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POL_HTLV2
ID   POL_HTLV2               Reviewed;        1461 AA.
AC   P03363;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Gag-Pro-Pol polyprotein;
DE   AltName: Full=Pr160Gag-Pro-Pol;
DE   Contains:
DE     RecName: Full=Matrix protein p19;
DE              Short=MA;
DE   Contains:
DE     RecName: Full=Capsid protein p24;
DE              Short=CA;
DE   Contains:
DE     RecName: Full=Nucleocapsid protein p15-pro;
DE              Short=NC';
DE              Short=NC-pro;
DE   Contains:
DE     RecName: Full=Protease;
DE              Short=PR;
DE              EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
DE   Contains:
DE     RecName: Full=p1;
DE   Contains:
DE     RecName: Full=Reverse transcriptase/ribonuclease H;
DE              Short=RT;
DE              EC=2.7.7.49 {ECO:0000255|PROSITE-ProRule:PRU00405};
DE              EC=2.7.7.7 {ECO:0000255|PROSITE-ProRule:PRU00405};
DE              EC=3.1.26.4 {ECO:0000255|PROSITE-ProRule:PRU00408};
DE   Contains:
DE     RecName: Full=Integrase;
DE              Short=IN;
DE              EC=2.7.7.- {ECO:0000305|PubMed:8623556};
DE              EC=3.1.-.- {ECO:0000305|PubMed:8623556};
GN   Name=gag-pro-pol;
OS   Human T-cell leukemia virus 2 (HTLV-2).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus.
OX   NCBI_TaxID=11909;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2582407; DOI=10.1073/pnas.82.10.3101;
RA   Shimotohno K., Takahashi Y., Shimizu N., Gojobori T., Golde D.W.,
RA   Chen I.S.Y., Miwa M., Sugimura T.;
RT   "Complete nucleotide sequence of an infectious clone of human T-cell
RT   leukemia virus type II: an open reading frame for the protease gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:3101-3105(1985).
RN   [2]
RP   RIBOSOMAL FRAMESHIFT.
RX   PubMed=2467996; DOI=10.1128/jvi.63.5.2400-2404.1989;
RA   Mador N., Panet A., Honigman A.;
RT   "Translation of gag, pro, and pol gene products of human T-cell leukemia
RT   virus type 2.";
RL   J. Virol. 63:2400-2404(1989).
RN   [3]
RP   RIBOSOMAL FRAMESHIFT.
RX   PubMed=8371359; DOI=10.1128/jvi.67.10.6273-6277.1993;
RA   Falk H., Mador N., Udi R., Panet A., Honigman A.;
RT   "Two cis-acting signals control ribosomal frameshift between human T-cell
RT   leukemia virus type II gag and pro genes.";
RL   J. Virol. 67:6273-6277(1993).
RN   [4]
RP   FUNCTION (INTEGRASE).
RX   PubMed=8623556; DOI=10.1006/viro.1996.0224;
RA   Balakrishnan M., Zastrow D., Jonsson C.B.;
RT   "Catalytic activities of the human T-cell leukemia virus type II
RT   integrase.";
RL   Virology 219:77-86(1996).
RN   [5]
RP   RIBOSOMAL FRAMESHIFT.
RX   PubMed=11222762; DOI=10.1093/nar/29.5.1125;
RA   Kim Y.-G., Maas S., Rich A.;
RT   "Comparative mutational analysis of cis-acting RNA signals for
RT   translational frameshifting in HIV-1 and HTLV-2.";
RL   Nucleic Acids Res. 29:1125-1131(2001).
RN   [6]
RP   STRUCTURE BY NMR OF 1-136.
RX   PubMed=9000634; DOI=10.1006/jmbi.1996.0700;
RA   Christensen A.M., Massiah M.A., Turner B.G., Sundquist W.I., Summers M.F.;
RT   "Three-dimensional structure of the HTLV-II matrix protein and comparative
RT   analysis of matrix proteins from the different classes of pathogenic human
RT   retroviruses.";
RL   J. Mol. Biol. 264:1117-1131(1996).
CC   -!- FUNCTION: [Gag-Pro-Pol polyprotein]: The matrix domain targets Gag,
CC       Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a
CC       multipartite membrane binding signal, that includes its myristoylated
CC       N-terminus. {ECO:0000250|UniProtKB:P03345}.
CC   -!- FUNCTION: [Matrix protein p19]: Matrix protein.
CC       {ECO:0000250|UniProtKB:P03345}.
CC   -!- FUNCTION: [Capsid protein p24]: Forms the spherical core of the virus
CC       that encapsulates the genomic RNA-nucleocapsid complex.
CC       {ECO:0000250|UniProtKB:P03362}.
CC   -!- FUNCTION: [Nucleocapsid protein p15-pro]: Binds strongly to viral
CC       nucleic acids and promote their aggregation. Also destabilizes the
CC       nucleic acids duplexes via highly structured zinc-binding motifs.
CC       {ECO:0000250|UniProtKB:P03345}.
CC   -!- FUNCTION: [Protease]: The aspartyl protease mediates proteolytic
CC       cleavages of Gag and Gag-Pol polyproteins during or shortly after the
CC       release of the virion from the plasma membrane. Cleavages take place as
CC       an ordered, step-wise cascade to yield mature proteins. This process is
CC       called maturation. Displays maximal activity during the budding process
CC       just prior to particle release from the cell (Potential). Cleaves the
CC       translation initiation factor eIF4G leading to the inhibition of host
CC       cap-dependent translation (By similarity).
CC       {ECO:0000250|UniProtKB:P03362, ECO:0000255|PROSITE-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-Pro binds to the primer-binding site (PBS) situated
CC       at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer
CC       to perform a short round of RNA-dependent minus-strand DNA synthesis.
CC       The reading proceeds through the U5 region and ends after the repeated
CC       (R) region which is present at both ends of viral RNA. The portion of
CC       the RNA-DNA heteroduplex is digested by the RNase H, resulting in a
CC       ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes
CC       with the identical R region situated at the 3' end of viral RNA. This
CC       template exchange, known as minus-strand DNA strong stop transfer, can
CC       be either intra- or intermolecular. RT uses the 3' end of this newly
CC       synthesized short ssDNA to perform the RNA-dependent minus-strand DNA
CC       synthesis of the whole template. RNase H digests the RNA template
CC       except for a polypurine tract (PPT) situated at the 5' end of the
CC       genome. It is not clear if both polymerase and RNase H activities are
CC       simultaneous. RNase H probably can proceed both in a polymerase-
CC       dependent (RNA cut into small fragments by the same RT performing DNA
CC       synthesis) and a polymerase-independent mode (cleavage of remaining RNA
CC       fragments by free RTs). Secondly, RT performs DNA-directed plus-strand
CC       DNA synthesis using the PPT that has not been removed by RNase H as
CC       primer. PPT and tRNA primers are then removed by RNase H. The 3' and 5'
CC       ssDNA PBS regions hybridize to form a circular dsDNA intermediate.
CC       Strand displacement synthesis by RT to the PBS and PPT ends produces a
CC       blunt ended, linear dsDNA copy of the viral genome that includes long
CC       terminal repeats (LTRs) at both ends (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. {ECO:0000305|PubMed:8623556}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00405};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00405};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
CC       Note=The RT polymerase active site binds 2 magnesium ions.
CC       {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 ribonuclease H (RNase H) activity.
CC       {ECO:0000250};
CC   -!- SUBUNIT: [Gag-Pro-Pol polyprotein]: Homodimer; the homodimers are part
CC       of the immature particles. Interacts with human TSG101 and NEDD4; these
CC       interactions are essential for budding and release of viral particles.
CC       {ECO:0000250|UniProtKB:P03345}.
CC   -!- SUBUNIT: [Matrix protein p19]: Homodimer; further assembles as
CC       homohexamers. {ECO:0000250|UniProtKB:P03345}.
CC   -!- INTERACTION:
CC       P03363; O14770: MEIS2; Xeno; NbExp=3; IntAct=EBI-9676133, EBI-2804934;
CC   -!- SUBCELLULAR LOCATION: [Matrix protein p19]: Virion
CC       {ECO:0000250|UniProtKB:P03345}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein p24]: Virion
CC       {ECO:0000250|UniProtKB:P03345}.
CC   -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p15-pro]: Virion
CC       {ECO:0000250|UniProtKB:P03345}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=3;
CC         Comment=This strategy of translation probably allows the virus to
CC         modulate the quantity of each viral protein. {ECO:0000305};
CC       Name=Gag-Pro-Pol polyprotein;
CC         IsoId=P03363-1; Sequence=Displayed;
CC       Name=Gag-Pro polyprotein;
CC         IsoId=P03353-1; Sequence=External;
CC       Name=Gag polyprotein;
CC         IsoId=P03346-1; Sequence=External;
CC   -!- DOMAIN: Gag polyprotein: Late-budding domains (L domains) are short
CC       sequence motifs essential for viral particle release. They can occur
CC       individually or in close proximity within structural proteins. They
CC       interacts with sorting cellular proteins of the multivesicular body
CC       (MVB) pathway. Most of these proteins are class E vacuolar protein
CC       sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes.
CC       Matrix protein p19 contains two L domains: a PTAP/PSAP motif which
CC       interacts with the UEV domain of TSG101, and a PPXY motif which binds
CC       to the WW domains of the ubiquitin ligase NEDD4.
CC       {ECO:0000250|UniProtKB:P03345}.
CC   -!- DOMAIN: [Capsid protein p24]: The capsid protein N-terminus seems to be
CC       involved in Gag-Gag interactions. {ECO:0000250|UniProtKB:P03362}.
CC   -!- PTM: [Matrix protein p19]: Phosphorylation of the matrix protein p19 by
CC       MAPK1 seems to play a role in budding. {ECO:0000250|UniProtKB:P03345}.
CC   -!- PTM: [Gag-Pro-Pol polyprotein]: Myristoylated. Myristoylation of the
CC       matrix (MA) domain mediates the transport and binding of Gag
CC       polyproteins to the host plasma membrane and is required for the
CC       assembly of viral particles. {ECO:0000250|UniProtKB:P03345}.
CC   -!- PTM: [Gag-Pro-Pol polyprotein]: Specific enzymatic cleavages by the
CC       viral protease yield mature proteins. The polyprotein is cleaved during
CC       and after budding, this process is termed maturation. The protease is
CC       autoproteolytically processed at its N- and C-termini.
CC       {ECO:0000250|UniProtKB:P03362}.
CC   -!- MISCELLANEOUS: The reverse transcriptase is an error-prone enzyme that
CC       lacks a proof-reading function. High mutations rate is a direct
CC       consequence of this characteristic. RT also displays frequent template
CC       swiching leading to high recombination rate. Recombination mostly
CC       occurs between homologous regions of the two copackaged RNA genomes. If
CC       these two RNA molecules derive from different viral strains, reverse
CC       transcription will give rise to highly recombinated proviral DNAs.
CC       {ECO:0000255|PROSITE-ProRule:PRU00405}.
CC   -!- MISCELLANEOUS: [Isoform Gag-Pro-Pol polyprotein]: Produced by -1
CC       ribosomal frameshifting at the gag-pol genes boundary.
CC       {ECO:0000269|PubMed:11222762, ECO:0000269|PubMed:2467996,
CC       ECO:0000269|PubMed:8371359}.
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DR   EMBL; M10060; AAB59885.1; ALT_SEQ; Genomic_DNA.
DR   PIR; A03962; GNLJH2.
DR   RefSeq; NP_041003.3; NC_001488.1.
DR   PDB; 1JVR; NMR; -; A=1-136.
DR   PDB; 6QBT; X-ray; 2.29 A; A=1217-1385.
DR   PDB; 6QBV; X-ray; 2.45 A; A/B/C/D=1217-1380.
DR   PDB; 6QBW; X-ray; 2.40 A; A=1217-1385.
DR   PDBsum; 1JVR; -.
DR   PDBsum; 6QBT; -.
DR   PDBsum; 6QBV; -.
DR   PDBsum; 6QBW; -.
DR   SMR; P03363; -.
DR   IntAct; P03363; 8.
DR   MINT; P03363; -.
DR   PRIDE; P03363; -.
DR   GeneID; 1491941; -.
DR   KEGG; vg:1491941; -.
DR   EvolutionaryTrace; P03363; -.
DR   Proteomes; UP000009254; Genome.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
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-EC.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.30; -; 1.
DR   Gene3D; 1.10.375.10; -; 1.
DR   Gene3D; 2.40.70.10; -; 1.
DR   Gene3D; 3.30.420.10; -; 2.
DR   Gene3D; 3.30.70.270; -; 2.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR003139; D_retro_matrix.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR045345; Gag_p24_C.
DR   InterPro; IPR000721; Gag_p24_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; IPR001995; Peptidase_A2_cat.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
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; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   Pfam; PF02228; Gag_p19; 1.
DR   Pfam; PF00607; Gag_p24; 1.
DR   Pfam; PF19317; Gag_p24_C; 1.
DR   Pfam; PF00552; IN_DBD_C; 1.
DR   Pfam; PF02022; Integrase_Zn; 1.
DR   Pfam; PF00075; RNase_H; 1.
DR   Pfam; PF00665; rve; 1.
DR   Pfam; PF00077; RVP; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00343; ZnF_C2HC; 2.
DR   SUPFAM; SSF47836; SSF47836; 1.
DR   SUPFAM; SSF47943; SSF47943; 1.
DR   SUPFAM; SSF50122; SSF50122; 1.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   SUPFAM; SSF57756; SSF57756; 1.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS51027; INTEGRASE_DBD; 1.
DR   PROSITE; PS50879; RNASE_H_1; 1.
DR   PROSITE; PS50878; RT_POL; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aspartyl protease; Capsid protein; DNA integration;
KW   DNA recombination; DNA-binding; Endonuclease;
KW   Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host translation shutoff by virus;
KW   Host gene expression shutoff by virus; Host-virus interaction; Hydrolase;
KW   Lipoprotein; Magnesium; Metal-binding; Multifunctional enzyme; Myristate;
KW   Nuclease; Nucleotidyltransferase; Protease; Reference proteome; Repeat;
KW   Ribosomal frameshifting; RNA-directed DNA polymerase; Transferase;
KW   Viral genome integration; Viral nucleoprotein; Virion;
KW   Virus entry into host cell; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..1461
FT                   /note="Gag-Pro-Pol polyprotein"
FT                   /id="PRO_0000085472"
FT   CHAIN           2..136
FT                   /note="Matrix protein p19"
FT                   /id="PRO_0000259946"
FT   CHAIN           137..350
FT                   /note="Capsid protein p24"
FT                   /id="PRO_0000259947"
FT   CHAIN           351..446
FT                   /note="Nucleocapsid protein p15-pro"
FT                   /id="PRO_0000259948"
FT   CHAIN           447..571
FT                   /note="Protease"
FT                   /id="PRO_0000261318"
FT   PEPTIDE         572..579
FT                   /note="p1"
FT                   /id="PRO_0000259949"
FT   CHAIN           580..1166
FT                   /note="Reverse transcriptase/ribonuclease H"
FT                   /id="PRO_0000259950"
FT   CHAIN           1167..1461
FT                   /note="Integrase"
FT                   /id="PRO_0000259951"
FT   DOMAIN          473..551
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT   DOMAIN          612..802
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   DOMAIN          1029..1164
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   DOMAIN          1218..1387
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   ZN_FING         361..378
FT                   /note="CCHC-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         384..401
FT                   /note="CCHC-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   DNA_BIND        1392..1441
FT                   /note="Integrase-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT   REGION          94..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           94..97
FT                   /note="PTAP/PSAP motif"
FT   MOTIF           124..127
FT                   /note="PPXY motif"
FT                   /evidence="ECO:0000250|UniProtKB:P03345"
FT   MOTIF           130..133
FT                   /note="PTAP/PSAP motif"
FT                   /evidence="ECO:0000250|UniProtKB:P03345"
FT   COMPBIAS        97..121
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        478
FT                   /note="For protease activity; shared with dimeric partner"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   BINDING         678
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:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         753
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:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         754
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:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         1038
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:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         1073
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:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         1095
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:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         1156
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:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         1229
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /ligand_note="catalytic; for integrase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   BINDING         1286
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /ligand_note="catalytic; for integrase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   SITE            136..137
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03362"
FT   SITE            350..351
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03362"
FT   SITE            446..447
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03362"
FT   SITE            571..572
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03362"
FT   SITE            579..580
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03362"
FT   SITE            1019..1020
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03362"
FT   SITE            1166..1167
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03362"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000255"
FT   STRAND          2..9
FT                   /evidence="ECO:0007829|PDB:1JVR"
FT   HELIX           21..33
FT                   /evidence="ECO:0007829|PDB:1JVR"
FT   TURN            40..42
FT                   /evidence="ECO:0007829|PDB:1JVR"
FT   HELIX           43..54
FT                   /evidence="ECO:0007829|PDB:1JVR"
FT   TURN            60..63
FT                   /evidence="ECO:0007829|PDB:1JVR"
FT   TURN            65..67
FT                   /evidence="ECO:0007829|PDB:1JVR"
FT   HELIX           68..71
FT                   /evidence="ECO:0007829|PDB:1JVR"
FT   HELIX           80..88
FT                   /evidence="ECO:0007829|PDB:1JVR"
FT   TURN            89..91
FT                   /evidence="ECO:0007829|PDB:1JVR"
FT   STRAND          99..103
FT                   /evidence="ECO:0007829|PDB:1JVR"
FT   STRAND          117..119
FT                   /evidence="ECO:0007829|PDB:1JVR"
FT   STRAND          1224..1235
FT                   /evidence="ECO:0007829|PDB:6QBT"
FT   STRAND          1238..1247
FT                   /evidence="ECO:0007829|PDB:6QBT"
FT   TURN            1248..1250
FT                   /evidence="ECO:0007829|PDB:6QBT"
FT   STRAND          1253..1259
FT                   /evidence="ECO:0007829|PDB:6QBT"
FT   HELIX           1263..1277
FT                   /evidence="ECO:0007829|PDB:6QBT"
FT   STRAND          1281..1284
FT                   /evidence="ECO:0007829|PDB:6QBT"
FT   HELIX           1289..1292
FT                   /evidence="ECO:0007829|PDB:6QBT"
FT   HELIX           1294..1302
FT                   /evidence="ECO:0007829|PDB:6QBT"
FT   STRAND          1306..1308
FT                   /evidence="ECO:0007829|PDB:6QBT"
FT   HELIX           1320..1338
FT                   /evidence="ECO:0007829|PDB:6QBT"
FT   STRAND          1339..1342
FT                   /evidence="ECO:0007829|PDB:6QBT"
FT   HELIX           1344..1357
FT                   /evidence="ECO:0007829|PDB:6QBT"
FT   TURN            1362..1364
FT                   /evidence="ECO:0007829|PDB:6QBT"
FT   HELIX           1368..1372
FT                   /evidence="ECO:0007829|PDB:6QBT"
SQ   SEQUENCE   1461 AA;  162402 MW;  2D2911076BDD1002 CRC64;
     MGQIHGLSPT PIPKAPRGLS THHWLNFLQA AYRLQPRPSD FDFQQLRRFL KLALKTPIWL
     NPIDYSLLAS LIPKGYPGRV VEIINILVKN QVSPSAPAAP VPTPICPTTT PPPPPPPSPE
     AHVPPPYVEP TTTQCFPILH PPGAPSAHRP WQMKDLQAIK QEVSSSALGS PQFMQTLRLA
     VQQFDPTAKD LQDLLQYLCS SLVVSLHHQQ LNTLITEAET RGMTGYNPMA GPLRMQANNP
     AQQGLRREYQ NLWLAAFSTL PGNTRDPSWA AILQGLEEPY CAFVERLNVA LDNGLPEGTP
     KEPILRSLAY SNANKECQKI LQARGHTNSP LGEMLRTCQA WTPKDKTKVL VVQPRRPPPT
     QPCFRCGKVG HWSRDCTQPR PPPGPCPLCQ DPSHWKRDCP QLKPPQEEGE PLLLDLPSTS
     GTTEEKNLLK GGDLISPHPD QDISILPLIP LRQQQQPILG VRISVMGQTP QPTQALLDTG
     ADLTVIPQTL VPGPVKLHDT LILGASGQTN TQFKLLQTPL HIFLPFRRSP VILSSCLLDT
     HNKWTIIGRD ALQQCQGLLY LPDDPSPHQL LPIATPNTIG LEHLPPPPQV DQFPLNLPER
     LQALNDLVSK ALEAGHIEPY SGPGNNPVFP VKKPNGKWRF IHDLRATNAI TTTLTSPSPG
     PPDLTSLPTA LPHLQTIDLT DAFFQIPLPK QYQPYFAFTI PQPCNYGPGT RYAWTVLPQG
     FKNSPTLFEQ QLAAVLNPMR KMFPTSTIVQ YMDDILLASP TNEELQQLSQ LTLQALTTHG
     LPISQEKTQQ TPGQIRFLGQ VISPNHITYE STPTIPIKSQ WTLTELQVIL GEIQWVSKGT
     PILRKHLQSL YSALHGYRDP RACITLTPQQ LHALHAIQQA LQHNCRGRLN PALPLLGLIS
     LSTSGTTSVI FQPKQNWPLA WLHTPHPPTS LCPWGHLLAC TILTLDKYTL QHYGQLCQSF
     HHNMSKQALC DFLRNSPHPS VGILIHHMGR FHNLGSQPSG PWKTLLHLPT LLQEPRLLRP
     IFTLSPVVLD TAPCLFSDGS PQKAAYVLWD QTILQQDITP LPSHETHSAQ KGELLALICG
     LRAAKPWPSL NIFLDSKYLI KYLHSLAIGA FLGTSAHQTL QAALPPLLQG KTIYLHHVRS
     HTNLPDPIST FNEYTDSLIL APLVPLTPQG LHGLTHCNQR ALVSFGATPR EAKSLVQTCH
     TCQTINSQHH MPRGYIRRGL LPNHIWQGDV THYKYKKYKY CLHVWVDTFS GAVSVSCKKK
     ETSCETISAV LQAISLLGKP LHINTDNGPA FLSQEFQEFC TSYRIKHSTH IPYNPTSSGL
     VERTNGVIKN LLNKYLLDCP NLPLDNAIHK ALWTLNQLNV MNPSGKTRWQ IHHSPPLPPI
     PEASTPPKPP PKWFYYKLPG LTNQRWKGPL QSLQEAAGAA LLSIDGSPRW IPWRFLKKAA
     CPRPDASELA EHAATDHQHH G
 
 
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