRATVYNTDLHFCRSKFTKQ--VDESQICAAGTNS--DACHGDSGGPLSAQVPfaGSWltFQ 263
Cdd:cd00190  126 -VSGWGRTSEgGPLPDVLQEVNVPIVSNAECKRAYSYGgtITDNMLCAGGLEGgkDACQGDSGGPLVCNDN--GRG--VL 200
                        250       260
                 ....*....|....*....|....*....
gi 281364084 264 YGLVSYGS--AACHSFSVYTNVTHHRDWI 290
Cdd:cd00190  201 VGIVSWGSgcARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
41-290 2.12e-53

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: 174.02  E-value: 2.12e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084    41 ITGGADAGLFSNPWMVKVL---GEKLCGGSLITSRFVLTAAHCIVSTH---MRVRLGEYktrfpgkdcsrcvpksyklrR 114
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQyggGRHFCGGSLISPRWVLTAAHCVRGSDpsnIRVRLGSH--------------------D 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084   115 IRLGEYDTRFPgkdccvpksyelaVDRKILHADYNL-NLDNDIGLLRMKSFVQYSDYVRPICL------LVEGHMAEspi 187
Cdd:smart00020  62 LSSGEEGQVIK-------------VSKVIIHPNYNPsTYDNDIALLKLKEPVTLSDNVRPICLpssnynVPAGTTCT--- 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084   188 fnITGWGVT--NDGTPSRRLQRATVYNTDLHFCRSKF--TKQVDESQICAAGTN--SDACHGDSGGPLSAQVpfaGSWlt 261
Cdd:smart00020 126 --VSGWGRTseGAGSLPDTLQEVNVPIVSNATCRRAYsgGGAITDNMLCAGGLEggKDACQGDSGGPLVCND---GRW-- 198
                          250       260       270
                   ....*....|....*....|....*....|.
gi 281364084   262 FQYGLVSYGS--AACHSFSVYTNVTHHRDWI 290
Cdd:smart00020 199 VLVGIVSWGSgcARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-294 3.29e-45

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 154.04  E-value: 3.29e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084   1 MK--FIAAGLALLVCSIQLgegapghlldSSCGTTKPEfiPMITGGADAGLFSNPWMVKVLGEK-----LCGGSLITSRF 73
Cdd:COG5640    1 MRrrRLLAALAAAALALAL----------AAAPAADAA--PAIVGGTPATVGEYPWMVALQSSNgpsgqFCGGTLIAPRW 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084  74 VLTAAHCIVS---THMRVRLGEYKTRFPGkdcsrcvpksyklrrirlGEydtrfpgkdccvpksyELAVDRKILHADYNL 150
Cdd:COG5640   69 VLTAAHCVDGdgpSDLRVVIGSTDLSTSG------------------GT----------------VVKVARIVVHPDYDP 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084 151 N-LDNDIGLLRMKSFVqysDYVRPICLLVEGHMAES-PIFNITGWGVT--NDGTPSRRLQRATVYNTDLHFCRSkFTKQV 226
Cdd:COG5640  115 AtPGNDIALLKLATPV---PGVAPAPLATSADAAAPgTPATVAGWGRTseGPGSQSGTLRKADVPVVSDATCAA-YGGFD 190
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281364084 227 DESQICAAGTN--SDACHGDSGGPLSAQVPfaGSWLtfQYGLVSYGSAAC--HSFSVYTNVTHHRDWIVNAI 294
Cdd:COG5640  191 GGTMLCAGYPEggKDACQGDSGGPLVVKDG--GGWV--LVGVVSWGGGPCaaGYPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
41-290 2.16e-40

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 140.27  E-value: 2.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084   41 ITGGADAGLFSNPWMVKVL---GEKLCGGSLITSRFVLTAAHCIVSTH-MRVRLGEYktrfpgkdcsrcvpksyklrRIR 116
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQlssGKHFCGGSLISENWVLTAAHCVSGASdVKVVLGAH--------------------NIV 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084  117 LGEydtrfpgkdccvPKSYELAVDRKILHADYNLN-LDNDIGLLRMKSFVQYSDYVRPICLLVEG--HMAESPIFnITGW 193
Cdd:pfam00089  61 LRE------------GGEQKFDVEKIIVHPNYNPDtLDNDIALLKLESPVTLGDTVRPICLPDASsdLPVGTTCT-VSGW 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364084  194 GVTNDGTPSRRLQRATVYNTDLHFCRSKFTKQVDESQICAAGTNSDACHGDSGGPLsaqvpFAGSwlTFQYGLVS--YGS 271
Cdd:pfam00089 128 GNTKTLGPSDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGAGGKDACQGDSGGPL-----VCSD--GELIGIVSwgYGC 200
                         250
                  ....*....|....*....
gi 281364084  272 AACHSFSVYTNVTHHRDWI 290
Cdd:pfam00089 201 ASGNYPGVYTPVSSYLDWI 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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