Conserved Protein Domain Family
retropepsin_like_LTR_2

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cd05484: retropepsin_like_LTR_2 
Retropepsins_like_LTR, pepsin-like aspartate proteases.
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-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: 133151
View PSSM: cd05484
Aligned: 22 rows
Threshold Bit Score: 106.522
Threshold Setting Gi: 170052543
Created: 4-Apr-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 67625694   336 KYVTIFFdGKPVKLQVDTGSDITLISRETWIKIgrpr-yqpTCHNAKSASGTNITLLGvi---qLPLTFGEKt-MTGKCY 410
gi 156398425   50 WKAEIEVnGQPITFKLDNGAAVSVISDQEPLINsye--lvkPKEVLRGPGGSRLSVLGic--idTCLKAQGKe-MKETLY 124
gi 170028367  312 KFLTVSInGSQASLQFDTGSDITVISRKQWCDNldspplspTKQIARTASGKSLSLLGel---rCQVTLGGVt-ITGTFY 387
gi 76154930   174 KFVSLLVnGKPIRLQLDTASDITLISKNTWRKLgcpr-iqpTEHVARNASGDIVKLTGei---mCEVQFRKH--KFIDVC 247
gi 115941764  268 WSSSILVdGNETHFKLDTGAAVTVLSDSTPWLNkhi--mrpTTKRLRGPGSTVLTVIGqm---tSTLRHRDKq-IKETLY 341
gi 17534869   358 PSLRLNVeGQQIDFTFDTGSDITLISVQNWQKIgkph-lekVHHKICCANGTEIAVKGrv---lVWFKVKGV--EYTEYV 431
gi 170071491   38 KGAETAIyGVPLDLQLDSGSGITIISRQNWVNVgspp-tspPDCNVQTASGDKLGIEAmf---rATYTIGGTh-KESNCY 112
gi 1353154    291 HRMSVEVcGKDVAFQLDTGSMITLISVKCWEKLgspp-lekVPHRISCANGTPMAVKGr-----CLVKFKLKgiEYTEYV 364
gi 115736827  414 WGAYLQVdGNTTHFKLDSGAAVTVLSDGLQWLRgik--lkpANKRLCGPGKTKLEVLGqi---kAILQHKNRr-VSETVY 487
gi 156359453  164 WSVELLVnGNASDFKLDSGSKVTVVSDQTPWIKgmq--leeVKTEFRGPGGVKLSHLMkgqipnATFQAGDKa-QHENVY 240
                          90
                  ....*....|....*..
Feature 1                          
gi 67625694   411 VSgnc-htNLLGIDWID 426
gi 156398425  125 VIknq-lhSLLSRNACV 140
gi 170028367  388 VTdk--qiNLFGLDWIE 402
gi 76154930   248 YLtnrhdlDLLGLDWIE 264
gi 115941764  342 VVkdq-esSLLSRKACR 357
gi 17534869   432 YVwnr-nnNLLGTSWMR 447
gi 170071491  113 VCsadlslNVLGSDLMD 129
gi 1353154    365 YVrdr-qtNLLGTSWLN 380
gi 115736827  488 VVrnq-dcSLLSRKACE 503
gi 156359453  241 VMgnq-rnNLLSKCGTR 256

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