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Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]

 POL_HV1A2               Reviewed;        1437 AA.
P03369;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 200.
RecName: Full=Gag-Pol polyprotein;
AltName: Full=Pr160Gag-Pol;
Contains:
RecName: Full=Matrix protein p17;
Short=MA;
Contains:
RecName: Full=Capsid protein p24;
Short=CA;
Contains:
RecName: Full=Spacer peptide 1 {ECO:0000250|UniProtKB:P12497};
Short=SP1;
AltName: Full=p2;
Contains:
RecName: Full=Nucleocapsid protein p7;
Short=NC;
Contains:
RecName: Full=Transframe peptide;
Short=TF;
Contains:
RecName: Full=p6-pol;
Short=p6*;
Contains:
RecName: Full=Protease;
EC=3.4.23.16;
AltName: Full=PR;
AltName: Full=Retropepsin;
Contains:
RecName: Full=Reverse transcriptase/ribonuclease H;
EC=2.7.7.49;
EC=2.7.7.7;
EC=3.1.26.13;
AltName: Full=Exoribonuclease H;
EC=3.1.13.2;
AltName: Full=p66 RT;
Contains:
RecName: Full=p51 RT;
Contains:
RecName: Full=p15;
Contains:
RecName: Full=Integrase;
Short=IN;
EC=2.7.7.- {ECO:0000250|UniProtKB:P04585};
EC=3.1.-.- {ECO:0000250|UniProtKB:P04585};
Name=gag-pol;
Human immunodeficiency virus type 1 group M subtype B (isolate
ARV2/SF2) (HIV-1).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Lentivirus; Primate lentivirus group.
NCBI_TaxID=11685;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE.
PubMed=2578227; DOI=10.1126/science.2578227;
Sanchez-Pescador R., Power M.D., Barr P.J., Steimer K.S.,
Stempien M.M., Brown-Shimer S.L., Gee W.W., Renard A., Randolph A.,
Levy J.A., Dina D., Luciw P.A.;
"Nucleotide sequence and expression of an AIDS-associated retrovirus
(ARV-2).";
Science 227:484-492(1985).
[2]
RIBOSOMAL FRAMESHIFT.
PubMed=2447506; DOI=10.1038/331280a0;
Jacks T., Power M.D., Masiarz F.R., Luciw P.A., Barr P.J.,
Varmus H.E.;
"Characterization of ribosomal frameshifting in HIV-1 gag-pol
expression.";
Nature 331:280-283(1988).
[3]
REVIEW.
PubMed=8791726;
Vogt V.M.;
"Proteolytic processing and particle maturation.";
Curr. Top. Microbiol. Immunol. 214:95-131(1996).
[4]
REVIEW.
PubMed=9878383; DOI=10.1006/jmbi.1998.2354;
Turner B.G., Summers M.F.;
"Structural biology of HIV.";
J. Mol. Biol. 285:1-32(1999).
[5]
REVIEW.
PubMed=11700285; DOI=10.1146/annurev.genet.35.102401.090551;
Negroni M., Buc H.;
"Mechanisms of retroviral recombination.";
Annu. Rev. Genet. 35:275-302(2001).
[6]
REVIEW.
PubMed=11983066; DOI=10.1186/gb-2002-3-4-reviews3006;
Dunn B.M., Goodenow M.M., Gustchina A., Wlodawer A.;
"Retroviral proteases.";
Genome Biol. 3:REVIEWS3006.1-REVIEWS3006.7(2002).
[7]
REVIEW.
PubMed=12873766; DOI=10.1016/S0005-2736(03)00163-9;
Scarlata S., Carter C.;
"Role of HIV-1 Gag domains in viral assembly.";
Biochim. Biophys. Acta 1614:62-72(2003).
[8]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 491-589.
PubMed=2548279; DOI=10.1126/science.2548279;
Wlodawer A., Miller M., Jaskolski M., Sathyanarayana B.K., Baldwin E.,
Weber I.T., Selk L.M., Clawson L., Schneider J., Kent S.B.H.;
"Conserved folding in retroviral proteases: crystal structure of a
synthetic HIV-1 protease.";
Science 245:616-621(1989).
[9]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 491-589 IN COMPLEX WITH
HALOPERIDOL.
PubMed=8340363;
Rutenber E.E., Fauman E.B., Keenan R.J., Fong S., Furth P.S.,
Ortiz de Montellano P.R., Meng E., Kuntz I.D., DeCamp D.L., Salto R.,
Rose J.R., Craik C.S., Stroud R.M.;
"Structure of a non-peptide inhibitor complexed with HIV-1 protease.
Developing a cycle of structure-based drug design.";
J. Biol. Chem. 268:15343-15346(1993).
[10]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 491-589 OF COMPLEX WITH INH.
Abbenante G., March D.R., Bergman D.A., Hunt P.A., Garnham B.,
Dancer R.J., Martin J.L., Fairlie D.P.;
"Regioselective structural and functional mimicry of peptides --design
of hydrolytically-stable cyclic peptidomimetic inhibitors of HIV-1
protease.";
J. Am. Chem. Soc. 117:10220-10226(1995).
[11]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 491-589 OF COMPLEX WITH INH.
March D.R., Abbenante G., Bergman D.A., Brinkworth R.I.,
Wickramasinghe W.A., Begun J., Martin J.L., Fairlie D.P.;
"Substrate-based cyclic peptidomimetics of Phe-Ile-Val that inhibit
HIV-1 protease using a novel enzyme-binding mode.";
J. Am. Chem. Soc. 118:3375-3379(1996).
[12]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 491-589.
PubMed=8841139; DOI=10.1021/bi9612733;
Rose R.B., Craik C.S., Douglas N.L., Stroud R.M.;
"Three-dimensional structures of HIV-1 and SIV protease product
complexes.";
Biochemistry 35:12933-12944(1996).
[13]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 491-589.
PubMed=8894111; DOI=10.1016/0968-0896(96)00147-2;
Rutenber E.E., McPhee F., Kaplan A.P., Gallion S.L., Hogan J.C. Jr.,
Craik C.S., Stroud R.M.;
"A new class of HIV-1 protease inhibitor: the crystallographic
structure, inhibition and chemical synthesis of an aminimide peptide
isostere.";
Bioorg. Med. Chem. 4:1545-1558(1996).
[14]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 491-589 IN COMPLEX WITH
MACROCYCLIC PEPTIDOMIMETIC INHIBITORS.
PubMed=10387041; DOI=10.1021/bi990174x;
Martin J.L., Begun J., Schindeler A., Wickramasinghe W.A., Alewood D.,
Alewood P.F., Bergman D.A., Brinkworth R.I., Abbenante G., March D.R.,
Reid R.C., Fairlie D.P.;
"Molecular recognition of macrocyclic peptidomimetic inhibitors by
HIV-1 protease.";
Biochemistry 38:7978-7988(1999).
[15]
X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS) OF 491-589 IN COMPLEX WITH THE
INHIBITOR JE-2147.
PubMed=10346931; DOI=10.1021/jm980637h;
Mimoto T., Kato R., Takaku H., Nojima S., Terashima K., Misawa S.,
Fukazawa T., Ueno T., Sato H., Shintani M., Kiso Y., Hayashi H.;
"Structure-activity relationship of small-sized HIV protease
inhibitors containing allophenylnorstatine.";
J. Med. Chem. 42:1789-1802(1999).
[16]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 491-589 IN COMPLEX WITH
MACROCYCLIC PEPTIDOMIMETIC INHIBITORS.
PubMed=11000004; DOI=10.1021/jm000013n;
Tyndall J.D., Reid R.C., Tyssen D.P., Jardine D.K., Todd B.,
Passmore M., March D.R., Pattenden L.K., Bergman D.A., Alewood D.,
Hu S.H., Alewood P.F., Birch C.J., Martin J.L., Fairlie D.P.;
"Synthesis, stability, antiviral activity, and protease-bound
structures of substrate-mimicking constrained macrocyclic inhibitors
of HIV-1 protease.";
J. Med. Chem. 43:3495-3504(2000).
[17]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 491-589 IN COMPLEX WITH
SUBSTRATE.
PubMed=10966816; DOI=10.1006/jmbi.2000.4018;
Prabu-Jeyabalan M., Nalivaika E.A., Schiffer C.A.;
"How does a symmetric dimer recognize an asymmetric substrate? A
substrate complex of HIV-1 protease.";
J. Mol. Biol. 301:1207-1220(2000).
[18]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 491-589 IN COMPLEX WITH
SUBSTRATES.
PubMed=12005435; DOI=10.1016/S0969-2126(02)00720-7;
Prabu-Jeyabalan M., Nalivaika E.A., Schiffer C.A.;
"Substrate shape determines specificity of recognition for HIV-1
protease: analysis of crystal structures of six substrate complexes.";
Structure 10:369-381(2002).
-!- FUNCTION: Gag-Pol polyprotein: Mediates, with Gag polyprotein, the
essential events in virion assembly, including binding the plasma
membrane, making the protein-protein interactions necessary to
create spherical particles, recruiting the viral Env proteins, and
packaging the genomic RNA via direct interactions with the RNA
packaging sequence (Psi). Gag-Pol polyprotein may regulate its own
translation, by the binding genomic RNA in the 5'-UTR. At low
concentration, the polyprotein would promote translation, whereas
at high concentration, the polyprotein would encapsidate genomic
RNA and then shut off translation. {ECO:0000250}.
-!- FUNCTION: Matrix protein p17: Targets the polyprotein to the
plasma membrane via a multipartite membrane-binding signal, that
includes its myristoylated N-terminus. Matrix protein is part of
the pre-integration complex. Implicated in the release from host
cell mediated by Vpu. Binds to RNA.
{ECO:0000250|UniProtKB:P12497}.
-!- FUNCTION: Capsid protein p24: Forms the conical core that
encapsulates the genomic RNA-nucleocapsid complex in the virion.
Most core are conical, with only 7% tubular. The core is
constituted by capsid protein hexamer subunits. The core is
disassembled soon after virion entry (By similarity). Host
restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral
capsids and cause premature capsid disassembly, leading to blocks
in reverse transcription. Capsid restriction by TRIM5 is one of
the factors which restricts HIV-1 to the human species. Host PIN1
apparently facilitates the virion uncoating. On the other hand,
interactions with PDZD8 or CYPA stabilize the capsid.
{ECO:0000250|UniProtKB:P04585, ECO:0000250|UniProtKB:P12497}.
-!- FUNCTION: Nucleocapsid protein p7: Encapsulates and protects viral
dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its
zinc fingers. Acts as a nucleic acid chaperone which is involved
in rearangement of nucleic acid secondary structure during gRNA
retrotranscription. Also facilitates template switch leading to
recombination. As part of the polyprotein, participates in gRNA
dimerization, packaging, tRNA incorporation and virion assembly.
{ECO:0000250|UniProtKB:P04585}.
-!- FUNCTION: Protease: Aspartyl protease that mediates proteolytic
cleavages of Gag and Gag-Pol polyproteins during or shortly after
the release of the virion from the plasma membrane. Cleavages take
place as an ordered, step-wise cascade to yield mature proteins.
This process is called maturation. Displays maximal activity
during the budding process just prior to particle release from the
cell. Also cleaves Nef and Vif, probably concomitantly with viral
structural proteins on maturation of virus particles. Hydrolyzes
host EIF4GI and PABP1 in order to shut off the capped cellular
mRNA translation. The resulting inhibition of cellular protein
synthesis serves to ensure maximal viral gene expression and to
evade host immune response (By similarity).
{ECO:0000250|UniProtKB:P04585, ECO:0000255|PROSITE-
ProRule:PRU00275}.
-!- FUNCTION: Reverse transcriptase/ribonuclease H: Multifunctional
enzyme that converts the viral RNA genome into dsDNA in the
cytoplasm, shortly after virus entry into the cell. This enzyme
displays a DNA polymerase activity that can copy either DNA or RNA
templates, and a ribonuclease H (RNase H) activity that cleaves
the RNA strand of RNA-DNA heteroduplexes in a partially processive
3' to 5' endonucleasic mode. Conversion of viral genomic RNA into
dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-
binding site (PBS) situated at the 5'-end of the viral RNA. RT
uses the 3' end of the tRNA primer to perform a short round of
RNA-dependent minus-strand DNA synthesis. The reading proceeds
through the U5 region and ends after the repeated (R) region which
is present at both ends of viral RNA. The portion of the RNA-DNA
heteroduplex is digested by the RNase H, resulting in a ssDNA
product attached to the tRNA primer. This ssDNA/tRNA hybridizes
with the identical R region situated at the 3' end of viral RNA.
This template exchange, known as minus-strand DNA strong stop
transfer, can be either intra- or intermolecular. RT uses the 3'
end of this newly synthesized short ssDNA to perform the RNA-
dependent minus-strand DNA synthesis of the whole template. RNase
H digests the RNA template except for two polypurine tracts (PPTs)
situated at the 5'-end and near the center of the genome. It is
not clear if both polymerase and RNase H activities are
simultaneous. RNase H probably can proceed both in a polymerase-
dependent (RNA cut into small fragments by the same RT performing
DNA synthesis) and a polymerase-independent mode (cleavage of
remaining RNA fragments by free RTs). Secondly, RT performs DNA-
directed plus-strand DNA synthesis using the PPTs that have not
been removed by RNase H as primers. PPTs and tRNA primers are then
removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to
form a circular dsDNA intermediate. Strand displacement synthesis
by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA
copy of the viral genome that includes long terminal repeats
(LTRs) at both ends. {ECO:0000250|UniProtKB:P04585}.
-!- FUNCTION: Integrase: Catalyzes viral DNA integration into the host
chromosome, by performing a series of DNA cutting and joining
reactions. This enzyme activity takes place after virion entry
into a cell and reverse transcription of the RNA genome in dsDNA.
The first step in the integration process is 3' processing. This
step requires a complex comprising the viral genome, matrix
protein, Vpr and integrase. This complex is called the pre-
integration complex (PIC). The integrase protein removes 2
nucleotides from each 3' end of the viral DNA, leaving recessed CA
OH's at the 3' ends. In the second step, the PIC enters cell
nucleus. This process is mediated through integrase and Vpr
proteins, and allows the virus to infect a non dividing cell. This
ability to enter the nucleus is specific of lentiviruses, other
retroviruses cannot and rely on cell division to access cell
chromosomes. In the third step, termed strand transfer, the
integrase protein joins the previously processed 3' ends to the 5'
ends of strands of target cellular DNA at the site of integration.
The 5'-ends are produced by integrase-catalyzed staggered cuts, 5
bp apart. A Y-shaped, gapped, recombination intermediate results,
with the 5'-ends of the viral DNA strands and the 3' ends of
target DNA strands remaining unjoined, flanking a gap of 5 bp. The
last step is viral DNA integration into host chromosome. This
involves host DNA repair synthesis in which the 5 bp gaps between
the unjoined strands are filled in and then ligated. Since this
process occurs at both cuts flanking the HIV genome, a 5 bp
duplication of host DNA is produced at the ends of HIV-1
integration. Alternatively, Integrase may catalyze the excision of
viral DNA just after strand transfer, this is termed
disintegration. {ECO:0000250|UniProtKB:P04585}.
-!- CATALYTIC ACTIVITY: Specific for a P1 residue that is hydrophobic,
and P1' variable, but often Pro. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
-!- CATALYTIC ACTIVITY: Endohydrolysis of RNA in RNA/DNA hybrids.
Three different cleavage modes: 1. sequence-specific internal
cleavage of RNA. Human immunodeficiency virus type 1 and Moloney
murine leukemia virus enzymes prefer to cleave the RNA strand one
nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed
cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end
directed cleavage 15-20 nucleotides away from the primer terminus.
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: 3'-end directed exonucleolytic cleavage of
viral RNA-DNA hybrid. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00405}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 2 magnesium ions for reverse transcriptase polymerase
activity. {ECO:0000250};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity.
Substrate-binding is a precondition for magnesium binding.
{ECO:0000250};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Magnesium ions are required for integrase activity. Binds at
least 1, maybe 2 magnesium ions. {ECO:0000250};
-!- ENZYME REGULATION: Protease: The viral protease is inhibited by
many synthetic protease inhibitors (PIs), such as amprenavir,
atazanavir, indinavir, loprinavir, nelfinavir, ritonavir and
saquinavir. Use of protease inhibitors in tritherapy regimens
permit more ambitious therapeutic strategies. Reverse
transcriptase/ribonuclease H: RT can be inhibited either by
nucleoside RT inhibitors (NRTIs) or by non nucleoside RT
inhibitors (NNRTIs). NRTIs act as chain terminators, whereas
NNRTIs inhibit DNA polymerization by binding a small hydrophobic
pocket near the RT active site and inducing an allosteric change
in this region. Classical NRTIs are abacavir, adefovir (PMEA),
didanosine (ddI), lamivudine (3TC), stavudine (d4T), tenofovir
(PMPA), zalcitabine (ddC), and zidovudine (AZT). Classical NNRTIs
are atevirdine (BHAP U-87201E), delavirdine, efavirenz (DMP-266),
emivirine (I-EBU), and nevirapine (BI-RG-587). The tritherapies
used as a basic effective treatment of AIDS associate two NRTIs
and one NNRTI. {ECO:0000250}.
-!- SUBUNIT: Matrix protein p17: Homotrimer; further assembles as
hexamers of trimers (By similarity). Matrix protein p17: Interacts
with gp41 (via C-terminus) (By similarity). Matrix protein p17:
interacts with host CALM1; this interaction induces a
conformational change in the Matrix protein, triggering exposure
of the myristate group (By similarity). Matrix protein p17:
interacts with host AP3D1; this interaction allows the polyprotein
trafficking to multivesicular bodies during virus assembly (By
similarity). Matrix protein p17: Part of the pre-integration
complex (PIC) which is composed of viral genome, matrix protein,
Vpr and integrase (By similarity). Capsid protein p24: Homodimer;
the homodimer further multimerizes as homohexamers or
homopentamers. Capsid protein p24: Interacts with human PPIA/CYPA
(By similarity); This interaction stabilizes the capsid. Capsid
protein p24: Interacts with human NUP153 (By similarity). Capsid
protein p24: Interacts with host PDZD8; this interaction
stabilizes the capsid (By similarity). Capsid protein p24:
Interacts with monkey TRIM5; this interaction destabilizes the
capsid (By similarity).Protease: Homodimer, whose active site
consists of two apposed aspartic acid residues. Reverse
transcriptase/ribonuclease H: Heterodimer of p66 RT and p51 RT (RT
p66/p51). Heterodimerization of RT is essential for DNA polymerase
activity. Despite the sequence identities, p66 RT and p51 RT have
distinct folding. Integrase: Homodimer; possibly can form
homotetramer. Integrase: Part of the pre-integration complex (PIC)
which is composed of viral genome, matrix protein, Vpr and
integrase. Integrase: Interacts with human SMARCB1/INI1 and human
PSIP1/LEDGF isoform 1. Integrase: Interacts with human KPNA3; this
interaction might play a role in nuclear import of the pre-
integration complex (By similarity). Integrase: Interacts with
human NUP153; this interaction might play a role in nuclear import
of the pre-integration complex (By similarity).
{ECO:0000250|UniProtKB:P04585, ECO:0000250|UniProtKB:P12497}.
-!- SUBCELLULAR LOCATION: Gag-Pol polyprotein: Host cell membrane;
Lipid-anchor. Host endosome, host multivesicular body. Note=These
locations are linked to virus assembly sites. The main location is
the cell membrane, but under some circumstances, late endosomal
compartments can serve as productive sites for virion assembly.
{ECO:0000250|UniProtKB:P12497}.
-!- SUBCELLULAR LOCATION: Matrix protein p17: Virion membrane; Lipid-
anchor {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein p24: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p7: Virion
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Reverse transcriptase/ribonuclease H: Virion
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Integrase: Virion {ECO:0000305}. Host
nucleus {ECO:0000305}. Host cytoplasm {ECO:0000305}. Note=Nuclear
at initial phase, cytoplasmic at assembly. {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Comment=Translation results in the formation of the Gag
polyprotein most of the time. Ribosomal frameshifting at the
gag-pol genes boundary occurs at low frequency and produces the
Gag-Pol polyprotein. This strategy of translation probably
allows the virus to modulate the quantity of each viral protein.
Maintenance of a correct Gag to Gag-Pol ratio is essential for
RNA dimerization and viral infectivity.
{ECO:0000269|PubMed:2447506};
Name=Gag-Pol polyprotein;
IsoId=P03369-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting.;
Name=Gag polyprotein;
IsoId=P03349-1; Sequence=External;
Note=Produced by conventional translation.;
-!- DOMAIN: Reverse transcriptase/ribonuclease H: RT is structured in
five subdomains: finger, palm, thumb, connection and RNase H.
Within the palm subdomain, the 'primer grip' region is thought to
be involved in the positioning of the primer terminus for
accommodating the incoming nucleotide. The RNase H domain
stabilizes the association of RT with primer-template.
{ECO:0000250}.
-!- DOMAIN: Reverse transcriptase/ribonuclease H: The tryptophan
repeat motif is involved in RT p66/p51 dimerization (By
similarity). {ECO:0000250}.
-!- DOMAIN: Integrase: The core domain contains the D-x(n)-D-x(35)-E
motif, named for the phylogenetically conserved glutamic acid and
aspartic acid residues and the invariant 35 amino acid spacing
between the second and third acidic residues. Each acidic residue
of the D,D(35)E motif is independently essential for the 3'-
processing and strand transfer activities of purified integrase
protein. {ECO:0000250}.
-!- PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the
viral protease yield mature proteins. The protease is released by
autocatalytic cleavage. The polyprotein is cleaved during and
after budding, this process is termed maturation. Proteolytic
cleavage of p66 RT removes the RNase H domain to yield the p51 RT
subunit. Nucleocapsid protein p7 might be further cleaved after
virus entry. {ECO:0000250|UniProtKB:P04585, ECO:0000255|PROSITE-
ProRule:PRU00405}.
-!- PTM: Matrix protein p17: Tyrosine phosphorylated presumably in the
virion by a host kinase. Phosphorylation is apparently not a major
regulator of membrane association. {ECO:0000250|UniProtKB:P04585}.
-!- PTM: Capsid protein p24: Phosphorylated possibly by host MAPK1;
this phosphorylation is necessary for Pin1-mediated virion
uncoating. {ECO:0000250|UniProtKB:P12493}.
-!- PTM: Nucleocapsid protein p7: Methylated by host PRMT6, impairing
its function by reducing RNA annealing and the initiation of
reverse transcription. {ECO:0000250|UniProtKB:P03347}.
-!- MISCELLANEOUS: Reverse transcriptase/ribonuclease H: Error-prone
enzyme that lacks a proof-reading function. High mutations rate is
a direct consequence of this characteristic. RT also displays
frequent template switching leading to high recombination rate.
Recombination mostly occurs between homologous regions of the two
copackaged RNA genomes. If these two RNA molecules derive from
different viral strains, reverse transcription will give rise to
highly recombinated proviral DNAs. {ECO:0000250}.
-!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M
(for Major), O (for Outlier), and N (for New, or Non-M, Non-O).
The vast majority of strains found worldwide belong to the group
M. Group O seems to be endemic to and largely confined to Cameroon
and neighboring countries in West Central Africa, where these
viruses represent a small minority of HIV-1 strains. The group N
is represented by a limited number of isolates from Cameroonian
persons. The group M is further subdivided in 9 clades or subtypes
(A to D, F to H, J and K).
-!- MISCELLANEOUS: Resistance to inhibitors associated with mutations
are observed both in viral protease and in reverse transcriptase.
Most of the time, single mutations confer only a modest reduction
in drug susceptibility. Combination of several mutations is
usually required to develop a high-level drug resistance. These
mutations are predominantly found in clade B viruses and not in
other genotypes. They are listed in the clade B representative
isolate HXB2 (AC P04585).
-!- WEB RESOURCE: Name=HIV drug resistance mutations;
URL="https://www.iasusa.org/content/hiv-drug-resistance-mutations";
-!- WEB RESOURCE: Name=hivdb; Note=HIV drug resistance database;
URL="http://hivdb.stanford.edu";
-!- WEB RESOURCE: Name=BioAfrica: HIV bioinformatics in Africa;
URL="http://www.bioafrica.net/index.html";
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EMBL; K02007; AAB59876.1; ALT_SEQ; Genomic_RNA.
PIR; A03968; GNVWA2.
PDB; 1AID; X-ray; 2.20 A; A/B=491-589.
PDB; 1B6J; X-ray; 1.85 A; A/B=491-589.
PDB; 1B6K; X-ray; 1.85 A; A/B=491-589.
PDB; 1B6L; X-ray; 1.75 A; A/B=491-589.
PDB; 1B6M; X-ray; 1.85 A; A/B=491-589.
PDB; 1B6P; X-ray; 2.00 A; A/B=491-589.
PDB; 1CPI; X-ray; 2.05 A; A/B=491-589.
PDB; 1D4K; X-ray; 1.85 A; A/B=491-589.
PDB; 1D4L; X-ray; 1.75 A; A/B=491-589.
PDB; 1F7A; X-ray; 2.00 A; A/B=491-589.
PDB; 1KJ4; X-ray; 2.90 A; A/B/C/D=491-589.
PDB; 1KJ7; X-ray; 2.00 A; A/B=491-589.
PDB; 1KJF; X-ray; 2.00 A; A/B=491-589.
PDB; 1KJG; X-ray; 2.00 A; A/B=491-589, P=1025-1034.
PDB; 1KJH; X-ray; 2.00 A; A/B=491-589.
PDB; 1KZK; X-ray; 1.09 A; A/B=491-589.
PDB; 1MT7; X-ray; 1.90 A; A/B=491-589.
PDB; 1MT8; X-ray; 2.15 A; A/B=491-589.
PDB; 1MT9; X-ray; 2.00 A; A/B=491-589.
PDB; 1MTB; X-ray; 2.50 A; A/B=491-589.
PDB; 1MTR; X-ray; 1.75 A; A/B=491-589.
PDB; 1N49; X-ray; 2.20 A; A/B/C/D=491-589.
PDB; 1T3R; X-ray; 1.20 A; A/B=491-589.
PDB; 1TSQ; X-ray; 2.00 A; A/B=491-589.
PDB; 1TSU; X-ray; 2.10 A; A/B=491-589.
PDB; 1YTG; X-ray; 2.30 A; A/B=491-589.
PDB; 1YTH; X-ray; 2.20 A; A/B=491-589.
PDB; 1Z1H; X-ray; 1.85 A; A/B=491-589.
PDB; 1Z1R; X-ray; 1.85 A; A/B=491-589.
PDB; 2AID; X-ray; 1.90 A; A/B=491-589.
PDB; 2F3K; X-ray; 1.60 A; A/B=491-588.
PDB; 2FGU; X-ray; 2.00 A; A/B=491-589.
PDB; 2FGV; X-ray; 1.50 A; A/B=491-589.
PDB; 2FNS; X-ray; 1.85 A; A/B=491-589.
PDB; 2FNT; X-ray; 1.44 A; A/B=491-589.
PDB; 2J9J; X-ray; 1.04 A; A/B=491-589.
PDB; 2J9K; X-ray; 1.20 A; A/B=491-589.
PDB; 2JE4; X-ray; 1.07 A; A/B=491-589.
PDB; 2NXD; X-ray; 2.00 A; A/B=491-589.
PDB; 2NXL; X-ray; 2.00 A; A/B=491-589.
PDB; 2NXM; X-ray; 2.25 A; A/B=491-589.
PDB; 2Q3K; X-ray; 2.00 A; A/B=491-589.
PDB; 2QHY; X-ray; 1.85 A; A/B=491-589.
PDB; 2QHZ; X-ray; 1.85 A; A/B=491-589.
PDB; 2QI0; X-ray; 2.10 A; A/B=491-589.
PDB; 2QI1; X-ray; 2.00 A; A/B=491-589.
PDB; 2QI3; X-ray; 1.95 A; A/B=491-589.
PDB; 2QI4; X-ray; 1.80 A; A/B=491-589.
PDB; 2QI5; X-ray; 1.85 A; A/B=491-589.
PDB; 2QI6; X-ray; 1.85 A; A/B=491-589.
PDB; 2QI7; X-ray; 1.85 A; A/B=491-589.
PDB; 3AID; X-ray; 2.50 A; A/B=491-589.
PDB; 3BXR; X-ray; 1.60 A; A/B=491-589.
PDB; 3BXS; X-ray; 1.60 A; A/B=491-589.
PDB; 3EKP; X-ray; 2.15 A; A/B/C/D=491-589.
PDB; 3EKQ; X-ray; 2.20 A; A/B=491-589.
PDB; 3EKT; X-ray; 1.97 A; A/B/C/D=491-589.
PDB; 3EKV; X-ray; 1.75 A; A/B=491-589.
PDB; 3EKW; X-ray; 1.60 A; A/B=491-589.
PDB; 3EKX; X-ray; 1.97 A; A/B=491-589.
PDB; 3EKY; X-ray; 1.80 A; A/B=491-589.
PDB; 3EL0; X-ray; 2.00 A; A/B=491-589.
PDB; 3EL1; X-ray; 1.70 A; A/B=491-589.
PDB; 3EL4; X-ray; 2.00 A; A/B=491-589.
PDB; 3EL5; X-ray; 1.60 A; A/B=491-589.
PDB; 3EL9; X-ray; 1.60 A; A/B=491-589.
PDB; 3EM3; X-ray; 2.20 A; A/B=491-589.
PDB; 3EM4; X-ray; 2.10 A; A/B/U/V=491-589.
PDB; 3EM6; X-ray; 2.10 A; A/B=491-589.
PDB; 3FSM; X-ray; 1.60 A; A=491-589.
PDB; 3GI0; X-ray; 1.80 A; A/B=491-589.
PDB; 3GI4; X-ray; 1.85 A; A/B=491-589.
PDB; 3GI5; X-ray; 1.80 A; A/B=491-589.
PDB; 3GI6; X-ray; 1.84 A; A/B=491-589.
PDB; 3HAU; X-ray; 1.30 A; A/B=491-589.
PDB; 3HAW; X-ray; 1.30 A; A/B=491-589.
PDB; 3HBO; X-ray; 1.71 A; A/B=491-589.
PDB; 3HDK; X-ray; 1.80 A; A/B=491-589.
PDB; 3HLO; X-ray; 1.60 A; A=491-589.
PDB; 3HVP; X-ray; 2.80 A; A=491-589.
PDB; 3HZC; X-ray; 1.45 A; A=491-589.
PDB; 3I2L; X-ray; 1.50 A; A/B=491-589.
PDB; 3I7E; X-ray; 1.70 A; A/B=491-589.
PDB; 3IAW; X-ray; 1.61 A; A=491-589.
PDB; 3KA2; X-ray; 1.40 A; A=491-589.
PDB; 3LZV; X-ray; 2.15 A; A/B=491-589.
PDB; 3MXD; X-ray; 1.95 A; A/B=491-589.
PDB; 3MXE; X-ray; 1.85 A; A/B=491-589.
PDB; 3NWQ; X-ray; 1.50 A; A/B=491-589.
PDB; 3NWX; X-ray; 1.90 A; A/B=491-589.
PDB; 3NXN; X-ray; 1.80 A; A=491-589.
PDB; 3NYG; X-ray; 1.45 A; A/B=491-589.
PDB; 3O9F; X-ray; 1.70 A; A/B=491-589.
PDB; 3O9G; X-ray; 1.65 A; A/B=491-589.
PDB; 3O9H; X-ray; 1.70 A; A/B=491-589.
PDB; 3O9I; X-ray; 1.45 A; A/B=491-589.
PDB; 3OXV; X-ray; 1.75 A; A/B/C/D=491-589.
PDB; 3OXW; X-ray; 1.95 A; A/B/C/D=491-589.
PDB; 3OXX; X-ray; 1.65 A; A/B/C/D=491-589.
PDB; 3OY4; X-ray; 1.76 A; A/B=491-589.
PDB; 3R4B; X-ray; 1.90 A; A/B=491-589.
PDB; 4EP2; X-ray; 1.90 A; A=486-589.
PDB; 4EP3; X-ray; 1.81 A; A=486-589.
PDB; 4EPJ; X-ray; 1.69 A; A=486-589.
PDB; 4EQ0; X-ray; 1.70 A; A=486-589.
PDB; 4EQJ; X-ray; 1.80 A; A=486-589.
PDB; 4F73; X-ray; 1.90 A; A/B=491-589.
PDB; 4F74; X-ray; 2.20 A; A/B=491-589.
PDB; 4F75; X-ray; 1.70 A; A/B=491-589.
PDB; 4F76; X-ray; 1.85 A; A/B=491-589.
PDB; 4HVP; X-ray; 2.30 A; A/B=491-589.
PDB; 4OBD; X-ray; 1.90 A; A/B/C/D=491-589.
PDB; 4OBF; X-ray; 1.68 A; A/B/C/D=491-589.
PDB; 4OBG; X-ray; 1.78 A; A/B/C/D=491-589.
PDB; 4OBH; X-ray; 1.85 A; A/B/C/D=491-589.
PDB; 4OBJ; X-ray; 1.75 A; A/B=491-589.
PDB; 4OBK; X-ray; 1.65 A; A/B=491-589.
PDB; 4QJ2; X-ray; 2.13 A; A/B/C/D=491-589.
PDB; 4QJ6; X-ray; 1.50 A; A/B/C/D=491-589.
PDB; 4QJ7; X-ray; 1.67 A; A/B/C/D=491-589.
PDB; 4QJ8; X-ray; 2.00 A; A/B/C/D=491-589.
PDB; 4QJ9; X-ray; 1.83 A; A/B=491-589.
PDB; 4QJA; X-ray; 1.54 A; A/B=491-589.
PDB; 7HVP; X-ray; 2.40 A; A/B=491-589.
PDB; 8HVP; X-ray; 2.50 A; A/B=491-589.
PDBsum; 1AID; -.
PDBsum; 1B6J; -.
PDBsum; 1B6K; -.
PDBsum; 1B6L; -.
PDBsum; 1B6M; -.
PDBsum; 1B6P; -.
PDBsum; 1CPI; -.
PDBsum; 1D4K; -.
PDBsum; 1D4L; -.
PDBsum; 1F7A; -.
PDBsum; 1KJ4; -.
PDBsum; 1KJ7; -.
PDBsum; 1KJF; -.
PDBsum; 1KJG; -.
PDBsum; 1KJH; -.
PDBsum; 1KZK; -.
PDBsum; 1MT7; -.
PDBsum; 1MT8; -.
PDBsum; 1MT9; -.
PDBsum; 1MTB; -.
PDBsum; 1MTR; -.
PDBsum; 1N49; -.
PDBsum; 1T3R; -.
PDBsum; 1TSQ; -.
PDBsum; 1TSU; -.
PDBsum; 1YTG; -.
PDBsum; 1YTH; -.
PDBsum; 1Z1H; -.
PDBsum; 1Z1R; -.
PDBsum; 2AID; -.
PDBsum; 2F3K; -.
PDBsum; 2FGU; -.
PDBsum; 2FGV; -.
PDBsum; 2FNS; -.
PDBsum; 2FNT; -.
PDBsum; 2J9J; -.
PDBsum; 2J9K; -.
PDBsum; 2JE4; -.
PDBsum; 2NXD; -.
PDBsum; 2NXL; -.
PDBsum; 2NXM; -.
PDBsum; 2Q3K; -.
PDBsum; 2QHY; -.
PDBsum; 2QHZ; -.
PDBsum; 2QI0; -.
PDBsum; 2QI1; -.
PDBsum; 2QI3; -.
PDBsum; 2QI4; -.
PDBsum; 2QI5; -.
PDBsum; 2QI6; -.
PDBsum; 2QI7; -.
PDBsum; 3AID; -.
PDBsum; 3BXR; -.
PDBsum; 3BXS; -.
PDBsum; 3EKP; -.
PDBsum; 3EKQ; -.
PDBsum; 3EKT; -.
PDBsum; 3EKV; -.
PDBsum; 3EKW; -.
PDBsum; 3EKX; -.
PDBsum; 3EKY; -.
PDBsum; 3EL0; -.
PDBsum; 3EL1; -.
PDBsum; 3EL4; -.
PDBsum; 3EL5; -.
PDBsum; 3EL9; -.
PDBsum; 3EM3; -.
PDBsum; 3EM4; -.
PDBsum; 3EM6; -.
PDBsum; 3FSM; -.
PDBsum; 3GI0; -.
PDBsum; 3GI4; -.
PDBsum; 3GI5; -.
PDBsum; 3GI6; -.
PDBsum; 3HAU; -.
PDBsum; 3HAW; -.
PDBsum; 3HBO; -.
PDBsum; 3HDK; -.
PDBsum; 3HLO; -.
PDBsum; 3HVP; -.
PDBsum; 3HZC; -.
PDBsum; 3I2L; -.
PDBsum; 3I7E; -.
PDBsum; 3IAW; -.
PDBsum; 3KA2; -.
PDBsum; 3LZV; -.
PDBsum; 3MXD; -.
PDBsum; 3MXE; -.
PDBsum; 3NWQ; -.
PDBsum; 3NWX; -.
PDBsum; 3NXN; -.
PDBsum; 3NYG; -.
PDBsum; 3O9F; -.
PDBsum; 3O9G; -.
PDBsum; 3O9H; -.
PDBsum; 3O9I; -.
PDBsum; 3OXV; -.
PDBsum; 3OXW; -.
PDBsum; 3OXX; -.
PDBsum; 3OY4; -.
PDBsum; 3R4B; -.
PDBsum; 4EP2; -.
PDBsum; 4EP3; -.
PDBsum; 4EPJ; -.
PDBsum; 4EQ0; -.
PDBsum; 4EQJ; -.
PDBsum; 4F73; -.
PDBsum; 4F74; -.
PDBsum; 4F75; -.
PDBsum; 4F76; -.
PDBsum; 4HVP; -.
PDBsum; 4OBD; -.
PDBsum; 4OBF; -.
PDBsum; 4OBG; -.
PDBsum; 4OBH; -.
PDBsum; 4OBJ; -.
PDBsum; 4OBK; -.
PDBsum; 4QJ2; -.
PDBsum; 4QJ6; -.
PDBsum; 4QJ7; -.
PDBsum; 4QJ8; -.
PDBsum; 4QJ9; -.
PDBsum; 4QJA; -.
PDBsum; 7HVP; -.
PDBsum; 8HVP; -.
ProteinModelPortal; P03369; -.
SMR; P03369; -.
BindingDB; P03369; -.
ChEMBL; CHEMBL3638331; -.
DrugBank; DB04454; Alpha-Aminobutyric Acid.
DrugBank; DB04886; Calanolide A.
DrugBank; DB07910; PHENYLALANINDIOL.
DrugBank; DB03149; Phenylalanylmethane.
DrugBank; DB05228; RDEA806.
OrthoDB; VOG09000135; -.
EvolutionaryTrace; P03369; -.
PRO; PR:P03369; -.
Proteomes; UP000007688; Genome.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004533; F:exoribonuclease H activity; IEA:UniProtKB-EC.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
GO; GO:0039651; P:induction by virus of host cysteine-type endopeptidase activity involved in apoptotic process; IEA:UniProtKB-KW.
GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-KW.
CDD; cd05482; HIV_retropepsin_like; 1.
Gene3D; 1.10.10.200; -; 1.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.375.10; -; 1.
Gene3D; 2.30.30.10; -; 1.
Gene3D; 2.40.70.10; -; 1.
Gene3D; 3.30.420.10; -; 2.
Gene3D; 4.10.60.10; -; 3.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR000721; Gag_p24.
InterPro; IPR036862; Integrase_C_dom_sf_retrovir.
InterPro; IPR001037; Integrase_C_retrovir.
InterPro; IPR001584; Integrase_cat-core.
InterPro; IPR017856; Integrase_Zn-bd_dom-like_N.
InterPro; IPR003308; Integrase_Zn-bd_dom_N.
InterPro; IPR000071; Lentvrl_matrix_N.
InterPro; IPR001995; Peptidase_A2_cat.
InterPro; IPR021109; Peptidase_aspartic_dom.
InterPro; IPR034170; Retropepsin-like_cat_dom.
InterPro; IPR018061; Retropepsins.
InterPro; IPR008916; Retrov_capsid_C.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR002156; RNaseH_domain.
InterPro; IPR036397; RNaseH_sf.
InterPro; IPR000477; RT_dom.
InterPro; IPR010659; RVT_connect.
InterPro; IPR010661; RVT_thumb.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF00540; Gag_p17; 1.
Pfam; PF00607; Gag_p24; 1.
Pfam; PF00552; IN_DBD_C; 1.
Pfam; PF02022; Integrase_Zn; 1.
Pfam; PF00075; RNase_H; 1.
Pfam; PF00665; rve; 1.
Pfam; PF00077; RVP; 1.
Pfam; PF00078; RVT_1; 1.
Pfam; PF06815; RVT_connect; 1.
Pfam; PF06817; RVT_thumb; 1.
Pfam; PF00098; zf-CCHC; 2.
PRINTS; PR00234; HIV1MATRIX.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF46919; SSF46919; 1.
SUPFAM; SSF47353; SSF47353; 1.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF50122; SSF50122; 1.
SUPFAM; SSF50630; SSF50630; 1.
SUPFAM; SSF53098; SSF53098; 2.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50175; ASP_PROT_RETROV; 1.
PROSITE; PS00141; ASP_PROTEASE; 1.
PROSITE; PS50994; INTEGRASE; 1.
PROSITE; PS51027; INTEGRASE_DBD; 1.
PROSITE; PS50879; RNASE_H; 1.
PROSITE; PS50878; RT_POL; 1.
PROSITE; PS50158; ZF_CCHC; 2.
PROSITE; PS50876; ZF_INTEGRASE; 1.
1: Evidence at protein level;
3D-structure; Activation of host caspases by virus; AIDS;
Aspartyl protease; Capsid protein; Complete proteome; DNA integration;
DNA recombination; DNA-binding; DNA-directed DNA polymerase;
Endonuclease; Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus; Host cell membrane;
Host cytoplasm; Host endosome; Host gene expression shutoff by virus;
Host membrane; Host nucleus; Host-virus interaction; Hydrolase;
Lipid-binding; Lipoprotein; Magnesium; Membrane; Metal-binding;
Modulation of host cell apoptosis by virus; Multifunctional enzyme;
Myristate; Nuclease; Nucleotidyltransferase; Phosphoprotein; Protease;
Repeat; Ribosomal frameshifting; RNA-binding;
RNA-directed DNA polymerase; Transferase; Viral genome integration;
Viral nucleoprotein; Viral penetration into host nucleus;
Viral release from host cell; Virion; Virion maturation;
Virus entry into host cell; Zinc; Zinc-finger.
INIT_MET 1 1 Removed; by host. {ECO:0000250}.
CHAIN 2 1437 Gag-Pol polyprotein.
/FTId=PRO_0000261260.
CHAIN 2 134 Matrix protein p17. {ECO:0000250}.
/FTId=PRO_0000042321.
CHAIN 135 365 Capsid protein p24. {ECO:0000250}.
/FTId=PRO_0000042322.
PEPTIDE 366 379 Spacer peptide 1. {ECO:0000250}.
/FTId=PRO_0000042323.
CHAIN 380 434 Nucleocapsid protein p7. {ECO:0000250}.
/FTId=PRO_0000042324.
PEPTIDE 435 442 Transframe peptide. {ECO:0000255}.
/FTId=PRO_0000246709.
CHAIN 443 490 p6-pol. {ECO:0000255}.
/FTId=PRO_0000042325.
CHAIN 491 589 Protease. {ECO:0000250}.
/FTId=PRO_0000038651.
CHAIN 590 1149 Reverse transcriptase/ribonuclease H.
{ECO:0000250}.
/FTId=PRO_0000042326.
CHAIN 590 1029 p51 RT. {ECO:0000250}.
/FTId=PRO_0000042327.
CHAIN 1030 1149 p15. {ECO:0000250}.
/FTId=PRO_0000042328.
CHAIN 1150 1437 Integrase. {ECO:0000250}.
/FTId=PRO_0000042329.
DOMAIN 510 579 Peptidase A2. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
DOMAIN 633 823 Reverse transcriptase.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
DOMAIN 1023 1146 RNase H. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
DOMAIN 1203 1353 Integrase catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00457}.
ZN_FING 392 409 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 413 430 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 1152 1193 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00450}.
DNA_BIND 1372 1419 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00506}.
REGION 7 31 Interaction with Gp41.
{ECO:0000250|UniProtKB:P12497}.
REGION 8 43 Interaction with host CALM1.
{ECO:0000250|UniProtKB:P04585}.
REGION 12 19 Interaction with host AP3D1.
{ECO:0000250|UniProtKB:P12497}.
REGION 14 33 Interaction with membrane
phosphatidylinositol 4,5-bisphosphate and
RNA. {ECO:0000250|UniProtKB:P12497}.
REGION 73 77 Interaction with membrane
phosphatidylinositol 4,5-bisphosphate.
{ECO:0000250|UniProtKB:P12497}.
REGION 191 229 Interaction with human PPIA/CYPA and
NUP153. {ECO:0000250|UniProtKB:P12497}.
REGION 279 365 Dimerization/Multimerization of capsid
protein p24.
{ECO:0000250|UniProtKB:P04585}.
REGION 491 495 Dimerization of protease.
{ECO:0000250|UniProtKB:P04585}.
REGION 539 545 Dimerization of protease.
{ECO:0000250|UniProtKB:P04585}.
REGION 578 590 Dimerization of protease.
{ECO:0000250|UniProtKB:P04585}.
REGION 816 824 RT 'primer grip'. {ECO:0000250}.
MOTIF 16 22 Nuclear export signal. {ECO:0000250}.
MOTIF 26 32 Nuclear localization signal.
{ECO:0000250}.
MOTIF 987 1003 Tryptophan repeat motif. {ECO:0000250}.
ACT_SITE 515 515 For protease activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU10094}.
METAL 699 699 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 774 774 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 775 775 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 1032 1032 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1067 1067 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1087 1087 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1138 1138 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1213 1213 Magnesium; catalytic; for integrase
activity. {ECO:0000250}.
METAL 1265 1265 Magnesium; catalytic; for integrase
activity. {ECO:0000250}.
METAL 1301 1301 Magnesium; catalytic; for integrase
activity. {ECO:0000250|UniProtKB:P04585}.
SITE 134 135 Cleavage; by viral protease.
{ECO:0000250}.
SITE 223 224 Cis/trans isomerization of proline
peptide bond; by human PPIA/CYPA.
{ECO:0000250}.
SITE 365 366 Cleavage; by viral protease.
{ECO:0000250}.
SITE 379 380 Cleavage; by viral protease.
{ECO:0000250}.
SITE 434 435 Cleavage; by viral protease.
{ECO:0000255}.
SITE 442 443 Cleavage; by viral protease.
{ECO:0000250}.
SITE 490 491 Cleavage; by viral protease.
{ECO:0000250}.
SITE 589 590 Cleavage; by viral protease.
{ECO:0000250}.
SITE 990 990 Essential for RT p66/p51
heterodimerization. {ECO:0000250}.
SITE 1003 1003 Essential for RT p66/p51
heterodimerization. {ECO:0000250}.
SITE 1029 1030 Cleavage; by viral protease; partial.
{ECO:0000250}.
SITE 1149 1150 Cleavage; by viral protease.
{ECO:0000250}.
MOD_RES 134 134 Phosphotyrosine; by host. {ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
STRAND 487 489 {ECO:0000244|PDB:4EPJ}.
STRAND 492 494 {ECO:0000244|PDB:4HVP}.
STRAND 495 497 {ECO:0000244|PDB:2J9J}.
STRAND 500 505 {ECO:0000244|PDB:2J9J}.
STRAND 508 514 {ECO:0000244|PDB:2J9J}.
STRAND 518 520 {ECO:0000244|PDB:2FNT}.
STRAND 522 525 {ECO:0000244|PDB:2FNT}.
STRAND 532 539 {ECO:0000244|PDB:2J9J}.
STRAND 542 556 {ECO:0000244|PDB:2J9J}.
STRAND 559 568 {ECO:0000244|PDB:2J9J}.
STRAND 571 575 {ECO:0000244|PDB:2FGV}.
HELIX 577 580 {ECO:0000244|PDB:2J9J}.
TURN 581 584 {ECO:0000244|PDB:2J9J}.
STRAND 586 588 {ECO:0000244|PDB:2J9J}.
HELIX 603 605 {ECO:0000244|PDB:3KA2}.
SEQUENCE 1437 AA; 162015 MW; FE17066A84A2B649 CRC64;
MGARASVLSG GELDKWEKIR LRPGGKKKYK LKHIVWASRE LERFAVNPGL LETSEGCRQI
LGQLQPSLQT GSEELRSLYN TVATLYCVHQ RIDVKDTKEA LEKIEEEQNK SKKKAQQAAA
AAGTGNSSQV SQNYPIVQNL QGQMVHQAIS PRTLNAWVKV VEEKAFSPEV IPMFSALSEG
ATPQDLNTML NTVGGHQAAM QMLKETINEE AAEWDRVHPV HAGPIAPGQM REPRGSDIAG
TTSTLQEQIG WMTNNPPIPV GEIYKRWIIL GLNKIVRMYS PTSILDIRQG PKEPFRDYVD
RFYKTLRAEQ ASQDVKNWMT ETLLVQNANP DCKTILKALG PAATLEEMMT ACQGVGGPGH
KARVLAEAMS QVTNPANIMM QRGNFRNQRK TVKCFNCGKE GHIAKNCRAP RKKGCWRCGR
EGHQMKDCTE RQANFLREDL AFLQGKAREF SSEQTRANSP TRRELQVWGG ENNSLSEAGA
DRQGTVSFNF PQITLWQRPL VTIRIGGQLK EALLDTGADD TVLEEMNLPG KWKPKMIGGI
GGFIKVRQYD QIPVEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNFP ISPIETVPVK
LKPGMDGPKV KQWPLTEEKI KALVEICTEM EKEGKISKIG PENPYNTPVF AIKKKDSTKW
RKLVDFRELN KRTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD KDFRKYTAFT
IPSINNETPG IRYQYNVLPQ GWKGSPAIFQ SSMTKILEPF RKQNPDIVIY QYMDDLYVGS
DLEIGQHRTK IEELRQHLLR WGFTTPDKKH QKEPPFLWMG YELHPDKWTV QPIMLPEKDS
WTVNDIQKLV GKLNWASQIY AGIKVKQLCK LLRGTKALTE VIPLTEEAEL ELAENREILK
EPVHEVYYDP SKDLVAEIQK QGQGQWTYQI YQEPFKNLKT GKYARMRGAH TNDVKQLTEA
VQKVSTESIV IWGKIPKFKL PIQKETWEAW WMEYWQATWI PEWEFVNTPP LVKLWYQLEK
EPIVGAETFY VDGAANRETK LGKAGYVTDR GRQKVVSIAD TTNQKTELQA IHLALQDSGL
EVNIVTDSQY ALGIIQAQPD KSESELVSQI IEQLIKKEKV YLAWVPAHKG IGGNEQVDKL
VSAGIRKVLF LNGIDKAQEE HEKYHSNWRA MASDFNLPPV VAKEIVASCD KCQLKGEAMH
GQVDCSPGIW QLDCTHLEGK IILVAVHVAS GYIEAEVIPA ETGQETAYFL LKLAGRWPVK
TIHTDNGSNF TSTTVKAACW WAGIKQEFGI PYNPQSQGVV ESMNNELKKI IGQVRDQAEH
LKTAVQMAVF IHNFKRKGGI GGYSAGERIV DIIATDIQTK ELQKQITKIQ NFRVYYRDNK
DPLWKGPAKL LWKGEGAVVI QDNSDIKVVP RRKAKIIRDY GKQMAGDDCV ASRQDED


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