NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24650778|ref|NP_651607|]
View 

uncharacterized protein Dmel_CG4815 [Drosophila melanogaster]

Protein Classification

serine protease family protein( domain architecture ID 229414)

trypsin-like serine protease family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
49-259 5.76e-31

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: 114.68  E-value: 5.76e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778  49 VGIQLFNGRKLvCSATLLTPRHILTAAHCFENLNRSKFHVIGGKsaefTWHGNNFNKNKLIRVQ---IHPKYAKMKFIAD 125
Cdd:cd00190  16 VSLQYTGGRHF-CGGSLISPRWVLTAAHCVYSSAPSNYTVRLGS----HDLSSNEGGGQVIKVKkviVHPNYNPSTYDND 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778 126 VAVAKTKYPL-RSKYIGYAQL--CRSVLHPRDKLIAAGWG--FEGGvwdeSRKKTFRSMKVGIVSKRDCEK--QLDRKMP 198
Cdd:cd00190  91 IALLKLKRPVtLSDNVRPICLpsSGYNLPAGTTCTVSGWGrtSEGG----PLPDVLQEVNVPIVSNAECKRaySYGGTIT 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24650778 199 PNIICAGAYN-NKTLCFGDSGGPLLLGR----QVCGINTWTFKCGNNEKPDVYMGVRYYAKFIKRT 259
Cdd:cd00190 167 DNMLCAGGLEgGKDACQGDSGGPLVCNDngrgVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
49-259 5.76e-31

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: 114.68  E-value: 5.76e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778  49 VGIQLFNGRKLvCSATLLTPRHILTAAHCFENLNRSKFHVIGGKsaefTWHGNNFNKNKLIRVQ---IHPKYAKMKFIAD 125
Cdd:cd00190  16 VSLQYTGGRHF-CGGSLISPRWVLTAAHCVYSSAPSNYTVRLGS----HDLSSNEGGGQVIKVKkviVHPNYNPSTYDND 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778 126 VAVAKTKYPL-RSKYIGYAQL--CRSVLHPRDKLIAAGWG--FEGGvwdeSRKKTFRSMKVGIVSKRDCEK--QLDRKMP 198
Cdd:cd00190  91 IALLKLKRPVtLSDNVRPICLpsSGYNLPAGTTCTVSGWGrtSEGG----PLPDVLQEVNVPIVSNAECKRaySYGGTIT 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24650778 199 PNIICAGAYN-NKTLCFGDSGGPLLLGR----QVCGINTWTFKCGNNEKPDVYMGVRYYAKFIKRT 259
Cdd:cd00190 167 DNMLCAGGLEgGKDACQGDSGGPLVCNDngrgVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
49-256 1.30e-30

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 113.69  E-value: 1.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778    49 VGIQlFNGRKLVCSATLLTPRHILTAAHCFEnlNRSKFHVIGGKSAEFTWHGNNFNKnKLIRVQIHPKYAKMKFIADVAV 128
Cdd:pfam00089  16 VSLQ-LSSGKHFCGGSLISENWVLTAAHCVS--GASDVKVVLGAHNIVLREGGEQKF-DVEKIIVHPNYNPDTLDNDIAL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778   129 AKTKYPLRS----KYIGYAQLCRSvLHPRDKLIAAGWGFeggVWDESRKKTFRSMKVGIVSKRDCEKQLDRKMPPNIICA 204
Cdd:pfam00089  92 LKLESPVTLgdtvRPICLPDASSD-LPVGTTCTVSGWGN---TKTLGPSDTLQEVTVPVVSRETCRSAYGGTVTDTMICA 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24650778   205 GAYNNKTlCFGDSGGPLL-LGRQVCGINTWTFKCGNNEKPDVYMGVRYYAKFI 256
Cdd:pfam00089 168 GAGGKDA-CQGDSGGPLVcSDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
49-256 1.42e-29

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: 111.23  E-value: 1.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778     49 VGIQlFNGRKLVCSATLLTPRHILTAAHCFENLNRSKFHVIGGksaefTWHGNNFNKNKLIRVQ---IHPKYAKMKFIAD 125
Cdd:smart00020  17 VSLQ-YGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLG-----SHDLSSGEEGQVIKVSkviIHPNYNPSTYDND 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778    126 VAVAKTKYPL-RSKYIGYAQL--CRSVLHPRDKLIAAGWGFEGGvWDESRKKTFRSMKVGIVSKRDCEKQL--DRKMPPN 200
Cdd:smart00020  91 IALLKLKEPVtLSDNVRPICLpsSNYNVPAGTTCTVSGWGRTSE-GAGSLPDTLQEVNVPIVSNATCRRAYsgGGAITDN 169
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778    201 IICAGAYNN-KTLCFGDSGGPLLLG---RQVCGINTWTFKCGNNEKPDVYMGVRYYAKFI 256
Cdd:smart00020 170 MLCAGGLEGgKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
33-264 2.24e-29

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 111.28  E-value: 2.24e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778  33 PRIYNGIKTTVESLGG-VGIQLFNG-RKLVCSATLLTPRHILTAAHCFENLNRSKFHVIGGKSaefTWHGNNFNKNKLIR 110
Cdd:COG5640  29 PAIVGGTPATVGEYPWmVALQSSNGpSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGST---DLSTSGGTVVKVAR 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778 111 VQIHPKYAKMKFIADVAVAKTKYPL-RSKYIGYAQLcRSVLHPRDKLIAAGWGF-EGGVWDESRkkTFRSMKVGIVSKRD 188
Cdd:COG5640 106 IVVHPDYDPATPGNDIALLKLATPVpGVAPAPLATS-ADAAAPGTPATVAGWGRtSEGPGSQSG--TLRKADVPVVSDAT 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778 189 CEKQLDRKmPPNIICAGAYN-NKTLCFGDSGGPLLL-----GRQVcGINTWTF-KCGNNeKPDVYMGVRYYAKFIKRTIN 261
Cdd:COG5640 183 CAAYGGFD-GGTMLCAGYPEgGKDACQGDSGGPLVVkdgggWVLV-GVVSWGGgPCAAG-YPGVYTRVSAYRDWIKSTAG 259

                ...
gi 24650778 262 RMG 264
Cdd:COG5640 260 GLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
49-259 5.76e-31

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: 114.68  E-value: 5.76e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778  49 VGIQLFNGRKLvCSATLLTPRHILTAAHCFENLNRSKFHVIGGKsaefTWHGNNFNKNKLIRVQ---IHPKYAKMKFIAD 125
Cdd:cd00190  16 VSLQYTGGRHF-CGGSLISPRWVLTAAHCVYSSAPSNYTVRLGS----HDLSSNEGGGQVIKVKkviVHPNYNPSTYDND 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778 126 VAVAKTKYPL-RSKYIGYAQL--CRSVLHPRDKLIAAGWG--FEGGvwdeSRKKTFRSMKVGIVSKRDCEK--QLDRKMP 198
Cdd:cd00190  91 IALLKLKRPVtLSDNVRPICLpsSGYNLPAGTTCTVSGWGrtSEGG----PLPDVLQEVNVPIVSNAECKRaySYGGTIT 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24650778 199 PNIICAGAYN-NKTLCFGDSGGPLLLGR----QVCGINTWTFKCGNNEKPDVYMGVRYYAKFIKRT 259
Cdd:cd00190 167 DNMLCAGGLEgGKDACQGDSGGPLVCNDngrgVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
49-256 1.30e-30

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 113.69  E-value: 1.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778    49 VGIQlFNGRKLVCSATLLTPRHILTAAHCFEnlNRSKFHVIGGKSAEFTWHGNNFNKnKLIRVQIHPKYAKMKFIADVAV 128
Cdd:pfam00089  16 VSLQ-LSSGKHFCGGSLISENWVLTAAHCVS--GASDVKVVLGAHNIVLREGGEQKF-DVEKIIVHPNYNPDTLDNDIAL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778   129 AKTKYPLRS----KYIGYAQLCRSvLHPRDKLIAAGWGFeggVWDESRKKTFRSMKVGIVSKRDCEKQLDRKMPPNIICA 204
Cdd:pfam00089  92 LKLESPVTLgdtvRPICLPDASSD-LPVGTTCTVSGWGN---TKTLGPSDTLQEVTVPVVSRETCRSAYGGTVTDTMICA 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24650778   205 GAYNNKTlCFGDSGGPLL-LGRQVCGINTWTFKCGNNEKPDVYMGVRYYAKFI 256
Cdd:pfam00089 168 GAGGKDA-CQGDSGGPLVcSDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
49-256 1.42e-29

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: 111.23  E-value: 1.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778     49 VGIQlFNGRKLVCSATLLTPRHILTAAHCFENLNRSKFHVIGGksaefTWHGNNFNKNKLIRVQ---IHPKYAKMKFIAD 125
Cdd:smart00020  17 VSLQ-YGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLG-----SHDLSSGEEGQVIKVSkviIHPNYNPSTYDND 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778    126 VAVAKTKYPL-RSKYIGYAQL--CRSVLHPRDKLIAAGWGFEGGvWDESRKKTFRSMKVGIVSKRDCEKQL--DRKMPPN 200
Cdd:smart00020  91 IALLKLKEPVtLSDNVRPICLpsSNYNVPAGTTCTVSGWGRTSE-GAGSLPDTLQEVNVPIVSNATCRRAYsgGGAITDN 169
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778    201 IICAGAYNN-KTLCFGDSGGPLLLG---RQVCGINTWTFKCGNNEKPDVYMGVRYYAKFI 256
Cdd:smart00020 170 MLCAGGLEGgKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
33-264 2.24e-29

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 111.28  E-value: 2.24e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778  33 PRIYNGIKTTVESLGG-VGIQLFNG-RKLVCSATLLTPRHILTAAHCFENLNRSKFHVIGGKSaefTWHGNNFNKNKLIR 110
Cdd:COG5640  29 PAIVGGTPATVGEYPWmVALQSSNGpSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGST---DLSTSGGTVVKVAR 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778 111 VQIHPKYAKMKFIADVAVAKTKYPL-RSKYIGYAQLcRSVLHPRDKLIAAGWGF-EGGVWDESRkkTFRSMKVGIVSKRD 188
Cdd:COG5640 106 IVVHPDYDPATPGNDIALLKLATPVpGVAPAPLATS-ADAAAPGTPATVAGWGRtSEGPGSQSG--TLRKADVPVVSDAT 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778 189 CEKQLDRKmPPNIICAGAYN-NKTLCFGDSGGPLLL-----GRQVcGINTWTF-KCGNNeKPDVYMGVRYYAKFIKRTIN 261
Cdd:COG5640 183 CAAYGGFD-GGTMLCAGYPEgGKDACQGDSGGPLVVkdgggWVLV-GVVSWGGgPCAAG-YPGVYTRVSAYRDWIKSTAG 259

                ...
gi 24650778 262 RMG 264
Cdd:COG5640 260 GLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
49-258 3.00e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 60.85  E-value: 3.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778  49 VGIQLFNGRKLVCSATLLTPRHILTAAHCFENLNRSKFHViggkSAEFT--WHGNNFNKNKLIRVQIHPKYAKMKFIA-D 125
Cdd:COG3591   2 VGRLETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWAT----NIVFVpgYNGGPYGTATATRFRVPPGWVASGDAGyD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778 126 VAVAKTKYPLRSK--YIGYAQLCRSVL--------HPRDKLIAAGWGFEGGVWDESrkktfrsmkvgivskrdcekqldr 195
Cdd:COG3591  78 YALLRLDEPLGDTtgWLGLAFNDAPLAgepvtiigYPGDRPKDLSLDCSGRVTGVQ------------------------ 133
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24650778 196 kmpPNIIcagAYNNKTlCFGDSGGPLLL----GRQVCGINTWTFKCGNNEkpdvymGVRYYAKFIKR 258
Cdd:COG3591 134 ---GNRL---SYDCDT-TGGSSGSPVLDdsdgGGRVVGVHSAGGADRANT------GVRLTSAIVAA 187
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
61-230 4.58e-03

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 36.63  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778    61 CSATLLTPR-HILTAAHCFENLNRSKFHVIggksaEFTWHGNNFNKNKLIRVQIHpkyakmkfiADVAVAKTKYPLRSky 139
Cdd:pfam13365   1 GTGFVVSSDgLVLTNAHVVDDAEEAAVELV-----SVVLADGREYPATVVARDPD---------LDLALLRVSGDGRG-- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24650778   140 IGYAQLCRSVLHPRDKLIAAgWGFEGGvwdeSRKKTFRSmkvGIVSKRDceKQLDRKMPPNIICAGAYNNKtlcfGDSGG 219
Cdd:pfam13365  65 LPPLPLGDSEPLVGGERVYA-VGYPLG----GEKLSLSE---GIVSGVD--EGRDGGDDGRVIQTDAALSP----GSSGG 130
                         170
                  ....*....|..
gi 24650778   220 PLLLGR-QVCGI 230
Cdd:pfam13365 131 PVFDADgRVVGI 142
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH