ID   POL_MMTVC               Reviewed;        1755 AA.
AC   P11283; Q9IZT3;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   27-MAR-2024, entry version 119.
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:0000269|PubMed:8091672};
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:0000305|PubMed:24124581};
DE              EC=3.1.-.- {ECO:0000305|PubMed:24124581};
GN   Name=gag-pro-pol;
OS   Mouse mammary tumor virus (strain C3H) (MMTV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus;
OC   Mouse mammary tumor virus.
OX   NCBI_TaxID=11759;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10982330; DOI=10.1128/jvi.74.19.8876-8883.2000;
RA   Hook L.M., Agafonova Y., Ross S.R., Turner S.J., Golovkina T.V.;
RT   "Genetics of mouse mammary tumor virus-induced mammary tumors: linkage of
RT   tumor induction to the gag gene.";
RL   J. Virol. 74:8876-8883(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 359-591 AND 857-970, AND RIBOSOMAL
RP   FRAMESHIFT.
RX   PubMed=3035577; DOI=10.1073/pnas.84.12.4298;
RA   Jacks T., Townsley K., Varmus H.E., Majors J.;
RT   "Two efficient ribosomal frameshifting events are required for synthesis of
RT   mouse mammary tumor virus gag-related polyproteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:4298-4302(1987).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-58; 65-116; 194-218; 227-241; 251-252; 270-276 AND
RP   362-591, PROTEOLYTIC CLEAVAGE (GAG-PRO-POL POLYPROTEIN), AND MYRISTOYLATION
RP   AT GLY-2.
RX   PubMed=2542570; DOI=10.1128/jvi.63.6.2543-2549.1989;
RA   Hizi A., Henderson L.E., Copeland T.D., Sowder R.C., Krutzsch H.C.,
RA   Oroszlan S.;
RT   "Analysis of gag proteins from mouse mammary tumor virus.";
RL   J. Virol. 63:2543-2549(1989).
RN   [4]
RP   PROTEIN SEQUENCE OF 497-512 AND 744-745, RIBOSOMAL FRAMESHIFT, SUBUNIT
RP   (NUCLEOCAPSID PROTEIN-DUTPASE), FUNCTION (NUCLEOCAPSID PROTEIN-DUTPASE),
RP   AND COFACTOR (NUCLEOCAPSID PROTEIN-DUTPASE).
RX   PubMed=8091672; DOI=10.1006/viro.1994.1547;
RA   Bergman A.C., Bjornberg O., Nord J., Nyman P.O., Rosengren A.M.;
RT   "The protein p30, encoded at the gag-pro junction of mouse mammary tumor
RT   virus, is a dUTPase fused with a nucleocapsid protein.";
RL   Virology 204:420-424(1994).
RN   [5]
RP   FUNCTION (INTEGRASE).
RX   PubMed=24124581; DOI=10.1371/journal.pone.0076638;
RA   Ballandras-Colas A., Naraharisetty H., Li X., Serrao E., Engelman A.;
RT   "Biochemical characterization of novel retroviral integrase proteins.";
RL   PLoS ONE 8:E76638-E76638(2013).
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).
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:0000305|PubMed:8091672}.
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:0000269|PubMed:24124581, ECO:0000303|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:0000269|PubMed:8091672};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-
CC         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:0000305|PubMed:8091672};
CC   -!- SUBUNIT: [Matrix protein p10]: Homodimer; when myristoylated.
CC       {ECO:0000250|UniProtKB:P03365}.
CC   -!- SUBUNIT: [Protease]: Homodimer. {ECO:0000250|UniProtKB:P03365}.
CC   -!- SUBUNIT: [Integrase]: Homooctamer. {ECO:0000303|PubMed:28458055}.
CC   -!- SUBUNIT: [Nucleocapsid protein-dUTPase]: Homotrimer.
CC       {ECO:0000269|PubMed:8091672, ECO:0000303|PubMed:28458055}.
CC   -!- SUBCELLULAR LOCATION: [Matrix protein p10]: Virion
CC       {ECO:0000250|UniProtKB:P10258}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein p27]: Virion
CC       {ECO:0000250|UniProtKB:P10258}.
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=P11283-1; Sequence=Displayed;
CC       Name=Gag-Pro polyprotein;
CC         IsoId=Q9IZT2-1; Sequence=External;
CC       Name=Gag polyprotein;
CC         IsoId=P11284-1; 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: [Protease]: Released by autocatalytic processing.
CC       {ECO:0000250|UniProtKB:P03365}.
CC   -!- PTM: [Gag-Pro-Pol polyprotein]: Specific enzymatic cleavages in vivo
CC       yield mature proteins. {ECO:0000269|PubMed:2542570}.
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:0000269|PubMed:2542570}.
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:3035577, ECO:0000269|PubMed:8091672}.
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DR   EMBL; AF228552; AAF31474.1; -; Genomic_DNA.
DR   EMBL; M16766; AAA66623.1; -; Genomic_RNA.
DR   EMBL; M16766; AAA66625.1; -; Genomic_RNA.
DR   PIR; B29029; B29029.
DR   BMRB; P11283; -.
DR   SMR; P11283; -.
DR   MEROPS; A02.010; -.
DR   iPTMnet; P11283; -.
DR   Proteomes; UP000006540; 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:0000166; F:nucleotide binding; 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   CDD; cd05482; HIV_retropepsin_like; 1.
DR   CDD; cd01645; RT_Rtv; 1.
DR   CDD; cd07557; trimeric_dUTPase; 1.
DR   Gene3D; 1.10.10.200; -; 1.
DR   Gene3D; 1.10.1200.30; -; 1.
DR   Gene3D; 2.70.40.10; -; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR   Gene3D; 1.10.375.10; Human Immunodeficiency Virus Type 1 Capsid Protein; 1.
DR   Gene3D; 2.30.30.10; Integrase, C-terminal domain superfamily, retroviral; 1.
DR   Gene3D; 1.10.150.490; Retroviral GAG p10 protein; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
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; 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   PANTHER; PTHR41694; ENDOGENOUS RETROVIRUS GROUP K MEMBER POL PROTEIN; 1.
DR   PANTHER; PTHR41694:SF3; RNA-DIRECTED DNA POLYMERASE-RELATED; 1.
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   Pfam; PF14787; zf-CCHC_5; 1.
DR   SMART; SM00343; ZnF_C2HC; 2.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF50122; DNA-binding domain of retroviral integrase; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF51283; dUTPase-like; 1.
DR   SUPFAM; SSF46919; N-terminal Zn binding domain of HIV integrase; 1.
DR   SUPFAM; SSF47836; Retroviral matrix proteins; 1.
DR   SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR   SUPFAM; SSF47943; Retrovirus capsid protein, N-terminal core domain; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 2.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 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   Aspartyl protease; Capsid protein; Direct protein sequencing;
KW   DNA integration; DNA recombination; DNA-binding;
KW   DNA-directed DNA polymerase; Endonuclease; Hydrolase; Lipoprotein;
KW   Magnesium; Metal-binding; Multifunctional enzyme; Myristate; Nuclease;
KW   Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
KW   Reference proteome; Repeat; Ribosomal frameshifting; 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; by host"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..1755
FT                   /note="Gag-Pro-Pol polyprotein"
FT                   /id="PRO_0000125493"
FT   CHAIN           2..99
FT                   /note="Matrix protein p10"
FT                   /id="PRO_0000403612"
FT   CHAIN           100..195
FT                   /note="Phosphorylated protein pp21"
FT                   /id="PRO_0000403613"
FT   CHAIN           196..228
FT                   /note="Protein p3"
FT                   /id="PRO_0000403614"
FT   CHAIN           229..254
FT                   /note="Protein p8"
FT                   /id="PRO_0000403615"
FT   CHAIN           255..269
FT                   /note="Protein n"
FT                   /id="PRO_0000403616"
FT   CHAIN           270..496
FT                   /note="Capsid protein p27"
FT                   /id="PRO_0000403617"
FT   CHAIN           497..745
FT                   /note="Nucleocapsid protein-dUTPase"
FT                   /id="PRO_0000403618"
FT   CHAIN           746..860
FT                   /note="Protease"
FT                   /id="PRO_0000403619"
FT   CHAIN           861..1437
FT                   /note="Reverse transcriptase/ribonuclease H"
FT                   /id="PRO_0000403620"
FT   CHAIN           1438..1755
FT                   /note="Integrase"
FT                   /id="PRO_0000403621"
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          154..193
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..605
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1715..1737
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:2542570"
FT   SITE            195..196
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000269|PubMed:2542570"
FT   SITE            228..229
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000269|PubMed:2542570"
FT   SITE            254..255
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000269|PubMed:2542570"
FT   SITE            269..270
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000269|PubMed:2542570"
FT   SITE            496..497
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000269|PubMed:2542570"
FT   SITE            745..746
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000269|PubMed:8091672"
FT   SITE            1437..1438
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000269|PubMed:8091672"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000269|PubMed:2542570"
FT   VARIANT         523
FT                   /note="E -> K"
FT   CONFLICT        857..860
FT                   /note="SQDL -> FTGF (in Ref. 2; AAA66625)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        867
FT                   /note="S -> T (in Ref. 2; AAA66625)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        952
FT                   /note="P -> L (in Ref. 2; AAA66625)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1755 AA;  197329 MW;  0E99A2ADD96823A4 CRC64;
     MGVSGSKGQK LFVSVLQRLL SERGLHVKES SAIEFYQFLI KVSPWFPEEG GLNLQDWKRV
     GREMKKYAAE HGTDSIPKQA YPIWLQLREI LTEQSDLVLL SAEAKSVTEE ELEEGLTGLL
     SASSQEKTYG TRGTAYAEID TEVDKLSEHI YDEPYEEKEK ADKNEEKDHV RKVKKIVQRK
     ENSEHKRKEK DQKAFLATDW NNDDLSPEDW DDLEEQAAHY HDDDELILPV KRKVDKKKPL
     ALRRKPLPPV GFAGAMAEAR EKGDLTFTFP VVFMGESDDD DTPVWEPLPL KTLKELQSAV
     RTMGPSAPYT LQVVDMVASQ WLTPSDWHQT ARATLSPGDY VLWRTEYEEK SKETVQKTAG
     KRKGKVSLDM LLGTGQFLSP SSQIKLSKDV LKDVTTNAVL AWRAIPPPGV KKTVLAGLKQ
     GNEESYETFI SRLEEAVYRM MPRGEGSDIL IKQLAWENAN SLCQDLIRPM RKTGTMQDYI
     RACLDASPAV VQGMAYAAAM RGQKYSTFVK QTYGGGKGGQ GSEGPVCFSC GKTGHIKRDC
     KEEKGSKRAP PGLCPRCKKG YHWKSECKSK FDKDGNPLPP LETNAENSKN LVKGQSPSPT
     QKGDKGKDSG LNPEAPPFTI HDLPRGTPGS AGLDLSSQKD LILSLEDGVS LVPTLVKGTL
     PEGTTGLIIG RSSNYKKGLE VLPGVIDSDF QGEIKVMVKA AKNAVIIHKG ERIAQLLLLP
     YLKLPNPIIK EERGSEGFGS TSHVHWVQEI SDSRPMLHIS LNGRRFLGLL DTGADKTCIA
     GRDWPANWPI HQTESSLQGL GMACGVARSS QPLRWQHEDK SGIIHPFVIP TLPFTLWGRD
     IMKEIKVRLM TDSPDDSQDL MIGAIESNLF ADQISWKSDQ PVWLNQWPLK QEKLQALQQL
     VTEQLQLGHL EESNSPWNTP VFVIKKKSGK WRLLQDLRAV NATMHDMGAL QPGLPSPVAV
     PKGWEIIIID LQDCFFNIKL HPEDCKRFAF SVPSPNFKRP YQRFQWKVLP QGMKNSPTLC
     QKFVDKAILT VRDKYQDSYI VHYMDDILLA HPSRSIVDEI LTSMIQALNK HGLVVSTEKI
     QKYDNLKYLG THIQGDAVSY QKLQIRTDKL RTLNDFQKLL GNINWIRPFL KLTTGELKPL
     FEILNGDSNP ISIRKLTPEA CKALQLVNER LSIARVKRLD LSRPWSLCIL KTEYTPTACL
     WQNGVLEWIH LPHISPKVIT PYDIFCTQLI IKGRHRSKEL FSKDPDYIVV PYTKVQFDLL
     LQEKEDWPIS LLGFLGEVHF HLPKDPLLTF TLQTAIIFPH MTSTTPLEKG IVIFTDGSAN
     GRSVTYIQGR EPIIKENTQN TAQQAEIVAV ITAFEEVSQS FNLYTDSKYV TGLFPEIETA
     TLSPRTKIYT ELRHLQRLIH KRQEKFYIGH IRGHTGLPGP LAQGNAYADS LTRILTALES
     AQESHALHHQ NAAALRFQFH ITREQAREIV KLCPNCPDWG HAPQLGVNPR GLKPRVLWQM
     DVTHVSEFGK LKYVHVTVDT YSHFTFATAR TGEATKDVLQ HLAQSFAYMG FPQKIKTDNA
     PAYVSRSIQE FLARWKISHV TGIPYNPQGQ AIVERTHQNI KAQLNKLQKA GKYYTPHHLL
     AHALFVLNHV NMDNQGHTAA ERHWGPISAD PKPMVMWKDL LAGSWKGPDV LITAGRGYAC
     VFPQDAETPI WVPDRFIRPF TERKEATPTP GTAEKTPPRD EKDQQKSPED ESSPHQREDG
     LATSAGVNLR SGGGS
//