Conserved Protein Domain Family
HIV_retropepsin_like

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cd05482: HIV_retropepsin_like 
Click on image for an interactive view with Cn3D
Retropepsins, pepsin-like aspartate proteases.
This is a subfamily of retropepsins. The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.
Statistics
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PSSM-Id: 133149
View PSSM: cd05482
Aligned: 24 rows
Threshold Bit Score: 69.9877
Threshold Setting Gi: 118099614
Created: 3-Mar-2008
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 3 residues -Click on image for an interactive view with Cn3D
Feature 1:catalytic motif [active site]
Evidence:
  • Comment:conserved catalytic motif DT/SG of retropepsin.
  • Citation:PMID 7664111

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                           ###                                                           
1B11_A         13 ILIFVn----gYPIKFLLDTGADITILNrrdfqvk--------nsiengrQNMIGVgGGKRGTNyi----nVHLEIRden 76
gi 115634871  353 SSVNIc----gEELECILDSGAETSIIPssvyhgqleeklgnpkqmpgffLNVTGIgGVQLPIEgyv-evpIELEGQt-- 425
gi 212651     601 PVKQRs-----VYITALLDSGADITIISeedwptdw-------pvmeaanPQIHGIgGGIPMRKsrdmievGVINRDgsl 668
gi 20091614    26 VTLVNsvsnkkVNAYAYLDTGSDAVVVPrdlwlkl--------glemthrSNVSAVgGIVTAWYt-----rINLEFLen- 91
1YTG_A         11 VTIRIg----gQLKEALLDTGADDTVLEemnlp------------gkwkpKMIGGIgGFIKVRQyd----qIPVEICgh- 69
gi 118099614   64 CTLYYrn--qsIILTGLLDTGADTSIITpgewpse--------wplqsstTTVTGVgGVTLASRtp----mLTVEID--- 126
1Q9P_A         11 VTIKIg----gQLKEALLDTGADDTVIEemslp------------grwkpKMIGGIgGFIKVRQyd----qIIIEIAgh- 69
gi 5733984    567 PDFQGpr---sIFVTALIDSGADVTVVAetewpss---------wpaeasQSIMGVgGATPSRRstnevqaVVINRDgsl 634
gi 118088797   27 PQKEGpr---tTLFTALLDSGADVTVIAeadwptn--------wpftshwQHIGGVgGTVPTKGaae--kvEIAIIDrrg 93
gi 126331483  128 MSLFVe----dRVISGILDSGADISVISatdwpes--------weviephQKLVGI-GTPEHILqs---anSLSWSDse- 190
                          90       100       110
                  ....*....|....*....|....*....|....
Feature 1                                           
1B11_A         77 yktqcIFGNVCVLedn-----slIQPLLGRDNMI 105
gi 115634871  426 -----VLGSFLVAknrgngtsaqHSVLVGCNILH 454
gi 212651     669 --erpLLLFPAVAm--------vRGSILGRDCLQ 692
gi 20091614    92 ----kHRNIIAFYqd-------dGDVLIGRNILD 114
1YTG_A         70 ----kAIGTVLVGp--------tPVNIIGRNLLT 91
gi 118099614  127 -----GRRATAVFslal--lpptVSCLIGRDVLA 153
1Q9P_A         70 ----kAIGTVLVGp--------tPVNIIGRNLLT 91
gi 5733984    635 --ekpALLTPLVAr--------vPGTLLGRDFLR 658
gi 118088797   94 mmeapVLVQPLVAp--------vEGSILGRDFLT 119
gi 126331483  191 ----gHRGTFKPYvl------diAQSLWGREVMS 214

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