POL_MMTVB
ID POL_MMTVB Reviewed; 1755 AA.
AC P03365;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Gag-Pro-Pol polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p10;
DE Contains:
DE RecName: Full=Phosphorylated protein pp21;
DE Contains:
DE RecName: Full=Protein p3;
DE Contains:
DE RecName: Full=Protein p8;
DE Contains:
DE RecName: Full=Protein n;
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;
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275, ECO:0000269|PubMed:1331110};
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=gag-pro-pol;
OS Mouse mammary tumor virus (strain BR6) (MMTV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11758;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RIBOSOMAL FRAMESHIFT.
RX PubMed=3027377; DOI=10.1128/jvi.61.2.480-490.1987;
RA Moore R., Dixon M., Smith R., Peters G., Dickson C.;
RT "Complete nucleotide sequence of a milk-transmitted mouse mammary tumor
RT virus: two frameshift suppression events are required for translation of
RT gag and pol.";
RL J. Virol. 61:480-490(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1434-1613.
RX PubMed=6197754; DOI=10.1126/science.6197754;
RA Chiu I.-M., Callahan R., Tronick S.R., Schlom J., Aaronson S.A.;
RT "Major pol gene progenitors in the evolution of oncoviruses.";
RL Science 223:364-370(1984).
RN [3]
RP SUBCELLULAR LOCATION (MATRIX PROTEIN P10), AND SUBCELLULAR LOCATION (CAPSID
RP PROTEIN P27).
RX PubMed=205999; DOI=10.1016/0042-6822(78)90420-8;
RA Cardiff R.D., Puentes M.J., Young L.J., Smith G.H., Teramoto Y.A.,
RA Altrock B.W., Pratt T.S.;
RT "Serological and biochemical characterization of the mouse mammary tumor
RT virus with localization of p10.";
RL Virology 85:157-167(1978).
RN [4]
RP PROTEOLYTIC CLEAVAGE (GAG-PRO-POL POLYPROTEIN), CHARACTERIZATION
RP (PROTEASE), SUBUNIT (PROTEASE), CATALYTIC ACTIVITY (PROTEASE), ACTIVITY
RP REGULATION (PROTEASE), AND BIOPHYSICOCHEMICAL PROPERTIES (PROTEASE).
RC STRAIN=p202;
RX PubMed=1331110; DOI=10.1016/s0021-9258(18)35956-8;
RA Menendez-Arias L., Young M., Oroszlan S.;
RT "Purification and characterization of the mouse mammary tumor virus
RT protease expressed in Escherichia coli.";
RL J. Biol. Chem. 267:24134-24139(1992).
RN [5]
RP SUBUNIT (MATRIX PROTEIN P10).
RX PubMed=26728401; DOI=10.1186/s12977-015-0235-8;
RA Dolezal M., Zabransky A., Dostal J., Vanek O., Brynda J., Lepsik M.,
RA Hadravova R., Pichova I.;
RT "Myristoylation drives dimerization of matrix protein from mouse mammary
RT tumor virus.";
RL Retrovirology 13:2-2(2016).
RN [6]
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).
RN [7] {ECO:0007744|PDB:3JCA, ECO:0007744|PDB:5CZ1, ECO:0007744|PDB:5CZ2, ECO:0007744|PDB:5D7U}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1645-1702 IN COMPLEX WITH
RP MAGNESIUM AND ZINC, AND SUBUNIT (INTEGRASE).
RX PubMed=26887496; DOI=10.1038/nature16955;
RA Ballandras-Colas A., Brown M., Cook N.J., Dewdney T.G., Demeler B.,
RA Cherepanov P., Lyumkis D., Engelman A.N.;
RT "Cryo-EM reveals a novel octameric integrase structure for betaretroviral
RT intasome function.";
RL Nature 530:358-361(2016).
CC -!- FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.
CC -!- FUNCTION: Nucleocapsid protein p14: Binds strongly to viral nucleic
CC acids and promote their aggregation. Also destabilizes the nucleic
CC acids duplexes via highly structured zinc-binding motifs.
CC {ECO:0000305}.
CC -!- FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}.
CC -!- FUNCTION: NC-dUTPase has dUTPase activity, thereby preventing
CC incorporation of uracil into DNA. {ECO:0000250|UniProtKB:P11283}.
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 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:0000250|UniProtKB:P11283}.
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:P11283};
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 Note=Magnesium ions are required for NC-dUTPase activity.
CC {ECO:0000250|UniProtKB:P11283};
CC -!- ACTIVITY REGULATION: [Protease]: Inhibited by pepstatin A.
CC {ECO:0000269|PubMed:1331110}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4-6. {ECO:0000269|PubMed:1331110};
CC -!- SUBUNIT: [Matrix protein p10]: Homodimer; when myristoylated.
CC {ECO:0000269|PubMed:26728401}.
CC -!- SUBUNIT: [Protease]: Homodimer. {ECO:0000269|PubMed:1331110}.
CC -!- SUBUNIT: [Integrase]: Homooctamer. {ECO:0000269|PubMed:26887496,
CC ECO:0000303|PubMed:28458055}.
CC -!- SUBUNIT: [Nucleocapsid protein-dUTPase]: Homotrimer.
CC {ECO:0000250|UniProtKB:P11283, ECO:0000303|PubMed:28458055}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p10]: Virion
CC {ECO:0000269|PubMed:6197754}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27]: Virion
CC {ECO:0000269|PubMed:6197754}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion
CC {ECO:0000250|UniProtKB:P10258}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P03365-1; Sequence=Displayed;
CC Name=Gag-Pro polyprotein;
CC IsoId=P10271-1; Sequence=External;
CC Name=Gag polyprotein;
CC IsoId=P10258-1; Sequence=External;
CC -!- DOMAIN: [Gag-Pro-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 Gag-p27 contains one L domain: a PTAP/PSAP motif, which interacts with
CC the UEV domain of TSG101. {ECO:0000305}.
CC -!- PTM: [Gag-Pro-Pol polyprotein]: Specific enzymatic cleavages in vivo
CC yield mature proteins. {ECO:0000269|PubMed:1331110}.
CC -!- PTM: [Protease]: Released by autocatalytic processing.
CC {ECO:0000269|PubMed:1331110}.
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:P11283}.
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:0000269|PubMed:3027377}.
CC -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC {ECO:0000305}.
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DR EMBL; M15122; AAA46542.1; -; Genomic_RNA.
DR EMBL; K01707; AAA46540.1; -; Genomic_RNA.
DR PIR; A05073; A05073.
DR PIR; C26795; GNMVMM.
DR PDB; 3JCA; EM; 4.80 A; A/B/E/F=1437-1701, C/D/G/H=1653-1701.
DR PDB; 5CZ1; X-ray; 1.70 A; A/B/C/D=1487-1648.
DR PDB; 5CZ2; X-ray; 2.72 A; A/B/C/D/E/F/G/H/I/J/K/L=1437-1646.
DR PDB; 5D7U; X-ray; 1.50 A; A/B=1648-1702.
DR PDBsum; 3JCA; -.
DR PDBsum; 5CZ1; -.
DR PDBsum; 5CZ2; -.
DR PDBsum; 5D7U; -.
DR SMR; P03365; -.
DR MEROPS; A02.010; -.
DR PRIDE; P03365; -.
DR Proteomes; UP000228400; 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; 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; 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; 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; 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 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Capsid protein; DNA integration;
KW DNA recombination; DNA-binding; DNA-directed DNA polymerase; Endonuclease;
KW Hydrolase; Lipoprotein; Magnesium; Metal-binding; Multifunctional enzyme;
KW Myristate; Nuclease; Nucleotidyltransferase; Protease; Reference proteome;
KW Repeat; Ribosomal frameshifting; 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; by host"
FT /evidence="ECO:0000255"
FT CHAIN 2..1755
FT /note="Gag-Pro-Pol polyprotein"
FT /id="PRO_0000125492"
FT CHAIN 2..99
FT /note="Matrix protein p10"
FT /id="PRO_0000442470"
FT CHAIN 100..195
FT /note="Phosphorylated protein pp21"
FT /id="PRO_0000442471"
FT CHAIN 196..228
FT /note="Protein p3"
FT /id="PRO_0000442472"
FT CHAIN 229..254
FT /note="Protein p8"
FT /id="PRO_0000442473"
FT CHAIN 255..269
FT /note="Protein n"
FT /id="PRO_0000442474"
FT CHAIN 270..496
FT /note="Capsid protein p27"
FT /id="PRO_0000442475"
FT CHAIN 497..745
FT /note="Nucleocapsid protein-dUTPase"
FT /id="PRO_0000442476"
FT CHAIN 746..860
FT /note="Protease"
FT /id="PRO_0000442477"
FT CHAIN 861..1436
FT /note="Reverse transcriptase/ribonuclease H"
FT /id="PRO_0000434771"
FT CHAIN 1437..1755
FT /note="Integrase"
FT /id="PRO_0000434772"
FT DOMAIN 766..841
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 905..1093
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 1307..1437
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 1490..1647
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 525..542
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 552..569
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 1436..1477
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT DNA_BIND 1653..1702
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT REGION 151..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..1755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 305..308
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 581..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1715..1736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 771
FT /note="Protease; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT BINDING 970
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 1045
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 1046
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 1316
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 1346
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 1366
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 1429
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 1445
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1473
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1476
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1501
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 1558
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 1594
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:0000269|PubMed:1331110"
FT SITE 195..196
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:1331110"
FT SITE 228..229
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:1331110"
FT SITE 254..255
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:1331110"
FT SITE 269..270
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:1331110"
FT SITE 496..497
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:1331110"
FT SITE 745..746
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:1331110"
FT SITE 1436..1437
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000305|PubMed:26887496"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:P11283"
FT CONFLICT 1481
FT /note="H -> S (in Ref. 2; AAA46540)"
FT /evidence="ECO:0000305"
FT HELIX 1438..1448
FT /evidence="ECO:0007829|PDB:5CZ2"
FT HELIX 1452..1459
FT /evidence="ECO:0007829|PDB:5CZ2"
FT HELIX 1463..1472
FT /evidence="ECO:0007829|PDB:5CZ2"
FT STRAND 1495..1504
FT /evidence="ECO:0007829|PDB:5CZ1"
FT HELIX 1506..1511
FT /evidence="ECO:0007829|PDB:5CZ1"
FT STRAND 1513..1519
FT /evidence="ECO:0007829|PDB:5CZ1"
FT TURN 1520..1522
FT /evidence="ECO:0007829|PDB:5CZ1"
FT STRAND 1525..1531
FT /evidence="ECO:0007829|PDB:5CZ1"
FT HELIX 1535..1549
FT /evidence="ECO:0007829|PDB:5CZ1"
FT STRAND 1552..1556
FT /evidence="ECO:0007829|PDB:5CZ1"
FT HELIX 1561..1564
FT /evidence="ECO:0007829|PDB:5CZ1"
FT HELIX 1566..1573
FT /evidence="ECO:0007829|PDB:5CZ1"
FT TURN 1574..1576
FT /evidence="ECO:0007829|PDB:5CZ1"
FT STRAND 1578..1580
FT /evidence="ECO:0007829|PDB:5CZ1"
FT HELIX 1587..1589
FT /evidence="ECO:0007829|PDB:5CZ1"
FT HELIX 1591..1605
FT /evidence="ECO:0007829|PDB:5CZ1"
FT TURN 1606..1609
FT /evidence="ECO:0007829|PDB:5CZ1"
FT HELIX 1610..1612
FT /evidence="ECO:0007829|PDB:5CZ1"
FT HELIX 1616..1629
FT /evidence="ECO:0007829|PDB:5CZ1"
FT HELIX 1639..1644
FT /evidence="ECO:0007829|PDB:5CZ1"
FT STRAND 1654..1658
FT /evidence="ECO:0007829|PDB:5D7U"
FT TURN 1660..1662
FT /evidence="ECO:0007829|PDB:5D7U"
FT STRAND 1665..1675
FT /evidence="ECO:0007829|PDB:5D7U"
FT STRAND 1678..1681
FT /evidence="ECO:0007829|PDB:5D7U"
FT STRAND 1690..1693
FT /evidence="ECO:0007829|PDB:5D7U"
FT HELIX 1694..1696
FT /evidence="ECO:0007829|PDB:5D7U"
FT STRAND 1697..1700
FT /evidence="ECO:0007829|PDB:5D7U"
SQ SEQUENCE 1755 AA; 197115 MW; 524B997C251D50F1 CRC64;
MGVSGSKGQK LFVSVLQRLL SERGLHVKES SAIEFYQFLI KVSPWFPEEG GLNLQDWKRV
GREMKRYAAE HGTDSIPKQA YPIWLQLREI LTEQSDLVLL SAEAKSVTEE ELEEGLTGLL
STSSQEKTYG TRGTAYAEID TEVDKLSEHI YDEPYEEKEK ADKNEEKDHV RKIKKVVQRK
ENSEGKRKEK DSKAFLATDW NDDDLSPEDW DDLEEQAAHY HDDDELILPV KRKVVKKKPQ
ALRRKPLPPV GFAGAMAEAR EKGDLTFTFP VVFMGESDED DTPVWEPLPL KTLKELQSAV
RTMGPSAPYT LQVVDMVASQ WLTPSDWHQT ARATLSPGDY VLWRTEYEEK SKEMVQKAAG
KRKGKVSLDM LLGTGQFLSP SSQIKLSKDV LKDVTTNAVL AWRAIPPPGV KKTVLAGLKQ
GNEESYETFI SRLEEAVYRM MPRGEGSDIL IKQLAWENAN SLCQDLIRPI RKTGTIQDYI
RACLDASPAV VQGMAYAAAM RGQKYSTFVK QTYGGGKGGQ GAEGPVCFSC GKTGHIRKDC
KDEKGSKRAP PGLCPRCKKG YHWKSECKSK FDKDGNPLPP LETNAENSKN LVKGQSPSPA
QKGDGVKGSG LNPEAPPFTI HDLPRGTPGS AGLDLSSQKD LILSLEDGVS LVPTLVKGTL
PEGTTGLIIG RSSNYKKGLE VLPGVIDSDF QGEIKVMVKA AKNAVIIHKG ERIAQLLLLP
YLKLPNPVIK EERGSEGFGS TSHVHWVQEI SDSRPMLHIY LNGRRFLGLL DTGADKTCIA
GRDWPANWPI HQTESSLQGL GMACGVARSS QPLRWQHEDK SGIIHPFVIP TLPFTLWGRD
IMKDIKVRLM TDSPDDSQDL MIGAIESNLF ADQISWKSDQ PVWLNQWPLK QEKLQALQQL
VTEQLQLGHL EESNSPWNTP VFVIKKKSGK WRLLQDLRAV NATMHDMGAL QPGLPSPVAV
PKGWEIIIID LQDCFFNIKL HPEDCKRFAF SVPSPNFKRP YQRFQWKVLP QGMKNSPTLC
QKFVDKAILT VRDKYQDSYI VHYMDDILLA HPSRSIVDEI LTSMIQALNK HGLVVSTEKI
QKYDNLKYLG THIQGDSVSY QKLQIRTDKL RTLNDFQKLL GNINWIRPFL KLTTGELKPL
FEILNGDSNP ISTRKLTPEA CKALQLMNER LSTARVKRLD LSQPWSLCIL KTEYTPTACL
WQDGVVEWIH LPHISPKVIT PYDIFCTQLI IKGRHRSKEL FSKDPDYIVV PYTKVQFDLL
LQEKEDWPIS LLGFLGEVHF HLPKDPLLTF TLQTAIIFPH MTSTTPLEKG IVIFTDGSAN
GRSVTYIQGR EPIIKENTQN TAQQAEIVAV ITAFEEVSQP FNLYTDSKYV TGLFPEIETA
TLSPRTKIYT ELKHLQRLIH KRQEKFYIGH IRGHTGLPGP LAQGNAYADS LTRILTALES
AQESHALHHQ NAAALRFQFH ITREQAREIV KLCPNCPDWG HAPQLGVNPR GLKPRVLWQM
DVTHVSEFGK LKYVHVTVDT YSHFTFATAR TGEATKDVLQ HLAQSFAYMG IPQKIKTDNA
PAYVSRSIQE FLARWKISHV TGIPYNPQGQ AIVERTHQNI KAQLNKLQKA GKYYTPHHLL
AHALFVLNHV NMDNQGHTAA ERHWGPISAD PKPMVMWKDL LTGSWKGPDV LITAGRGYAC
VFPQDAETPI WVPDRFIRPF TERKEATPTP GTAEKTPPRD EKDQQESPKN ESSPHQREDG
LATSAGVDLR SGGGP
