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Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Nucleocapsid protein p7 (NC); 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_SIVM1               Reviewed;        1448 AA.
P05896;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
02-OCT-2007, sequence version 2.
07-JUN-2017, entry version 156.
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=Nucleocapsid protein p7;
Short=NC;
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;
Simian immunodeficiency virus (isolate Mm142-83) (SIV-mac) (Simian
immunodeficiency virus rhesus monkey).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Lentivirus; Primate lentivirus group.
NCBI_TaxID=11733;
NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3649576; DOI=10.1038/328543a0;
Chakrabarti L., Guyader M., Alizon M., Daniel M.D., Desrosiers R.C.,
Tiollais P., Sonigo P.;
"Sequence of simian immunodeficiency virus from macaque and its
relationship to other human and simian retroviruses.";
Nature 328:543-547(1987).
[2]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 498-595.
PubMed=9485411; DOI=10.1021/bi9716074;
Rose R.B., Craik C.S., Stroud R.M.;
"Domain flexibility in retroviral proteases: structural implications
for drug resistant mutations.";
Biochemistry 37:2607-2621(1998).
-!- FUNCTION: Gag-Pol polyprotein and Gag polyprotein may regulate
their own translation, by the binding genomic RNA in the 5'-UTR.
At low concentration, Gag-Pol and Gag would promote translation,
whereas at high concentration, the polyproteins encapsidate
genomic RNA and then shutt off translation (By similarity).
{ECO:0000250}.
-!- FUNCTION: Matrix protein p17 has two main functions: in infected
cell, it targets Gag and Gag-pol polyproteins to the plasma
membrane via a multipartite membrane-binding signal, that includes
its myristointegration complex. The myristoylation signal and the
NLS exert conflicting influences its subcellular localization. The
key regulation of these motifs might be phosphorylation of a
portion of MA molecules on the C-terminal tyrosine at the time of
virus maturation, by virion-associated cellular tyrosine kinase.
Implicated in the release from host cell mediated by Vpu (By
similarity). {ECO:0000250}.
-!- FUNCTION: Capsid protein p24 forms the conical core that
encapsulates the genomic RNA-nucleocapsid complex in the virion.
The core is constituted by capsid protein hexamer subunits. The
core is disassembled soon after virion entry. Interaction with
host PPIA/CYPA protects the virus from restriction by host TRIM5-
alpha and from an unknown antiviral activity in host cells. This
capsid restriction by TRIM5 is one of the factors which restricts
SIV to the simian species (By similarity). {ECO:0000250}.
-!- FUNCTION: Nucleocapsid protein p7 encapsulates and protects viral
dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc
fingers. Facilitates rearangement of nucleic acid secondary
structure during retrotranscription of genomic RNA. This
capability is referred to as nucleic acid chaperone activity (By
similarity). {ECO:0000250}.
-!- FUNCTION: The aspartyl protease mediates proteolytic cleavages of
Gag and Gag-Pol polyproteins during or shortly after the release
of the virion from the plasma membrane. Cleavages take place as an
ordered, step-wise cascade to yield mature proteins. This process
is called maturation. Displays maximal activity during the budding
process just prior to particle release from the cell. Also cleaves
Nef and Vif, probably concomitantly with viral structural proteins
on maturation of virus particles. Hydrolyzes host EIF4GI and PABP1
in order to shut off the capped cellular mRNA translation. The
resulting inhibition of cellular protein synthesis serves to
ensure maximal viral gene expression and to evade host immune
response (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00275}.
-!- FUNCTION: Reverse transcriptase/ribonuclease H (RT) is a
multifunctional enzyme that converts the viral dimeric 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 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 can probably proceed both
in a polymerase-dependent (RNA cut into small fragments by the
same RT performing DNA synthesis) and a polymerase-independent
mode (cleavage of remaining RNA fragments by free RTs). Secondly,
RT performs DNA-directed plus-strand DNA synthesis using the PPTs
that have not been removed by RNase H as primers. PPTs and tRNA
primers are then removed by RNase H. The 3' and 5' ssDNA PBS
regions hybridize to form a circular dsDNA intermediate. Strand
displacement synthesis by RT to the PBS and PPT ends produces a
blunt ended, linear dsDNA copy of the viral genome that includes
long terminal repeats (LTRs) at both ends (By similarity).
{ECO:0000250}.
-!- 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 SIV genome, a 5 bp
duplication of host DNA is produced at the ends of SIV
integration. Alternatively, Integrase may catalyze the excision of
viral DNA just after strand transfer, this is termed
disintegration (By similarity). {ECO:0000250}.
-!- 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.
-!- CATALYTIC ACTIVITY: 3'-end directed exonucleolytic cleavage of
viral RNA-DNA hybrid.
-!- 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: The viral protease is inhibited by many
synthetic protease inhibitors (PIs), such as amprenavir,
atazanavir, indinavir, loprinavir, nelfinavir, ritonavir and
saquinavir. RT can be inhibited either by nucleoside RT inhibitors
(NRTIs) or by non nucleoside RT inhibitors (NNRTIs). NRTIs act as
chain terminators, whereas NNRTIs inhibit DNA polymerization by
binding a small hydrophobic pocket near the RT active site and
inducing an allosteric change in this region. Classical NRTIs are
abacavir, adefovir (PMEA), didanosine (ddI), lamivudine (3TC),
stavudine (d4T), tenofovir (PMPA), zalcitabine (ddC), and
zidovudine (AZT). Classical NNRTIs are atevirdine (BHAP U-87201E),
delavirdine, efavirenz (DMP-266), emivirine (I-EBU), and
nevirapine (BI-RG-587). The tritherapies used as a basic effective
treatment of AIDS associate two NRTIs and one NNRTI. Use of
protease inhibitors in tritherapy regimens permit more ambitious
therapeutic strategies.
-!- SUBUNIT: Matrix protein p17 is a trimer. Interacts with gp120. The
protease is a homodimer, whose active site consists of two apposed
aspartic acid residues. The reverse transcriptase is a heterodimer
of p66 RT and p51 RT (RT p66/p51). Heterodimerization of RT is
essential for DNA polymerase activity. Despite the sequence
identities, p66 RT and p51 RT have distinct folding. The integrase
is a homodimer and possibly a homotetramer (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Matrix protein p17: Virion {ECO:0000305}.
Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host
cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Note=Following virus entry, the nuclear localization signal (NLS)
of the matrix protein participates with Vpr to the nuclear
localization of the viral genome. During virus production, the
nuclear export activity of the matrix protein counteracts the NLS
to maintain the Gag and Gag-Pol polyproteins in the cytoplasm,
thereby directing unspliced RNA to the plasma membrane (By
similarity). {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.;
Name=Gag-Pol polyprotein;
IsoId=P05896-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting.;
Name=Gag polyprotein;
IsoId=P05894-1; Sequence=External;
Note=Produced by conventional translation.;
-!- DOMAIN: The p66 RT is structured in five subdomains: finger, palm,
thumb, connection and RNase H. Within the palm subdomain, the
'primer grip' region is thought to be involved in the positioning
of the primer terminus for accommodating the incoming nucleotide.
The RNase H domain stabilizes the association of RT with primer-
template (By similarity). {ECO:0000250}.
-!- DOMAIN: The tryptophan repeat motif is involved in RT p66/p51
dimerization. {ECO:0000250}.
-!- PTM: 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.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
-!- PTM: Capsid protein p24 is phosphorylated.
-!- MISCELLANEOUS: This is a macaque isolate.
-!- MISCELLANEOUS: The reverse transcriptase is an error-prone enzyme
that lacks a proof-reading function. High mutations rate is a
direct consequence of this characteristic. RT also displays
frequent template switching leading to high recombination rate.
Recombination mostly occurs between homologous regions of the two
copackaged RNA genomes. If these two RNA molecules derive from
different viral strains, reverse transcription will give rise to
highly recombinated proviral DNAs.
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EMBL; Y00277; CAA68380.1; -; Genomic_DNA.
PDB; 1AZ5; X-ray; 2.00 A; A=498-595.
PDB; 1C6V; X-ray; 3.00 A; A/B/C/D=1205-1368.
PDB; 1SIV; X-ray; 2.50 A; A/B=498-596.
PDB; 1TCW; X-ray; 2.40 A; A/B=498-596.
PDB; 1YTI; X-ray; 2.20 A; A=498-595.
PDB; 1YTJ; X-ray; 2.50 A; A=498-595.
PDBsum; 1AZ5; -.
PDBsum; 1C6V; -.
PDBsum; 1SIV; -.
PDBsum; 1TCW; -.
PDBsum; 1YTI; -.
PDBsum; 1YTJ; -.
ProteinModelPortal; P05896; -.
SMR; P05896; -.
DrugBank; DB04191; Skf 107457.
OrthoDB; VOG09000135; -.
EvolutionaryTrace; P05896; -.
PRO; PR:P05896; -.
Proteomes; UP000007220; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
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: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: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; -; 2.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR000721; Gag_p24.
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_dom.
InterPro; IPR002156; RNaseH_domain.
InterPro; IPR000477; RT_dom.
InterPro; IPR010659; RVT_connect.
InterPro; IPR010661; RVT_thumb.
InterPro; IPR001878; Znf_CCHC.
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; 1.
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; 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 gene expression shutoff by virus; Host membrane;
Host nucleus; Host-virus interaction; Hydrolase; Lipoprotein;
Magnesium; Membrane; Metal-binding; 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; Virion; Virion maturation;
Virus entry into host cell; Virus exit from host cell; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed; by host. {ECO:0000250}.
CHAIN 2 1448 Gag-Pol polyprotein.
/FTId=PRO_0000306035.
CHAIN 2 135 Matrix protein p17. {ECO:0000250}.
/FTId=PRO_0000306036.
CHAIN 136 364 Capsid protein p24. {ECO:0000250}.
/FTId=PRO_0000306037.
CHAIN 365 433 Nucleocapsid protein p7. {ECO:0000250}.
/FTId=PRO_0000306038.
CHAIN 434 500 p6-pol. {ECO:0000255}.
/FTId=PRO_0000306039.
CHAIN 501 596 Protease. {ECO:0000250}.
/FTId=PRO_0000306040.
CHAIN 597 1155 Reverse transcriptase/ribonuclease H.
{ECO:0000250}.
/FTId=PRO_0000306041.
CHAIN 597 1035 p51 RT. {ECO:0000250}.
/FTId=PRO_0000306042.
CHAIN 1036 1155 p15. {ECO:0000250}.
/FTId=PRO_0000306043.
CHAIN 1156 1448 Integrase. {ECO:0000250}.
/FTId=PRO_0000306044.
DOMAIN 517 586 Peptidase A2. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
DOMAIN 640 830 Reverse transcriptase.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
DOMAIN 1029 1152 RNase H. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
DOMAIN 1209 1359 Integrase catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00457}.
ZN_FING 391 408 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 412 429 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 1158 1199 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00450}.
DNA_BIND 1378 1425 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00506}.
REGION 823 831 RT 'primer grip'. {ECO:0000250}.
MOTIF 16 22 Nuclear export signal. {ECO:0000250}.
MOTIF 26 32 Nuclear localization signal.
{ECO:0000250}.
MOTIF 993 1009 Tryptophan repeat motif. {ECO:0000250}.
ACT_SITE 522 522 For protease activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU10094}.
METAL 706 706 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 781 781 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 782 782 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 1038 1038 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1073 1073 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1093 1093 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1144 1144 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1219 1219 Magnesium; catalytic; for integrase
activity. {ECO:0000250}.
METAL 1271 1271 Magnesium; catalytic; for integrase
activity. {ECO:0000250}.
SITE 135 136 Cleavage; by viral protease.
{ECO:0000250}.
SITE 364 365 Cleavage; by viral protease.
{ECO:0000250}.
SITE 433 434 Cleavage; by viral protease.
{ECO:0000250}.
SITE 500 501 Cleavage; by viral protease.
{ECO:0000250}.
SITE 596 597 Cleavage; by viral protease.
{ECO:0000250}.
SITE 996 996 Essential for RT p66/p51
heterodimerization. {ECO:0000250}.
SITE 1009 1009 Essential for RT p66/p51
heterodimerization. {ECO:0000250}.
SITE 1035 1036 Cleavage; by viral protease.
{ECO:0000250}.
SITE 1155 1156 Cleavage; by viral protease.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
STRAND 502 504 {ECO:0000244|PDB:1AZ5}.
STRAND 507 512 {ECO:0000244|PDB:1AZ5}.
STRAND 515 521 {ECO:0000244|PDB:1AZ5}.
STRAND 525 527 {ECO:0000244|PDB:1YTI}.
STRAND 540 544 {ECO:0000244|PDB:1AZ5}.
STRAND 551 563 {ECO:0000244|PDB:1AZ5}.
STRAND 566 575 {ECO:0000244|PDB:1AZ5}.
HELIX 584 589 {ECO:0000244|PDB:1AZ5}.
STRAND 593 595 {ECO:0000244|PDB:1TCW}.
STRAND 1215 1223 {ECO:0000244|PDB:1C6V}.
STRAND 1226 1232 {ECO:0000244|PDB:1C6V}.
STRAND 1239 1243 {ECO:0000244|PDB:1C6V}.
HELIX 1249 1260 {ECO:0000244|PDB:1C6V}.
STRAND 1267 1269 {ECO:0000244|PDB:1C6V}.
HELIX 1280 1288 {ECO:0000244|PDB:1C6V}.
STRAND 1291 1293 {ECO:0000244|PDB:1C6V}.
TURN 1309 1311 {ECO:0000244|PDB:1C6V}.
HELIX 1312 1318 {ECO:0000244|PDB:1C6V}.
TURN 1319 1322 {ECO:0000244|PDB:1C6V}.
STRAND 1323 1325 {ECO:0000244|PDB:1C6V}.
HELIX 1327 1339 {ECO:0000244|PDB:1C6V}.
STRAND 1344 1347 {ECO:0000244|PDB:1C6V}.
HELIX 1351 1363 {ECO:0000244|PDB:1C6V}.
SEQUENCE 1448 AA; 163372 MW; 460D13331B3E68E5 CRC64;
MGARNSVLSG KKADELEKIR LRPGGKKKYM LKHVVWAANE LDRFGLAESL LENKEGCQKI
LSVLAPLVPT GSENLKSLYN TVCVIWCIHA EEKVKHTEEA KQIVQRHLVM ETGTAETMPK
TSRPTAPFSG RGGNYPVQQI GGNYTHLPLS PRTLNAWVKL IEEKKFGAEV VSGFQALSEG
CLPYDINQML NCVGDHQAAM QIIRDIINEE AADWDLQHPQ QAPQQGQLRE PSGSDIAGTT
STVEEQIQWM YRQQNPIPVG NIYRRWIQLG LQKCVRMYNP TNILDVKQGP KEPFQSYVDR
FYKSLRAEQT DPAVKNWMTQ TLLIQNANPD CKLVLKGLGT NPTLEEMLTA CQGVGGPGQK
ARLMAEALKE ALAPAPIPFA AAQQKGPRKP IKCWNCGKEG HSARQCRAPR RQGCWKCGKM
DHVMAKCPNR QAGFFRPWPL GKEAPQFPHG SSASGADANC SPRRTSCGSA KELHALGQAA
ERKQREALQG GDRGFAAPQF SLWRRPVVTA HIEGQPVEVL LDTGADDSIV TGIELGPHYT
PKIVGGIGGF INTKEYKNVE IEVLGKRIKG TIMTGDTPIN IFGRNLLTAL GMSLNLPIAK
VEPVKSPLKP GKDGPKLKQW PLSKEKIVAL REICEKMEKD GQLEEAPPTN PYNTPTFAIK
KKDKNKWRML IDFRELNRVT QDFTEVQLGI PHPAGLAKRK RITVLDIGDA YFSIPLDEEF
RQYTAFTLPS VNNAEPGKRY IYKVLPQGWK GSPAIFQYTM RHVLEPFRKA NPDVTLVQYM
DDILIASDRT DLEHDRVVLQ LKELLNSIGF SSPEEKFQKD PPFQWMGYEL WPTKWKLQKI
ELPQRETWTV NDIQKLVGVL NWAAQIYPGI KTKHLCRLIR GKMTLTEEVQ WTEMAEAEYE
ENKIILSQEQ EGCYYQESKP LEATVIKSQD NQWSYKIHQE DKILKVGKFA KIKNTHTNGV
RLLAHVIQKI GKEAIVIWGQ VPKFHLPVEK DVWEQWWTDY WQVTWIPEWD FISTPPLVRL
VFNLVKDPIE GEETYYVDGS CSKQSKEGKA GYITDRGKDK VKVLEQTTNQ QAELEAFLMA
LTDSGPKANI IVDSQYVMGI ITGCPTESES RLVNQIIEEM IKKTEIYVAW VPAHKGIGGN
QEIDHLVSQG IRQVLFLEKI EPAQEEHSKY HSNIKELVFK FGLPRLVAKQ IVDTCDKCHQ
KGEAIHGQVN SDLGTWQMDC THLEGKIVIV AVHVASGFIE AEVIPQETGR QTALFLLKLA
SRWPITHLHT DNGANFASQE VKMVAWWAGI EHTFGVPYNP QSQGVVEAMN HHLKNQIDRI
REQANSVETI VLMAVHCMNF KRRGGIGDMT PAERLINMIT TEQEIQFQQS KNSKFKNFRV
YYREGRDQLW KGPGELLWKG EGAVILKVGT DIKVVPRRKA KIIKDYGGGK EMDSSSHMED
TGEAREVA


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