POL_WMSV
ID POL_WMSV Reviewed; 1687 AA.
AC P03359; A0A0U3TYK5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Gag-Pol polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p15;
DE Short=MA;
DE Contains:
DE RecName: Full=RNA-binding phosphoprotein p12;
DE AltName: Full=pp12;
DE Contains:
DE RecName: Full=Capsid protein p30;
DE Short=CA;
DE Contains:
DE RecName: Full=Nucleocapsid protein p10-Pol;
DE Short=NC-pol;
DE Contains:
DE RecName: Full=Protease;
DE Short=PR;
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
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 AltName: Full=p80;
DE Contains:
DE RecName: Full=Integrase;
DE Short=IN;
DE EC=2.7.7.-;
DE EC=3.1.-.-;
DE AltName: Full=p46;
GN Name=pol;
OS Woolly monkey sarcoma virus (WMSV) (Smian sarcoma-associated virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11970;
OH NCBI_TaxID=9518; Lagothrix (woolly monkeys).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSAV;
RX PubMed=26637454; DOI=10.1128/jvi.02745-15;
RA Alfano N., Kolokotronis S.O., Tsangaras K., Roca A.L., Xu W., Eiden M.V.,
RA Greenwood A.D.;
RT "Episodic diversifying selection shaped the genomes of gibbon ape leukemia
RT virus and related gammaretroviruses.";
RL J. Virol. 90:1757-1772(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1390-1687.
RX PubMed=6298772; DOI=10.1073/pnas.80.3.731;
RA Devare S.G., Reddy E.P., Law J.D., Robbins K.C., Aaronson S.A.;
RT "Nucleotide sequence of the simian sarcoma virus genome: demonstration that
RT its acquired cellular sequences encode the transforming gene product
RT p28sis.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:731-735(1983).
CC -!- FUNCTION: [Gag-Pol polyprotein]: Plays a role in budding and is
CC processed by the viral protease during virion maturation outside the
CC cell. During budding, it recruits, in a PPXY-dependent or independent
CC manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules
CC to Gag-Pol, or to Gag-Pol binding host factors. Interaction with HECT
CC ubiquitin ligases probably links the viral protein to the host ESCRT
CC pathway and facilitates release. {ECO:0000250|UniProtKB:P03332}.
CC -!- FUNCTION: [Matrix protein p15]: Targets Gag and gag-pol polyproteins to
CC the plasma membrane via a multipartite membrane binding signal, that
CC includes its myristoylated N-terminus. Also mediates nuclear
CC localization of the pre-integration complex.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- FUNCTION: [RNA-binding phosphoprotein p12]: Constituent of the pre-
CC integration complex (PIC) which tethers the latter to mitotic
CC chromosomes. This allows the integration of the viral genome into the
CC host DNA. {ECO:0000250|UniProtKB:P03355}.
CC -!- FUNCTION: [Capsid protein p30]: Forms the spherical core of the virion
CC that encapsulates the genomic RNA-nucleocapsid complex.
CC {ECO:0000250|UniProtKB:P03336}.
CC -!- FUNCTION: [Nucleocapsid protein p10-Pol]: Involved in the packaging and
CC encapsidation of two copies of the genome (By similarity). Binds with
CC high affinity to conserved UCUG elements within the packaging signal,
CC located near the 5'-end of the genome (By similarity). This binding is
CC dependent on genome dimerization (By similarity). Acts as a nucleic
CC acid chaperone which is involved in rearrangement of nucleic acid
CC secondary structures during gRNA retrotranscription (By similarity).
CC {ECO:0000250|UniProtKB:P03332, ECO:0000250|UniProtKB:P03355}.
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. {ECO:0000255|PROSITE-
CC ProRule:PRU00275}.
CC -!- FUNCTION: [Reverse transcriptase/ribonuclease H]: RT is a
CC multifunctional enzyme that converts the viral dimeric RNA genome into
CC dsDNA in the cytoplasm, shortly after virus entry into the cell. This
CC enzyme displays a DNA polymerase activity that can copy either DNA or
CC RNA templates, and a ribonuclease H (RNase H) activity that cleaves the
CC RNA 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 binds to the primer-binding site (PBS) situated at
CC the 5' end of the viral RNA. RT uses the 3' end of the tRNA primer to
CC perform a short round of RNA-dependent minus-strand DNA synthesis. The
CC reading proceeds through the U5 region and ends after the repeated (R)
CC region which is present at both ends of viral RNA. The portion of the
CC RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA
CC product attached to the tRNA primer. This ssDNA/tRNA hybridizes with
CC 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 primers. PPT and tRNA primers are then removed by RNase H. The 3' and
CC 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate.
CC Strand displacement synthesis by RT to the PBS and PPT ends produces a
CC blunt ended, linear dsDNA copy of the viral genome that includes long
CC terminal repeats (LTRs) at both ends. {ECO:0000255}.
CC -!- FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host
CC chromosome, by performing a series of DNA cutting and joining
CC reactions. This enzyme activity takes place after virion entry into a
CC cell and reverse transcription of the RNA genome in dsDNA. The first
CC step in the integration process is 3' processing. This step requires a
CC complex comprising the viral genome, matrix protein and integrase. This
CC complex is called the pre-integration complex (PIC). The integrase
CC protein removes 2 nucleotides from each 3' end of the viral DNA,
CC leaving recessed CA OH's at the 3' ends. In the second step that
CC requires cell division, the PIC enters cell nucleus. In the third step,
CC termed strand transfer, the integrase protein joins the previously
CC processed 3' ends to the 5' ends of strands of target cellular DNA at
CC the site of integration. The last step is viral DNA integration into
CC host chromosome. {ECO:0000250|UniProtKB:P03355}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
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;
CC Evidence={ECO:0000250|UniProtKB:P03355};
CC Note=Binds 1 magnesium ion for ribonuclease H (RNase H) activity.
CC {ECO:0000250|UniProtKB:P03355};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P03355};
CC Note=Magnesium ions are required for integrase activity. Binds at least
CC 1, maybe 2 magnesium ions. {ECO:0000250|UniProtKB:P03355};
CC -!- ACTIVITY REGULATION: [Protease]: Most efficiently inhibited by
CC Amprenavir, which is able to block Gag-Pol processing in infected
CC cells. {ECO:0000250|UniProtKB:P03355}.
CC -!- SUBUNIT: [Capsid protein p30]: Homohexamer; further associates as
CC homomultimer (By similarity). The virus core is composed of a lattice
CC formed from hexagonal rings, each containing six capsid monomers.
CC {ECO:0000250|UniProtKB:P03355}.
CC -!- SUBUNIT: [Gag-Pol polyprotein]: Interacts (via PPXY motif) with host
CC NEDD4 (By similarity). Interacts (via PSAP motif) with host TSG101.
CC {ECO:0000250|UniProtKB:P03355}.
CC -!- SUBUNIT: [Reverse transcriptase/ribonuclease H]: The reverse
CC transcriptase is a monomer (Potential). Interacts (via RNase domains)
CC with host release factor ETF1; this interaction is essential for
CC translational readthrough of amber codon between viral gag and pol
CC genes, as well as for viral replication. {ECO:0000250|UniProtKB:P03355,
CC ECO:0000305}.
CC -!- SUBUNIT: [Integrase]: Homodimer. {ECO:0000250|UniProtKB:P03355}.
CC -!- SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Virion
CC {ECO:0000250|UniProtKB:P03332}. Host cell membrane
CC {ECO:0000250|UniProtKB:P03332}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P03332}. Host late endosome membrane
CC {ECO:0000250|UniProtKB:P03332}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular body
CC {ECO:0000250|UniProtKB:P26807}. Note=These locations are probably
CC linked to virus assembly sites. {ECO:0000250|UniProtKB:P03355}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p15]: Virion
CC {ECO:0000250|UniProtKB:P03355}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p30]: Virion
CC {ECO:0000250|UniProtKB:P03355}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p10-Pol]: Virion
CC {ECO:0000250|UniProtKB:P03355}.
CC -!- SUBCELLULAR LOCATION: [Protease]: Virion
CC {ECO:0000250|UniProtKB:P03355}.
CC -!- SUBCELLULAR LOCATION: [RNA-binding phosphoprotein p12]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P03355}. Note=Localizes to the host cytoplasm
CC early in infection and binds to the mitotic chromosomes later on.
CC {ECO:0000250|UniProtKB:P03355}.
CC -!- DOMAIN: Gag polyprotein: Late-budding domains (L domains) are short
CC sequence motifs essential for viral particle budding. They recruit
CC proteins of the host ESCRT machinery (Endosomal Sorting Complex
CC Required for Transport) or ESCRT-associated proteins. RNA-binding
CC phosphoprotein p12 contains one L domain: a PPXY motif which
CC potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin
CC ligase. Matrix protein p15 contains one L domain: a PTAP/PSAP motif,
CC which potentially interacts with the UEV domain of TSG101.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral
CC protease yield mature proteins. The protease is released by
CC autocatalytic cleavage. The polyprotein is cleaved during and after
CC budding, this process is termed maturation.
CC {ECO:0000250|UniProtKB:P03355}.
CC -!- PTM: [RNA-binding phosphoprotein p12]: Phosphorylated on serine
CC residues. {ECO:0000250|UniProtKB:P03355}.
CC -!- MISCELLANEOUS: [Gag-Pol polyprotein]: This protein is translated as a
CC gag-pol fusion protein by episodic readthrough of the gag protein
CC termination codon. Readthrough of the terminator codon TAG occurs
CC between the codons for 521-Asp and 523-Gly.
CC {ECO:0000250|UniProtKB:P03355}.
CC -!- MISCELLANEOUS: [Nucleocapsid protein p10-Pol]: Nucleocapsid protein
CC p10-Pol released from Pol polyprotein (NC-pol) is a few amino acids
CC shorter than the nucleocapsid protein p10 released from Gag polyprotein
CC (NC-gag). {ECO:0000250|UniProtKB:P03355}.
CC -!- MISCELLANEOUS: [Reverse transcriptase/ribonuclease H]: The reverse
CC transcriptase is an error-prone enzyme that lacks a proof-reading
CC function. High mutations rate is a direct consequence of this
CC characteristic. RT also displays frequent template swiching leading to
CC high recombination rate. Recombination mostly occurs between homologous
CC regions of the two copackaged RNA genomes. If these two RNA molecules
CC derive from different viral strains, reverse transcription will give
CC rise to highly recombinated proviral DNAs. {ECO:0000255|PROSITE-
CC ProRule:PRU00405}.
CC -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ALV83312.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA24515.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; KT724051; ALV83312.1; ALT_INIT; Genomic_DNA.
DR EMBL; V01201; CAA24515.1; ALT_SEQ; Genomic_DNA.
DR PIR; A05071; A05071.
DR RefSeq; YP_001165470.1; NC_009424.4.
DR BindingDB; P03359; -.
DR ChEMBL; CHEMBL2983; -.
DR GeneID; 5176146; -.
DR KEGG; vg:5176146; -.
DR Proteomes; UP000167400; Genome.
DR Proteomes; UP000203831; Genome.
DR GO; GO:0044185; C:host cell late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR GO; GO:0019068; P:virion assembly; IEA:InterPro.
DR Gene3D; 1.10.150.180; -; 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; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000840; G_retro_matrix.
DR InterPro; IPR036946; G_retro_matrix_sf.
DR InterPro; IPR003036; Gag_P30.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR040643; MLVIN_C.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR018061; Retropepsins.
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; IPR041577; RT_RNaseH_2.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR InterPro; IPR015416; Znf_H2C2_histone_UAS-bd.
DR Pfam; PF01140; Gag_MA; 1.
DR Pfam; PF02093; Gag_p30; 1.
DR Pfam; PF18697; MLVIN_C; 1.
DR Pfam; PF00075; RNase_H; 1.
DR Pfam; PF17919; RT_RNaseH_2; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR Pfam; PF09337; zf-H2C2; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Capsid protein; Coiled coil; DNA integration;
KW DNA recombination; DNA-binding; DNA-directed DNA polymerase; Endonuclease;
KW Host cell membrane; Host cytoplasm; Host endosome; Host membrane;
KW Host-virus interaction; Hydrolase; Lipoprotein; Magnesium; Membrane;
KW Metal-binding; Multifunctional enzyme; Myristate; Nuclease;
KW Nucleotidyltransferase; Phosphoprotein; Protease; RNA-binding;
KW RNA-directed DNA polymerase; Transferase; Viral genome integration;
KW Viral matrix protein; Viral nucleoprotein; Virion;
KW Virus entry into host cell; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..1687
FT /note="Gag-Pol polyprotein"
FT /id="PRO_0000125497"
FT CHAIN 2..128
FT /note="Matrix protein p15"
FT /id="PRO_0000442867"
FT CHAIN 129..196
FT /note="RNA-binding phosphoprotein p12"
FT /id="PRO_0000442868"
FT CHAIN 197..455
FT /note="Capsid protein p30"
FT /id="PRO_0000442869"
FT CHAIN 456..517
FT /note="Nucleocapsid protein p10-Pol"
FT /id="PRO_0000442870"
FT CHAIN 518..641
FT /note="Protease"
FT /id="PRO_0000442871"
FT CHAIN 642..1310
FT /note="Reverse transcriptase/ribonuclease H"
FT /id="PRO_0000442872"
FT CHAIN 1311..1683
FT /note="Integrase"
FT /id="PRO_0000442873"
FT DOMAIN 544..614
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 721..912
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 1153..1299
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 1394..1552
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 490..507
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 1339..1377
FT /note="HHCC-type"
FT /evidence="ECO:0000250|UniProtKB:P03355"
FT REGION 96..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 408..455
FT /evidence="ECO:0000255"
FT MOTIF 108..111
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT MOTIF 140..143
FT /note="PPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT COMPBIAS 141..160
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 549
FT /note="Protease; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT BINDING 789
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 863
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 864
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 1180
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 1200
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 1221
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 1291
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 1405
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 1464
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 128..129
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03355"
FT SITE 196..197
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03355"
FT SITE 455..456
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03355"
FT SITE 517..518
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03355"
FT SITE 641..642
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03355"
FT SITE 1310..1311
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03355"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1687 AA; 188011 MW; 4E5B6C98176DE554 CRC64;
MGQNNSTPLS LTLDHWKDVR TRAHNLSVKI RKGKWQTFCS SEWPTFGVGW PPEGTFNLSV
IFAVKRIVFQ ETGGHPDQVP YIVVWQDLAQ SPPPWVPPSA KIAVVSSPEN TRGPSAGRPS
APPRPPIYPA TDDLLLLSEP PPYPAALPPP LAPPAVGPAP GQAPDSSDPE GPAAGTRSRR
ARSPADDSGP DSTVILPLRA IGPPAEPNGL VPLQYWPFSS ADLYNWKSNH PSFSENPAGL
TGLLESLMFS HQPTWDDCQQ LLQILFTTEE RERILLEARK NVLGDNGAPT QLENLINEAF
PLNRPQWDYN TAAGRERLLV YRRTLVAGLK GAARRPTNLA KVREVLQGPA EPPSVFLERL
MEAYRRYTPF DPSEEGQQAA VAMAFIGQSA PDIKKKLQRL EGLQDYSLQD LVREAEKVYH
KRETEEERQE REKKEAEERE RRRDRRQEKN LTRILAAVVS ERGSRDRQTG NLSNRARKTP
RDGRPPLDKD QCAYCKEKGH WARECPQKKN VREAKVLALD DQGSRGSDPL PEPRVTLTVE
GTPIEFLVDT GAEHSVLTQP MGKVGSRRTV VEGATGSKVY PWTTKRLLKI GHKQVTHSFL
VIPECPAPLL GRDLLTKLKA QIQFSAEGPQ VTWEDRPTMC LVLNLEEEYR LHEKPVPSSI
DPSWLQLFPT VWAERAGMGL ANQVPPVVVE LRSGASPVAV RQYPMSKEAR EGIRPHIQRF
LDLGVLVPCQ SPWNTPLLPV KKPGTNDYRP VQDLREINKR VQDIHPTVPN PYNLLSSLPP
SHTWYSVLDL KDAFFCLKLH PNSQPLFAFE WRDPEKGNTG QLTWTRLPQG FKNSPTLFDE
ALHRDLAPFR ALNPQVVLLQ YVDDLLVAAP TYRDCKEGTQ KLLQELSKLG YRVSAKKAQL
CQKEVTYLGY LLKEGKRWLT PARKATVMKI PPPTTPRQVR EFLGTAGFCR LWIPGFASLA
APLYPLTKES IPFIWTEEHQ KAFDRIKEAL LSAPALALPD LTKPFTLYVD ERAGVARGVL
TQTLGPWRRP VAYLSKKLDP VASGWPTCLK AVAAVALLLK DADKLTLGQN VTVIASHSLE
SIVRQPPDRW MTNARMTHYQ SLLLNERVSF APPAVLNPAT LLPVESEATP VHRCSEILAE
ETGTRRDLKD QPLPGVPAWY TDGSSFIAEG KRRAGAAIVD GKRTVWASSL PEGTSAQKAE
LVALTQALRL AEGKDINIYT DSRYAFATAH IHGAIYKQRG LLTSAGKDIK NKEEILALLE
AIHLPKRVAI IHCPGHQKGN DPVATGNRRA DEAAKQAALS TRVLAETTKP QELIXPAQVK
TRPGELTPDR GKEFIQRLHQ LTHLGPEKLL QLVNRTSLLI PNLQSAVREV TSQCQACAMT
NAVTTYRETG KRQRGDRPGV YWEVDFTEVK PGRYGNRYLL VFIDTFSGWV EAFPTKTETA
LTVCKKILEE ILPRFGIPKV LGSDNGPAFV AQVSQGLATQ LGINWKLHCA YRPQSSGQVE
RMNRTIKETL TKLALETGXK DWVALLPLAL LRARNTPGRF GLTPYEILYG GPPPILESGG
TLGPDDNFLP VLFTHLKALE VVRTQIWDQI KEVYKPGTVA IPHPFQVGDQ VLVRRHRPGS
LEPRWKGPYL VLLTTPTAVK VDGIAAWVHA SHLKPAPPSA PDESWELEKA DHPLKLRIRR
RRNESAK
