1TZS


Conserved Protein Domain Family
Cathespin_E

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cd05486: Cathespin_E 
Click on image for an interactive view with Cn3D
Cathepsin E, non-lysosomal aspartic protease.
Cathepsin E is an intracellular, non-lysosomal aspartic protease expressed in a variety of cells and tissues. The protease has proposed physiological roles in antigen presentation by the MHC class II system, in the biogenesis of the vasoconstrictor peptide endothelin, and in neurodegeneration associated with brain ischemia and aging. Cathepsin E is the only A1 aspartic protease that exists as a homodimer with a disulfide bridge linking the two monomers. Like many other aspartic proteases, it is synthesized as a zymogen which is catalytically inactive towards its natural substrates at neutral pH and which auto-activates in an acidic environment. The overall structure follows the general fold of aspartic proteases of the A1 family, it is composed of two structurally similar beta barrel lobes, each lobe contributing an aspartic acid residue to form a catalytic dyad that acts to cleave the substrate peptide bond. The catalytic Asp residues are contained in an Asp-Thr-Gly-Ser/thr motif in both N- and C-terminal lobes of the enzyme. The aspartic acid residues act together to allow a water molecule to attack the peptide bond. One aspartic acid residue (in its deprotonated form) activates the attacking water molecule, whereas the other aspartic acid residue (in its protonated form) polarizes the peptide carbonyl, increasing its susceptibility to attack. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).
Statistics
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PSSM-Id: 133153
View PSSM: cd05486
Aligned: 4 rows
Threshold Bit Score: 596.481
Threshold Setting Gi: 46395759
Created: 9-Jan-2008
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 2 residues -Click on image for an interactive view with Cn3D
Feature 1:catalytic residue [active site]
Evidence:
  • Comment:The two ASPs at the active site plays key catalytic roles in the pepsin family and conserved for all family members.
  • Comment:Predicted based on homologous proteins woth structures.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                          #                                                             
1TZS_A        25 YFGTISIGSPPQNFTVIFDTGSSNLWVPSVYCTSPACKTHSRFQPsqSSTYSQPGQSFSIQYGTGSLSGIIGaDQVSVEG 104
gi 118102416  79 YFGQISIGTPPQNFTVVFDTGSSNLWVPSIYCTSKACTKHARFQPshSSTYQPLGIPVSIQYGTGSLTGIIGsDQVTVEG 158
gi 46395761   74 YFGEISVGTPPQNFTVIFDTGSSNLWVPSVYCISQACAQHDRFQPqlSSTYESNGNNFSLQYGTGSLSGVIGiDAVTVEG 153
gi 46395759   74 YFGQISIGTPPQQFTVIFDTGSSNLWVPSIYCTSQACTKHNRYRPseSTTYVSNGEAFFIQYGTGNLTGILGiDQVTVQG 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                        
1TZS_A       105 lTVVGQQFGESVTEPGqTFVDAEFDGILGLGYPSLAVggvTPVFDNMMAQNLVDLPMFSVYMSSNPeggaGSELIFGGYD 184
gi 118102416 159 mTVYNQPFAESVSEPGkTFQDSEFDGILGLAYPSLAVdgvTPVFDNMMAQDLVEMPIFSVYMSANPdsslGGEVLFGGFD 238
gi 46395761  154 iLVQNQQFGESVSEPGsTFVDAEFDGILGLGYPSIAVgdcTPVFDNMIAQNLVELPMFSVYMSRNPnsavGGELVFGGFD 233
gi 46395759  154 iTVQSQTFAESVSEPGsTFQDSNFDGILGLAYPNLAVdncIPVFDNMIAQNLVELPLFGVYMNRDPnsadGGELVLGGFD 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                   #                                    
1TZS_A       185 HSHFsGSLNWVPVTkqaYWQIALDNIQVGGTVMFCseGCQAIVDTGTSLITGPSDKIKQLQNAIGAapvDGEYAVECANL 264
gi 118102416 239 PSRFlGTLHWVPVTqqgYWQIQLDNVQVGGTVAFCadGCQAIVDTGTSLLTGPTKDIKEMQRYIGAtamDGEYIVDCGRL 318
gi 46395761  234 ASRFsGQLNWVPVTnqgYWQIQLDNVQINGEVLFCsgGCQAIVDTGTSLITGPSSDIVQLQNIIGAsaaNGDYEVDCSVL 313
gi 46395759  234 TSRFsGQLNWVPITvqgYWQIQVDSIQVAGQVIFCsdGCQAIVDTGTSLITGPSGDIEQLQNYIGVtntNGEYGVSCSTL 313
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
Feature 1                                                                                    
1TZS_A       265 NVMPDVTFTINGVPYTLSPTAYtlldfvdgmqfCSSGFQGLDIHPPAGPLWILGDVFIRQFYSVFDRGNNRVGLAP 340
gi 118102416 319 SSMPIVTFTINGIPYVLSAQAYtlmeqsdgvdiCLSGFQGMDVPPPAGPLWILGDVFIRQYYSVFDRGNNRVGFAP 394
gi 46395761  314 NEMPTVTFTINGIGYQMTPQQYtlqd---gggvCSSGFQGLDIPPPAGPLWILGDVFIGQYYSVFDRGNNRVGLAP 386
gi 46395759  314 SLMPSVTFTINGLDYSLTPEQYmled---gggyCSSGFQGLDISPPSGPLWILGDVFIGQYYSVFDRGNNRVGFAP 386

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