1B11,2I1A


Conserved Protein Domain Family
retropepsin_like

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cd00303: retropepsin_like 
Click on image for an interactive view with Cn3D
Retropepsins; pepsin-like aspartate proteases.
The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements, as well as eukaryotic dna-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. While fungal and mammalian pepsins are bilobal proteins with structurally related N and C-terminals, 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: 133136
View PSSM: cd00303
Aligned: 206 rows
Threshold Bit Score: 41.9384
Threshold Setting Gi: 74012205
Created: 6-Mar-2002
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 7 residues -Click on image for an interactive view with Cn3D
Feature 1:inhibitor binding site
Evidence:
  • Structure:1b11_a,Feline Immunodeficiency Virus Protease complexed with inhibitor Tl-3-093.
    View structure with Cn3D

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 ILIFVng--yPIKFLLDTGADITILNrrdfqvk----nsiengrQNMIGVg---gGKRGTny---inVHLEIrdenyktq 80
gi 119197289  535 APVTInq--qELMVLINTGSEINLLSqkytemlnl-lmenkpqvTMVVQTg---eVTSFYvfc--dkVSVQIrd------ 600
gi 116504666  637 FRAQLgg--iDVVCLVDCGSELNLFPekllerahlaldlegscwALKGVNg---gPVGLRgvckdvsLVIGGh------- 704
gi 162681116  492 TYVRLedfkdPILALVDHGSEINIMSrkiyeknkw-pidinhdwVIRVVNn---qQGVLHgacpavkTRIGDv------- 560
gi 71148689   700 VEGVFgg--eKVKFLLDSGSELNLVTrrvweqtgvpidedgkrwSLRGIGg---eSVSLLgcardapVQIGGk------- 767
gi 162673539  530 VKVRDie--ePIVALVDHGCEINLMSkdlykkqkw-pidmehgwAIRAANn---tWGESYgac--ldVKIRIgd-----v 596
gi 89179365    90 TFTKIgd--kNYKVIVDSGSCINAVSsamiaklglkvvshpnpyKVSWINdtalnVQERClv----pLQFSIy------- 156
gi 110288772  494 IFFVInn--hRARVIIDGGSCKNLLSsdlvkklglttrthphpyHIQWLNd---sGRAKVtqvcrvlFSIGSy------- 561
gi 56407688   407 GKCKIpg--aTCSFIIDGGSCTNVISedvvnamkiptiqhpqpyKLQWLNd---dGELKVhkqalisISIGKy------- 474
gi 110288772  973 TKFVVkd--rACRTIIVNESCNNFVSldlveklelltqpnpqpyYIKWFNs---cGKFKVnri--vrINFSIgd-----y 1040
                          90       100
                  ....*....|....*....|....*.
Feature 1                           #       
1B11_A         81 cIFGNVCVLedns-liqPLLGRDNMI 105
gi 119197289  601 iITHTLFLIfkgg-dqqLILGRPWQF 625
gi 116504666  705 nFDHYFFVSrddmethdCILGQPWIQ 730
gi 162681116  561 eVEQNFFVQnsa--typVILGQPYIT 584
gi 71148689   768 nFDHHFFVStrehgdydGILGQPWLD 793
gi 162673539  597 vTEQHFFVQhtt--sypLILGQPYIT 620
gi 89179365   157 kDKVWCDILkmd--vgqVILGRPWLF 180
gi 110288772  562 aDSVDCDVVpmq--acsLLLGCPWEH 585
gi 56407688   475 qDDVLCDVIpmh--achILLGRPWQY 498
gi 110288772 1041 hDTVNFDLVpmq--acsLLFGQPWVF 1064

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