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P03367

- POL_HV1BR

UniProt

P03367 - POL_HV1BR

Protein

Gag-Pol polyprotein

Gene

gag-pol

Organism
Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 176 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shutt off translation By similarity.By similarity
    Matrix protein p17 has two main functions: in infected cell, it targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. The second function is to play a role in nuclear localization of the viral genome at the very start of cell infection. Matrix protein is the part of the pre-integration complex. It binds in the cytoplasm the human BAF protein which prevent autointegration of the viral genome, and might be included in virions at the ration of zero to 3 BAF dimer per virion. The myristoylation signal and the NLS thus exert conflicting influences its subcellular localization. The key regulation of these motifs might be phosphorylation of a portion of MA molecules on the C-terminal tyrosine at the time of virus maturation, by virion-associated cellular tyrosine kinase. Implicated in the release from host cell mediated by Vpu By similarity.By similarity
    Capsid protein p24 forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry. Interaction with human PPIA/CYPA protects the virus from restriction by human TRIM5-alpha and from an unknown antiviral activity in human cells. This capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species By similarity.By similarity
    Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. Facilitates rearangement of nucleic acid secondary structure during retrotranscription of genomic RNA. This capability is referred to as nucleic acid chaperone activity By similarity.By similarity
    The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response By similarity.PROSITE-ProRule annotation
    Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends By similarity.By similarity
    Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration By similarity.By similarity

    Catalytic activityi

    Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.PROSITE-ProRule annotation
    Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
    3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.
    Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).PROSITE-ProRule annotation

    Cofactori

    Binds 2 magnesium ions for reverse transcriptase polymerase activity.By similarity
    Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding By similarity.By similarity
    Magnesium ions for integrase activity. Binds at least 1, maybe 2 magnesium ions By similarity.By similarity

    Enzyme regulationi

    The viral protease is inhibited by many synthetic protease inhibitors (PIs), such as amprenavir, atazanavir, indinavir, loprinavir, nelfinavir, ritonavir and saquinavir. RT can be inhibited either by nucleoside RT inhibitors (NRTIs) or by non nucleoside RT inhibitors (NNRTIs). NRTIs act as chain terminators, whereas NNRTIs inhibit DNA polymerization by binding a small hydrophobic pocket near the RT active site and inducing an allosteric change in this region. Classical NRTIs are abacavir, adefovir (PMEA), didanosine (ddI), lamivudine (3TC), stavudine (d4T), tenofovir (PMPA), zalcitabine (ddC), and zidovudine (AZT). Classical NNRTIs are atevirdine (BHAP U-87201E), delavirdine, efavirenz (DMP-266), emivirine (I-EBU), and nevirapine (BI-RG-587). The tritherapies used as a basic effective treatment of AIDS associate two NRTIs and one NNRTI. Use of protease inhibitors in tritherapy regimens permit more ambitious therapeutic strategies By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei132 – 1332Cleavage; by viral proteaseBy similarity
    Sitei221 – 2222Cis/trans isomerization of proline peptide bond; by human PPIA/CYPABy similarity
    Sitei363 – 3642Cleavage; by viral proteaseBy similarity
    Sitei377 – 3782Cleavage; by viral proteaseBy similarity
    Sitei432 – 4332Cleavage; by viral proteaseSequence Analysis
    Sitei440 – 4412Cleavage; by viral proteaseBy similarity
    Sitei500 – 5012Cleavage; by viral proteaseBy similarity
    Active sitei525 – 5251For protease activity; shared with dimeric partnerPROSITE-ProRule annotation
    Sitei599 – 6002Cleavage; by viral proteaseBy similarity
    Metal bindingi709 – 7091Magnesium; catalytic; for reverse transcriptase activityBy similarity
    Metal bindingi784 – 7841Magnesium; catalytic; for reverse transcriptase activityBy similarity
    Metal bindingi785 – 7851Magnesium; catalytic; for reverse transcriptase activityBy similarity
    Sitei1000 – 10001Essential for RT p66/p51 heterodimerizationBy similarity
    Sitei1013 – 10131Essential for RT p66/p51 heterodimerizationBy similarity
    Sitei1039 – 10402Cleavage; by viral protease; partialBy similarity
    Metal bindingi1042 – 10421Magnesium; catalytic; for RNase H activityBy similarity
    Metal bindingi1077 – 10771Magnesium; catalytic; for RNase H activityBy similarity
    Metal bindingi1097 – 10971Magnesium; catalytic; for RNase H activityBy similarity
    Metal bindingi1148 – 11481Magnesium; catalytic; for RNase H activityBy similarity
    Sitei1159 – 11602Cleavage; by viral proteaseBy similarity
    Metal bindingi1223 – 12231Magnesium; catalytic; for integrase activityBy similarity
    Metal bindingi1275 – 12751Magnesium; catalytic; for integrase activityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri390 – 40718CCHC-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri411 – 42818CCHC-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1162 – 120342Integrase-typePROSITE-ProRule annotationAdd
    BLAST
    DNA bindingi1382 – 142948Integrase-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. DNA-directed DNA polymerase activity Source: UniProtKB-KW
    4. exoribonuclease H activity Source: UniProtKB-EC
    5. RNA binding Source: UniProtKB-KW
    6. RNA-directed DNA polymerase activity Source: UniProtKB-KW
    7. RNA-DNA hybrid ribonuclease activity Source: InterPro
    8. structural molecule activity Source: InterPro
    9. zinc ion binding Source: InterPro

    GO - Biological processi

    1. DNA integration Source: UniProtKB-KW
    2. DNA recombination Source: UniProtKB-KW
    3. establishment of integrated proviral latency Source: UniProtKB-KW
    4. induction by virus of host cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB-KW
    5. suppression by virus of host gene expression Source: UniProtKB-KW
    6. viral entry into host cell Source: UniProtKB-KW
    7. viral penetration into host nucleus Source: UniProtKB-KW
    8. viral release from host cell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aspartyl protease, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-directed DNA polymerase, Transferase

    Keywords - Biological processi

    Activation of host caspases by virus, DNA integration, DNA recombination, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Modulation of host cell apoptosis by virus, Viral genome integration, Viral penetration into host nucleus, Virion maturation, Virus entry into host cell, Virus exit from host cell

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding, RNA-binding, Viral nucleoprotein, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gag-Pol polyprotein
    Alternative name(s):
    Pr160Gag-Pol
    Cleaved into the following 11 chains:
    Matrix protein p17
    Short name:
    MA
    Capsid protein p24
    Short name:
    CA
    Transframe peptide
    Short name:
    TF
    p6-pol
    Short name:
    p6*
    Alternative name(s):
    PR
    Retropepsin
    Alternative name(s):
    Exoribonuclease H (EC:3.1.13.2)
    p66 RT
    Integrase
    Short name:
    IN
    Gene namesi
    Name:gag-pol
    OrganismiHuman immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1)
    Taxonomic identifieri11686 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007692: Genome

    Subcellular locationi

    Chain Matrix protein p17 : Virion Curated. Host nucleus By similarity. Host cytoplasm By similarity. Host cell membrane Curated; Lipid-anchor Curated
    Note: Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane By similarity.By similarity
    Chain Integrase : Virion Curated. Host nucleus Curated. Host cytoplasm Curated
    Note: Nuclear at initial phase, cytoplasmic at assembly.Curated

    GO - Cellular componenti

    1. host cell cytoplasm Source: UniProtKB-SubCell
    2. host cell nucleus Source: UniProtKB-SubCell
    3. host cell plasma membrane Source: UniProtKB-SubCell
    4. intracellular Source: GOC
    5. membrane Source: UniProtKB-KW
    6. viral nucleocapsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Host cell membrane, Host cytoplasm, Host membrane, Host nucleus, Membrane, Virion

    Pathology & Biotechi

    Keywords - Diseasei

    AIDS

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by hostBy similarity
    Chaini2 – 14471446Gag-Pol polyproteinPRO_0000261264Add
    BLAST
    Chaini2 – 132131Matrix protein p17By similarityPRO_0000042330Add
    BLAST
    Chaini133 – 363231Capsid protein p24By similarityPRO_0000042331Add
    BLAST
    Peptidei364 – 37714Spacer peptide p2By similarityPRO_0000042332Add
    BLAST
    Chaini378 – 43255Nucleocapsid protein p7By similarityPRO_0000042333Add
    BLAST
    Peptidei433 – 4408Transframe peptideSequence AnalysisPRO_0000246712
    Chaini441 – 50060p6-polSequence AnalysisPRO_0000042334Add
    BLAST
    Chaini501 – 59999ProteaseBy similarityPRO_0000038652Add
    BLAST
    Chaini600 – 1159560Reverse transcriptase/ribonuclease HBy similarityPRO_0000042335Add
    BLAST
    Chaini600 – 1039440p51 RTBy similarityPRO_0000042336Add
    BLAST
    Chaini1040 – 1159120p15By similarityPRO_0000042337Add
    BLAST
    Chaini1160 – 1447288IntegraseBy similarityPRO_0000042338Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
    Modified residuei132 – 1321Phosphotyrosine; by hostBy similarity

    Post-translational modificationi

    Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. Nucleocapsid protein p7 might be further cleaved after virus entry By similarity.PROSITE-ProRule annotation
    Capsid protein p24 is phosphorylated.By similarity
    Matrix protein p17 is tyrosine phosphorylated presumably in the virion by a host kinase. This modification targets the matrix protein to the nucleus By similarity.By similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein

    Interactioni

    Subunit structurei

    Pre-integration complex interacts with human HMGA1. Matrix protein p17 is a trimer. Interacts with gp120 and human BAF. Capsid is a homodimer. Interacts with human PPIA/CYPA. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues. The reverse transcriptase is a heterodimer of p66 RT and p51 RT (RT p66/p51). Heterodimerization of RT is essential for DNA polymerase activity. Despite the sequence identities, p66 RT and p51 RT have distinct folding. Integrase is a homodimer and possibly can form homotetramer. Integrase interacts with human SMARCB1/INI1 and human PSIP1/LEDGF isoform 1 Integrase interacts with human KPNA3; this interaction might play a role in nuclear import of the pre-integration complex. Integrase interacts with human NUP153; this interaction might play a role in nuclear import of the pre-integration complex By similarity.By similarity

    Protein-protein interaction databases

    MINTiMINT-1506499.

    Structurei

    Secondary structure

    1
    1447
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi502 – 5043
    Beta strandi505 – 5073
    Beta strandi510 – 5156
    Beta strandi518 – 5247
    Beta strandi529 – 5335
    Beta strandi542 – 5498
    Beta strandi552 – 56615
    Beta strandi569 – 57810
    Beta strandi581 – 5855
    Helixi587 – 5904
    Turni591 – 5944
    Beta strandi596 – 5983
    Helixi627 – 64216
    Beta strandi645 – 6484
    Beta strandi659 – 6635
    Beta strandi668 – 6747
    Helixi677 – 6826
    Turni697 – 7015
    Beta strandi702 – 7098
    Helixi711 – 7166
    Helixi721 – 7244
    Helixi725 – 7273
    Beta strandi729 – 7313
    Helixi734 – 7363
    Beta strandi741 – 7477
    Helixi754 – 7585
    Helixi760 – 77314
    Beta strandi777 – 7826
    Beta strandi785 – 7906
    Helixi794 – 80916
    Helixi828 – 8303
    Turni835 – 8373
    Beta strandi849 – 8524
    Helixi853 – 86614
    Turni867 – 8693
    Helixi876 – 8816
    Helixi896 – 90914
    Beta strandi926 – 9283
    Beta strandi935 – 94511
    Beta strandi947 – 9548
    Helixi963 – 98220
    Beta strandi987 – 9926
    Helixi994 – 10007
    Helixi1001 – 10033
    Beta strandi1012 – 10154
    Helixi1020 – 10245
    Beta strandi1352 – 136110
    Helixi1370 – 13734
    Turni1374 – 13774

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A8GX-ray2.50A/B501-599[»]
    1A8KX-ray2.00A/B/D/E501-599[»]
    1A94X-ray2.00A/B/D/E501-599[»]
    1AAQX-ray2.50A/B501-599[»]
    1D4SX-ray2.50A/B501-599[»]
    1D4YX-ray1.97A/B501-599[»]
    1DAZX-ray1.55C/D501-1378[»]
    1DIFX-ray1.70A/B501-599[»]
    1FQXX-ray3.10A/B501-599[»]
    1HHPX-ray2.70A501-599[»]
    1HNIX-ray2.80B600-1025[»]
    1HPOX-ray2.50A/B501-599[»]
    1HPXX-ray2.00A/B501-599[»]
    1HSGX-ray2.00A/B501-599[»]
    1HVLX-ray1.80A/B501-599[»]
    1IIQX-ray1.83A/B501-599[»]
    1IZIX-ray2.15A/B501-599[»]
    1LZQX-ray2.20A/B501-599[»]
    1M0BX-ray2.45A/B501-599[»]
    1MRWX-ray2.00A/B501-599[»]
    1MRXX-ray2.00A/B501-599[»]
    1MSMX-ray2.00A/B501-599[»]
    1MSNX-ray2.00A/B501-599[»]
    1NH0X-ray1.03A/B501-599[»]
    1RL8X-ray2.00A/B501-599[»]
    1SDTX-ray1.30A/B501-599[»]
    1SDUX-ray1.25A/B501-599[»]
    1SDVX-ray1.40A/B501-599[»]
    1SGUX-ray1.90A/B501-599[»]
    1SH9X-ray2.50A/B501-599[»]
    1SP5X-ray1.80A/B501-599[»]
    I559-563[»]
    1U8GX-ray2.20A/B501-599[»]
    1UPJX-ray2.22A501-599[»]
    1XL2X-ray1.50A/B501-599[»]
    1XL5X-ray1.73A/B501-599[»]
    1Z8CX-ray2.20A/B501-599[»]
    1ZBGX-ray2.00A/B501-599[»]
    1ZJ7X-ray1.93A501-599[»]
    1ZLFX-ray2.30A/B501-599[»]
    1ZPKX-ray1.65A/B501-599[»]
    1ZTZX-ray2.15A/B501-599[»]
    2A1EX-ray1.30A/B501-599[»]
    2AZ8X-ray2.00A501-599[»]
    2AZ9X-ray2.50A501-599[»]
    2AZBX-ray2.03A501-599[»]
    2AZCX-ray2.01A/B501-599[»]
    2B7ZX-ray2.20A/B501-599[»]
    2BB9X-ray1.35A/B501-599[»]
    2FDEX-ray2.70A/B501-599[»]
    2FNDmodel-P501-599[»]
    2HB2X-ray2.30A501-598[»]
    2HB4X-ray2.15A501-598[»]
    2HC0X-ray1.30A/B501-598[»]
    2HNDX-ray2.50B606-1027[»]
    2HNYX-ray2.50B606-1027[»]
    2IENX-ray1.30A/B501-599[»]
    2O4KX-ray1.60A/B501-599[»]
    2O4LX-ray1.33A/B501-599[»]
    2O4NX-ray2.00A/B501-599[»]
    2O4PX-ray1.80A/B501-598[»]
    2O4SX-ray1.54A/B501-599[»]
    2P3BX-ray2.10A/B501-599[»]
    2PK5X-ray1.90A/B501-599[»]
    2PK6X-ray1.45A/B501-599[»]
    2PQZX-ray1.55A/B501-599[»]
    2PWCX-ray1.78A/B501-599[»]
    2PWRX-ray1.50A/B501-599[»]
    2PYMX-ray1.90A/B501-599[»]
    2PYNX-ray1.85A/B501-599[»]
    2Q63X-ray2.20A/B501-599[»]
    2Q64X-ray2.50A/B501-599[»]
    2QAKX-ray2.20A/B501-599[»]
    2QCIX-ray1.20A/B501-599[»]
    2QD6X-ray1.28A/B501-599[»]
    2QD7X-ray1.11A/B501-599[»]
    2QD8X-ray1.35A/B501-599[»]
    2QHCX-ray2.80A/B501-599[»]
    2QNNX-ray1.48A/B501-599[»]
    2QNPX-ray1.41A/B501-599[»]
    2QNQX-ray2.30A/B501-599[»]
    2R43X-ray1.58A/B501-599[»]
    2UPJX-ray3.00A/B501-599[»]
    2Z4OX-ray1.60A/B501-599[»]
    2ZGAX-ray1.65A501-599[»]
    2ZYEneutron diffraction1.90A/B501-599[»]
    3A2OX-ray0.88A/B501-599[»]
    3BHEX-ray1.75A/B501-599[»]
    3BVAX-ray1.05A/B501-599[»]
    3BVBX-ray1.30A/B501-599[»]
    3CKTX-ray1.65A/B501-599[»]
    3DJKX-ray1.00A/B501-599[»]
    3DK1X-ray1.07A/B501-599[»]
    3FX5X-ray0.93A/B501-599[»]
    3GGUX-ray1.80A/B501-599[»]
    3H5BX-ray1.29A/B501-599[»]
    3I6OX-ray1.17A/B501-599[»]
    3I8WX-ray1.70A501-599[»]
    3JVWX-ray1.80A/B501-599[»]
    3JVYX-ray1.60A/B501-599[»]
    3JW2X-ray1.80A/B501-599[»]
    3KDBX-ray1.66A/B501-599[»]
    3KDCX-ray2.20A/B501-599[»]
    3KDDX-ray1.80A/B501-599[»]
    3NDUX-ray1.25A/B/C/D501-599[»]
    3NDWX-ray1.14A/B501-599[»]
    3NDXX-ray1.03A/B501-599[»]
    3NLSX-ray1.70A/B501-599[»]
    3PWMX-ray1.46A/B501-599[»]
    3PWRX-ray1.45A/B501-599[»]
    3QBFX-ray1.45A/B501-599[»]
    3QIHX-ray1.39A/B501-599[»]
    3QN8X-ray1.38A/B501-599[»]
    3QP0X-ray1.45A/B501-599[»]
    3QPJX-ray1.61A/B501-599[»]
    3QRMX-ray1.73A/B501-599[»]
    3QROX-ray1.62A/B501-599[»]
    3QRSX-ray1.59A/B501-599[»]
    3ST5X-ray1.45A/B501-599[»]
    3T11X-ray2.22A/B501-599[»]
    3T3CX-ray2.10A/B501-599[»]
    3TOFX-ray1.45A/B501-599[»]
    3TOGX-ray1.24A/B/C/D501-599[»]
    3TOHX-ray1.12A/B501-599[»]
    3TTPX-ray2.23A/B501-599[»]
    3U7SX-ray2.05A/B501-599[»]
    3UCBX-ray1.38A/B501-599[»]
    3UF3X-ray1.63A/B501-599[»]
    3UFNX-ray1.45A/B501-599[»]
    3UHLX-ray2.20A/B/C/D501-599[»]
    3VF5X-ray1.25A/B501-599[»]
    3VF7X-ray1.30A/B501-599[»]
    3VFBX-ray1.55A/B501-599[»]
    4DFGX-ray1.23A/B501-599[»]
    4FAFX-ray2.10D361-367[»]
    4FE6X-ray2.00A501-599[»]
    4FL8X-ray1.20A/B501-599[»]
    4FLGX-ray1.31A/B501-599[»]
    4FM6X-ray1.40A/B501-599[»]
    4GB2X-ray1.79A/B501-599[»]
    4HDBX-ray1.49A/B501-599[»]
    4HDFX-ray1.29A/B501-599[»]
    4HDPX-ray1.22A/B501-599[»]
    4HE9X-ray1.06A/B501-599[»]
    4HEGX-ray1.46A/B501-599[»]
    4HLAX-ray1.95A/B501-599[»]
    4J54X-ray1.55A/B501-599[»]
    4J55X-ray1.31A/B501-599[»]
    4J5JX-ray1.80A/B501-599[»]
    4JECOther2.00A/B501-599[»]
    4LL3X-ray1.95A/B501-599[»]
    7UPJX-ray2.00A/B501-599[»]
    ProteinModelPortaliP03367.
    SMRiP03367. Positions 1-432, 501-1156, 1160-1429.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03367.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini520 – 58970Peptidase A2PROSITE-ProRule annotationAdd
    BLAST
    Domaini643 – 833191Reverse transcriptasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1033 – 1156124RNase HPROSITE-ProRule annotationAdd
    BLAST
    Domaini1213 – 1363151Integrase catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni826 – 8349RT 'primer grip'By similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi16 – 227Nuclear export signalBy similarity
    Motifi26 – 327Nuclear localization signalBy similarity
    Motifi997 – 101317Tryptophan repeat motifBy similarityAdd
    BLAST

    Domaini

    The reverse transcriptase/ribonuclease H (RT) is structured in five subdomains: finger, palm, thumb, connection and RNase H. Within the palm subdomain, the 'primer grip' region is thought to be involved in the positioning of the primer terminus for accommodating the incoming nucleotide. The RNase H domain stabilizes the association of RT with primer-template By similarity.By similarity
    The tryptophan repeat motif is involved in RT p66/p51 dimerization.By similarity
    Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein By similarity.By similarity

    Sequence similaritiesi

    Contains 2 CCHC-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 integrase catalytic domain.PROSITE-ProRule annotation
    Contains 1 integrase-type DNA-binding domain.PROSITE-ProRule annotation
    Contains 1 integrase-type zinc finger.PROSITE-ProRule annotation
    Contains 1 peptidase A2 domain.PROSITE-ProRule annotation
    Contains 1 reverse transcriptase domain.PROSITE-ProRule annotation
    Contains 1 RNase H domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri390 – 40718CCHC-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri411 – 42818CCHC-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1162 – 120342Integrase-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Family and domain databases

    Gene3Di1.10.10.200. 1 hit.
    1.10.1200.30. 1 hit.
    1.10.150.90. 1 hit.
    1.10.375.10. 1 hit.
    2.30.30.10. 1 hit.
    2.40.70.10. 1 hit.
    3.30.420.10. 2 hits.
    4.10.60.10. 1 hit.
    InterProiIPR001969. Aspartic_peptidase_AS.
    IPR000721. Gag_p24.
    IPR001037. Integrase_C_retrovir.
    IPR001584. Integrase_cat-core.
    IPR017856. Integrase_Zn-bd_dom-like_N.
    IPR003308. Integrase_Zn-bd_dom_N.
    IPR000071. Lentvrl_matrix_N.
    IPR012344. Matrix_N_HIV/RSV.
    IPR018061. Pept_A2A_retrovirus_sg.
    IPR001995. Peptidase_A2_cat.
    IPR021109. Peptidase_aspartic_dom.
    IPR008916. Retrov_capsid_C.
    IPR008919. Retrov_capsid_N.
    IPR010999. Retrovr_matrix_N.
    IPR012337. RNaseH-like_dom.
    IPR002156. RNaseH_domain.
    IPR000477. RT_dom.
    IPR010659. RVT_connect.
    IPR010661. RVT_thumb.
    IPR001878. Znf_CCHC.
    [Graphical view]
    PfamiPF00540. Gag_p17. 1 hit.
    PF00607. Gag_p24. 1 hit.
    PF00552. IN_DBD_C. 1 hit.
    PF02022. Integrase_Zn. 1 hit.
    PF00075. RNase_H. 1 hit.
    PF00665. rve. 1 hit.
    PF00077. RVP. 1 hit.
    PF00078. RVT_1. 1 hit.
    PF06815. RVT_connect. 1 hit.
    PF06817. RVT_thumb. 1 hit.
    PF00098. zf-CCHC. 2 hits.
    [Graphical view]
    PRINTSiPR00234. HIV1MATRIX.
    SMARTiSM00343. ZnF_C2HC. 2 hits.
    [Graphical view]
    SUPFAMiSSF46919. SSF46919. 1 hit.
    SSF47353. SSF47353. 1 hit.
    SSF47836. SSF47836. 1 hit.
    SSF47943. SSF47943. 1 hit.
    SSF50122. SSF50122. 1 hit.
    SSF50630. SSF50630. 1 hit.
    SSF53098. SSF53098. 2 hits.
    SSF57756. SSF57756. 1 hit.
    PROSITEiPS50175. ASP_PROT_RETROV. 1 hit.
    PS00141. ASP_PROTEASE. 1 hit.
    PS50994. INTEGRASE. 1 hit.
    PS51027. INTEGRASE_DBD. 1 hit.
    PS50879. RNASE_H. 1 hit.
    PS50878. RT_POL. 1 hit.
    PS50158. ZF_CCHC. 2 hits.
    PS50876. ZF_INTEGRASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by ribosomal frameshifting. Align

    Note: Translation results in the formation of the Gag polyprotein most of the time. Ribosomal frameshifting at the gag-pol genes boundary occurs at low frequency and produces the Gag-Pol polyprotein. This strategy of translation probably allows the virus to modulate the quantity of each viral protein. Maintenance of a correct Gag to Gag-Pol ratio is essential for RNA dimerization and viral infectivity.

    Isoform Gag-Pol polyprotein (identifier: P03367-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGARASVLSG GELDRWEKIR LRPGGKKKYK LKHIVWASRE LERFAVNPGL     50
    LETSEGCRQI LGQLQPSLQT GSEELRSLYN TVATLYCVHQ RIEIKDTKEA 100
    LDKIEEEQNK SKKKAQQAAA DTGHSSQVSQ NYPIVQNIQG QMVHQAISPR 150
    TLNAWVKVVE EKAFSPEVIP MFSALSEGAT PQDLNTMLNT VGGHQAAMQM 200
    LKETINEEAA EWDRVHPVHA GPIAPGQMRE PRGSDIAGTT STLQEQIGWM 250
    TNNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF 300
    YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPA ATLEEMMTAC 350
    QGVGGPGHKA RVLAEAMSQV TNSATIMMQR GNFRNQRKIV KCFNCGKEGH 400
    IARNCRAPRK KGCWKCGKEG HQMKDCTERQ ANFLREDLAF LQGKAREFSS 450
    EQTRANSPTI SSEQTRANSP TRRELQVWGR DNNSLSEAGA DRQGTVSFNF 500
    PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEEMSLPG RWKPKMIGGI 550
    GGFIKVRQYD QILIEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNFP 600
    ISPIETVPVK LKPGMDGPKV KQWPLTEEKI KALVEICTEM EKEGKISKIG 650
    PENPYNTPVF AIKKKDSTKW RKLVDFRELN KRTQDFWEVQ LGIPHPAGLK 700
    KKKSVTVLDV GDAYFSVPLD EDFRKYTAFT IPSINNETPG IRYQYNVLPQ 750
    GWKGSPAIFQ SSMTKILEPF RKQNPDIVIY QYMDDLYVGS DLEIGQHRTK 800
    IEELRQHLLR WGLTTPDKKH QKEPPFLWMG YELHPDKWTV QPIVLPEKDS 850
    WTVNDIQKLV GKLNWASQIY PGIKVRQLCK LLRGTKALTE VIPLTEEAEL 900
    ELAENREILK EPVHGVYYDP SKDLIAEIQK QGQGQWTYQI YQEPFKNLKT 950
    GKYARTRGAH TNDVKQLTEA VQKITTESIV IWGKTPKFKL PIQKETWETW 1000
    WTEYWQATWI PEWEFVNTPP LVKLWYQLEK EPIVGAETFY VDGAASRETK 1050
    LGKAGYVTNR GRQKVVTLTD TTNQKTELQA IHLALQDSGL EVNIVTDSQY 1100
    ALGIIQAQPD KSESELVNQI IEQLIKKEKV YLAWVPAHKG IGGNEQVDKL 1150
    VSAGIRKVLF LDGIDKAQDE HEKYHSNWRA MASDFNLPPV VAKEIVASCD 1200
    KCQLKGEAMH GQVDCSPGIW QLDCTHLEGK VILVAVHVAS GYIEAEVIPA 1250
    ETGQETAYFL LKLAGRWPVK TIHTDNGSNF TSTTVKAACW WAGIKQEFGI 1300
    PYNPQSQGVV ESMNKELKKI IGQVRDQAEH LKTAVQMAVF IHNFKRKGGI 1350
    GGYSAGERIV DIIATDIQTK ELQKQITKIQ NFRVYYRDSR DPLWKGPAKL 1400
    LWKGEGAVVI QDNSDIKVVP RRKAKIIRDY GKQMAGDDCV ASRQDED 1447

    Note: Produced by -1 ribosomal frameshifting.

    Length:1,447
    Mass (Da):163,279
    Last modified:January 23, 2007 - v3
    Checksum:iB41D8D00F0940740
    GO
    Isoform Gag polyprotein (identifier: P03348-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry P03348.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Produced by conventional translation.

    Length:512
    Mass (Da):57,226
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02013 Genomic RNA. No translation available.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Web resourcesi

    HIV drug resistance mutations
    hivdb

    HIV drug resistance database

    BioAfrica: HIV bioinformatics in Africa

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02013 Genomic RNA. No translation available.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A8G X-ray 2.50 A/B 501-599 [» ]
    1A8K X-ray 2.00 A/B/D/E 501-599 [» ]
    1A94 X-ray 2.00 A/B/D/E 501-599 [» ]
    1AAQ X-ray 2.50 A/B 501-599 [» ]
    1D4S X-ray 2.50 A/B 501-599 [» ]
    1D4Y X-ray 1.97 A/B 501-599 [» ]
    1DAZ X-ray 1.55 C/D 501-1378 [» ]
    1DIF X-ray 1.70 A/B 501-599 [» ]
    1FQX X-ray 3.10 A/B 501-599 [» ]
    1HHP X-ray 2.70 A 501-599 [» ]
    1HNI X-ray 2.80 B 600-1025 [» ]
    1HPO X-ray 2.50 A/B 501-599 [» ]
    1HPX X-ray 2.00 A/B 501-599 [» ]
    1HSG X-ray 2.00 A/B 501-599 [» ]
    1HVL X-ray 1.80 A/B 501-599 [» ]
    1IIQ X-ray 1.83 A/B 501-599 [» ]
    1IZI X-ray 2.15 A/B 501-599 [» ]
    1LZQ X-ray 2.20 A/B 501-599 [» ]
    1M0B X-ray 2.45 A/B 501-599 [» ]
    1MRW X-ray 2.00 A/B 501-599 [» ]
    1MRX X-ray 2.00 A/B 501-599 [» ]
    1MSM X-ray 2.00 A/B 501-599 [» ]
    1MSN X-ray 2.00 A/B 501-599 [» ]
    1NH0 X-ray 1.03 A/B 501-599 [» ]
    1RL8 X-ray 2.00 A/B 501-599 [» ]
    1SDT X-ray 1.30 A/B 501-599 [» ]
    1SDU X-ray 1.25 A/B 501-599 [» ]
    1SDV X-ray 1.40 A/B 501-599 [» ]
    1SGU X-ray 1.90 A/B 501-599 [» ]
    1SH9 X-ray 2.50 A/B 501-599 [» ]
    1SP5 X-ray 1.80 A/B 501-599 [» ]
    I 559-563 [» ]
    1U8G X-ray 2.20 A/B 501-599 [» ]
    1UPJ X-ray 2.22 A 501-599 [» ]
    1XL2 X-ray 1.50 A/B 501-599 [» ]
    1XL5 X-ray 1.73 A/B 501-599 [» ]
    1Z8C X-ray 2.20 A/B 501-599 [» ]
    1ZBG X-ray 2.00 A/B 501-599 [» ]
    1ZJ7 X-ray 1.93 A 501-599 [» ]
    1ZLF X-ray 2.30 A/B 501-599 [» ]
    1ZPK X-ray 1.65 A/B 501-599 [» ]
    1ZTZ X-ray 2.15 A/B 501-599 [» ]
    2A1E X-ray 1.30 A/B 501-599 [» ]
    2AZ8 X-ray 2.00 A 501-599 [» ]
    2AZ9 X-ray 2.50 A 501-599 [» ]
    2AZB X-ray 2.03 A 501-599 [» ]
    2AZC X-ray 2.01 A/B 501-599 [» ]
    2B7Z X-ray 2.20 A/B 501-599 [» ]
    2BB9 X-ray 1.35 A/B 501-599 [» ]
    2FDE X-ray 2.70 A/B 501-599 [» ]
    2FND model - P 501-599 [» ]
    2HB2 X-ray 2.30 A 501-598 [» ]
    2HB4 X-ray 2.15 A 501-598 [» ]
    2HC0 X-ray 1.30 A/B 501-598 [» ]
    2HND X-ray 2.50 B 606-1027 [» ]
    2HNY X-ray 2.50 B 606-1027 [» ]
    2IEN X-ray 1.30 A/B 501-599 [» ]
    2O4K X-ray 1.60 A/B 501-599 [» ]
    2O4L X-ray 1.33 A/B 501-599 [» ]
    2O4N X-ray 2.00 A/B 501-599 [» ]
    2O4P X-ray 1.80 A/B 501-598 [» ]
    2O4S X-ray 1.54 A/B 501-599 [» ]
    2P3B X-ray 2.10 A/B 501-599 [» ]
    2PK5 X-ray 1.90 A/B 501-599 [» ]
    2PK6 X-ray 1.45 A/B 501-599 [» ]
    2PQZ X-ray 1.55 A/B 501-599 [» ]
    2PWC X-ray 1.78 A/B 501-599 [» ]
    2PWR X-ray 1.50 A/B 501-599 [» ]
    2PYM X-ray 1.90 A/B 501-599 [» ]
    2PYN X-ray 1.85 A/B 501-599 [» ]
    2Q63 X-ray 2.20 A/B 501-599 [» ]
    2Q64 X-ray 2.50 A/B 501-599 [» ]
    2QAK X-ray 2.20 A/B 501-599 [» ]
    2QCI X-ray 1.20 A/B 501-599 [» ]
    2QD6 X-ray 1.28 A/B 501-599 [» ]
    2QD7 X-ray 1.11 A/B 501-599 [» ]
    2QD8 X-ray 1.35 A/B 501-599 [» ]
    2QHC X-ray 2.80 A/B 501-599 [» ]
    2QNN X-ray 1.48 A/B 501-599 [» ]
    2QNP X-ray 1.41 A/B 501-599 [» ]
    2QNQ X-ray 2.30 A/B 501-599 [» ]
    2R43 X-ray 1.58 A/B 501-599 [» ]
    2UPJ X-ray 3.00 A/B 501-599 [» ]
    2Z4O X-ray 1.60 A/B 501-599 [» ]
    2ZGA X-ray 1.65 A 501-599 [» ]
    2ZYE neutron diffraction 1.90 A/B 501-599 [» ]
    3A2O X-ray 0.88 A/B 501-599 [» ]
    3BHE X-ray 1.75 A/B 501-599 [» ]
    3BVA X-ray 1.05 A/B 501-599 [» ]
    3BVB X-ray 1.30 A/B 501-599 [» ]
    3CKT X-ray 1.65 A/B 501-599 [» ]
    3DJK X-ray 1.00 A/B 501-599 [» ]
    3DK1 X-ray 1.07 A/B 501-599 [» ]
    3FX5 X-ray 0.93 A/B 501-599 [» ]
    3GGU X-ray 1.80 A/B 501-599 [» ]
    3H5B X-ray 1.29 A/B 501-599 [» ]
    3I6O X-ray 1.17 A/B 501-599 [» ]
    3I8W X-ray 1.70 A 501-599 [» ]
    3JVW X-ray 1.80 A/B 501-599 [» ]
    3JVY X-ray 1.60 A/B 501-599 [» ]
    3JW2 X-ray 1.80 A/B 501-599 [» ]
    3KDB X-ray 1.66 A/B 501-599 [» ]
    3KDC X-ray 2.20 A/B 501-599 [» ]
    3KDD X-ray 1.80 A/B 501-599 [» ]
    3NDU X-ray 1.25 A/B/C/D 501-599 [» ]
    3NDW X-ray 1.14 A/B 501-599 [» ]
    3NDX X-ray 1.03 A/B 501-599 [» ]
    3NLS X-ray 1.70 A/B 501-599 [» ]
    3PWM X-ray 1.46 A/B 501-599 [» ]
    3PWR X-ray 1.45 A/B 501-599 [» ]
    3QBF X-ray 1.45 A/B 501-599 [» ]
    3QIH X-ray 1.39 A/B 501-599 [» ]
    3QN8 X-ray 1.38 A/B 501-599 [» ]
    3QP0 X-ray 1.45 A/B 501-599 [» ]
    3QPJ X-ray 1.61 A/B 501-599 [» ]
    3QRM X-ray 1.73 A/B 501-599 [» ]
    3QRO X-ray 1.62 A/B 501-599 [» ]
    3QRS X-ray 1.59 A/B 501-599 [» ]
    3ST5 X-ray 1.45 A/B 501-599 [» ]
    3T11 X-ray 2.22 A/B 501-599 [» ]
    3T3C X-ray 2.10 A/B 501-599 [» ]
    3TOF X-ray 1.45 A/B 501-599 [» ]
    3TOG X-ray 1.24 A/B/C/D 501-599 [» ]
    3TOH X-ray 1.12 A/B 501-599 [» ]
    3TTP X-ray 2.23 A/B 501-599 [» ]
    3U7S X-ray 2.05 A/B 501-599 [» ]
    3UCB X-ray 1.38 A/B 501-599 [» ]
    3UF3 X-ray 1.63 A/B 501-599 [» ]
    3UFN X-ray 1.45 A/B 501-599 [» ]
    3UHL X-ray 2.20 A/B/C/D 501-599 [» ]
    3VF5 X-ray 1.25 A/B 501-599 [» ]
    3VF7 X-ray 1.30 A/B 501-599 [» ]
    3VFB X-ray 1.55 A/B 501-599 [» ]
    4DFG X-ray 1.23 A/B 501-599 [» ]
    4FAF X-ray 2.10 D 361-367 [» ]
    4FE6 X-ray 2.00 A 501-599 [» ]
    4FL8 X-ray 1.20 A/B 501-599 [» ]
    4FLG X-ray 1.31 A/B 501-599 [» ]
    4FM6 X-ray 1.40 A/B 501-599 [» ]
    4GB2 X-ray 1.79 A/B 501-599 [» ]
    4HDB X-ray 1.49 A/B 501-599 [» ]
    4HDF X-ray 1.29 A/B 501-599 [» ]
    4HDP X-ray 1.22 A/B 501-599 [» ]
    4HE9 X-ray 1.06 A/B 501-599 [» ]
    4HEG X-ray 1.46 A/B 501-599 [» ]
    4HLA X-ray 1.95 A/B 501-599 [» ]
    4J54 X-ray 1.55 A/B 501-599 [» ]
    4J55 X-ray 1.31 A/B 501-599 [» ]
    4J5J X-ray 1.80 A/B 501-599 [» ]
    4JEC Other 2.00 A/B 501-599 [» ]
    4LL3 X-ray 1.95 A/B 501-599 [» ]
    7UPJ X-ray 2.00 A/B 501-599 [» ]
    ProteinModelPortali P03367.
    SMRi P03367. Positions 1-432, 501-1156, 1160-1429.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1506499.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P03367.

    Family and domain databases

    Gene3Di 1.10.10.200. 1 hit.
    1.10.1200.30. 1 hit.
    1.10.150.90. 1 hit.
    1.10.375.10. 1 hit.
    2.30.30.10. 1 hit.
    2.40.70.10. 1 hit.
    3.30.420.10. 2 hits.
    4.10.60.10. 1 hit.
    InterProi IPR001969. Aspartic_peptidase_AS.
    IPR000721. Gag_p24.
    IPR001037. Integrase_C_retrovir.
    IPR001584. Integrase_cat-core.
    IPR017856. Integrase_Zn-bd_dom-like_N.
    IPR003308. Integrase_Zn-bd_dom_N.
    IPR000071. Lentvrl_matrix_N.
    IPR012344. Matrix_N_HIV/RSV.
    IPR018061. Pept_A2A_retrovirus_sg.
    IPR001995. Peptidase_A2_cat.
    IPR021109. Peptidase_aspartic_dom.
    IPR008916. Retrov_capsid_C.
    IPR008919. Retrov_capsid_N.
    IPR010999. Retrovr_matrix_N.
    IPR012337. RNaseH-like_dom.
    IPR002156. RNaseH_domain.
    IPR000477. RT_dom.
    IPR010659. RVT_connect.
    IPR010661. RVT_thumb.
    IPR001878. Znf_CCHC.
    [Graphical view ]
    Pfami PF00540. Gag_p17. 1 hit.
    PF00607. Gag_p24. 1 hit.
    PF00552. IN_DBD_C. 1 hit.
    PF02022. Integrase_Zn. 1 hit.
    PF00075. RNase_H. 1 hit.
    PF00665. rve. 1 hit.
    PF00077. RVP. 1 hit.
    PF00078. RVT_1. 1 hit.
    PF06815. RVT_connect. 1 hit.
    PF06817. RVT_thumb. 1 hit.
    PF00098. zf-CCHC. 2 hits.
    [Graphical view ]
    PRINTSi PR00234. HIV1MATRIX.
    SMARTi SM00343. ZnF_C2HC. 2 hits.
    [Graphical view ]
    SUPFAMi SSF46919. SSF46919. 1 hit.
    SSF47353. SSF47353. 1 hit.
    SSF47836. SSF47836. 1 hit.
    SSF47943. SSF47943. 1 hit.
    SSF50122. SSF50122. 1 hit.
    SSF50630. SSF50630. 1 hit.
    SSF53098. SSF53098. 2 hits.
    SSF57756. SSF57756. 1 hit.
    PROSITEi PS50175. ASP_PROT_RETROV. 1 hit.
    PS00141. ASP_PROTEASE. 1 hit.
    PS50994. INTEGRASE. 1 hit.
    PS51027. INTEGRASE_DBD. 1 hit.
    PS50879. RNASE_H. 1 hit.
    PS50878. RT_POL. 1 hit.
    PS50158. ZF_CCHC. 2 hits.
    PS50876. ZF_INTEGRASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the AIDS virus, LAV."
      Wain-Hobson S., Sonigo P., Danos O., Cole S., Alizon M.
      Cell 40:9-17(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Genetic variability of the AIDS virus: nucleotide sequence analysis of two isolates from African patients."
      Alizon M., Wain-Hobson S., Montagnier L., Sonigo P.
      Cell 46:63-74(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 455-467.
    3. "Cleavage of recombinant and cell derived human immunodeficiency virus 1 (HIV-1) Nef protein by HIV-1 protease."
      Gaedigk-Nitschko K., Schoen A., Wachinger G., Erfle V., Kohleisen B.
      FEBS Lett. 357:275-278(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF NEF BY VIRAL PROTEASE.
    4. "Intravirion processing of the human immunodeficiency virus type 1 Vif protein by the viral protease may be correlated with Vif function."
      Khan M.A., Akari H., Kao S., Aberham C., Davis D., Buckler-White A., Strebel K.
      J. Virol. 76:9112-9123(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF VIF BY VIRAL PROTEASE.
    5. "Proteolytic processing and particle maturation."
      Vogt V.M.
      Curr. Top. Microbiol. Immunol. 214:95-131(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    6. Cited for: REVIEW.
    7. "Mechanisms of retroviral recombination."
      Negroni M., Buc H.
      Annu. Rev. Genet. 35:275-302(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    8. Cited for: REVIEW.
    9. "Role of HIV-1 Gag domains in viral assembly."
      Scarlata S., Carter C.
      Biochim. Biophys. Acta 1614:62-72(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    10. "The three-dimensional structure of the aspartyl protease from the HIV-1 isolate BRU."
      Spinelli S., Liu Q.Z., Alzari P.M., Hirel P.H., Poljak R.J.
      Biochimie 73:1391-1396(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 501-599.
    11. "Structure of HIV-1 reverse transcriptase/DNA complex at 7 A resolution showing active site locations."
      Arnold E., Jacobo-Molina A., Nanni R.G., Williams R.L., Lu X., Ding J., Clark A.D. Jr., Zhang A., Ferris A.L., Clark P., Hizi A., Hughes S.H.
      Nature 357:85-89(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 600-1026.
    12. "Crystal structure at 1.9-A resolution of human immunodeficiency virus (HIV) II protease complexed with L-735,524, an orally bioavailable inhibitor of the HIV proteases."
      Chen Z., Li Y., Chen E., Hall D.L., Darke P.L., Culberson C., Shafer J.A., Kuo L.C.
      J. Biol. Chem. 269:26344-26348(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 501-599 IN COMPLEX WITH THE INHIBITOR L-736,524.
    13. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 501-599.
    14. "Inhibition and catalytic mechanism of HIV-1 aspartic protease."
      Silva A.M., Cachau R.E., Sham H.L., Erickson J.W.
      J. Mol. Biol. 255:321-346(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 501-599 IN COMPLEX WITH THE DIFLUOROKETONE CONTAINING INHIBITOR A79285.
    15. "Crystallographic analysis of human immunodeficiency virus 1 protease with an analog of the conserved CA-p2 substrate -- interactions with frequently occurring glutamic acid residue at P2' position of substrates."
      Weber I.T., Wu J., Adomat J.M., Harrison R.W., Kimmel A.R., Wondrak E.M., Louis J.M.
      Eur. J. Biochem. 249:523-530(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 501-599.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 501-599.
    17. "X-ray structure and conformational dynamics of the HIV-1 protease in complex with the inhibitor SDZ283-910: agreement of time-resolved spectroscopy and molecular dynamics simulations."
      Ringhofer S., Kallen J., Dutzler R., Billich A., Visser A.J., Scholz D., Steinhauser O., Schreiber H., Auer M., Kungl A.J.
      J. Mol. Biol. 286:1147-1159(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 501-599 IN COMPLEX WITH INHIBITOR SDZ283-910.
    18. "A distinct binding mode of a hydroxyethylamine isostere inhibitor of HIV-1 protease."
      Dohnalek J., Hasek J., Duskova J., Petrokova H., Hradilek M., Soucek M., Konvalinka J., Brynda J., Sedlacek J., Fabry M.
      Acta Crystallogr. D 57:472-476(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 501-599 IN COMPLEX WITH A PEPTIDOMIMETIC INHIBITOR.
    19. "Hydroxyethylamine isostere of an HIV-1 protease inhibitor prefers its amine to the hydroxy group in binding to catalytic aspartates. A synchrotron study of HIV-1 protease in complex with a peptidomimetic inhibitor."
      Dohnalek J., Hasek J., Duskova J., Petrokova H., Hradilek M., Soucek M., Konvalinka J., Brynda J., Sedlacek J., Fabry M.
      J. Med. Chem. 45:1432-1438(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 501-599.
    20. "An ethylenamine inhibitor binds tightly to both wild type and mutant HIV-1 proteases. Structure and energy study."
      Skalova T., Hasek J., Dohnalek J., Petrokova H., Buchtelova E., Duskova J., Soucek M., Majer P., Uhlikova T., Konvalinka J.
      J. Med. Chem. 46:1636-1644(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 501-599 IN COMPLEX WITH AN ETHYLENAMINE PEPTIDOMIMETIC INHIBITOR.
    21. "Role of hydroxyl group and R/S configuration of isostere in binding properties of HIV-1 protease inhibitors."
      Petrokova H., Duskova J., Dohnalek J., Skalova T., Vondrackova-Buchtelova E., Soucek M., Konvalinka J., Brynda J., Fabry M., Sedlacek J., Hasek J.
      Eur. J. Biochem. 271:4451-4461(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 501-599 IN COMPLEX WITH AN ETHYLENEAMINE INHIBITOR.
    22. "A structural and thermodynamic escape mechanism from a drug resistant mutation of the HIV-1 protease."
      Vega S., Kang L.W., Velazquez-Campoy A., Kiso Y., Amzel L.M., Freire E.
      Proteins 55:594-602(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 501-599 IN COMPLEX WITH THE INHIBITOR KNI-577.
    23. "A phenylnorstatine inhibitor binding to HIV-1 protease: geometry, protonation, and subsite-pocket interactions analyzed at atomic resolution."
      Brynda J., Rezacova P., Fabry M., Horejsi M., Stouracova R., Sedlacek J., Soucek M., Hradilek M., Lepsik M., Konvalinka J.
      J. Med. Chem. 47:2030-2036(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.03 ANGSTROMS) OF 501-599 IN COMPLEX WITH A PEPTIDOMIMETIC INHIBITOR.
    24. "High resolution crystal structures of HIV-1 protease with a potent non-peptide inhibitor (UIC-94017) active against multi-drug-resistant clinical strains."
      Tie Y., Boross P.I., Wang Y.-F., Gaddis L., Hussain A.K., Leshchenko S., Ghosh A.K., Louis J.M., Harrison R.W., Weber I.T.
      J. Mol. Biol. 338:341-352(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 501-599 IN COMPLEX WITH THE INHIBITOR UIC-94017.
    25. "Crystal structures of HIV protease V82A and L90M mutants reveal changes in the indinavir-binding site."
      Mahalingam B., Wang Y.-F., Boross P.I., Tozser J., Louis J.M., Harrison R.W., Weber I.T.
      Eur. J. Biochem. 271:1516-1524(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 501-599.
    26. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 501-599.
    27. "Inhibitor binding at the protein interface in crystals of a HIV-1 protease complex."
      Brynda J., Rezacova P., Fabry M., Horejsi M., Stouracova R., Soucek M., Hradilek M., Konvalinka J., Sedlacek J.
      Acta Crystallogr. D 60:1943-1948(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 501-599 IN COMPLEX WITH A PEPTIDOMIMETIC INHIBITOR.

    Entry informationi

    Entry nameiPOL_HV1BR
    AccessioniPrimary (citable) accession number: P03367
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 176 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Capsid protein p24 is able to bind macaque TRIM5-alpha or owl monkey TRIMCyp, preventing reverse transcription of the viral genome and succesfull infection of macaque or owl monkey by HIV-1.By similarity
    The reverse transcriptase is an error-prone enzyme that lacks a proof-reading function. High mutations rate is a direct consequence of this characteristic. RT also displays frequent template switching leading to high recombination rate. Recombination mostly occurs between homologous regions of the two copackaged RNA genomes. If these two RNA molecules derive from different viral strains, reverse transcription will give rise to highly recombinated proviral DNAs.
    HIV-1 lineages are divided in three main groups, M (for Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast majority of strains found worldwide belong to the group M. Group O seems to be endemic to and largely confined to Cameroon and neighboring countries in West Central Africa, where these viruses represent a small minority of HIV-1 strains. The group N is represented by a limited number of isolates from Cameroonian persons. The group M is further subdivided in 9 clades or subtypes (A to D, F to H, J and K).
    Resistance to inhibitors associated with mutations are observed both in viral protease and in reverse transcriptase. Most of the time, single mutations confer only a modest reduction in drug susceptibility. Combination of several mutations is usually required to develop a high-level drug resistance. These mutations are predominantly found in clade B viruses and not in other genotypes. They are listed in the clade B representative isolate HXB2 (AC P04585).

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3