POL_JSRV
ID POL_JSRV Reviewed; 1726 AA.
AC P31623;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Gag-Pro-Pol polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p10;
DE Contains:
DE RecName: Full=Phosphorylated protein;
DE Contains:
DE RecName: Full=p12;
DE Contains:
DE RecName: Full=Capsid protein p27;
DE Contains:
DE RecName: Full=Nucleocapsid protein-dUTPase;
DE Short=NC-dUTPase;
DE EC=3.6.1.23 {ECO:0000250|UniProtKB:P11283};
DE Contains:
DE RecName: Full=Protease 17 kDa {ECO:0000250|UniProtKB:P07572};
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
DE Contains:
DE RecName: Full=Protease 13 kDa {ECO:0000250|UniProtKB:P07572};
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
DE Contains:
DE RecName: Full=G-patch peptide {ECO:0000250|UniProtKB:P07572};
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:P11283};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P11283};
GN Name=pol;
OS Sheep pulmonary adenomatosis virus (Jaagsiekte sheep retrovirus) (JSRV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11746;
OH NCBI_TaxID=9940; Ovis aries (Sheep).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=JSRV-SA;
RX PubMed=1629959; DOI=10.1128/jvi.66.8.4930-4939.1992;
RA York D.F., Vigne R., Verwoerd D.W., Querat G.;
RT "Nucleotide sequence of the jaagsiekte retrovirus, an exogenous and
RT endogenous type D and B retrovirus of sheep and goats.";
RL J. Virol. 66:4930-4939(1992).
RN [2]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=24298557; DOI=10.1155/2013/984028;
RA Huang X., Cheng Q., Du Z.;
RT "A genome-wide analysis of RNA pseudoknots that stimulate efficient -1
RT ribosomal frameshifting or readthrough in animal viruses.";
RL Biomed. Res. Int. 2013:984028-984028(2013).
RN [3]
RP REVIEW (INTEGRASE).
RX PubMed=28458055; DOI=10.1016/j.sbi.2017.04.005;
RA Engelman A.N., Cherepanov P.;
RT "Retroviral intasomes arising.";
RL Curr. Opin. Struct. Biol. 47:23-29(2017).
CC -!- FUNCTION: [Matrix protein p10]: Matrix protein.
CC {ECO:0000250|UniProtKB:P07572}.
CC -!- FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein.
CC {ECO:0000250|UniProtKB:P07572}.
CC -!- FUNCTION: [Capsid protein p27]: Capsid protein.
CC {ECO:0000250|UniProtKB:P07572}.
CC -!- FUNCTION: [Protease 17 kDa]: 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.
CC {ECO:0000250|UniProtKB:P07572, ECO:0000255|PROSITE-ProRule:PRU00275}.
CC -!- FUNCTION: [Protease 13 kDa]: 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.
CC {ECO:0000250|UniProtKB:P07572, ECO:0000255|PROSITE-ProRule:PRU00275}.
CC -!- FUNCTION: [G-patch peptide]: Enhances the activity of the reverse
CC transcriptase. May be part of the mature RT.
CC {ECO:0000250|UniProtKB:P07572}.
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 perfom 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 perfom 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|PROSITE-
CC ProRule:PRU00405}.
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:28458055}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;
CC Evidence={ECO:0000250|UniProtKB:P07570};
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 -!- SUBUNIT: [Protease 17 kDa]: Homodimer. {ECO:0000250|UniProtKB:P07570}.
CC -!- SUBUNIT: [Reverse transcriptase/ribonuclease H]: Interacts with the G-
CC patch peptide. {ECO:0000250|UniProtKB:P07570}.
CC -!- SUBUNIT: [G-patch peptide]: Interacts with the reverse
CC transcriptase/ribonuclease H. {ECO:0000250|UniProtKB:P07570}.
CC -!- SUBUNIT: [Nucleocapsid protein-dUTPase]: Homotrimer.
CC {ECO:0000250|UniProtKB:P07570}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p10]: Virion
CC {ECO:0000250|UniProtKB:P07572}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27]: Virion
CC {ECO:0000250|UniProtKB:P07572}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion
CC {ECO:0000250|UniProtKB:P07572}.
CC -!- SUBCELLULAR LOCATION: [Protease 13 kDa]: Virion
CC {ECO:0000250|UniProtKB:P07572}.
CC -!- SUBCELLULAR LOCATION: [Protease 17 kDa]: Virion
CC {ECO:0000250|UniProtKB:P07572}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P31623-1; Sequence=Displayed;
CC Name=Gag-Pro polyprotein;
CC IsoId=P31625-1; Sequence=External;
CC Name=Gag polyprotein;
CC IsoId=P31622-1; 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 Gag-p12 contains two L domains: a PTAP/PSAP motif which interacts with
CC the UEV domain of TSG101, and a PPXY motif which binds to the WW
CC domains of the ubiquitin ligase NEDD4. Gag-p27 contains one L domain: a
CC PTAP/PSAP motif which interacts with the UEV domain of TSG101.
CC {ECO:0000250|UniProtKB:P07572}.
CC -!- DOMAIN: [Protease 17 kDa]: The glycine-rich G-patch domain (GPD) is
CC present at the C-terminus of the protease from which it is then
CC detached by the protease itself. {ECO:0000250|UniProtKB:P07572}.
CC -!- PTM: [Protease 17 kDa]: Released by autocatalytic processing. The
CC protease can undergo further autoprocessing to yield 2 shorter but
CC enzymatically active forms of 12 kDa and 13 kDa.
CC {ECO:0000250|UniProtKB:P07572}.
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:P10258}.
CC -!- PTM: [Gag-Pro-Pol polyprotein]: Specific enzymatic cleavages in vivo
CC yield mature proteins. {ECO:0000250|UniProtKB:P07572}.
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 -!- MISCELLANEOUS: [Isoform Gag-Pro-Pol polyprotein]: Produced by -1
CC ribosomal frameshiftings between gag-pro and pro-pol.
CC {ECO:0000305|PubMed:24298557}.
CC -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA89182.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M80216; AAA89182.1; ALT_INIT; Genomic_RNA.
DR PIR; C42740; GNMVJA.
DR RefSeq; NP_041186.1; NC_001494.1.
DR GeneID; 1490020; -.
DR KEGG; vg:1490020; -.
DR Proteomes; UP000007215; 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-KW.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
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 CDD; cd05482; HIV_retropepsin_like; 1.
DR CDD; cd07557; trimeric_dUTPase; 1.
DR Gene3D; 1.10.10.200; -; 1.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.490; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR Gene3D; 2.30.30.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 2.70.40.10; -; 1.
DR Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.270; -; 2.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR003322; B_retro_matrix.
DR InterPro; IPR038124; B_retro_matrix_sf.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR000721; Gag_p24_N.
DR InterPro; IPR017856; Integrase-like_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; IPR034170; Retropepsin-like_cat_dom.
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; IPR010661; RVT_thumb.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00692; dUTPase; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF02337; Gag_p10; 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; PF06817; RVT_thumb; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF46919; SSF46919; 1.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF50122; SSF50122; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF51283; SSF51283; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF57756; SSF57756; 2.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50174; G_PATCH; 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.
DR PROSITE; PS50876; ZF_INTEGRASE; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; DNA integration; DNA recombination; DNA-binding;
KW DNA-directed DNA polymerase; Endonuclease; Hydrolase; Lipoprotein;
KW Magnesium; Metal-binding; Multifunctional enzyme; Myristate; Nuclease;
KW Nucleotidyltransferase; Protease; Repeat; Ribosomal frameshifting;
KW RNA-binding; RNA-directed DNA polymerase; Transferase;
KW Viral genome integration; Viral matrix protein; Viral nucleoprotein;
KW Virion; Virus entry into host cell; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250|UniProtKB:P07572"
FT CHAIN 2..1726
FT /note="Gag-Pro-Pol polyprotein"
FT /id="PRO_0000125490"
FT CHAIN 2..99
FT /note="Matrix protein p10"
FT /id="PRO_0000443130"
FT CHAIN 100..167
FT /note="Phosphorylated protein"
FT /id="PRO_0000443131"
FT CHAIN 168..256
FT /note="p12"
FT /id="PRO_0000443132"
FT CHAIN 257..477
FT /note="Capsid protein p27"
FT /id="PRO_0000443133"
FT CHAIN 478..713
FT /note="Nucleocapsid protein-dUTPase"
FT /id="PRO_0000443134"
FT CHAIN 714..865
FT /note="Protease 17 kDa"
FT /id="PRO_0000443135"
FT CHAIN 714..831
FT /note="Protease 13 kDa"
FT /id="PRO_0000443136"
FT PEPTIDE 832..865
FT /note="G-patch peptide"
FT /id="PRO_0000443137"
FT CHAIN 866..1446
FT /note="Reverse transcriptase/ribonuclease H"
FT /id="PRO_0000434769"
FT CHAIN 1447..1726
FT /note="Integrase"
FT /id="PRO_0000434770"
FT DOMAIN 734..810
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 821..866
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT DOMAIN 911..1099
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 1313..1444
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 1500..1659
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 507..524
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 1446..1487
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT DNA_BIND 1665..1714
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT REGION 103..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 202..205
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000305"
FT MOTIF 208..211
FT /note="PPXY motif"
FT /evidence="ECO:0000305"
FT MOTIF 287..290
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000250|UniProtKB:P10258"
FT COMPBIAS 115..131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 739
FT /note="Protease; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT BINDING 976
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 1051
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 1052
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 1322
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="for RNase H activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 1351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="for RNase H activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 1371
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="for RNase H activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 1436
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="for RNase H activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 1455
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1459
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1483
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1486
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1511
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 1568
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 1604
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000250|UniProtKB:P03354"
FT SITE 99..100
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 256..257
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 477..478
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 713..714
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07572"
FT SITE 831..832
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07572"
FT SITE 865..866
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07572"
FT SITE 1446..1447
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03365"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:P11283"
SQ SEQUENCE 1726 AA; 193421 MW; ACA8108A7C6A1A5B CRC64;
MGHTHSRQLF VHMLSVMLKH RGITVSKTKL INFLSFIEEV CPWFPREGTV NLETWKKVGE
QIRTHYTLHG PEKVPVETLS FWTLIRDCLD FDNDELKRLG NLLKQEEDPL HTPDSVPSYD
PPPPPPPSLK MHPSDNDDSL SSTDEAELDE EAAKYHQEDW GFLAQEKGAL TSKDELVECF
KNLTIALQNA GIQLPSNNNT FPSAPPFPPA YTPTVMAGLD PPPGFPPPSK HMSPLQKALR
QAQRLGEVVS DFSLAFPVFE NNNQRYYESL PFKQLKELKI ACSQYGPTAP FTIAMIESLG
TQALPPNDWK QTARACLSGG DYLLWKSEFF EQCARIADVN RQQGIQTSYE MLIGEGPYQA
TDTQLNFLPG AYAQISNAAR QAWKKLPSSS TKTEDLSKVR QGPDEPYQDF VARLLDTIGK
IMSDEKAGMV LAKQLAFENA NSACQAALRP YRKKGDLSDF IRICADIGPS YMQGIAMAAA
LQGKSIKEVL FQQQARNKKG LQKSGNSGCF VCGQPGHRAA VCPQKHQTSV NTPNLCPRCK
KGKHWARDCR SKTDVQGNPL PPVSGNLGEG PAPGPETMLW GNTAGSKRTI ADLCRATRGS
AGLDLCATSY TVLTPEMGVQ TLATGVFGPL PPGTVGLLLG RSSASLKGIL IHPGVIDSDY
TGEIKILASA PNKIIVINAG QRIAQLLLVP LVIQGKTINR DRQDKGFGSS DAYWVQNVTE
ARPELELRIN ANFFRGVLDT GADISVISDK YWPTTWPKQM AISTLQGIGQ TTNPEQSSSL
LTWKDKDGHT GQFKPYILPY LPVNLWGRDI LSKMGVYLYS PSPTVTDLML DQGLLPNQGL
GKQHQGIILP LDLKPNQDRK GLGCFPLGTS DSPVTHADPI DWKSEEPVWV DQWPLTQEKL
SAAQQLVQEQ LRLGHIEPST SAWNSPIFVI KKKSGKWRLL QDLRKVNETM MHMGALQPGL
PTPSAIPDKS YIIVIDLKDC FYTIPLAPQD CKRFAFSLPS VNFKEPMQRY QWRVLPQGMT
NSPTLCQKFV ATAIAPVRQR FPQLYLVHYM DDILLAHTDE HLLYQAFSIL KQHLSLNGLV
IADEKIQTHF PYNYLGFSLY PRVYNTQLVK LQTDHLKTLN DFQKLLGDIN WIRPYLKLPT
YTLQPLFDIL KGDSDPASPR TLSLEGRTAL QSIEEAIRQQ QITYCDYQRS WGLYILPTPR
APTGVLYQDK PLRWIYLSAT PTKHLLPYYE LVAKIIAKGR HEAIQYFGME PPFICVPYAL
EQQDWLFQFS DNWSIAFANY PGQITHHYPS DKLLQFASSH AFIFPKIVRR QPIPEATLIF
TDGSSNGTAA LIINHQTYYA QTSFSSAQVV ELFAVHQALL TVPTSFNLFT DSSYVVGALQ
MIETVPIIGT TSPEVLNLFT LIQQVLHCRQ HPCFFGHIRA HSTLPGALVQ GNHTADVLTK
QVFFQSAIDA ARKSHDLHHQ NSHSLRLQFK ISREAARQIV KSCSTCPQFF VLPQYGVNPR
GLRPNHLWQT DVTHIPQFGR LKYVHVSIDT FSNFLMASLH TGESTRHCIQ HLLFCFSTSG
IPQTLKTDNG PGYTSRSFQR FCLSFQIHHK TGIPYNPQGQ GIVERAHQRI KHQLLKQKKG
NELYSPSPHN ALNHALYVLN FLTLDTEGNS AAQRFWGERS SCKKPLVRWK DPLTNLWYGP
DPVLIWGRGH VCVFPQDAEA PRWIPERLVR AAEELPDASD ATHDPE
