POL_FLV
ID POL_FLV Reviewed; 1712 AA.
AC P10273; O89811;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Gag-Pol polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p15;
DE Contains:
DE RecName: Full=RNA-binding phosphoprotein p12;
DE AltName: Full=pp12;
DE Contains:
DE RecName: Full=Capsid protein p30;
DE Contains:
DE RecName: Full=Nucleocapsid protein p10-Pol;
DE Short=NC-pol;
DE Contains:
DE RecName: Full=Protease;
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 Contains:
DE RecName: Full=Integrase;
DE Short=IN;
DE EC=2.7.7.- {ECO:0000250|UniProtKB:P03355};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P03355};
GN Name=pol;
OS Feline leukemia virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11768;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rickard subgroup A;
RX PubMed=9696797; DOI=10.1128/jvi.72.9.7048-7056.1998;
RA Chen H., Bechtel M.K., Shi Y., Phipps A., Mathes L.E., Hayes K.A.,
RA Roy-Burman P.;
RT "Pathogenicity induced by feline leukemia virus, Rickard strain, subgroup A
RT plasmid DNA (pFRA).";
RL J. Virol. 72:7048-7056(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-706.
RX PubMed=6328019; DOI=10.1128/jvi.50.3.884-894.1984;
RA Laprevotte I., Hampe A., Sherr C.J., Galibert F.;
RT "Nucleotide sequence of the gag gene and gag-pol junction of feline
RT leukemia virus.";
RL J. Virol. 50:884-894(1984).
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 (By
CC similarity). {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 (By
CC similarity). Interacts (via LYPX(n)L motif) with host PDCD6IP (By
CC similarity). {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 (By similarity).
CC {ECO:0000250|UniProtKB:P03355, ECO:0000305}.
CC -!- SUBUNIT: [Integrase]: Homodimer (By similarity).
CC {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-Pol polyprotein]: Late-budding domains (L domains) are
CC short sequence motifs essential for viral particle release. They can
CC occur individually or in close proximity within structural proteins.
CC They interacts with sorting cellular proteins of the multivesicular
CC body (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 RNA-binding phosphoprotein p12 contains one L domain: a PPXY motif
CC which potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin
CC ligase. PPXY motif is essential for virus egress. Matrix protein p15
CC contains one L domain: a PTAP/PSAP motif, which potentially interacts
CC with the UEV domain of TSG101. The junction between the matrix protein
CC p15 and RNA-binding phosphoprotein p12 also contains one L domain: a
CC LYPX(n)L motif which potentially interacts with PDCD6IP. Both PSAP and
CC LYPX(n)L domains might play little to no role in budding and possibly
CC drive residual virus release. contains. {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 506-Asp and 508-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=AAA43056.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAA43056.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC31801.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF052723; AAC31801.1; ALT_INIT; Genomic_DNA.
DR EMBL; K01803; AAA43056.2; ALT_SEQ; Genomic_RNA.
DR RefSeq; NP_047255.1; NC_001940.1.
DR SMR; P10273; -.
DR MEROPS; A02.008; -.
DR GeneID; 1724726; -.
DR KEGG; vg:1724726; -.
DR Proteomes; UP000118006; 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; IPR039464; Gag-pol_Znf-H3C2.
DR InterPro; IPR002079; Gag_p12.
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 Pfam; PF01140; Gag_MA; 1.
DR Pfam; PF01141; Gag_p12; 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; PF16721; zf-H3C2; 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; DNA integration; DNA recombination;
KW DNA-binding; DNA-directed DNA polymerase; Endonuclease; Host cell membrane;
KW Host cytoplasm; Host endosome; Host membrane; Host-virus interaction;
KW Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW Multifunctional enzyme; Myristate; Nuclease; Nucleotidyltransferase;
KW Phosphoprotein; Protease; RNA-binding; RNA-directed DNA polymerase;
KW Transferase; Viral genome integration; Viral matrix protein;
KW Viral nucleoprotein; Virion; Virus entry into host cell; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..1712
FT /note="Gag-Pol polyprotein"
FT /id="PRO_0000259718"
FT CHAIN 2..127
FT /note="Matrix protein p15"
FT /id="PRO_0000442878"
FT CHAIN 128..197
FT /note="RNA-binding phosphoprotein p12"
FT /id="PRO_0000442879"
FT CHAIN 198..445
FT /note="Capsid protein p30"
FT /id="PRO_0000442880"
FT CHAIN 446..502
FT /note="Nucleocapsid protein p10-Pol"
FT /id="PRO_0000442881"
FT CHAIN 503..627
FT /note="Protease"
FT /id="PRO_0000026126"
FT CHAIN 628..1297
FT /note="Reverse transcriptase/ribonuclease H"
FT /id="PRO_0000026127"
FT CHAIN 1298..1712
FT /note="Integrase"
FT /id="PRO_0000442882"
FT DOMAIN 529..599
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 708..899
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 1141..1287
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 1411..1569
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 473..490
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 1354..1394
FT /note="HHCC-type"
FT /evidence="ECO:0000250|UniProtKB:P03355"
FT REGION 97..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1676..1703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 107..110
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT MOTIF 126..130
FT /note="LYPX(n)L motif"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT MOTIF 157..160
FT /note="PPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT COMPBIAS 97..118
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 534
FT /note="Protease; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT BINDING 776
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 850
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 851
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 1150
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 1188
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 1209
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 1279
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 1422
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 1481
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 127..128
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03355"
FT SITE 197..198
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03355"
FT SITE 445..446
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03355"
FT SITE 502..503
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03355"
FT SITE 627..628
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03355"
FT SITE 1297..1298
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"
FT VARIANT 5
FT /note="I -> V"
FT /evidence="ECO:0000305|PubMed:6328019"
FT VARIANT 74
FT /note="Y -> H"
FT /evidence="ECO:0000305|PubMed:6328019"
FT VARIANT 130
FT /note="L -> V"
FT /evidence="ECO:0000305|PubMed:6328019"
FT VARIANT 133
FT /note="S -> P"
FT /evidence="ECO:0000305|PubMed:6328019"
FT VARIANT 175
FT /note="T -> A"
FT /evidence="ECO:0000305|PubMed:6328019"
FT VARIANT 460
FT /note="S -> N"
FT /evidence="ECO:0000305|PubMed:6328019"
FT VARIANT 505
FT /note="G -> E"
FT /evidence="ECO:0000305|PubMed:6328019"
FT VARIANT 523
FT /note="K -> R"
FT /evidence="ECO:0000305|PubMed:6328019"
FT VARIANT 620
FT /note="K -> R"
FT /evidence="ECO:0000305|PubMed:6328019"
SQ SEQUENCE 1712 AA; 192423 MW; BE91DA74846B5817 CRC64;
MGQTITTPLS LTLDHWSEVR ARAHNQGVEV RKKKWITLCE AEWVMMNVGW PREGTFSLDN
ISQVEKKIFA PGPYGHPDQV PYITTWRSLA TDPPSWVRPF LPPPKPPTPL PQPLSPQPSA
PLTSSLYPVL PKSDPPKPPV LPPDPSSPLI DLLTEEPPPY PGGHGPPPSG PRTPTASPIA
SRLRERRENP AEESQALPLR EGPNNRPQYW PFSASDLYNW KSHNPPFSQD PVALTNLIES
ILVTHQPTWD DCQQLLQALL TGEERQRVLL EARKQVPGED GRPTQLPNVI DETFPLTRPN
WDFATPAGRE HLRLYRQLLL AGLRGAARRP TNLAQVKQVV QGKEETPAAF LERLKEAYRM
YTPYDPEDPG QAASVILSFI YQSSPDIRNK LQRLEGLQGF TLSDLLKEAE KIYNKRETPE
EREERLWQRQ EERDKKRHKE MTKVLATVVA QNRDKDREES KLGDQRKIPL GKDQCAYCKE
KGHWVRDCPK RPRKKPANST LLNLGDQESQ GQDPPPEPRI TLKIGGQPVT FLVDTGAQHS
VLTRPDGPLS DRTALVQGAT GSKNYRWTTD RRVQLATGKV THSFLYVPEC PYPLLGRDLL
TKLKAQIHFT GEGANVVGPK GLPLQVLTLQ LEEEYRLFEP ESTQKQEMDI WLKNFPQAWA
ETGGMGTAHC QAPVLIQLKA TATPISIRQY PMPHEAYQGI KPHIRRMLDQ GILKPCQSPW
NTPLLPVKKP GTEDYRPVQD LREVNKRVED IHPTVPNPYN LLSTLPPSHP WYTVLDLKDA
FFCLRLHSES QLLFAFEWRD PEIGLSGQLT WTRLPQGFKN SPTLFDEALH SDLADFRVRY
PALVLLQYVD DLLLAAATRT ECLEGTKALL ETLGNKGYRA SAKKAQICLQ EVTYLGYSLK
DGQRWLTKAR KEAILSIPVP KNSRQVREFL GTAGYCRLWI PGFAELAAPL YPLTRPGTLF
QWGTEQQLAF EDIKKALLSS PALGLPDITK PFELFIDENS GFAKGVLVQK LGPWKRPVAY
LSKKLDTVAS GWPPCLRMVA AIAILVKDAG KLTLGQPLTI LTSHPVEALV RQPPNKWLSN
ARMTHYQAML LDAERVHFGP TVSLNPATLL PLPSGGNHHD CLQILAETHG TRPDLTDQPL
PDADLTWYTD GSSFIRNGER EAGAAVTTES EVIWAAPLPP GTSAQRAELI ALTQALKMAE
GKKLTVYTDS RYAFATTHVH GEIYRRRGLL TSEGKEIKNK NEILALLEAL FLPKRLSIIH
CPGHQKGDSP QAKGNRLADD TAKKAATETH SSLTVLPTEL IEGPKRPPWE YDDSDLDLVQ
KLEAHYEPKR GTWEYRGKTI MPEKYAKELI SHLHKLTHLS ARKMKTLLER EETGFYLPNR
DLHLRQVTES CRACAQINAG KIKFGPDVRA RGRRPGTHWE VDFTEIKPGM YGYKYLLVFI
DTFSGWAEAY PAKHETAKVV AKKLLEEIFP RYGIPQVLGS DNGPAFISQV SQSVATLLGI
NWKLHCAYRP QSSGQVERMN RSIKETLTKL TLETGSKDWV LLLPLVLYRV RNTPGPHGLT
PFEILYGAPP PMAHFFDTDI SSFATSPTMQ AHLRALQLVQ EEIQRPLAAA YREKLETPVV
PHPFKPGDSV WVRRHQTKNL EPRWKGPHIV LLTTPTALKV DGVAAWIHAS HVKAAGPTTN
QDLSDSPSSD DPSRWKVQRT QNPLKIRLSR GT
