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Conserved domains on  [gi|24581077|ref|NP_722785|]
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uncharacterized protein Dmel_CG17234 [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 ...
27-243 1.57e-62

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: 195.57  E-value: 1.57e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077  27 IIGGEPIGIEQVPWQVSLQYF-GDHVCGGSIYSENIIVTAAHCFFDEEGNRlddqgYQVRAGSA---LTDSNGTLVDVAA 102
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSN-----YTVRLGSHdlsSNEGGGQVIKVKK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077 103 LIIHEEYAFDLNINDIAIVRLSTPLEFTSKVQPIPLAKTN--PYPRSIALVSGWGvsyiLNDSTNLYPTHLQGLALHIKS 180
Cdd:cd00190  76 VIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWG----RTSEGGPLPDVLQEVNVPIVS 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581077 181 IFSCR-------LFDPSLLCAGTY--GRTACHGDSGGPLVVNK----QLVGVVSWGRkGCVSS---AFFVSVPYFREWI 243
Cdd:cd00190 152 NAECKraysyggTITDNMLCAGGLegGKDACQGDSGGPLVCNDngrgVLVGIVSWGS-GCARPnypGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
27-243 1.57e-62

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: 195.57  E-value: 1.57e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077  27 IIGGEPIGIEQVPWQVSLQYF-GDHVCGGSIYSENIIVTAAHCFFDEEGNRlddqgYQVRAGSA---LTDSNGTLVDVAA 102
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSN-----YTVRLGSHdlsSNEGGGQVIKVKK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077 103 LIIHEEYAFDLNINDIAIVRLSTPLEFTSKVQPIPLAKTN--PYPRSIALVSGWGvsyiLNDSTNLYPTHLQGLALHIKS 180
Cdd:cd00190  76 VIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWG----RTSEGGPLPDVLQEVNVPIVS 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581077 181 IFSCR-------LFDPSLLCAGTY--GRTACHGDSGGPLVVNK----QLVGVVSWGRkGCVSS---AFFVSVPYFREWI 243
Cdd:cd00190 152 NAECKraysyggTITDNMLCAGGLegGKDACQGDSGGPLVCNDngrgVLVGIVSWGS-GCARPnypGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
26-243 1.81e-62

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: 195.20  E-value: 1.81e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077     26 RIIGGEPIGIEQVPWQVSLQYFGD-HVCGGSIYSENIIVTAAHCFfdeegNRLDDQGYQVRAGS--ALTDSNGTLVDVAA 102
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCV-----RGSDPSNIRVRLGShdLSSGEEGQVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077    103 LIIHEEYAFDLNINDIAIVRLSTPLEFTSKVQPIPLAKTN--PYPRSIALVSGWGvsyILNDSTNLYPTHLQGLALHIKS 180
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWG---RTSEGAGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24581077    181 IFSCR-------LFDPSLLCAGTY--GRTACHGDSGGPLVVNK---QLVGVVSWGRkGCVSS---AFFVSVPYFREWI 243
Cdd:smart00020 153 NATCRraysgggAITDNMLCAGGLegGKDACQGDSGGPLVCNDgrwVLVGIVSWGS-GCARPgkpGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
24-249 4.19e-56

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 180.23  E-value: 4.19e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077  24 EQRIIGGEPIGIEQVPWQVSLQY---FGDHVCGGSIYSENIIVTAAHCFFDEegnrlDDQGYQVRAGSA-LTDSNGTLVD 99
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVDGD-----GPSDLRVVIGSTdLSTSGGTVVK 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077 100 VAALIIHEEYAFDLNINDIAIVRLSTPLeftSKVQPIPLAKTN--PYPRSIALVSGWGVsyiLNDSTNLYPTHLQGLALH 177
Cdd:COG5640 103 VARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSAdaAAPGTPATVAGWGR---TSEGPGSQSGTLRKADVP 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077 178 IKSIFSCRLF----DPSLLCAGTY--GRTACHGDSGGPLVVNK----QLVGVVSWGRKGCVSSAF--FVSVPYFREWILN 245
Cdd:COG5640 177 VVSDATCAAYggfdGGTMLCAGYPegGKDACQGDSGGPLVVKDgggwVLVGVVSWGGGPCAAGYPgvYTRVSAYRDWIKS 256

                ....
gi 24581077 246 AIAS 249
Cdd:COG5640 257 TAGG 260
Trypsin pfam00089
Trypsin;
27-243 1.03e-48

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 159.92  E-value: 1.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077    27 IIGGEPIGIEQVPWQVSLQYFGD-HVCGGSIYSENIIVTAAHCFfdeegnrLDDQGYQVRAGS---ALTDSNGTLVDVAA 102
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCV-------SGASDVKVVLGAhniVLREGGEQKFDVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077   103 LIIHEEYAFDLNINDIAIVRLSTPLEFTSKVQPIPLAKTNPY--PRSIALVSGWGvsyilNDSTNLYPTHLQGLALHIKS 180
Cdd:pfam00089  74 IIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDlpVGTTCTVSGWG-----NTKTLGPSDTLQEVTVPVVS 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581077   181 IFSCRLFDP-----SLLCAGTYGRTACHGDSGGPLVVNKQ-LVGVVSWGrKGCVSS---AFFVSVPYFREWI 243
Cdd:pfam00089 149 RETCRSAYGgtvtdTMICAGAGGKDACQGDSGGPLVCSDGeLIGIVSWG-YGCASGnypGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
27-243 1.57e-62

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: 195.57  E-value: 1.57e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077  27 IIGGEPIGIEQVPWQVSLQYF-GDHVCGGSIYSENIIVTAAHCFFDEEGNRlddqgYQVRAGSA---LTDSNGTLVDVAA 102
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSN-----YTVRLGSHdlsSNEGGGQVIKVKK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077 103 LIIHEEYAFDLNINDIAIVRLSTPLEFTSKVQPIPLAKTN--PYPRSIALVSGWGvsyiLNDSTNLYPTHLQGLALHIKS 180
Cdd:cd00190  76 VIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWG----RTSEGGPLPDVLQEVNVPIVS 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581077 181 IFSCR-------LFDPSLLCAGTY--GRTACHGDSGGPLVVNK----QLVGVVSWGRkGCVSS---AFFVSVPYFREWI 243
Cdd:cd00190 152 NAECKraysyggTITDNMLCAGGLegGKDACQGDSGGPLVCNDngrgVLVGIVSWGS-GCARPnypGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
26-243 1.81e-62

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: 195.20  E-value: 1.81e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077     26 RIIGGEPIGIEQVPWQVSLQYFGD-HVCGGSIYSENIIVTAAHCFfdeegNRLDDQGYQVRAGS--ALTDSNGTLVDVAA 102
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCV-----RGSDPSNIRVRLGShdLSSGEEGQVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077    103 LIIHEEYAFDLNINDIAIVRLSTPLEFTSKVQPIPLAKTN--PYPRSIALVSGWGvsyILNDSTNLYPTHLQGLALHIKS 180
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWG---RTSEGAGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24581077    181 IFSCR-------LFDPSLLCAGTY--GRTACHGDSGGPLVVNK---QLVGVVSWGRkGCVSS---AFFVSVPYFREWI 243
Cdd:smart00020 153 NATCRraysgggAITDNMLCAGGLegGKDACQGDSGGPLVCNDgrwVLVGIVSWGS-GCARPgkpGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
24-249 4.19e-56

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 180.23  E-value: 4.19e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077  24 EQRIIGGEPIGIEQVPWQVSLQY---FGDHVCGGSIYSENIIVTAAHCFFDEegnrlDDQGYQVRAGSA-LTDSNGTLVD 99
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVDGD-----GPSDLRVVIGSTdLSTSGGTVVK 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077 100 VAALIIHEEYAFDLNINDIAIVRLSTPLeftSKVQPIPLAKTN--PYPRSIALVSGWGVsyiLNDSTNLYPTHLQGLALH 177
Cdd:COG5640 103 VARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSAdaAAPGTPATVAGWGR---TSEGPGSQSGTLRKADVP 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077 178 IKSIFSCRLF----DPSLLCAGTY--GRTACHGDSGGPLVVNK----QLVGVVSWGRKGCVSSAF--FVSVPYFREWILN 245
Cdd:COG5640 177 VVSDATCAAYggfdGGTMLCAGYPegGKDACQGDSGGPLVVKDgggwVLVGVVSWGGGPCAAGYPgvYTRVSAYRDWIKS 256

                ....
gi 24581077 246 AIAS 249
Cdd:COG5640 257 TAGG 260
Trypsin pfam00089
Trypsin;
27-243 1.03e-48

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 159.92  E-value: 1.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077    27 IIGGEPIGIEQVPWQVSLQYFGD-HVCGGSIYSENIIVTAAHCFfdeegnrLDDQGYQVRAGS---ALTDSNGTLVDVAA 102
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCV-------SGASDVKVVLGAhniVLREGGEQKFDVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077   103 LIIHEEYAFDLNINDIAIVRLSTPLEFTSKVQPIPLAKTNPY--PRSIALVSGWGvsyilNDSTNLYPTHLQGLALHIKS 180
Cdd:pfam00089  74 IIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDlpVGTTCTVSGWG-----NTKTLGPSDTLQEVTVPVVS 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581077   181 IFSCRLFDP-----SLLCAGTYGRTACHGDSGGPLVVNKQ-LVGVVSWGrKGCVSS---AFFVSVPYFREWI 243
Cdd:pfam00089 149 RETCRSAYGgtvtdTMICAGAGGKDACQGDSGGPLVCSDGeLIGIVSWG-YGCASGnypGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
48-249 8.60e-12

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 62.39  E-value: 8.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077  48 GDHVCGGSIYSENIIVTAAHCFFDEEGNRLdDQGYQVRAGsaLTDSNGTLVDVAALIIHEEYAFDLNIN-DIAIVRLSTP 126
Cdd:COG3591  10 GGGVCTGTLIGPNLVLTAGHCVYDGAGGGW-ATNIVFVPG--YNGGPYGTATATRFRVPPGWVASGDAGyDYALLRLDEP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581077 127 LefTSKVQPIPLAKTNPYPRSIAL-VSGwgvsyilndstnlYPthlQGLALHIKSIFSCRLF--DPSLLcagTYGRTACH 203
Cdd:COG3591  87 L--GDTTGWLGLAFNDAPLAGEPVtIIG-------------YP---GDRPKDLSLDCSGRVTgvQGNRL---SYDCDTTG 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 24581077 204 GDSGGPLVVNK----QLVGVVSWGRKGCVSSAffvsvPYFREWILNAIAS 249
Cdd:COG3591 146 GSSGSPVLDDSdgggRVVGVHSAGGADRANTG-----VRLTSAIVAALRA 190
 
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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