Conserved Protein Domain Family
retropepsin_like_LTR_1

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cd05481: retropepsin_like_LTR_1 
Retropepsins_like_LTR; pepsin-like aspartate protease from retrotransposons with long terminal repeats.
Retropepsin of retrotransposons with long terminal repeats are pepsin-like aspartate proteases. 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: 133148
View PSSM: cd05481
Aligned: 29 rows
Threshold Bit Score: 68.8279
Threshold Setting Gi: 115695257
Created: 17-Jan-2008
Updated: 17-Jan-2013
Structure
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Aligned Rows:
 
catalytic motifCatalytic
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                         ###                                                             
gi 115700010  486 CPHKSGQ--HYLYLKIDSGASANTITVRTakqiygdkwrqvvkrTPVKLVAYGEISIPCVgt----ldIKCRYKSPe--- 556
gi 72077674   331 QEIIIDDd-VCVDFKLDSGAQVNILPENIfrktk-----lsldkTPVTLRSYSRHIMKPVgk----trCKVLVGKHe--- 397
gi 156342048   55 ASMQLRD--EQVKFQLDCGATVNILPIDKyvqifndpsharlkkTNKTLQMFNKTELKPIg------tVKIESVNPk--- 123
gi 115949104  302 VKLVVNN--RLVIFKLDTGAQTNLLPESVyqslip---rpklhpARVRLTGYSGVVIPVKgr----cyVQVEYKGLt--- 369
gi 115717985  305 AEMMIDD--NPVKFQIDSGATVNVIPKKYvksk--------idtRDAELRMYNETTLMAEg------rVKIILRNPknk- 367
gi 115685177  347 ARMMINE--KAVDFQVDSGASANILPLRHlegad-----yvlkpSKKKLMMWNEITMAIEg------vSRVKMLNPktk- 412
gi 72011027   234 AEMLVEN--RPANFQIDSGASVNVISKSLvpsae------divkENIILKMYNRSRLQAEg------rAKVVLRNTknn- 298
gi 115757350  193 AKFRINDe-DEIGMQVDCGATCNVIHLEDvpsgt------eltsTNQVLIVYGQGTVPVAg------kCKLHLRNVknn- 258
gi 115927375  226 AAFLIRG--NKISMQVDSGATCNVIPKRHvpdnv------einyGTRRLSLYGNKATVDGig-----vCNIVLKNPknh- 291
gi 170054925  311 WFEEAVIdnLKVKFKLDCGAQCNVLPLKVakritn----klqrsKTKYIVSYSGEKTKVEgdlttaanYKDTKSNTrgvt 386
                          90       100
                  ....*....|....*....|....*.
Feature 1                                   
gi 115700010  557 --wYTHTFYVAdvn-gpAILWLLGCT 579
gi 72077674   398 ---YLLTFQVVggy-gkPLIGRRDCE 419
gi 156342048  124 --nEDAILLVVnqg-hrPILGAQAIQ 146
gi 115949104  370 ---HNMAVLVTpgd-rqPLLGLQACE 391
gi 115717985  368 -kkYRVDFMVVkennrvPLLGRNTSE 392
gi 115685177  413 -qkYSVEFIVVdkd-ftPLLGSTVSQ 436
gi 72011027   299 -kkYRVNFIVVken-lvPLLSGPAAQ 322
gi 115757350  259 -krYLVPFVVVkgevtrPLLGASTGQ 283
gi 115927375  292 -rkYDVKFVVVhed-ctPLIGARMSQ 315
gi 170054925  387 lrfCRCWNHELra--stELVGASTEL 410

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