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Conserved domains on  [gi|23171530|gb|AAF55391|]
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uncharacterized protein Dmel_CG17477 [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 ...
27-250 3.08e-63

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: 197.88  E-value: 3.08e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530  27 IVGGQNAAEGDAPYQVSLQTLLGSHLCGGAIISDRWIITAGHCVKGYPTSRLQVATGTI---RYAEPGAVYYPDAIYLHC 103
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHdlsSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530 104 NYDSPKYQNDIGLLHLNESITFNALTQAVELPTS--PFPRGaSELVFTGWGSQSAAGSLPSQLQRVQQQHLNSPACESMM 181
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAG-TTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23171530 182 SAYEDLElgPCHICA-YRQANIGACHGDSGGPLVHQ----GTLVGILNFFVPCAQ-GVPDIFMNIMYYRDWMRQT 250
Cdd:cd00190 160 SYGGTIT--DNMLCAgGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARpNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
27-250 3.08e-63

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: 197.88  E-value: 3.08e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530  27 IVGGQNAAEGDAPYQVSLQTLLGSHLCGGAIISDRWIITAGHCVKGYPTSRLQVATGTI---RYAEPGAVYYPDAIYLHC 103
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHdlsSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530 104 NYDSPKYQNDIGLLHLNESITFNALTQAVELPTS--PFPRGaSELVFTGWGSQSAAGSLPSQLQRVQQQHLNSPACESMM 181
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAG-TTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23171530 182 SAYEDLElgPCHICA-YRQANIGACHGDSGGPLVHQ----GTLVGILNFFVPCAQ-GVPDIFMNIMYYRDWMRQT 250
Cdd:cd00190 160 SYGGTIT--DNMLCAgGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARpNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
27-246 3.44e-61

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: 192.89  E-value: 3.44e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530     27 IVGGQNAAEGDAPYQVSLQTLLGSHLCGGAIISDRWIITAGHCVKGYPTSRLQVATGT--IRYAEPGAVYYPDAIYLHCN 104
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGShdLSSGEEGQVIKVSKVIIHPN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530    105 YDSPKYQNDIGLLHLNESITFNALTQAVELPTS--PFPRGaSELVFTGWGS-QSAAGSLPSQLQRVQQQHLNSPACESMM 181
Cdd:smart00020  82 YNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAG-TTCTVSGWGRtSEGAGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530    182 SAYEDLElgPCHICA-YRQANIGACHGDSGGPLVHQ---GTLVGILNFFVPCAQ-GVPDIFMNIMYYRDW 246
Cdd:smart00020 161 SGGGAIT--DNMLCAgGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARpGKPGVYTRVSSYLDW 228
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-255 2.65e-54

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 176.38  E-value: 2.65e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530   1 MSLARFLFYILVFSSL----YCDLLALEHFIVGGQNAAEGDAPYQVSLQTLLG--SHLCGGAIISDRWIITAGHCVKGYP 74
Cdd:COG5640   1 MRRRRLLAALAAAALAlalaAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGpsGQFCGGTLIAPRWVLTAAHCVDGDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530  75 TSRLQVATGTI-RYAEPGAVYYPDAIYLHCNYDSPKYQNDIGLLHLNESITFNAltqAVELPTSPFPRGA-SELVFTGWG 152
Cdd:COG5640  81 PSDLRVVIGSTdLSTSGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAAPgTPATVAGWG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530 153 SQSA-AGSLPSQLQRVQQQHLNSPACESMMSAYEDLElgpchICA-YRQANIGACHGDSGGPLVHQ----GTLVGILNF- 225
Cdd:COG5640 158 RTSEgPGSQSGTLRKADVPVVSDATCAAYGGFDGGTM-----LCAgYPEGGKDACQGDSGGPLVVKdgggWVLVGVVSWg 232
                       250       260       270
                ....*....|....*....|....*....|
gi 23171530 226 FVPCAQGVPDIFMNIMYYRDWMRQTMSGNG 255
Cdd:COG5640 233 GGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 262
Trypsin pfam00089
Trypsin;
27-247 1.46e-47

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 157.60  E-value: 1.46e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530    27 IVGGQNAAEGDAPYQVSLQTLLGSHLCGGAIISDRWIITAGHCVKGYPTSRLQVATGTIRYAEPGAVYYP-DAIYLHCNY 105
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDvEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530   106 DSPKYQNDIGLLHLNESITFNALTQAVELPT--SPFPRGASELVfTGWGSQSAAGsLPSQLQRVQQQHLNSPACESMMSA 183
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCTV-SGWGNTKTLG-PSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23171530   184 YedleLGPCHICAYRQAnIGACHGDSGGPLV-HQGTLVGILNFFVPCAQG-VPDIFMNIMYYRDWM 247
Cdd:pfam00089 159 T----VTDTMICAGAGG-KDACQGDSGGPLVcSDGELIGIVSWGYGCASGnYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
27-250 3.08e-63

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: 197.88  E-value: 3.08e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530  27 IVGGQNAAEGDAPYQVSLQTLLGSHLCGGAIISDRWIITAGHCVKGYPTSRLQVATGTI---RYAEPGAVYYPDAIYLHC 103
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHdlsSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530 104 NYDSPKYQNDIGLLHLNESITFNALTQAVELPTS--PFPRGaSELVFTGWGSQSAAGSLPSQLQRVQQQHLNSPACESMM 181
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAG-TTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23171530 182 SAYEDLElgPCHICA-YRQANIGACHGDSGGPLVHQ----GTLVGILNFFVPCAQ-GVPDIFMNIMYYRDWMRQT 250
Cdd:cd00190 160 SYGGTIT--DNMLCAgGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARpNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
27-246 3.44e-61

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: 192.89  E-value: 3.44e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530     27 IVGGQNAAEGDAPYQVSLQTLLGSHLCGGAIISDRWIITAGHCVKGYPTSRLQVATGT--IRYAEPGAVYYPDAIYLHCN 104
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGShdLSSGEEGQVIKVSKVIIHPN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530    105 YDSPKYQNDIGLLHLNESITFNALTQAVELPTS--PFPRGaSELVFTGWGS-QSAAGSLPSQLQRVQQQHLNSPACESMM 181
Cdd:smart00020  82 YNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAG-TTCTVSGWGRtSEGAGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530    182 SAYEDLElgPCHICA-YRQANIGACHGDSGGPLVHQ---GTLVGILNFFVPCAQ-GVPDIFMNIMYYRDW 246
Cdd:smart00020 161 SGGGAIT--DNMLCAgGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARpGKPGVYTRVSSYLDW 228
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-255 2.65e-54

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 176.38  E-value: 2.65e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530   1 MSLARFLFYILVFSSL----YCDLLALEHFIVGGQNAAEGDAPYQVSLQTLLG--SHLCGGAIISDRWIITAGHCVKGYP 74
Cdd:COG5640   1 MRRRRLLAALAAAALAlalaAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGpsGQFCGGTLIAPRWVLTAAHCVDGDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530  75 TSRLQVATGTI-RYAEPGAVYYPDAIYLHCNYDSPKYQNDIGLLHLNESITFNAltqAVELPTSPFPRGA-SELVFTGWG 152
Cdd:COG5640  81 PSDLRVVIGSTdLSTSGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVA---PAPLATSADAAAPgTPATVAGWG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530 153 SQSA-AGSLPSQLQRVQQQHLNSPACESMMSAYEDLElgpchICA-YRQANIGACHGDSGGPLVHQ----GTLVGILNF- 225
Cdd:COG5640 158 RTSEgPGSQSGTLRKADVPVVSDATCAAYGGFDGGTM-----LCAgYPEGGKDACQGDSGGPLVVKdgggWVLVGVVSWg 232
                       250       260       270
                ....*....|....*....|....*....|
gi 23171530 226 FVPCAQGVPDIFMNIMYYRDWMRQTMSGNG 255
Cdd:COG5640 233 GGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 262
Trypsin pfam00089
Trypsin;
27-247 1.46e-47

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 157.60  E-value: 1.46e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530    27 IVGGQNAAEGDAPYQVSLQTLLGSHLCGGAIISDRWIITAGHCVKGYPTSRLQVATGTIRYAEPGAVYYP-DAIYLHCNY 105
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDvEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530   106 DSPKYQNDIGLLHLNESITFNALTQAVELPT--SPFPRGASELVfTGWGSQSAAGsLPSQLQRVQQQHLNSPACESMMSA 183
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCTV-SGWGNTKTLG-PSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23171530   184 YedleLGPCHICAYRQAnIGACHGDSGGPLV-HQGTLVGILNFFVPCAQG-VPDIFMNIMYYRDWM 247
Cdd:pfam00089 159 T----VTDTMICAGAGG-KDACQGDSGGPLVcSDGELIGIVSWGYGCASGnYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
44-225 2.14e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 50.06  E-value: 2.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530  44 LQTLLGSHLCGGAIISDRWIITAGHCVKGYPT----SRLQVATGtiRYAEPGAVYYPDAIYLHCNYD-SPKYQNDIGLLH 118
Cdd:COG3591   5 LETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGggwaTNIVFVPG--YNGGPYGTATATRFRVPPGWVaSGDAGYDYALLR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23171530 119 LNESITfnALTQAVELPTSPFPRGASELVFTGWGsqsaaGSLPSQLQRVQQQHLNSPACESMmsayedlelgpchicayr 198
Cdd:COG3591  83 LDEPLG--DTTGWLGLAFNDAPLAGEPVTIIGYP-----GDRPKDLSLDCSGRVTGVQGNRL------------------ 137
                       170       180       190
                ....*....|....*....|....*....|.
gi 23171530 199 QANIGACHGDSGGPLVH----QGTLVGILNF 225
Cdd:COG3591 138 SYDCDTTGGSSGSPVLDdsdgGGRVVGVHSA 168
 
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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