POL_HV2RO
ID POL_HV2RO Reviewed; 1464 AA.
AC P04584; Q76629;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Gag-Pol polyprotein;
DE AltName: Full=Pr160Gag-Pol;
DE Contains:
DE RecName: Full=Matrix protein p17;
DE Short=MA;
DE Contains:
DE RecName: Full=Capsid protein p24;
DE Short=CA;
DE Contains:
DE RecName: Full=Spacer peptide 1 {ECO:0000250|UniProtKB:P12497};
DE Short=SP1;
DE AltName: Full=p2;
DE Contains:
DE RecName: Full=Nucleocapsid protein p7;
DE Short=NC;
DE Contains:
DE RecName: Full=Transframe peptide;
DE Short=TF;
DE Contains:
DE RecName: Full=p6-pol;
DE Short=p6*;
DE Contains:
DE RecName: Full=Protease;
DE EC=3.4.23.47;
DE AltName: Full=PR;
DE AltName: Full=Retropepsin;
DE Contains:
DE RecName: Full=Reverse transcriptase/ribonuclease H;
DE EC=2.7.7.49;
DE EC=2.7.7.7;
DE EC=3.1.26.13;
DE AltName: Full=Exoribonuclease H;
DE EC=3.1.13.2;
DE AltName: Full=p66 RT;
DE Contains:
DE RecName: Full=p51 RT;
DE Contains:
DE RecName: Full=p15;
DE Contains:
DE RecName: Full=Integrase;
DE Short=IN;
DE EC=2.7.7.- {ECO:0000250|UniProtKB:P04585};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P04585};
GN Name=gag-pol;
OS Human immunodeficiency virus type 2 subtype A (isolate ROD) (HIV-2).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11720;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3031510; DOI=10.1038/326662a0;
RA Guyader M., Emerman M., Sonigo P., Clavel F., Montagnier L., Alizon M.;
RT "Genome organization and transactivation of the human immunodeficiency
RT virus type 2.";
RL Nature 326:662-669(1987).
RN [2]
RP REVIEW.
RX PubMed=8791726; DOI=10.1007/978-3-642-80145-7_4;
RA Vogt V.M.;
RT "Proteolytic processing and particle maturation.";
RL Curr. Top. Microbiol. Immunol. 214:95-131(1996).
RN [3]
RP REVIEW.
RX PubMed=9878383; DOI=10.1006/jmbi.1998.2354;
RA Turner B.G., Summers M.F.;
RT "Structural biology of HIV.";
RL J. Mol. Biol. 285:1-32(1999).
RN [4]
RP REVIEW.
RX PubMed=11700285; DOI=10.1146/annurev.genet.35.102401.090551;
RA Negroni M., Buc H.;
RT "Mechanisms of retroviral recombination.";
RL Annu. Rev. Genet. 35:275-302(2001).
RN [5]
RP REVIEW.
RX PubMed=11983066; DOI=10.1186/gb-2002-3-4-reviews3006;
RA Dunn B.M., Goodenow M.M., Gustchina A., Wlodawer A.;
RT "Retroviral proteases.";
RL Genome Biol. 3:REVIEWS3006.1-REVIEWS3006.7(2002).
RN [6]
RP 3D-STRUCTURE MODELING OF 514-612.
RX PubMed=1946342; DOI=10.1002/prot.340100406;
RA Gustchina A., Weber I.T.;
RT "Comparative analysis of the sequences and structures of HIV-1 and HIV-2
RT proteases.";
RL Proteins 10:325-339(1991).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 514-612 IN COMPLEX WITH A REDUCED
RP AMIDE INHIBITOR.
RX PubMed=8378311; DOI=10.1073/pnas.90.18.8387;
RA Tong L., Pav S., Pargellis C., Do F., Lamarre D., Anderson P.C.;
RT "Crystal structure of human immunodeficiency virus (HIV) type 2 protease in
RT complex with a reduced amide inhibitor and comparison with HIV-1 protease
RT structures.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8387-8391(1993).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 514-612 IN COMPLEX WITH THE
RP INHIBITORS U75875 AND U92163.
RX PubMed=8514751; DOI=10.1016/s0021-9258(19)38625-9;
RA Mulichak A.M., Hui J.O., Tomasselli A.G., Heinrikson R.L., Curry K.A.,
RA Tomich C.S., Thaisrivongs S., Sawyer T.K., Watenpaugh K.D.;
RT "The crystallographic structure of the protease from human immunodeficiency
RT virus type 2 with two synthetic peptidic transition state analog
RT inhibitors.";
RL J. Biol. Chem. 268:13103-13109(1993).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 514-612 IN COMPLEX WITH THE
RP INHIBITOR L-736,524.
RX PubMed=7929352; DOI=10.1016/s0021-9258(18)47199-2;
RA Chen Z., Li Y., Chen E., Hall D.L., Darke P.L., Culberson C., Shafer J.A.,
RA Kuo L.C.;
RT "Crystal structure at 1.9-A resolution of human immunodeficiency virus
RT (HIV) II protease complexed with L-735,524, an orally bioavailable
RT inhibitor of the HIV proteases.";
RL J. Biol. Chem. 269:26344-26348(1994).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 514-612 IN COMPLEX WITH THE
RP INHIBITOR CGP 53820.
RX PubMed=7613867; DOI=10.1016/s0969-2126(01)00169-1;
RA Priestle J.P., Fassler A., Rosel J., Tintelnot-Blomley M., Strop P.,
RA Gruetter M.G.;
RT "Comparative analysis of the X-ray structures of HIV-1 and HIV-2 proteases
RT in complex with CGP 53820, a novel pseudosymmetric inhibitor.";
RL Structure 3:381-389(1995).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 514-612 IN COMPLEX WITH
RP INHIBITORS.
RX PubMed=7743130; DOI=10.1016/s0969-2126(01)00133-2;
RA Tong L., Pav S., Mui S., Lamarre D., Yoakim C., Beaulieu P.L.,
RA Anderson P.C.;
RT "Crystal structures of HIV-2 protease in complex with inhibitors containing
RT the hydroxyethylamine dipeptide isostere.";
RL Structure 3:33-40(1995).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 514-612 IN COMPLEX WITH THE
RP INHIBITORS U096333 AND U097410.
RX PubMed=7658450; DOI=10.1021/jm00018a023;
RA Thaisrivongs S., Watenpaugh K.D., Howe W.J., Tomich P.K., Dolak L.A.,
RA Chong K.-T., Tomich C.C., Tomasselli A.G., Turner S.R., Strohbach J.W.,
RA Mulichak A.M., Janakiraman M.N., Moon J.B., Lynn J.C., Horng M.-M.,
RA Hinshaw R.R., Curry K.A., Rothrock D.J.;
RT "Structure-based design of novel HIV protease inhibitors: carboxamide-
RT containing 4-hydroxycoumarins and 4-hydroxy-2-pyrones as potent nonpeptidic
RT inhibitors.";
RL J. Med. Chem. 38:3624-3637(1995).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 514-612.
RX PubMed=7783120; DOI=10.1021/jm00011a008;
RA Romines K.R., Watenpaugh K.D., Tomich P.K., Howe W.J., Morris J.K.,
RA Lovasz K.D., Mulichak A.M., Finzel B.C., Lynn J.C., Horng M.-M.,
RA Schwende F.J., Ruwart M.J., Zipp G.L., Chong K.-T., Dolak L.A., Toth L.N.,
RA Howard G.M., Rush B.D., Wilkinson K.F., Possert P.L., Dalga R.J.,
RA Hinshaw R.R.;
RT "Use of medium-sized cycloalkyl rings to enhance secondary binding:
RT discovery of a new class of human immunodeficiency virus (HIV) protease
RT inhibitors.";
RL J. Med. Chem. 38:1884-1891(1995).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 514-612 IN COMPLEX WITH
RP (HYDROXYETHYL)AMIDE ISOSTERE CONTAINING INHIBITORS.
RX PubMed=9216835; DOI=10.1021/jm9606608;
RA Beaulieu P.L., Wernic D., Abraham A., Anderson P.C., Bogri T., Bousquet Y.,
RA Croteau G., Guse I., Lamarre D., Liard F., Paris W., Thibeault D., Pav S.,
RA Tong L.;
RT "Potent HIV protease inhibitors containing a novel (hydroxyethyl)amide
RT isostere.";
RL J. Med. Chem. 40:2164-2176(1997).
RN [15]
RP STRUCTURE BY NMR OF 1172-1226.
RX PubMed=9368756; DOI=10.1016/s0960-9822(06)00332-0;
RA Eijkelenboom A.P.A.M., van den Ent F.M.I., Vos A., Doreleijers J.F.,
RA Hard K., Tullius T.D., Plasterk R.H.A., Kaptein R., Boelens R.;
RT "The solution structure of the amino-terminal HHCC domain of HIV-2
RT integrase: a three-helix bundle stabilized by zinc.";
RL Curr. Biol. 7:739-746(1997).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 613-1167.
RX PubMed=12386343; DOI=10.1073/pnas.222366699;
RA Ren J.S., Bird L.E., Chamberlain P.P., Stewart-Jones G.B., Stuart D.I.,
RA Stammers D.K.;
RT "Structure of HIV-2 reverse transcriptase at 2.35-A resolution and the
RT mechanism of resistance to non-nucleoside inhibitors.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14410-14415(2002).
CC -!- FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the
CC essential events in virion assembly, including binding the plasma
CC membrane, making the protein-protein interactions necessary to create
CC spherical particles, recruiting the viral Env proteins, and packaging
CC the genomic RNA via direct interactions with the RNA packaging sequence
CC (Psi). Gag-Pol polyprotein may regulate its own translation, by the
CC binding genomic RNA in the 5'-UTR. At low concentration, the
CC polyprotein would promote translation, whereas at high concentration,
CC the polyprotein would encapsidate genomic RNA and then shut off
CC translation. {ECO:0000250}.
CC -!- FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma
CC membrane via a multipartite membrane-binding signal, that includes its
CC myristoylated N-terminus. Matrix protein is part of the pre-integration
CC complex. Implicated in the release from host cell mediated by Vpu.
CC Binds to RNA. {ECO:0000250|UniProtKB:P12497}.
CC -!- FUNCTION: [Capsid protein p24]: Forms the conical core that
CC encapsulates the genomic RNA-nucleocapsid complex in the virion. Most
CC core are conical, with only 7% tubular. The core is constituted by
CC capsid protein hexamer subunits. The core is disassembled soon after
CC virion entry (By similarity). Host restriction factors such as TRIM5-
CC alpha or TRIMCyp bind retroviral capsids and cause premature capsid
CC disassembly, leading to blocks in reverse transcription. Capsid
CC restriction by TRIM5 is one of the factors which restricts HIV-1 to the
CC human species. Host PIN1 apparently facilitates the virion uncoating.
CC On the other hand, interactions with PDZD8 or CYPA stabilize the
CC capsid. {ECO:0000250|UniProtKB:P04585, ECO:0000250|UniProtKB:P12497}.
CC -!- FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral
CC dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc
CC fingers. Acts as a nucleic acid chaperone which is involved in
CC rearangement of nucleic acid secondary structure during gRNA
CC retrotranscription. Also facilitates template switch leading to
CC recombination. As part of the polyprotein, participates in gRNA
CC dimerization, packaging, tRNA incorporation and virion assembly.
CC {ECO:0000250|UniProtKB:P04585}.
CC -!- FUNCTION: [Protease]: Aspartyl protease that mediates proteolytic
CC cleavages of Gag and Gag-Pol polyproteins during or shortly after the
CC release of the virion from the plasma membrane. Cleavages take place as
CC an ordered, step-wise cascade to yield mature proteins. This process is
CC called maturation. Displays maximal activity during the budding process
CC just prior to particle release from the cell. Also cleaves Nef and Vif,
CC probably concomitantly with viral structural proteins on maturation of
CC virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off
CC the capped cellular mRNA translation. The resulting inhibition of
CC cellular protein synthesis serves to ensure maximal viral gene
CC expression and to evade host immune response (By similarity).
CC {ECO:0000250|UniProtKB:P04585, ECO:0000255|PROSITE-ProRule:PRU00275}.
CC -!- FUNCTION: [Reverse transcriptase/ribonuclease H]: Multifunctional
CC enzyme that converts the viral RNA genome into dsDNA in the cytoplasm,
CC shortly after virus entry into the cell. This enzyme displays a DNA
CC polymerase activity that can copy either DNA or RNA templates, and a
CC ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-
CC DNA heteroduplexes in a partially processive 3' to 5' endonucleasic
CC mode. Conversion of viral genomic RNA into dsDNA requires many steps. A
CC tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-
CC end of the viral RNA. RT uses the 3' end of the tRNA primer to perform
CC a short round of RNA-dependent minus-strand DNA synthesis. The reading
CC proceeds through the U5 region and ends after the repeated (R) region
CC which is present at both ends of viral RNA. The portion of the RNA-DNA
CC heteroduplex is digested by the RNase H, resulting in a ssDNA product
CC attached to the tRNA primer. This ssDNA/tRNA hybridizes with the
CC identical R region situated at the 3' end of viral RNA. This template
CC exchange, known as minus-strand DNA strong stop transfer, can be either
CC intra- or intermolecular. RT uses the 3' end of this newly synthesized
CC short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of
CC the whole template. RNase H digests the RNA template except for two
CC polypurine tracts (PPTs) situated at the 5'-end and near the center of
CC the genome. It is not clear if both polymerase and RNase H activities
CC are simultaneous. RNase H probably can proceed both in a polymerase-
CC dependent (RNA cut into small fragments by the same RT performing DNA
CC synthesis) and a polymerase-independent mode (cleavage of remaining RNA
CC fragments by free RTs). Secondly, RT performs DNA-directed plus-strand
CC DNA synthesis using the PPTs that have not been removed by RNase H as
CC primers. PPTs and tRNA primers are then removed by RNase H. The 3' and
CC 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate.
CC Strand displacement synthesis by RT to the PBS and PPT ends produces a
CC blunt ended, linear dsDNA copy of the viral genome that includes long
CC terminal repeats (LTRs) at both ends. {ECO:0000250|UniProtKB:P04585}.
CC -!- FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host
CC chromosome, by performing a series of DNA cutting and joining
CC reactions. This enzyme activity takes place after virion entry into a
CC cell and reverse transcription of the RNA genome in dsDNA. The first
CC step in the integration process is 3' processing. This step requires a
CC complex comprising the viral genome, matrix protein, Vpr and integrase.
CC This complex is called the pre-integration complex (PIC). The integrase
CC protein removes 2 nucleotides from each 3' end of the viral DNA,
CC leaving recessed CA OH's at the 3' ends. In the second step, the PIC
CC enters cell nucleus. This process is mediated through integrase and Vpr
CC proteins, and allows the virus to infect a non dividing cell. This
CC ability to enter the nucleus is specific of lentiviruses, other
CC retroviruses cannot and rely on cell division to access cell
CC chromosomes. In the third step, termed strand transfer, the integrase
CC protein joins the previously processed 3' ends to the 5' ends of
CC strands of target cellular DNA at the site of integration. The 5'-ends
CC are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-
CC shaped, gapped, recombination intermediate results, with the 5'-ends of
CC the viral DNA strands and the 3' ends of target DNA strands remaining
CC unjoined, flanking a gap of 5 bp. The last step is viral DNA
CC integration into host chromosome. This involves host DNA repair
CC synthesis in which the 5 bp gaps between the unjoined strands are
CC filled in and then ligated. Since this process occurs at both cuts
CC flanking the HIV genome, a 5 bp duplication of host DNA is produced at
CC the ends of HIV-1 integration. Alternatively, Integrase may catalyze
CC the excision of viral DNA just after strand transfer, this is termed
CC disintegration. {ECO:0000250|UniProtKB:P04585}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase for which the P1 residue is preferably
CC hydrophobic.; EC=3.4.23.47; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00275};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different
CC cleavage modes: 1. sequence-specific internal cleavage of RNA. Human
CC immunodeficiency virus type 1 and Moloney murine leukemia virus
CC enzymes prefer to cleave the RNA strand one nucleotide away from the
CC RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides
CC from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides
CC away from the primer terminus.; EC=3.1.26.13; Evidence={ECO:0000250};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA
CC hybrid.; EC=3.1.13.2; Evidence={ECO:0000250};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions for reverse transcriptase polymerase
CC activity. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity.
CC Substrate-binding is a precondition for magnesium binding.
CC {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Magnesium ions are required for integrase activity. Binds at least
CC 1, maybe 2 magnesium ions. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Protease: The viral protease is inhibited by many
CC synthetic protease inhibitors (PIs), such as amprenavir, atazanavir,
CC indinavir, loprinavir, nelfinavir, ritonavir and saquinavir. Use of
CC protease inhibitors in tritherapy regimens permit more ambitious
CC therapeutic strategies. Reverse transcriptase/ribonuclease H: RT can be
CC inhibited either by nucleoside RT inhibitors (NRTIs) or by non
CC nucleoside RT inhibitors (NNRTIs). NRTIs act as chain terminators,
CC whereas NNRTIs inhibit DNA polymerization by binding a small
CC hydrophobic pocket near the RT active site and inducing an allosteric
CC change in this region. Classical NRTIs are abacavir, adefovir (PMEA),
CC didanosine (ddI), lamivudine (3TC), stavudine (d4T), tenofovir (PMPA),
CC zalcitabine (ddC), and zidovudine (AZT). Classical NNRTIs are
CC atevirdine (BHAP U-87201E), delavirdine, efavirenz (DMP-266), emivirine
CC (I-EBU), and nevirapine (BI-RG-587). The tritherapies used as a basic
CC effective treatment of AIDS associate two NRTIs and one NNRTI.
CC {ECO:0000250}.
CC -!- SUBUNIT: [Matrix protein p17]: Homotrimer; further assembles as
CC hexamers of trimers. Interacts with gp41 (via C-terminus). Interacts
CC with host CALM1; this interaction induces a conformational change in
CC the Matrix protein, triggering exposure of the myristate group.
CC Interacts with host AP3D1; this interaction allows the polyprotein
CC trafficking to multivesicular bodies during virus assembly. Part of the
CC pre-integration complex (PIC) which is composed of viral genome, matrix
CC protein, Vpr and integrase. {ECO:0000250|UniProtKB:P04591,
CC ECO:0000250|UniProtKB:P12493}.
CC -!- SUBUNIT: [Capsid protein p24]: Homodimer; the homodimer further
CC multimerizes as homohexamers or homopentamers. Interacts with human
CC PPIA/CYPA. Interacts with human NUP153. Interacts with host PDZD8; this
CC interaction stabilizes the capsid. Interacts with monkey TRIM5; this
CC interaction destabilizes the capsid. {ECO:0000250|UniProtKB:P03348,
CC ECO:0000250|UniProtKB:P04591, ECO:0000250|UniProtKB:P12493}.
CC -!- SUBUNIT: [Protease]: Homodimer, whose active site consists of two
CC apposed aspartic acid residues. {ECO:0000250|UniProtKB:P04585,
CC ECO:0000250|UniProtKB:P12497}.
CC -!- SUBUNIT: [Reverse transcriptase/ribonuclease H]: Heterodimer of p66 RT
CC and p51 RT (RT p66/p51) (By similarity). Heterodimerization of RT is
CC essential for DNA polymerase activity (By similarity). The overall
CC folding of the subdomains is similar in p66 RT and p51 RT but the
CC spatial arrangements of the subdomains are dramatically different (By
CC similarity). {ECO:0000250|UniProtKB:P03366}.
CC -!- SUBUNIT: [Integrase]: Homotetramer; may further associate as a
CC homohexadecamer (By similarity). Part of the pre-integration complex
CC (PIC) which is composed of viral genome, matrix protein, Vpr and
CC integrase. Interacts with human SMARCB1/INI1 and human PSIP1/LEDGF
CC isoform 1. Interacts with human KPNA3; this interaction might play a
CC role in nuclear import of the pre-integration complex (By similarity).
CC Interacts with human NUP153; this interaction might play a role in
CC nuclear import of the pre-integration complex (By similarity).
CC {ECO:0000250|UniProtKB:P03367, ECO:0000250|UniProtKB:P04585,
CC ECO:0000250|UniProtKB:P12497}.
CC -!- SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-
CC anchor. Host endosome, host multivesicular body. Note=These locations
CC are linked to virus assembly sites. The main location is the cell
CC membrane, but under some circumstances, late endosomal compartments can
CC serve as productive sites for virion assembly.
CC {ECO:0000250|UniProtKB:P12497}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane; Lipid-
CC anchor {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Reverse transcriptase/ribonuclease H]: Virion
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Integrase]: Virion {ECO:0000305}. Host nucleus
CC {ECO:0000305}. Host cytoplasm {ECO:0000305}. Note=Nuclear at initial
CC phase, cytoplasmic at assembly. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=Translation results in the formation of the Gag polyprotein
CC most of the time. Ribosomal frameshifting at the gag-pol genes
CC boundary occurs at low frequency and produces the Gag-Pol
CC polyprotein. This strategy of translation probably allows the virus
CC to modulate the quantity of each viral protein. Maintenance of a
CC correct Gag to Gag-Pol ratio is essential for RNA dimerization and
CC viral infectivity.;
CC Name=Gag-Pol polyprotein;
CC IsoId=P04584-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P04590-1; Sequence=External;
CC -!- DOMAIN: [Reverse transcriptase/ribonuclease H]: RT is structured in
CC five subdomains: finger, palm, thumb, connection and RNase H. Within
CC the palm subdomain, the 'primer grip' region is thought to be involved
CC in the positioning of the primer terminus for accommodating the
CC incoming nucleotide. The RNase H domain stabilizes the association of
CC RT with primer-template. {ECO:0000250}.
CC -!- DOMAIN: [Reverse transcriptase/ribonuclease H]: The tryptophan repeat
CC motif is involved in RT p66/p51 dimerization (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: [Integrase]: The core domain contains the D-x(n)-D-x(35)-E
CC motif, named for the phylogenetically conserved glutamic acid and
CC aspartic acid residues and the invariant 35 amino acid spacing between
CC the second and third acidic residues. Each acidic residue of the
CC D,D(35)E motif is independently essential for the 3'-processing and
CC strand transfer activities of purified integrase protein.
CC {ECO:0000250}.
CC -!- PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral
CC protease yield mature proteins. The protease is released by
CC autocatalytic cleavage. The polyprotein is cleaved during and after
CC budding, this process is termed maturation. Proteolytic cleavage of p66
CC RT removes the RNase H domain to yield the p51 RT subunit. Nucleocapsid
CC protein p7 might be further cleaved after virus entry.
CC {ECO:0000250|UniProtKB:P04585, ECO:0000255|PROSITE-ProRule:PRU00405}.
CC -!- MISCELLANEOUS: [Reverse transcriptase/ribonuclease H]: Error-prone
CC enzyme that lacks a proof-reading function. High mutations rate is a
CC direct consequence of this characteristic. RT also displays frequent
CC template switching leading to high recombination rate. Recombination
CC mostly occurs between homologous regions of the two copackaged RNA
CC genomes. If these two RNA molecules derive from different viral
CC strains, reverse transcription will give rise to highly recombinated
CC proviral DNAs. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Gag-Pol polyprotein]: Produced by -1 ribosomal
CC frameshifting.
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DR EMBL; X05291; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; M15390; AAB00764.1; ALT_SEQ; Genomic_DNA.
DR PIR; B26262; GNLJG2.
DR PDB; 1E0E; NMR; -; A/B=1172-1226.
DR PDB; 1HII; X-ray; 2.30 A; A/B=514-612.
DR PDB; 1HSH; X-ray; 1.90 A; A/B/C/D=514-612.
DR PDB; 1HSI; X-ray; 2.50 A; A/B=514-612.
DR PDB; 1IDA; X-ray; 1.70 A; A/B=514-612.
DR PDB; 1IDB; X-ray; 2.20 A; A/B=514-612.
DR PDB; 1IVP; X-ray; 2.50 A; A/B=514-612.
DR PDB; 1IVQ; X-ray; 2.60 A; A/B=514-612.
DR PDB; 1JLD; X-ray; 2.50 A; A/B=514-612.
DR PDB; 1MU2; X-ray; 2.35 A; A=613-1167, B=618-1043.
DR PDB; 2HPE; X-ray; 2.00 A; A/B=514-612.
DR PDB; 2HPF; X-ray; 3.00 A; A/B=514-612.
DR PDB; 2K4E; NMR; -; A=2-135.
DR PDB; 2K4H; NMR; -; A=2-135.
DR PDB; 2K4I; NMR; -; A=2-135.
DR PDB; 2MIP; X-ray; 2.20 A; A/B/C/D=514-612.
DR PDB; 3EBZ; X-ray; 1.20 A; A/B=514-612.
DR PDB; 3EC0; X-ray; 1.18 A; A/B=514-612.
DR PDB; 3ECG; X-ray; 1.18 A; A/B=514-612.
DR PDB; 3F9K; X-ray; 3.20 A; A/B/E/F/I/J/M/N/Q/R/U/V/Y/Z/c/d/g/h/k/l/o/p/s/t=1173-1380.
DR PDB; 3UPJ; X-ray; 2.50 A; A/B=514-612.
DR PDB; 4UPJ; X-ray; 1.90 A; A/B=514-612.
DR PDB; 5UPJ; X-ray; 2.30 A; A/B=514-612.
DR PDB; 6UPJ; X-ray; 2.34 A; A/B=514-612.
DR PDBsum; 1E0E; -.
DR PDBsum; 1HII; -.
DR PDBsum; 1HSH; -.
DR PDBsum; 1HSI; -.
DR PDBsum; 1IDA; -.
DR PDBsum; 1IDB; -.
DR PDBsum; 1IVP; -.
DR PDBsum; 1IVQ; -.
DR PDBsum; 1JLD; -.
DR PDBsum; 1MU2; -.
DR PDBsum; 2HPE; -.
DR PDBsum; 2HPF; -.
DR PDBsum; 2K4E; -.
DR PDBsum; 2K4H; -.
DR PDBsum; 2K4I; -.
DR PDBsum; 2MIP; -.
DR PDBsum; 3EBZ; -.
DR PDBsum; 3EC0; -.
DR PDBsum; 3ECG; -.
DR PDBsum; 3F9K; -.
DR PDBsum; 3UPJ; -.
DR PDBsum; 4UPJ; -.
DR PDBsum; 5UPJ; -.
DR PDBsum; 6UPJ; -.
DR BMRB; P04584; -.
DR SMR; P04584; -.
DR IntAct; P04584; 1.
DR DrugBank; DB07634; (2,6-Dimethylphenoxy)acetic acid.
DR DrugBank; DB08664; ({3-[1-(4-Hydroxy-2-oxo-2H-chromen-3-yl)-propyl]-phenylcarbamoyl}-methyl)-carbamic acid tert-butyl ester.
DR DrugBank; DB08286; 1-Naphthoxyacetic acid.
DR DrugBank; DB08474; 3-(CARBOXYAMIDE(2-CARBOXYAMIDE-2-TERTBUTYLETHYL))PENTAN.
DR DrugBank; DB04490; 3-(Mercaptomethylene)Pyridine.
DR DrugBank; DB08663; 4-HYDROXY-7-METHOXY-3-(1-PHENYL-PROPYL)-CHROMEN-2-ONE.
DR DrugBank; DB08686; 5,6,7,8,9,10-HEXAHYDRO-4-HYDROXY-3-(1-PHENYLPROPYL)CYCLOOCTA[B]PYRAN-2-ONE.
DR DrugBank; DB07581; 5-AMINO-6-CYCLOHEXYL-4-HYDROXY-2-ISOPROPYL-HEXANOIC ACID.
DR DrugBank; DB08274; 6,7,8,9-TETRAHYDRO-4-HYDROXY-3-(1-PHENYLPROPYL)CYCLOHEPTA[B]PYRAN-2-ONE.
DR DrugBank; DB08231; Myristic acid.
DR DrugBank; DB08421; PIPERIDINE-2-CARBOXYLIC ACID TERT-BUTYLAMIDE.
DR DrugBank; DB02428; Quinaldic Acid.
DR MEROPS; A02.002; -.
DR PRIDE; P04584; -.
DR ABCD; P04584; 1 sequenced antibody.
DR BioCyc; MetaCyc:MON-16108; -.
DR EvolutionaryTrace; P04584; -.
DR PRO; PR:P04584; -.
DR Proteomes; UP000007426; Genome.
DR Proteomes; UP000246871; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004533; F:exoribonuclease H activity; IEA:UniProtKB-EC.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR CDD; cd05482; HIV_retropepsin_like; 1.
DR Gene3D; 1.10.10.200; -; 1.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.90; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR Gene3D; 2.30.30.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.270; -; 3.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR000721; Gag_p24_N.
DR InterPro; IPR017856; Integrase-like_N.
DR InterPro; IPR036862; Integrase_C_dom_sf_retrovir.
DR InterPro; IPR001037; Integrase_C_retrovir.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR003308; Integrase_Zn-bd_dom_N.
DR InterPro; IPR000071; Lentvrl_matrix_N.
DR InterPro; IPR012344; Matrix_HIV/RSV_N.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR034170; Retropepsin-like_cat_dom.
DR InterPro; IPR018061; Retropepsins.
DR InterPro; IPR008916; Retrov_capsid_C.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR010659; RVT_connect.
DR InterPro; IPR010661; RVT_thumb.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00540; Gag_p17; 1.
DR Pfam; PF00607; Gag_p24; 1.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF00552; IN_DBD_C; 1.
DR Pfam; PF02022; Integrase_Zn; 1.
DR Pfam; PF00075; RNase_H; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF06815; RVT_connect; 1.
DR Pfam; PF06817; RVT_thumb; 1.
DR Pfam; PF00098; zf-CCHC; 2.
DR PRINTS; PR00234; HIV1MATRIX.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF46919; SSF46919; 1.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF50122; SSF50122; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS51027; INTEGRASE_DBD; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
DR PROSITE; PS50876; ZF_INTEGRASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; AIDS; Aspartyl protease; Capsid protein; DNA integration;
KW DNA recombination; DNA-binding; DNA-directed DNA polymerase; Endonuclease;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus; Host cell membrane;
KW Host cytoplasm; Host endosome; Host gene expression shutoff by virus;
KW Host membrane; Host nucleus; Host-virus interaction; Hydrolase;
KW Lipid-binding; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW Multifunctional enzyme; Myristate; Nuclease; Nucleotidyltransferase;
KW Phosphoprotein; Protease; Reference proteome; Repeat;
KW Ribosomal frameshifting; RNA-binding; RNA-directed DNA polymerase;
KW Transferase; Viral genome integration; Viral nucleoprotein;
KW Viral penetration into host nucleus; Viral release from host cell; Virion;
KW Virion maturation; Virus entry into host cell; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..1464
FT /note="Gag-Pol polyprotein"
FT /id="PRO_0000261298"
FT CHAIN 2..135
FT /note="Matrix protein p17"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042537"
FT CHAIN 136..365
FT /note="Capsid protein p24"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042538"
FT PEPTIDE 366..382
FT /note="Spacer peptide 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042539"
FT CHAIN 383..431
FT /note="Nucleocapsid protein p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042541"
FT PEPTIDE 432..445
FT /note="Transframe peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000246747"
FT CHAIN 446..513
FT /note="p6-pol"
FT /evidence="ECO:0000255"
FT /id="PRO_0000042543"
FT CHAIN 514..612
FT /note="Protease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038674"
FT CHAIN 613..1171
FT /note="Reverse transcriptase/ribonuclease H"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042544"
FT CHAIN 613..1051
FT /note="p51 RT"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042545"
FT CHAIN 1052..1171
FT /note="p15"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042546"
FT CHAIN 1172..1464
FT /note="Integrase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042547"
FT DOMAIN 533..602
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 656..846
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 1045..1168
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 1224..1375
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 389..406
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 410..427
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 1174..1215
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT DNA_BIND 1394..1441
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT REGION 7..31
FT /note="Interaction with Gp41"
FT /evidence="ECO:0000250|UniProtKB:P12497"
FT REGION 111..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..228
FT /note="Interaction with human PPIA/CYPA and NUP153"
FT /evidence="ECO:0000250|UniProtKB:P12497"
FT REGION 279..365
FT /note="Dimerization/Multimerization of capsid protein p24"
FT /evidence="ECO:0000250|UniProtKB:P04585"
FT REGION 432..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..518
FT /note="Dimerization of protease"
FT /evidence="ECO:0000250|UniProtKB:P04585"
FT REGION 562..568
FT /note="Dimerization of protease"
FT /evidence="ECO:0000250|UniProtKB:P04585"
FT REGION 601..613
FT /note="Dimerization of protease"
FT /evidence="ECO:0000250|UniProtKB:P04585"
FT REGION 839..847
FT /note="RT 'primer grip'"
FT /evidence="ECO:0000250"
FT MOTIF 16..22
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOTIF 26..32
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 1009..1025
FT /note="Tryptophan repeat motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 115..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 538
FT /note="For protease activity; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT BINDING 722
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000250"
FT BINDING 797
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000250"
FT BINDING 798
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000250"
FT BINDING 1054
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000250"
FT BINDING 1089
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000250"
FT BINDING 1109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000250"
FT BINDING 1160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000250"
FT BINDING 1183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000250"
FT BINDING 1287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000250"
FT BINDING 1323
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000250|UniProtKB:P04585"
FT SITE 135..136
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 222..223
FT /note="Cis/trans isomerization of proline peptide bond; by
FT human PPIA/CYPA"
FT /evidence="ECO:0000250"
FT SITE 365..366
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 382..383
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 431..432
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255"
FT SITE 445..446
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 513..514
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 612..613
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 1012
FT /note="Essential for RT p66/p51 heterodimerization"
FT /evidence="ECO:0000250"
FT SITE 1025
FT /note="Essential for RT p66/p51 heterodimerization"
FT /evidence="ECO:0000250"
FT SITE 1051..1052
FT /note="Cleavage; by viral protease; partial"
FT /evidence="ECO:0000250"
FT SITE 1171..1172
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT MOD_RES 135
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:2K4E"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:2K4E"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:2K4E"
FT HELIX 31..44
FT /evidence="ECO:0007829|PDB:2K4E"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:2K4E"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:2K4E"
FT TURN 65..70
FT /evidence="ECO:0007829|PDB:2K4E"
FT HELIX 73..90
FT /evidence="ECO:0007829|PDB:2K4E"
FT HELIX 97..115
FT /evidence="ECO:0007829|PDB:2K4E"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:1IDB"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:3EC0"
FT STRAND 523..528
FT /evidence="ECO:0007829|PDB:3EC0"
FT STRAND 531..537
FT /evidence="ECO:0007829|PDB:3EC0"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:2HPE"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:3EC0"
FT STRAND 556..562
FT /evidence="ECO:0007829|PDB:3EC0"
FT STRAND 565..579
FT /evidence="ECO:0007829|PDB:3EC0"
FT STRAND 582..591
FT /evidence="ECO:0007829|PDB:3EC0"
FT STRAND 594..598
FT /evidence="ECO:0007829|PDB:2HPF"
FT HELIX 600..606
FT /evidence="ECO:0007829|PDB:3EC0"
FT STRAND 609..611
FT /evidence="ECO:0007829|PDB:3EC0"
FT HELIX 640..655
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 658..661
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 672..674
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:1MU2"
FT HELIX 690..695
FT /evidence="ECO:0007829|PDB:1MU2"
FT HELIX 709..711
FT /evidence="ECO:0007829|PDB:1MU2"
FT HELIX 712..714
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 716..722
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 724..726
FT /evidence="ECO:0007829|PDB:1MU2"
FT HELIX 727..729
FT /evidence="ECO:0007829|PDB:1MU2"
FT TURN 734..736
FT /evidence="ECO:0007829|PDB:1MU2"
FT HELIX 737..740
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 742..744
FT /evidence="ECO:0007829|PDB:1MU2"
FT HELIX 747..749
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 755..760
FT /evidence="ECO:0007829|PDB:1MU2"
FT HELIX 768..786
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 790..795
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 798..803
FT /evidence="ECO:0007829|PDB:1MU2"
FT HELIX 807..823
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 836..841
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 844..846
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 848..853
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 854..856
FT /evidence="ECO:0007829|PDB:1MU2"
FT HELIX 866..882
FT /evidence="ECO:0007829|PDB:1MU2"
FT HELIX 889..892
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 897..899
FT /evidence="ECO:0007829|PDB:1MU2"
FT HELIX 909..922
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 926..929
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 938..943
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 945..947
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 949..955
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 958..965
FT /evidence="ECO:0007829|PDB:1MU2"
FT HELIX 975..994
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 999..1004
FT /evidence="ECO:0007829|PDB:1MU2"
FT HELIX 1006..1015
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 1024..1027
FT /evidence="ECO:0007829|PDB:1MU2"
FT HELIX 1032..1037
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 1040..1043
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 1049..1057
FT /evidence="ECO:0007829|PDB:1MU2"
FT TURN 1059..1061
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 1064..1070
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 1075..1082
FT /evidence="ECO:0007829|PDB:1MU2"
FT HELIX 1085..1098
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 1102..1109
FT /evidence="ECO:0007829|PDB:1MU2"
FT HELIX 1111..1118
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 1122..1125
FT /evidence="ECO:0007829|PDB:1MU2"
FT HELIX 1127..1138
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 1140..1146
FT /evidence="ECO:0007829|PDB:1MU2"
FT STRAND 1149..1151
FT /evidence="ECO:0007829|PDB:1MU2"
FT HELIX 1156..1164
FT /evidence="ECO:0007829|PDB:1MU2"
FT TURN 1173..1175
FT /evidence="ECO:0007829|PDB:1E0E"
FT HELIX 1176..1186
FT /evidence="ECO:0007829|PDB:3F9K"
FT HELIX 1190..1197
FT /evidence="ECO:0007829|PDB:3F9K"
FT HELIX 1201..1209
FT /evidence="ECO:0007829|PDB:3F9K"
FT TURN 1212..1216
FT /evidence="ECO:0007829|PDB:3F9K"
FT STRAND 1231..1239
FT /evidence="ECO:0007829|PDB:3F9K"
FT STRAND 1242..1249
FT /evidence="ECO:0007829|PDB:3F9K"
FT TURN 1250..1252
FT /evidence="ECO:0007829|PDB:3F9K"
FT STRAND 1255..1262
FT /evidence="ECO:0007829|PDB:3F9K"
FT HELIX 1265..1276
FT /evidence="ECO:0007829|PDB:3F9K"
FT STRAND 1282..1286
FT /evidence="ECO:0007829|PDB:3F9K"
FT TURN 1290..1292
FT /evidence="ECO:0007829|PDB:3F9K"
FT HELIX 1295..1304
FT /evidence="ECO:0007829|PDB:3F9K"
FT STRAND 1307..1312
FT /evidence="ECO:0007829|PDB:3F9K"
FT HELIX 1321..1335
FT /evidence="ECO:0007829|PDB:3F9K"
FT HELIX 1337..1339
FT /evidence="ECO:0007829|PDB:3F9K"
FT HELIX 1343..1356
FT /evidence="ECO:0007829|PDB:3F9K"
FT TURN 1361..1364
FT /evidence="ECO:0007829|PDB:3F9K"
FT HELIX 1367..1376
FT /evidence="ECO:0007829|PDB:3F9K"
SQ SEQUENCE 1464 AA; 164645 MW; A594A43F3E9ADB60 CRC64;
MGARNSVLRG KKADELERIR LRPGGKKKYR LKHIVWAANK LDRFGLAESL LESKEGCQKI
LTVLDPMVPT GSENLKSLFN TVCVIWCIHA EEKVKDTEGA KQIVRRHLVA ETGTAEKMPS
TSRPTAPSSE KGGNYPVQHV GGNYTHIPLS PRTLNAWVKL VEEKKFGAEV VPGFQALSEG
CTPYDINQML NCVGDHQAAM QIIREIINEE AAEWDVQHPI PGPLPAGQLR EPRGSDIAGT
TSTVEEQIQW MFRPQNPVPV GNIYRRWIQI GLQKCVRMYN PTNILDIKQG PKEPFQSYVD
RFYKSLRAEQ TDPAVKNWMT QTLLVQNANP DCKLVLKGLG MNPTLEEMLT ACQGVGGPGQ
KARLMAEALK EVIGPAPIPF AAAQQRKAFK CWNCGKEGHS ARQCRAPRRQ GCWKCGKPGH
IMTNCPDRQA GFLRTGPLGK EAPQLPRGPS SAGADTNSTP SGSSSGSTGE IYAAREKTER
AERETIQGSD RGLTAPRAGG DTIQGATNRG LAAPQFSLWK RPVVTAYIEG QPVEVLLDTG
ADDSIVAGIE LGNNYSPKIV GGIGGFINTK EYKNVEIEVL NKKVRATIMT GDTPINIFGR
NILTALGMSL NLPVAKVEPI KIMLKPGKDG PKLRQWPLTK EKIEALKEIC EKMEKEGQLE
EAPPTNPYNT PTFAIKKKDK NKWRMLIDFR ELNKVTQDFT EIQLGIPHPA GLAKKRRITV
LDVGDAYFSI PLHEDFRPYT AFTLPSVNNA EPGKRYIYKV LPQGWKGSPA IFQHTMRQVL
EPFRKANKDV IIIQYMDDIL IASDRTDLEH DRVVLQLKEL LNGLGFSTPD EKFQKDPPYH
WMGYELWPTK WKLQKIQLPQ KEIWTVNDIQ KLVGVLNWAA QLYPGIKTKH LCRLIRGKMT
LTEEVQWTEL AEAELEENRI ILSQEQEGHY YQEEKELEAT VQKDQENQWT YKIHQEEKIL
KVGKYAKVKN THTNGIRLLA QVVQKIGKEA LVIWGRIPKF HLPVEREIWE QWWDNYWQVT
WIPDWDFVST PPLVRLAFNL VGDPIPGAET FYTDGSCNRQ SKEGKAGYVT DRGKDKVKKL
EQTTNQQAEL EAFAMALTDS GPKVNIIVDS QYVMGISASQ PTESESKIVN QIIEEMIKKE
AIYVAWVPAH KGIGGNQEVD HLVSQGIRQV LFLEKIEPAQ EEHEKYHSNV KELSHKFGIP
NLVARQIVNS CAQCQQKGEA IHGQVNAELG TWQMDCTHLE GKIIIVAVHV ASGFIEAEVI
PQESGRQTAL FLLKLASRWP ITHLHTDNGA NFTSQEVKMV AWWIGIEQSF GVPYNPQSQG
VVEAMNHHLK NQISRIREQA NTIETIVLMA IHCMNFKRRG GIGDMTPSER LINMITTEQE
IQFLQAKNSK LKDFRVYFRE GRDQLWKGPG ELLWKGEGAV LVKVGTDIKI IPRRKAKIIR
DYGGRQEMDS GSHLEGARED GEMA
