ID   POL_HV1BR               Reviewed;        1447 AA.
AC   P03367;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 246.
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=3.4.23.16;
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 1 group M subtype B (isolate BRU/LAI)
OS   (HIV-1).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus;
OC   Lentivirus humimdef1; Human immunodeficiency virus type 1.
OX   NCBI_TaxID=11686;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2981635; DOI=10.1016/0092-8674(85)90303-4;
RA   Wain-Hobson S., Sonigo P., Danos O., Cole S., Alizon M.;
RT   "Nucleotide sequence of the AIDS virus, LAV.";
RL   Cell 40:9-17(1985).
RN   [2]
RP   SEQUENCE REVISION TO 455-467.
RX   PubMed=2424612; DOI=10.1016/0092-8674(86)90860-3;
RA   Alizon M., Wain-Hobson S., Montagnier L., Sonigo P.;
RT   "Genetic variability of the AIDS virus: nucleotide sequence analysis of two
RT   isolates from African patients.";
RL   Cell 46:63-74(1986).
RN   [3]
RP   CLEAVAGE OF NEF BY VIRAL PROTEASE.
RX   PubMed=7835426; DOI=10.1016/0014-5793(94)01370-g;
RA   Gaedigk-Nitschko K., Schoen A., Wachinger G., Erfle V., Kohleisen B.;
RT   "Cleavage of recombinant and cell derived human immunodeficiency virus 1
RT   (HIV-1) Nef protein by HIV-1 protease.";
RL   FEBS Lett. 357:275-278(1995).
RN   [4]
RP   CLEAVAGE OF VIF BY VIRAL PROTEASE.
RX   PubMed=12186895; DOI=10.1128/jvi.76.18.9112-9123.2002;
RA   Khan M.A., Akari H., Kao S., Aberham C., Davis D., Buckler-White A.,
RA   Strebel K.;
RT   "Intravirion processing of the human immunodeficiency virus type 1 Vif
RT   protein by the viral protease may be correlated with Vif function.";
RL   J. Virol. 76:9112-9123(2002).
RN   [5]
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   [6]
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   [7]
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   [8]
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   [9]
RP   REVIEW.
RX   PubMed=12873766; DOI=10.1016/s0005-2736(03)00163-9;
RA   Scarlata S., Carter C.;
RT   "Role of HIV-1 Gag domains in viral assembly.";
RL   Biochim. Biophys. Acta 1614:62-72(2003).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 501-599.
RX   PubMed=1799632; DOI=10.1016/0300-9084(91)90169-2;
RA   Spinelli S., Liu Q.Z., Alzari P.M., Hirel P.H., Poljak R.J.;
RT   "The three-dimensional structure of the aspartyl protease from the HIV-1
RT   isolate BRU.";
RL   Biochimie 73:1391-1396(1991).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 600-1026.
RX   PubMed=1374166; DOI=10.1038/357085a0;
RA   Arnold E., Jacobo-Molina A., Nanni R.G., Williams R.L., Lu X., Ding J.,
RA   Clark A.D. Jr., Zhang A., Ferris A.L., Clark P., Hizi A., Hughes S.H.;
RT   "Structure of HIV-1 reverse transcriptase/DNA complex at 7 A resolution
RT   showing active site locations.";
RL   Nature 357:85-89(1992).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 501-599 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   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 501-599.
RX   PubMed=8893827; DOI=10.1021/jm960541s;
RA   Thaisrivongs S., Skulnick H.I., Turner S.R., Strohbach J.W., Tommasi R.A.,
RA   Johnson P.D., Aristoff P.A., Judge T.M., Gammill R.B., Morris J.K.,
RA   Romines K.R., Chrusciel R.A., Hinshaw R.R., Chong K.-T., Tarpley W.G.,
RA   Poppe S.M., Slade D.E., Lynn J.C., Horng M.-M., Tomich P.K., Seest E.P.,
RA   Dolak L.A., Howe W.J., Howard G.M., Schwende F.J., Toth L.N., Padbury G.E.,
RA   Wilson G.J., Shiou L., Zipp G.L., Wilkinson K.F., Rush B.D., Ruwart M.J.,
RA   Koeplinger K.A., Zhao Z., Cole S., Zaya R.M., Kakuk T.J., Janakiraman M.N.,
RA   Watenpaugh K.D.;
RT   "Structure-based design of HIV protease inhibitors: sulfonamide-containing
RT   5,6-dihydro-4-hydroxy-2-pyrones as non-peptidic inhibitors.";
RL   J. Med. Chem. 39:4349-4353(1996).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 501-599 IN COMPLEX WITH THE
RP   DIFLUOROKETONE CONTAINING INHIBITOR A79285.
RX   PubMed=8551523; DOI=10.1006/jmbi.1996.0026;
RA   Silva A.M., Cachau R.E., Sham H.L., Erickson J.W.;
RT   "Inhibition and catalytic mechanism of HIV-1 aspartic protease.";
RL   J. Mol. Biol. 255:321-346(1996).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 501-599.
RX   PubMed=9370363; DOI=10.1111/j.1432-1033.1997.00523.x;
RA   Weber I.T., Wu J., Adomat J.M., Harrison R.W., Kimmel A.R., Wondrak E.M.,
RA   Louis J.M.;
RT   "Crystallographic analysis of human immunodeficiency virus 1 protease with
RT   an analog of the conserved CA-p2 substrate -- interactions with frequently
RT   occurring glutamic acid residue at P2' position of substrates.";
RL   Eur. J. Biochem. 249:523-530(1997).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 501-599.
RX   PubMed=9521772; DOI=10.1021/bi972183g;
RA   Wu J., Adomat J.M., Ridky T.W., Louis J.M., Leis J., Harrison R.W.,
RA   Weber I.T.;
RT   "Structural basis for specificity of retroviral proteases.";
RL   Biochemistry 37:4518-4526(1998).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 501-599 IN COMPLEX WITH INHIBITOR
RP   SDZ283-910.
RX   PubMed=10047488; DOI=10.1006/jmbi.1998.2533;
RA   Ringhofer S., Kallen J., Dutzler R., Billich A., Visser A.J., Scholz D.,
RA   Steinhauser O., Schreiber H., Auer M., Kungl A.J.;
RT   "X-ray structure and conformational dynamics of the HIV-1 protease in
RT   complex with the inhibitor SDZ283-910: agreement of time-resolved
RT   spectroscopy and molecular dynamics simulations.";
RL   J. Mol. Biol. 286:1147-1159(1999).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 501-599 IN COMPLEX WITH A
RP   PEPTIDOMIMETIC INHIBITOR.
RX   PubMed=11223536; DOI=10.1107/s0907444900018928;
RA   Dohnalek J., Hasek J., Duskova J., Petrokova H., Hradilek M., Soucek M.,
RA   Konvalinka J., Brynda J., Sedlacek J., Fabry M.;
RT   "A distinct binding mode of a hydroxyethylamine isostere inhibitor of HIV-1
RT   protease.";
RL   Acta Crystallogr. D 57:472-476(2001).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 501-599.
RX   PubMed=11906284; DOI=10.1021/jm010979e;
RA   Dohnalek J., Hasek J., Duskova J., Petrokova H., Hradilek M., Soucek M.,
RA   Konvalinka J., Brynda J., Sedlacek J., Fabry M.;
RT   "Hydroxyethylamine isostere of an HIV-1 protease inhibitor prefers its
RT   amine to the hydroxy group in binding to catalytic aspartates. A
RT   synchrotron study of HIV-1 protease in complex with a peptidomimetic
RT   inhibitor.";
RL   J. Med. Chem. 45:1432-1438(2002).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 501-599 IN COMPLEX WITH AN
RP   ETHYLENAMINE PEPTIDOMIMETIC INHIBITOR.
RX   PubMed=12699382; DOI=10.1021/jm021079g;
RA   Skalova T., Hasek J., Dohnalek J., Petrokova H., Buchtelova E., Duskova J.,
RA   Soucek M., Majer P., Uhlikova T., Konvalinka J.;
RT   "An ethylenamine inhibitor binds tightly to both wild type and mutant HIV-1
RT   proteases. Structure and energy study.";
RL   J. Med. Chem. 46:1636-1644(2003).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 501-599 IN COMPLEX WITH AN
RP   ETHYLENEAMINE INHIBITOR.
RX   PubMed=15560786; DOI=10.1111/j.1432-1033.2004.04384.x;
RA   Petrokova H., Duskova J., Dohnalek J., Skalova T.,
RA   Vondrackova-Buchtelova E., Soucek M., Konvalinka J., Brynda J., Fabry M.,
RA   Sedlacek J., Hasek J.;
RT   "Role of hydroxyl group and R/S configuration of isostere in binding
RT   properties of HIV-1 protease inhibitors.";
RL   Eur. J. Biochem. 271:4451-4461(2004).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 501-599 IN COMPLEX WITH THE
RP   INHIBITOR KNI-577.
RX   PubMed=15103623; DOI=10.1002/prot.20069;
RA   Vega S., Kang L.W., Velazquez-Campoy A., Kiso Y., Amzel L.M., Freire E.;
RT   "A structural and thermodynamic escape mechanism from a drug resistant
RT   mutation of the HIV-1 protease.";
RL   Proteins 55:594-602(2004).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (1.03 ANGSTROMS) OF 501-599 IN COMPLEX WITH A
RP   PEPTIDOMIMETIC INHIBITOR.
RX   PubMed=15056001; DOI=10.1021/jm031105q;
RA   Brynda J., Rezacova P., Fabry M., Horejsi M., Stouracova R., Sedlacek J.,
RA   Soucek M., Hradilek M., Lepsik M., Konvalinka J.;
RT   "A phenylnorstatine inhibitor binding to HIV-1 protease: geometry,
RT   protonation, and subsite-pocket interactions analyzed at atomic
RT   resolution.";
RL   J. Med. Chem. 47:2030-2036(2004).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 501-599 IN COMPLEX WITH THE
RP   INHIBITOR UIC-94017.
RX   PubMed=15066436; DOI=10.1016/j.jmb.2004.02.052;
RA   Tie Y., Boross P.I., Wang Y.-F., Gaddis L., Hussain A.K., Leshchenko S.,
RA   Ghosh A.K., Louis J.M., Harrison R.W., Weber I.T.;
RT   "High resolution crystal structures of HIV-1 protease with a potent non-
RT   peptide inhibitor (UIC-94017) active against multi-drug-resistant clinical
RT   strains.";
RL   J. Mol. Biol. 338:341-352(2004).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 501-599.
RX   PubMed=15066177; DOI=10.1111/j.1432-1033.2004.04060.x;
RA   Mahalingam B., Wang Y.-F., Boross P.I., Tozser J., Louis J.M.,
RA   Harrison R.W., Weber I.T.;
RT   "Crystal structures of HIV protease V82A and L90M mutants reveal changes in
RT   the indinavir-binding site.";
RL   Eur. J. Biochem. 271:1516-1524(2004).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 501-599.
RX   PubMed=15379553; DOI=10.1021/bi049459m;
RA   Clemente J.C., Moose R.E., Hemrajani R., Whitford L.R., Govindasamy L.,
RA   Reutzel R., McKenna R., Agbandje-McKenna M., Goodenow M.M., Dunn B.M.;
RT   "Comparing the accumulation of active- and nonactive-site mutations in the
RT   HIV-1 protease.";
RL   Biochemistry 43:12141-12151(2004).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 501-599 IN COMPLEX WITH A
RP   PEPTIDOMIMETIC INHIBITOR.
RX   PubMed=15502300; DOI=10.1107/s0907444904021572;
RA   Brynda J., Rezacova P., Fabry M., Horejsi M., Stouracova R., Soucek M.,
RA   Hradilek M., Konvalinka J., Sedlacek J.;
RT   "Inhibitor binding at the protein interface in crystals of a HIV-1 protease
RT   complex.";
RL   Acta Crystallogr. D 60:1943-1948(2004).
RN   [28]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF 1160-1447, AND SUBUNIT
RP   (INTEGRASE).
RX   PubMed=28059769; DOI=10.1126/science.aah5163;
RA   Passos D.O., Li M., Yang R., Rebensburg S.V., Ghirlando R., Jeon Y.,
RA   Shkriabai N., Kvaratskhelia M., Craigie R., Lyumkis D.;
RT   "Cryo-EM structures and atomic model of the HIV-1 strand transfer complex
RT   intasome.";
RL   Science 355:89-92(2017).
CC   -!- FUNCTION: Gag-Pol polyprotein and Gag polyprotein may regulate their
CC       own translation, by the binding genomic RNA in the 5'-UTR. At low
CC       concentration, Gag-Pol and Gag would promote translation, whereas at
CC       high concentration, the polyproteins encapsidate genomic RNA and then
CC       shut off translation (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Matrix protein p17 targets Gag and Gag-pol polyproteins to
CC       the plasma membrane via a multipartite membrane-binding signal, that
CC       includes its myristoylated N-terminus (By similarity). Matrix protein
CC       is part of the pre-integration complex. Implicated in the release from
CC       host cell mediated by Vpu. Binds to RNA (By similarity). {ECO:0000250,
CC       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: The aspartyl protease mediates proteolytic cleavages of Gag
CC       and Gag-Pol polyproteins during or shortly after the release of the
CC       virion from the plasma membrane. Cleavages take place as an ordered,
CC       step-wise cascade to yield mature proteins. This process is called
CC       maturation. Displays maximal activity during the budding process just
CC       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. Also mediates cleavage of
CC       host YTHDF3. Mediates cleavage of host CARD8, thereby activating the
CC       CARD8 inflammasome, leading to the clearance of latent HIV-1 in patient
CC       CD4(+) T-cells after viral reactivation; in contrast, HIV-1 can evade
CC       CARD8-sensing when its protease remains inactive in infected cells
CC       prior to viral budding (By similarity). {ECO:0000255|PROSITE-
CC       ProRule:PRU00275}.
CC   -!- FUNCTION: Reverse transcriptase/ribonuclease H (RT) is a
CC       multifunctional enzyme that converts the viral RNA genome into dsDNA in
CC       the cytoplasm, shortly after virus entry into the cell. This enzyme
CC       displays a DNA polymerase activity that can copy either DNA or RNA
CC       templates, and a ribonuclease H (RNase H) activity that cleaves the RNA
CC       strand of RNA-DNA heteroduplexes in a partially processive 3' to 5'
CC       endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires
CC       many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS)
CC       situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA
CC       primer to perform a short round of RNA-dependent minus-strand DNA
CC       synthesis. The reading proceeds through the U5 region and ends after
CC       the repeated (R) region which is present at both ends of viral RNA. The
CC       portion of the RNA-DNA heteroduplex is digested by the RNase H,
CC       resulting in a ssDNA product attached to the tRNA primer. This
CC       ssDNA/tRNA hybridizes with the identical R region situated at the 3'
CC       end of viral RNA. This template exchange, known as minus-strand DNA
CC       strong stop transfer, can be either intra- or intermolecular. RT uses
CC       the 3' end of this newly synthesized short ssDNA to perform the RNA-
CC       dependent minus-strand DNA synthesis of the whole template. RNase H
CC       digests the RNA template except for two polypurine tracts (PPTs)
CC       situated at the 5'-end and near the center of the genome. It is not
CC       clear if both polymerase and RNase H activities are simultaneous. RNase
CC       H probably can proceed both in a polymerase-dependent (RNA cut into
CC       small fragments by the same RT performing DNA synthesis) and a
CC       polymerase-independent mode (cleavage of remaining RNA fragments by
CC       free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis
CC       using the PPTs that have not been removed by RNase H as primers. PPTs
CC       and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS
CC       regions hybridize to form a circular dsDNA intermediate. Strand
CC       displacement synthesis by RT to the PBS and PPT ends produces a blunt
CC       ended, linear dsDNA copy of the viral genome that includes long
CC       terminal repeats (LTRs) at both ends (By similarity). {ECO:0000250}.
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=Specific for a P1 residue that is hydrophobic, and P1'
CC         variable, but often Pro.; EC=3.4.23.16;
CC         Evidence={ECO:0000255|PROSITE-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;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA
CC         hybrid.; EC=3.1.13.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC         diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC         COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC         EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC         diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC         COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC         EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-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: The viral protease is inhibited by many synthetic
CC       protease inhibitors (PIs), such as amprenavir, atazanavir, indinavir,
CC       loprinavir, nelfinavir, ritonavir and saquinavir. RT can be inhibited
CC       either by nucleoside RT inhibitors (NRTIs) or by non nucleoside RT
CC       inhibitors (NNRTIs). NRTIs act as chain terminators, whereas NNRTIs
CC       inhibit DNA polymerization by binding a small hydrophobic pocket near
CC       the RT active site and inducing an allosteric change in this region.
CC       Classical NRTIs are abacavir, adefovir (PMEA), didanosine (ddI),
CC       lamivudine (3TC), stavudine (d4T), tenofovir (PMPA), zalcitabine (ddC),
CC       and zidovudine (AZT). Classical NNRTIs are atevirdine (BHAP U-87201E),
CC       delavirdine, efavirenz (DMP-266), emivirine (I-EBU), and nevirapine
CC       (BI-RG-587). The tritherapies used as a basic effective treatment of
CC       AIDS associate two NRTIs and one NNRTI. Use of protease inhibitors in
CC       tritherapy regimens permit more ambitious therapeutic strategies (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: [Matrix protein p17]: Homotrimer; further assembles as
CC       hexamers of trimers (By similarity). Interacts with gp41 (via C-
CC       terminus) (By similarity). Interacts with host CALM1; this interaction
CC       induces a conformational change in the Matrix protein, triggering
CC       exposure of the myristate group (By similarity). Interacts with host
CC       AP3D1; this interaction allows the polyprotein trafficking to
CC       multivesicular bodies during virus assembly (By similarity). Part of
CC       the pre-integration complex (PIC) which is composed of viral genome,
CC       matrix protein, Vpr and integrase (By similarity).
CC       {ECO:0000250|UniProtKB:P04585, ECO:0000250|UniProtKB:P12497}.
CC   -!- SUBUNIT: [Capsid protein p24]: Homodimer; the homodimer further
CC       multimerizes as homohexamers or homopentamers. Interacts with human
CC       PPIA/CYPA (By similarity); This interaction stabilizes the capsid.
CC       Interacts with human NUP153 (By similarity). Interacts with host PDZD8;
CC       this interaction stabilizes the capsid (By similarity). Interacts with
CC       monkey TRIM5; this interaction destabilizes the capsid (By similarity).
CC       {ECO:0000250|UniProtKB:P04585, ECO:0000250|UniProtKB:P12497}.
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 (PubMed:28059769). 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:P04585, ECO:0000250|UniProtKB:P12497,
CC       ECO:0000269|PubMed:28059769}.
CC   -!- SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane
CC       {ECO:0000250|UniProtKB:P12493}; Lipid-anchor. Host endosome, host
CC       multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These
CC       locations are linked to virus assembly sites. The main location is the
CC       cell membrane, but under some circumstances, late endosomal
CC       compartments can serve as productive sites for virion assembly.
CC       {ECO:0000250|UniProtKB:P12493}.
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=P03367-1; Sequence=Displayed;
CC       Name=Gag polyprotein;
CC         IsoId=P03348-1; 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   -!- PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the
CC       virion by a host kinase. Phosphorylation is apparently not a major
CC       regulator of membrane association. {ECO:0000250|UniProtKB:P04585}.
CC   -!- PTM: [Capsid protein p24]: Phosphorylated possibly by host MAPK1; this
CC       phosphorylation is necessary for Pin1-mediated virion uncoating.
CC       {ECO:0000250|UniProtKB:P12493}.
CC   -!- PTM: [Nucleocapsid protein p7]: Methylated by host PRMT6, impairing its
CC       function by reducing RNA annealing and the initiation of reverse
CC       transcription. {ECO:0000250|UniProtKB:P03347}.
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: HIV-1 lineages are divided in three main groups, M (for
CC       Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast
CC       majority of strains found worldwide belong to the group M. Group O
CC       seems to be endemic to and largely confined to Cameroon and neighboring
CC       countries in West Central Africa, where these viruses represent a small
CC       minority of HIV-1 strains. The group N is represented by a limited
CC       number of isolates from Cameroonian persons. The group M is further
CC       subdivided in 9 clades or subtypes (A to D, F to H, J and K).
CC   -!- MISCELLANEOUS: Resistance to inhibitors associated with mutations are
CC       observed both in viral protease and in reverse transcriptase. Most of
CC       the time, single mutations confer only a modest reduction in drug
CC       susceptibility. Combination of several mutations is usually required to
CC       develop a high-level drug resistance. These mutations are predominantly
CC       found in clade B viruses and not in other genotypes. They are listed in
CC       the clade B representative isolate HXB2 (AC P04585).
CC   -!- MISCELLANEOUS: [Isoform Gag-Pol polyprotein]: Produced by -1 ribosomal
CC       frameshifting.
CC   -!- WEB RESOURCE: Name=HIV drug resistance mutations;
CC       URL="https://www.iasusa.org/hiv-drug-resistance/hiv-drug-resistance-mutations/";
CC   -!- WEB RESOURCE: Name=hivdb; Note=HIV drug resistance database;
CC       URL="https://hivdb.stanford.edu";
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DR   EMBL; K02013; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   PDB; 1A8G; X-ray; 2.50 A; A/B=501-599.
DR   PDB; 1A8K; X-ray; 2.00 A; A/B/D/E=501-599.
DR   PDB; 1A94; X-ray; 2.00 A; A/B/D/E=501-599.
DR   PDB; 1AAQ; X-ray; 2.50 A; A/B=501-599.
DR   PDB; 1D4S; X-ray; 2.50 A; A/B=501-599.
DR   PDB; 1D4Y; X-ray; 1.97 A; A/B=501-599.
DR   PDB; 1DAZ; X-ray; 1.55 A; C/D=501-599.
DR   PDB; 1DIF; X-ray; 1.70 A; A/B=501-599.
DR   PDB; 1FQX; X-ray; 3.10 A; A/B=501-599.
DR   PDB; 1HHP; X-ray; 2.70 A; A=501-599.
DR   PDB; 1HNI; X-ray; 2.80 A; B=600-1026.
DR   PDB; 1HPO; X-ray; 2.50 A; A/B=501-599.
DR   PDB; 1HPX; X-ray; 2.00 A; A/B=501-599.
DR   PDB; 1HSG; X-ray; 2.00 A; A/B=501-599.
DR   PDB; 1HVL; X-ray; 1.80 A; A/B=501-599.
DR   PDB; 1IIQ; X-ray; 1.83 A; A/B=501-599.
DR   PDB; 1IZI; X-ray; 2.15 A; A/B=501-599.
DR   PDB; 1LZQ; X-ray; 2.20 A; A/B=501-599.
DR   PDB; 1M0B; X-ray; 2.45 A; A/B=501-599.
DR   PDB; 1MRW; X-ray; 2.00 A; A/B=501-599.
DR   PDB; 1MRX; X-ray; 2.00 A; A/B=501-599.
DR   PDB; 1MSM; X-ray; 2.00 A; A/B=501-599.
DR   PDB; 1MSN; X-ray; 2.00 A; A/B=501-599.
DR   PDB; 1NH0; X-ray; 1.03 A; A/B=501-599.
DR   PDB; 1RL8; X-ray; 2.00 A; A/B=501-599.
DR   PDB; 1SDT; X-ray; 1.30 A; A/B=501-599.
DR   PDB; 1SDU; X-ray; 1.25 A; A/B=501-599.
DR   PDB; 1SDV; X-ray; 1.40 A; A/B=501-599.
DR   PDB; 1SGU; X-ray; 1.90 A; A/B=501-599.
DR   PDB; 1SH9; X-ray; 2.50 A; A/B=501-599.
DR   PDB; 1SP5; X-ray; 1.80 A; A/B=501-599, I=559-563.
DR   PDB; 1U8G; X-ray; 2.20 A; A/B=501-599.
DR   PDB; 1UPJ; X-ray; 2.22 A; A=501-599.
DR   PDB; 1XL2; X-ray; 1.50 A; A/B=501-599.
DR   PDB; 1XL5; X-ray; 1.73 A; A/B=501-599.
DR   PDB; 1Z8C; X-ray; 2.20 A; A/B=501-599.
DR   PDB; 1ZBG; X-ray; 2.00 A; A/B=501-599.
DR   PDB; 1ZJ7; X-ray; 1.93 A; A=501-599.
DR   PDB; 1ZLF; X-ray; 2.30 A; A/B=501-599.
DR   PDB; 1ZPK; X-ray; 1.65 A; A/B=501-599.
DR   PDB; 1ZTZ; X-ray; 2.15 A; A/B=501-599.
DR   PDB; 2A1E; X-ray; 1.30 A; A/B=501-599.
DR   PDB; 2AZ8; X-ray; 2.00 A; A=501-599.
DR   PDB; 2AZ9; X-ray; 2.50 A; A=501-599.
DR   PDB; 2AZB; X-ray; 2.03 A; A=501-599.
DR   PDB; 2AZC; X-ray; 2.01 A; A/B=501-599.
DR   PDB; 2B7Z; X-ray; 2.20 A; A/B=501-599.
DR   PDB; 2BB9; X-ray; 1.35 A; A/B=501-599.
DR   PDB; 2FDE; X-ray; 2.70 A; A/B=501-599.
DR   PDB; 2HB2; X-ray; 2.30 A; A=501-599.
DR   PDB; 2HB4; X-ray; 2.15 A; A=501-599.
DR   PDB; 2HC0; X-ray; 1.30 A; A/B=501-599.
DR   PDB; 2HND; X-ray; 2.50 A; B=606-1027.
DR   PDB; 2HNY; X-ray; 2.50 A; B=606-1027.
DR   PDB; 2IEN; X-ray; 1.30 A; A/B=501-599.
DR   PDB; 2O4K; X-ray; 1.60 A; A/B=501-599.
DR   PDB; 2O4L; X-ray; 1.33 A; A/B=501-599.
DR   PDB; 2O4N; X-ray; 2.00 A; A/B=501-599.
DR   PDB; 2O4P; X-ray; 1.80 A; A/B=501-599.
DR   PDB; 2O4S; X-ray; 1.54 A; A/B=501-599.
DR   PDB; 2P3B; X-ray; 2.10 A; A/B=501-599.
DR   PDB; 2PK5; X-ray; 1.90 A; A/B=501-599.
DR   PDB; 2PK6; X-ray; 1.45 A; A/B=501-599.
DR   PDB; 2PQZ; X-ray; 1.55 A; A/B=501-599.
DR   PDB; 2PWC; X-ray; 1.78 A; A/B=501-599.
DR   PDB; 2PWR; X-ray; 1.50 A; A/B=501-599.
DR   PDB; 2PYM; X-ray; 1.90 A; A/B=501-599.
DR   PDB; 2PYN; X-ray; 1.85 A; A/B=501-599.
DR   PDB; 2Q63; X-ray; 2.20 A; A/B=501-599.
DR   PDB; 2Q64; X-ray; 2.50 A; A/B=501-599.
DR   PDB; 2QAK; X-ray; 2.20 A; A/B=501-599.
DR   PDB; 2QCI; X-ray; 1.20 A; A/B=501-599.
DR   PDB; 2QD6; X-ray; 1.28 A; A/B=501-599.
DR   PDB; 2QD7; X-ray; 1.11 A; A/B=501-599.
DR   PDB; 2QD8; X-ray; 1.35 A; A/B=501-599.
DR   PDB; 2QHC; X-ray; 2.80 A; A/B=501-599.
DR   PDB; 2QNN; X-ray; 1.48 A; A/B=501-599.
DR   PDB; 2QNP; X-ray; 1.41 A; A/B=501-599.
DR   PDB; 2QNQ; X-ray; 2.30 A; A/B=501-599.
DR   PDB; 2R43; X-ray; 1.58 A; A/B=501-599.
DR   PDB; 2UPJ; X-ray; 3.00 A; A/B=501-599.
DR   PDB; 2Z4O; X-ray; 1.60 A; A/B=501-599.
DR   PDB; 2ZGA; X-ray; 1.65 A; A=501-599.
DR   PDB; 2ZYE; Neutron; 1.90 A; A/B=501-599.
DR   PDB; 3A2O; X-ray; 0.88 A; A/B=501-599.
DR   PDB; 3BHE; X-ray; 1.75 A; A/B=501-599.
DR   PDB; 3BVA; X-ray; 1.05 A; A/B=501-599.
DR   PDB; 3BVB; X-ray; 1.30 A; A/B=501-599.
DR   PDB; 3CKT; X-ray; 1.65 A; A/B=501-599.
DR   PDB; 3DJK; X-ray; 1.00 A; A/B=501-599.
DR   PDB; 3DK1; X-ray; 1.07 A; A/B=501-599.
DR   PDB; 3FX5; X-ray; 0.93 A; A/B=501-599.
DR   PDB; 3GGU; X-ray; 1.80 A; A/B=501-599.
DR   PDB; 3H5B; X-ray; 1.29 A; A/B=501-599.
DR   PDB; 3I6O; X-ray; 1.17 A; A/B=501-599.
DR   PDB; 3I8W; X-ray; 1.70 A; A=501-599.
DR   PDB; 3JVW; X-ray; 1.80 A; A/B=501-599.
DR   PDB; 3JVY; X-ray; 1.60 A; A/B=501-599.
DR   PDB; 3JW2; X-ray; 1.80 A; A/B=501-599.
DR   PDB; 3KDB; X-ray; 1.66 A; A/B=501-599.
DR   PDB; 3KDC; X-ray; 2.20 A; A/B=501-599.
DR   PDB; 3KDD; X-ray; 1.80 A; A/B=501-599.
DR   PDB; 3NDU; X-ray; 1.25 A; A/B/C/D=501-599.
DR   PDB; 3NDW; X-ray; 1.14 A; A/B=501-599.
DR   PDB; 3NDX; X-ray; 1.03 A; A/B=501-599.
DR   PDB; 3NLS; X-ray; 1.70 A; A/B=501-599.
DR   PDB; 3PWM; X-ray; 1.46 A; A/B=501-599.
DR   PDB; 3PWR; X-ray; 1.45 A; A/B=501-599.
DR   PDB; 3QBF; X-ray; 1.45 A; A/B=501-599.
DR   PDB; 3QIH; X-ray; 1.39 A; A/B=501-599.
DR   PDB; 3QN8; X-ray; 1.38 A; A/B=501-599.
DR   PDB; 3QP0; X-ray; 1.45 A; A/B=501-599.
DR   PDB; 3QPJ; X-ray; 1.61 A; A/B=501-599.
DR   PDB; 3QRM; X-ray; 1.73 A; A/B=501-599.
DR   PDB; 3QRO; X-ray; 1.62 A; A/B=501-599.
DR   PDB; 3QRS; X-ray; 1.59 A; A/B=501-599.
DR   PDB; 3ST5; X-ray; 1.45 A; A/B=501-599.
DR   PDB; 3T11; X-ray; 2.22 A; A/B=501-599.
DR   PDB; 3T3C; X-ray; 2.10 A; A/B=501-599.
DR   PDB; 3TOF; X-ray; 1.45 A; A/B=501-599.
DR   PDB; 3TOG; X-ray; 1.24 A; A/B/C/D=501-599.
DR   PDB; 3TOH; X-ray; 1.12 A; A/B=501-599.
DR   PDB; 3TTP; X-ray; 2.23 A; A/B=501-599.
DR   PDB; 3U7S; X-ray; 2.05 A; A/B=501-599.
DR   PDB; 3UCB; X-ray; 1.38 A; A/B=501-599.
DR   PDB; 3UF3; X-ray; 1.63 A; A/B=501-599.
DR   PDB; 3UFN; X-ray; 1.45 A; A/B=501-599.
DR   PDB; 3UHL; X-ray; 2.20 A; A/B/C/D=501-599.
DR   PDB; 3VF5; X-ray; 1.25 A; A/B=501-599.
DR   PDB; 3VF7; X-ray; 1.30 A; A/B=501-599.
DR   PDB; 3VFB; X-ray; 1.55 A; A/B=501-599.
DR   PDB; 4DFG; X-ray; 1.23 A; A/B=501-599.
DR   PDB; 4FAF; X-ray; 2.10 A; D=361-367.
DR   PDB; 4FE6; X-ray; 2.00 A; A=501-599.
DR   PDB; 4FL8; X-ray; 1.20 A; A/B=501-599.
DR   PDB; 4FLG; X-ray; 1.31 A; A/B=501-599.
DR   PDB; 4FM6; X-ray; 1.40 A; A/B=501-599.
DR   PDB; 4GB2; X-ray; 1.79 A; A/B=501-599.
DR   PDB; 4HDB; X-ray; 1.49 A; A/B=501-599.
DR   PDB; 4HDF; X-ray; 1.29 A; A/B=501-599.
DR   PDB; 4HDP; X-ray; 1.22 A; A/B=501-599.
DR   PDB; 4HE9; X-ray; 1.06 A; A/B=501-599.
DR   PDB; 4HEG; X-ray; 1.46 A; A/B=501-599.
DR   PDB; 4HLA; X-ray; 1.95 A; A/B=501-599.
DR   PDB; 4J54; X-ray; 1.55 A; A/B=501-599.
DR   PDB; 4J55; X-ray; 1.31 A; A/B=501-599.
DR   PDB; 4J5J; X-ray; 1.80 A; A/B=501-599.
DR   PDB; 4JEC; Other; 2.00 A; A/B=501-599.
DR   PDB; 4LL3; X-ray; 1.95 A; A/B=501-599.
DR   PDB; 5E5K; Other; 1.75 A; A/B=501-599.
DR   PDB; 5YOK; X-ray; 0.85 A; A/B=500-599.
DR   PDB; 6BSH; X-ray; 2.65 A; A=600-1156.
DR   PDB; 6P9A; X-ray; 1.66 A; A/B=501-599.
DR   PDB; 6P9B; X-ray; 1.75 A; A/B=501-599.
DR   PDB; 6UWB; X-ray; 1.95 A; A/B=501-599.
DR   PDB; 6UWC; X-ray; 1.95 A; A/B=501-599.
DR   PDB; 6VCE; X-ray; 1.18 A; A/B=501-599.
DR   PDB; 6VLM; X-ray; 2.32 A; A/B=1208-1371.
DR   PDB; 6VOD; X-ray; 1.25 A; A/B=501-599.
DR   PDB; 6VOE; X-ray; 1.30 A; A/B=501-599.
DR   PDB; 7DZM; X-ray; 2.25 A; C=180-188.
DR   PDB; 7DZN; X-ray; 2.63 A; C=180-188.
DR   PDB; 7M9G; X-ray; 1.87 A; A/B=501-599.
DR   PDB; 7M9H; X-ray; 1.89 A; A/B=501-599.
DR   PDB; 7M9I; X-ray; 1.82 A; A/B=501-599.
DR   PDB; 7M9J; X-ray; 1.86 A; A/B=501-599.
DR   PDB; 7M9K; X-ray; 1.84 A; A/B=501-599.
DR   PDB; 7M9L; X-ray; 1.75 A; A/B=501-599.
DR   PDB; 7M9M; X-ray; 1.88 A; A/B=501-599.
DR   PDB; 7M9N; X-ray; 1.82 A; A/B=501-599.
DR   PDB; 7M9O; X-ray; 1.90 A; A/B=501-599.
DR   PDB; 7M9P; X-ray; 1.82 A; A/B=501-599.
DR   PDB; 7M9Q; X-ray; 1.95 A; A/B=501-599.
DR   PDB; 7M9V; X-ray; 1.89 A; A/B=501-599.
DR   PDB; 7M9W; X-ray; 1.90 A; A/B=501-599.
DR   PDB; 7M9X; X-ray; 1.83 A; A/B=501-599.
DR   PDB; 7M9Z; X-ray; 1.83 A; A/B=501-599.
DR   PDB; 7MA0; X-ray; 1.92 A; A/B=501-599.
DR   PDB; 7MA1; X-ray; 1.85 A; A/B=501-599.
DR   PDB; 7MA2; X-ray; 1.87 A; A/B=501-599.
DR   PDB; 7MA3; X-ray; 1.97 A; A/B=501-599.
DR   PDB; 7MA4; X-ray; 1.99 A; A/B=501-599.
DR   PDB; 7MA5; X-ray; 1.98 A; A/B=501-599.
DR   PDB; 7MA6; X-ray; 2.00 A; A/B=501-599.
DR   PDB; 7MA7; X-ray; 1.92 A; A/B=501-599.
DR   PDB; 7MA8; X-ray; 1.90 A; A/B=501-599.
DR   PDB; 7MA9; X-ray; 1.90 A; A/B=501-599.
DR   PDB; 7MAA; X-ray; 1.93 A; A/B=501-599.
DR   PDB; 7MAB; X-ray; 1.88 A; A/B=501-599.
DR   PDB; 7MAC; X-ray; 1.70 A; A/B=501-599.
DR   PDB; 7MAD; X-ray; 1.70 A; A/B=501-599.
DR   PDB; 7MAE; X-ray; 1.74 A; A/B=501-599.
DR   PDB; 7MAF; X-ray; 1.90 A; A/B=501-599.
DR   PDB; 7MAG; X-ray; 1.92 A; A/B=501-599.
DR   PDB; 7MAH; X-ray; 1.88 A; A/B=501-599.
DR   PDB; 7MAI; X-ray; 1.79 A; A/B=501-599.
DR   PDB; 7MAJ; X-ray; 1.87 A; A/B=501-599.
DR   PDB; 7MAK; X-ray; 1.97 A; A/B=501-599.
DR   PDB; 7MAL; X-ray; 1.90 A; A/B=501-599.
DR   PDB; 7MAN; X-ray; 1.89 A; A/B=501-599.
DR   PDB; 7MAO; X-ray; 1.86 A; A/B=501-599.
DR   PDB; 7MAP; X-ray; 1.95 A; A/B=501-599.
DR   PDB; 7MAQ; X-ray; 1.93 A; A/B=501-599.
DR   PDB; 7MAR; X-ray; 1.70 A; A/B/C/D=501-599.
DR   PDB; 7MAS; X-ray; 1.50 A; A/B/C/D=501-599.
DR   PDB; 7N6T; X-ray; 1.32 A; A/B=501-599.
DR   PDB; 7N6V; X-ray; 1.39 A; A/B=501-599.
DR   PDB; 7N6X; X-ray; 1.47 A; A/B=501-599.
DR   PDB; 7TO5; X-ray; 1.13 A; A/B=501-599.
DR   PDB; 7TO6; X-ray; 1.21 A; A/B=501-599.
DR   PDB; 7UPJ; X-ray; 2.00 A; A/B=501-599.
DR   PDB; 8DCH; X-ray; 1.25 A; A/B=501-599.
DR   PDB; 8DCI; X-ray; 1.62 A; A/B=501-599.
DR   PDB; 8FUI; X-ray; 1.25 A; A/B=501-599.
DR   PDB; 8FUJ; X-ray; 1.12 A; A/B=501-599.
DR   PDB; 8VB1; X-ray; 1.30 A; A/B=501-599.
DR   PDB; 9YKP; X-ray; 1.96 A; A/B=501-599.
DR   PDB; 9YRA; X-ray; 1.91 A; A/B=501-599.
DR   PDB; 9YRR; X-ray; 1.89 A; A/B=501-599.
DR   PDB; 9YRY; X-ray; 1.95 A; A/B=501-599.
DR   BMRB; P03367; -.
DR   MDposit; P03367; -.
DR   MDRepo; P03367; -.
DR   SMR; P03367; -.
DR   IntAct; P03367; 2.
DR   MINT; P03367; -.
DR   BindingDB; P03367; -.
DR   ChEMBL; CHEMBL3638326; -.
DR   DrugBank; DB08428; 3(S)-AMINO-4-PHENYL-BUTAN-2(S)-OL.
DR   DrugBank; DB08662; 3-[1-(4-BROMO-PHENYL)-2-METHYL-PROPYL]-4-HYDROXY-CHROMEN-2-ONE.
DR   DrugBank; DB08041; 3-BENZYLOXYCARBONYLAMINO-2-HYDROXY-4-PHENYL-BUTYRIC ACID.
DR   DrugBank; DB07505; N-({(3R,4R)-4-[(benzyloxy)methyl]pyrrolidin-3-yl}methyl)-N-(2-methylpropyl)benzenesulfonamide.
DR   DrugBank; DB07327; R-95845.
DR   DrugCentral; P03367; -.
DR   ABCD; P03367; 1 sequenced antibody.
DR   EvolutionaryTrace; P03367; -.
DR   PRO; PR:P03367; -.
DR   GO; GO:0043657; C:host cell; IEA:GOC.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; ISS:UniProtKB.
DR   GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
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:0046718; P:symbiont entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0052151; P:symbiont-mediated activation of host apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0039657; P:symbiont-mediated suppression of host gene expression; 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   GO; GO:0075523; P:viral translational frameshifting; IEA:UniProtKB-KW.
DR   CDD; cd05482; HIV_retropepsin_like; 1.
DR   CDD; cd01645; RT_Rtv; 1.
DR   FunFam; 1.10.1200.30:FF:000001; Gag polyprotein; 1.
DR   FunFam; 1.10.150.90:FF:000001; Gag polyprotein; 1.
DR   FunFam; 1.10.375.10:FF:000001; Gag polyprotein; 1.
DR   FunFam; 1.20.5.760:FF:000001; Gag polyprotein; 1.
DR   FunFam; 4.10.60.10:FF:000001; Gag polyprotein; 1.
DR   FunFam; 2.40.70.10:FF:000001; Gag-Pol polyprotein; 1.
DR   FunFam; 3.30.420.10:FF:000025; Gag-Pol polyprotein; 1.
DR   FunFam; 2.30.30.10:FF:000001; POL polyprotein; 1.
DR   FunFam; 3.30.420.10:FF:000017; POL polyprotein; 1.
DR   FunFam; 3.30.70.270:FF:000016; POL polyprotein; 1.
DR   Gene3D; 1.10.10.200; -; 1.
DR   Gene3D; 1.10.1200.30; -; 1.
DR   Gene3D; 3.30.70.270; -; 3.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR   Gene3D; 1.10.375.10; Human Immunodeficiency Virus Type 1 Capsid Protein; 1.
DR   Gene3D; 1.10.150.90; Immunodeficiency lentiviruses, gag gene matrix protein p17; 1.
DR   Gene3D; 2.30.30.10; Integrase, C-terminal domain superfamily, retroviral; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
DR   Gene3D; 1.20.5.760; Single helix bin; 1.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR045345; Gag_p24_C.
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   PANTHER; PTHR41694; ENDOGENOUS RETROVIRUS GROUP K MEMBER POL PROTEIN; 1.
DR   PANTHER; PTHR41694:SF3; RNA-DIRECTED DNA POLYMERASE-RELATED; 1.
DR   Pfam; PF00540; Gag_p17; 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; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF50122; DNA-binding domain of retroviral integrase; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF46919; N-terminal Zn binding domain of HIV integrase; 1.
DR   SUPFAM; SSF47836; Retroviral matrix proteins; 1.
DR   SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR   SUPFAM; SSF47943; Retrovirus capsid protein, N-terminal core domain; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 2.
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.
DR   PDBsum; 1A8G; -.
DR   PDBsum; 1A8K; -.
DR   PDBsum; 1A94; -.
DR   PDBsum; 1AAQ; -.
DR   PDBsum; 1D4S; -.
DR   PDBsum; 1D4Y; -.
DR   PDBsum; 1DAZ; -.
DR   PDBsum; 1DIF; -.
DR   PDBsum; 1FQX; -.
DR   PDBsum; 1HHP; -.
DR   PDBsum; 1HNI; -.
DR   PDBsum; 1HPO; -.
DR   PDBsum; 1HPX; -.
DR   PDBsum; 1HSG; -.
DR   PDBsum; 1HVL; -.
DR   PDBsum; 1IIQ; -.
DR   PDBsum; 1IZI; -.
DR   PDBsum; 1LZQ; -.
DR   PDBsum; 1M0B; -.
DR   PDBsum; 1MRW; -.
DR   PDBsum; 1MRX; -.
DR   PDBsum; 1MSM; -.
DR   PDBsum; 1MSN; -.
DR   PDBsum; 1NH0; -.
DR   PDBsum; 1RL8; -.
DR   PDBsum; 1SDT; -.
DR   PDBsum; 1SDU; -.
DR   PDBsum; 1SDV; -.
DR   PDBsum; 1SGU; -.
DR   PDBsum; 1SH9; -.
DR   PDBsum; 1SP5; -.
DR   PDBsum; 1U8G; -.
DR   PDBsum; 1UPJ; -.
DR   PDBsum; 1XL2; -.
DR   PDBsum; 1XL5; -.
DR   PDBsum; 1Z8C; -.
DR   PDBsum; 1ZBG; -.
DR   PDBsum; 1ZJ7; -.
DR   PDBsum; 1ZLF; -.
DR   PDBsum; 1ZPK; -.
DR   PDBsum; 1ZTZ; -.
DR   PDBsum; 2A1E; -.
DR   PDBsum; 2AZ8; -.
DR   PDBsum; 2AZ9; -.
DR   PDBsum; 2AZB; -.
DR   PDBsum; 2AZC; -.
DR   PDBsum; 2B7Z; -.
DR   PDBsum; 2BB9; -.
DR   PDBsum; 2FDE; -.
DR   PDBsum; 2HB2; -.
DR   PDBsum; 2HB4; -.
DR   PDBsum; 2HC0; -.
DR   PDBsum; 2HND; -.
DR   PDBsum; 2HNY; -.
DR   PDBsum; 2IEN; -.
DR   PDBsum; 2O4K; -.
DR   PDBsum; 2O4L; -.
DR   PDBsum; 2O4N; -.
DR   PDBsum; 2O4P; -.
DR   PDBsum; 2O4S; -.
DR   PDBsum; 2P3B; -.
DR   PDBsum; 2PK5; -.
DR   PDBsum; 2PK6; -.
DR   PDBsum; 2PQZ; -.
DR   PDBsum; 2PWC; -.
DR   PDBsum; 2PWR; -.
DR   PDBsum; 2PYM; -.
DR   PDBsum; 2PYN; -.
DR   PDBsum; 2Q63; -.
DR   PDBsum; 2Q64; -.
DR   PDBsum; 2QAK; -.
DR   PDBsum; 2QCI; -.
DR   PDBsum; 2QD6; -.
DR   PDBsum; 2QD7; -.
DR   PDBsum; 2QD8; -.
DR   PDBsum; 2QHC; -.
DR   PDBsum; 2QNN; -.
DR   PDBsum; 2QNP; -.
DR   PDBsum; 2QNQ; -.
DR   PDBsum; 2R43; -.
DR   PDBsum; 2UPJ; -.
DR   PDBsum; 2Z4O; -.
DR   PDBsum; 2ZGA; -.
DR   PDBsum; 2ZYE; -.
DR   PDBsum; 3A2O; -.
DR   PDBsum; 3BHE; -.
DR   PDBsum; 3BVA; -.
DR   PDBsum; 3BVB; -.
DR   PDBsum; 3CKT; -.
DR   PDBsum; 3DJK; -.
DR   PDBsum; 3DK1; -.
DR   PDBsum; 3FX5; -.
DR   PDBsum; 3GGU; -.
DR   PDBsum; 3H5B; -.
DR   PDBsum; 3I6O; -.
DR   PDBsum; 3I8W; -.
DR   PDBsum; 3JVW; -.
DR   PDBsum; 3JVY; -.
DR   PDBsum; 3JW2; -.
DR   PDBsum; 3KDB; -.
DR   PDBsum; 3KDC; -.
DR   PDBsum; 3KDD; -.
DR   PDBsum; 3NDU; -.
DR   PDBsum; 3NDW; -.
DR   PDBsum; 3NDX; -.
DR   PDBsum; 3NLS; -.
DR   PDBsum; 3PWM; -.
DR   PDBsum; 3PWR; -.
DR   PDBsum; 3QBF; -.
DR   PDBsum; 3QIH; -.
DR   PDBsum; 3QN8; -.
DR   PDBsum; 3QP0; -.
DR   PDBsum; 3QPJ; -.
DR   PDBsum; 3QRM; -.
DR   PDBsum; 3QRO; -.
DR   PDBsum; 3QRS; -.
DR   PDBsum; 3ST5; -.
DR   PDBsum; 3T11; -.
DR   PDBsum; 3T3C; -.
DR   PDBsum; 3TOF; -.
DR   PDBsum; 3TOG; -.
DR   PDBsum; 3TOH; -.
DR   PDBsum; 3TTP; -.
DR   PDBsum; 3U7S; -.
DR   PDBsum; 3UCB; -.
DR   PDBsum; 3UF3; -.
DR   PDBsum; 3UFN; -.
DR   PDBsum; 3UHL; -.
DR   PDBsum; 3VF5; -.
DR   PDBsum; 3VF7; -.
DR   PDBsum; 3VFB; -.
DR   PDBsum; 4DFG; -.
DR   PDBsum; 4FAF; -.
DR   PDBsum; 4FE6; -.
DR   PDBsum; 4FL8; -.
DR   PDBsum; 4FLG; -.
DR   PDBsum; 4FM6; -.
DR   PDBsum; 4GB2; -.
DR   PDBsum; 4HDB; -.
DR   PDBsum; 4HDF; -.
DR   PDBsum; 4HDP; -.
DR   PDBsum; 4HE9; -.
DR   PDBsum; 4HEG; -.
DR   PDBsum; 4HLA; -.
DR   PDBsum; 4J54; -.
DR   PDBsum; 4J55; -.
DR   PDBsum; 4J5J; -.
DR   PDBsum; 4JEC; -.
DR   PDBsum; 4LL3; -.
DR   PDBsum; 5E5K; -.
DR   PDBsum; 5YOK; -.
DR   PDBsum; 6BSH; -.
DR   PDBsum; 6P9A; -.
DR   PDBsum; 6P9B; -.
DR   PDBsum; 6UWB; -.
DR   PDBsum; 6UWC; -.
DR   PDBsum; 6VCE; -.
DR   PDBsum; 6VLM; -.
DR   PDBsum; 6VOD; -.
DR   PDBsum; 6VOE; -.
DR   PDBsum; 7DZM; -.
DR   PDBsum; 7DZN; -.
DR   PDBsum; 7M9G; -.
DR   PDBsum; 7M9H; -.
DR   PDBsum; 7M9I; -.
DR   PDBsum; 7M9J; -.
DR   PDBsum; 7M9K; -.
DR   PDBsum; 7M9L; -.
DR   PDBsum; 7M9M; -.
DR   PDBsum; 7M9N; -.
DR   PDBsum; 7M9O; -.
DR   PDBsum; 7M9P; -.
DR   PDBsum; 7M9Q; -.
DR   PDBsum; 7M9V; -.
DR   PDBsum; 7M9W; -.
DR   PDBsum; 7M9X; -.
DR   PDBsum; 7M9Z; -.
DR   PDBsum; 7MA0; -.
DR   PDBsum; 7MA1; -.
DR   PDBsum; 7MA2; -.
DR   PDBsum; 7MA3; -.
DR   PDBsum; 7MA4; -.
DR   PDBsum; 7MA5; -.
DR   PDBsum; 7MA6; -.
DR   PDBsum; 7MA7; -.
DR   PDBsum; 7MA8; -.
DR   PDBsum; 7MA9; -.
DR   PDBsum; 7MAA; -.
DR   PDBsum; 7MAB; -.
DR   PDBsum; 7MAC; -.
DR   PDBsum; 7MAD; -.
DR   PDBsum; 7MAE; -.
DR   PDBsum; 7MAF; -.
DR   PDBsum; 7MAG; -.
DR   PDBsum; 7MAH; -.
DR   PDBsum; 7MAI; -.
DR   PDBsum; 7MAJ; -.
DR   PDBsum; 7MAK; -.
DR   PDBsum; 7MAL; -.
DR   PDBsum; 7MAN; -.
DR   PDBsum; 7MAO; -.
DR   PDBsum; 7MAP; -.
DR   PDBsum; 7MAQ; -.
DR   PDBsum; 7MAR; -.
DR   PDBsum; 7MAS; -.
DR   PDBsum; 7N6T; -.
DR   PDBsum; 7N6V; -.
DR   PDBsum; 7N6X; -.
DR   PDBsum; 7TO5; -.
DR   PDBsum; 7TO6; -.
DR   PDBsum; 7UPJ; -.
DR   PDBsum; 8DCH; -.
DR   PDBsum; 8DCI; -.
DR   PDBsum; 8FUI; -.
DR   PDBsum; 8FUJ; -.
DR   PDBsum; 8VB1; -.
DR   PDBsum; 9YKP; -.
DR   PDBsum; 9YRA; -.
DR   PDBsum; 9YRR; -.
DR   PDBsum; 9YRY; -.
PE   1: Evidence at protein level;
KW   3D-structure; Activation of host caspases by virus; AIDS;
KW   Aspartyl protease; Capsid protein; DNA integration; DNA recombination;
KW   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   Modulation of host cell apoptosis by virus; Multifunctional enzyme;
KW   Myristate; Nuclease; Nucleotidyltransferase; Phosphoprotein; Protease;
KW   Repeat; 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..1447
FT                   /note="Gag-Pol polyprotein"
FT                   /id="PRO_0000261264"
FT   CHAIN           2..132
FT                   /note="Matrix protein p17"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000042330"
FT   CHAIN           133..363
FT                   /note="Capsid protein p24"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000042331"
FT   PEPTIDE         364..377
FT                   /note="Spacer peptide 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000042332"
FT   CHAIN           378..432
FT                   /note="Nucleocapsid protein p7"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000042333"
FT   PEPTIDE         433..440
FT                   /note="Transframe peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000246712"
FT   CHAIN           441..500
FT                   /note="p6-pol"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000042334"
FT   CHAIN           501..599
FT                   /note="Protease"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038652"
FT   CHAIN           600..1159
FT                   /note="Reverse transcriptase/ribonuclease H"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000042335"
FT   CHAIN           600..1039
FT                   /note="p51 RT"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000042336"
FT   CHAIN           1040..1159
FT                   /note="p15"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000042337"
FT   CHAIN           1160..1447
FT                   /note="Integrase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000042338"
FT   DOMAIN          520..589
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT   DOMAIN          643..833
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   DOMAIN          1033..1156
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   DOMAIN          1213..1363
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   ZN_FING         390..407
FT                   /note="CCHC-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         411..428
FT                   /note="CCHC-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         1162..1203
FT                   /note="Integrase-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   DNA_BIND        1382..1429
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          8..43
FT                   /note="Interaction with host CALM1"
FT                   /evidence="ECO:0000250|UniProtKB:P04585"
FT   REGION          12..19
FT                   /note="Interaction with host AP3D1"
FT                   /evidence="ECO:0000250|UniProtKB:P12497"
FT   REGION          14..33
FT                   /note="Interaction with membrane phosphatidylinositol 4,5-
FT                   bisphosphate and RNA"
FT                   /evidence="ECO:0000250|UniProtKB:P12497"
FT   REGION          73..77
FT                   /note="Interaction with membrane phosphatidylinositol 4,5-
FT                   bisphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P12497"
FT   REGION          106..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..227
FT                   /note="Interaction with human PPIA/CYPA and NUP153"
FT                   /evidence="ECO:0000250|UniProtKB:P12497"
FT   REGION          277..363
FT                   /note="Dimerization/Multimerization of capsid protein p24"
FT                   /evidence="ECO:0000250|UniProtKB:P04585"
FT   REGION          447..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..505
FT                   /note="Dimerization of protease"
FT                   /evidence="ECO:0000250|UniProtKB:P04585"
FT   REGION          549..555
FT                   /note="Dimerization of protease"
FT                   /evidence="ECO:0000250|UniProtKB:P04585"
FT   REGION          588..600
FT                   /note="Dimerization of protease"
FT                   /evidence="ECO:0000250|UniProtKB:P04585"
FT   REGION          826..834
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           997..1013
FT                   /note="Tryptophan repeat motif"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        450..470
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        525
FT                   /note="For protease activity; shared with dimeric partner"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   BINDING         709
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         784
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         785
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         1042
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         1077
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         1097
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         1148
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         1171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   BINDING         1175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   BINDING         1199
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   BINDING         1202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT   BINDING         1223
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         1275
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         1311
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            132..133
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   SITE            221..222
FT                   /note="Cis/trans isomerization of proline peptide bond; by
FT                   human PPIA/CYPA"
FT                   /evidence="ECO:0000250"
FT   SITE            363..364
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   SITE            377..378
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   SITE            432..433
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000255"
FT   SITE            440..441
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   SITE            500..501
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   SITE            599..600
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   SITE            1000
FT                   /note="Essential for RT p66/p51 heterodimerization"
FT                   /evidence="ECO:0000250"
FT   SITE            1013
FT                   /note="Essential for RT p66/p51 heterodimerization"
FT                   /evidence="ECO:0000250"
FT   SITE            1039..1040
FT                   /note="Cleavage; by viral protease; partial"
FT                   /evidence="ECO:0000250"
FT   SITE            1159..1160
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         132
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          502..504
FT                   /evidence="ECO:0007829|PDB:3DK1"
FT   STRAND          505..507
FT                   /evidence="ECO:0007829|PDB:5YOK"
FT   STRAND          510..515
FT                   /evidence="ECO:0007829|PDB:5YOK"
FT   STRAND          518..524
FT                   /evidence="ECO:0007829|PDB:5YOK"
FT   STRAND          528..530
FT                   /evidence="ECO:0007829|PDB:1NH0"
FT   STRAND          532..535
FT                   /evidence="ECO:0007829|PDB:5YOK"
FT   STRAND          542..549
FT                   /evidence="ECO:0007829|PDB:5YOK"
FT   STRAND          552..566
FT                   /evidence="ECO:0007829|PDB:5YOK"
FT   STRAND          569..578
FT                   /evidence="ECO:0007829|PDB:5YOK"
FT   STRAND          581..585
FT                   /evidence="ECO:0007829|PDB:3NDX"
FT   HELIX           587..590
FT                   /evidence="ECO:0007829|PDB:5YOK"
FT   TURN            591..594
FT                   /evidence="ECO:0007829|PDB:5YOK"
FT   STRAND          596..598
FT                   /evidence="ECO:0007829|PDB:5YOK"
FT   HELIX           604..608
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   HELIX           616..618
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   HELIX           620..624
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   HELIX           627..642
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   STRAND          645..648
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   STRAND          659..663
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   STRAND          668..674
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   HELIX           677..682
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   TURN            688..691
FT                   /evidence="ECO:0007829|PDB:1HNI"
FT   TURN            697..701
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   STRAND          702..709
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   HELIX           711..716
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   HELIX           721..724
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   HELIX           725..727
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   STRAND          729..731
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   HELIX           734..736
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   STRAND          741..747
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   HELIX           754..758
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   HELIX           760..773
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   STRAND          777..782
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   STRAND          785..790
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   HELIX           794..809
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   HELIX           818..820
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   HELIX           828..830
FT                   /evidence="ECO:0007829|PDB:2HNY"
FT   STRAND          831..833
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   TURN            835..837
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   HELIX           841..843
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   STRAND          849..852
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   HELIX           853..866
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   TURN            867..869
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   HELIX           876..881
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   HELIX           893..895
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   HELIX           896..909
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   STRAND          920..922
FT                   /evidence="ECO:0007829|PDB:1HNI"
FT   STRAND          925..932
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   STRAND          935..945
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   STRAND          947..954
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   STRAND          957..959
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   HELIX           963..982
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   STRAND          987..992
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   HELIX           994..1000
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   HELIX           1001..1003
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   STRAND          1004..1007
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   STRAND          1012..1015
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   HELIX           1020..1024
FT                   /evidence="ECO:0007829|PDB:2HND"
FT   STRAND          1036..1045
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   TURN            1047..1049
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   STRAND          1051..1058
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   STRAND          1063..1070
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   HELIX           1073..1086
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   STRAND          1090..1097
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   HELIX           1099..1106
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   HELIX           1115..1126
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   STRAND          1128..1134
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   STRAND          1137..1139
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   HELIX           1144..1151
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   TURN            1152..1155
FT                   /evidence="ECO:0007829|PDB:6BSH"
FT   STRAND          1219..1227
FT                   /evidence="ECO:0007829|PDB:6VLM"
FT   STRAND          1230..1237
FT                   /evidence="ECO:0007829|PDB:6VLM"
FT   TURN            1238..1241
FT                   /evidence="ECO:0007829|PDB:6VLM"
FT   STRAND          1242..1251
FT                   /evidence="ECO:0007829|PDB:6VLM"
FT   HELIX           1253..1266
FT                   /evidence="ECO:0007829|PDB:6VLM"
FT   STRAND          1271..1273
FT                   /evidence="ECO:0007829|PDB:6VLM"
FT   HELIX           1278..1281
FT                   /evidence="ECO:0007829|PDB:6VLM"
FT   HELIX           1283..1292
FT                   /evidence="ECO:0007829|PDB:6VLM"
FT   HELIX           1304..1324
FT                   /evidence="ECO:0007829|PDB:6VLM"
FT   HELIX           1325..1327
FT                   /evidence="ECO:0007829|PDB:6VLM"
FT   HELIX           1331..1344
FT                   /evidence="ECO:0007829|PDB:6VLM"
FT   HELIX           1355..1368
FT                   /evidence="ECO:0007829|PDB:6VLM"
SQ   SEQUENCE   1447 AA;  163279 MW;  B41D8D00F0940740 CRC64;
     MGARASVLSG GELDRWEKIR LRPGGKKKYK LKHIVWASRE LERFAVNPGL LETSEGCRQI
     LGQLQPSLQT GSEELRSLYN TVATLYCVHQ RIEIKDTKEA LDKIEEEQNK SKKKAQQAAA
     DTGHSSQVSQ NYPIVQNIQG QMVHQAISPR TLNAWVKVVE EKAFSPEVIP MFSALSEGAT
     PQDLNTMLNT VGGHQAAMQM LKETINEEAA EWDRVHPVHA GPIAPGQMRE PRGSDIAGTT
     STLQEQIGWM TNNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF
     YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPA ATLEEMMTAC QGVGGPGHKA
     RVLAEAMSQV TNSATIMMQR GNFRNQRKIV KCFNCGKEGH IARNCRAPRK KGCWKCGKEG
     HQMKDCTERQ ANFLREDLAF LQGKAREFSS EQTRANSPTI SSEQTRANSP TRRELQVWGR
     DNNSLSEAGA DRQGTVSFNF PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEEMSLPG
     RWKPKMIGGI GGFIKVRQYD QILIEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNFP
     ISPIETVPVK LKPGMDGPKV KQWPLTEEKI KALVEICTEM EKEGKISKIG PENPYNTPVF
     AIKKKDSTKW RKLVDFRELN KRTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD
     EDFRKYTAFT IPSINNETPG IRYQYNVLPQ GWKGSPAIFQ SSMTKILEPF RKQNPDIVIY
     QYMDDLYVGS DLEIGQHRTK IEELRQHLLR WGLTTPDKKH QKEPPFLWMG YELHPDKWTV
     QPIVLPEKDS WTVNDIQKLV GKLNWASQIY PGIKVRQLCK LLRGTKALTE VIPLTEEAEL
     ELAENREILK EPVHGVYYDP SKDLIAEIQK QGQGQWTYQI YQEPFKNLKT GKYARTRGAH
     TNDVKQLTEA VQKITTESIV IWGKTPKFKL PIQKETWETW WTEYWQATWI PEWEFVNTPP
     LVKLWYQLEK EPIVGAETFY VDGAASRETK LGKAGYVTNR GRQKVVTLTD TTNQKTELQA
     IHLALQDSGL EVNIVTDSQY ALGIIQAQPD KSESELVNQI IEQLIKKEKV YLAWVPAHKG
     IGGNEQVDKL VSAGIRKVLF LDGIDKAQDE HEKYHSNWRA MASDFNLPPV VAKEIVASCD
     KCQLKGEAMH GQVDCSPGIW QLDCTHLEGK VILVAVHVAS GYIEAEVIPA ETGQETAYFL
     LKLAGRWPVK TIHTDNGSNF TSTTVKAACW WAGIKQEFGI PYNPQSQGVV ESMNKELKKI
     IGQVRDQAEH LKTAVQMAVF IHNFKRKGGI GGYSAGERIV DIIATDIQTK ELQKQITKIQ
     NFRVYYRDSR DPLWKGPAKL LWKGEGAVVI QDNSDIKVVP RRKAKIIRDY GKQMAGDDCV
     ASRQDED
//