POL_MPMV
ID POL_MPMV Reviewed; 1771 AA.
AC P07572; O56224;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Gag-Pro-Pol polyprotein;
DE AltName: Full=Pr180;
DE Contains:
DE RecName: Full=Matrix protein p10;
DE Contains:
DE RecName: Full=Phosphorylated protein pp24;
DE Contains:
DE RecName: Full=Phosphorylated protein pp18;
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:P07570};
DE Contains:
DE RecName: Full=Protease 17 kDa {ECO:0000303|PubMed:16257973};
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275, ECO:0000269|PubMed:9636364};
DE Contains:
DE RecName: Full=Protease 13 kDa {ECO:0000303|PubMed:16257973};
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275, ECO:0000269|PubMed:9636364};
DE Contains:
DE RecName: Full=G-patch peptide {ECO:0000303|PubMed:22171253};
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 Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11855;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RIBOSOMAL FRAMESHIFT.
RC STRAIN=Clone 6A;
RX PubMed=2421920; DOI=10.1016/0092-8674(86)90323-5;
RA Sonigo P., Barker C., Hunter E., Wain-Hobson S.;
RT "Nucleotide sequence of Mason-Pfizer monkey virus: an immunosuppressive D-
RT type retrovirus.";
RL Cell 45:375-385(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Chappey C.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEOLYTIC CLEAVAGE (PROTEASE 17 KDA), CATALYTIC ACTIVITY (PROTEASE 17
RP KDA), FUNCTION (PROTEASE 17 KDA), PROTEOLYTIC CLEAVAGE (GAG-PRO
RP POLYPROTEIN), SUBCELLULAR LOCATION (PROTEASE 17 KDA), SUBCELLULAR LOCATION
RP (PROTEASE 13 KDA), CATALYTIC ACTIVITY (PROTEASE 13 KDA), AND FUNCTION
RP (PROTEASE 13 KDA).
RX PubMed=9636364; DOI=10.1006/viro.1998.9173;
RA Zabransky A., Andreansky M., Hruskova-Heidingsfeldova O., Havlicek V.,
RA Hunter E., Ruml T., Pichova I.;
RT "Three active forms of aspartic proteinase from Mason-Pfizer monkey
RT virus.";
RL Virology 245:250-256(1998).
RN [4]
RP DOMAIN (GAG-PRO-POL POLYPROTEIN), AND MUTAGENESIS OF 203-PRO--TYR-205 AND
RP 210-PRO--PRO-211.
RX PubMed=12915562; DOI=10.1128/jvi.77.17.9474-9485.2003;
RA Gottwein E., Bodem J., Mueller B., Schmechel A., Zentgraf H.,
RA Kraeusslich H.G.;
RT "The Mason-Pfizer monkey virus PPPY and PSAP motifs both contribute to
RT virus release.";
RL J. Virol. 77:9474-9485(2003).
RN [5]
RP PROTEOLYTIC CLEAVAGE (PROTEASE 17 KDA), DOMAIN (PROTEASE 17 KDA), AND
RP MUTAGENESIS OF ASN-868; ALA-873; GLN-874 AND TYR-880.
RX PubMed=16257973; DOI=10.1074/jbc.m508031200;
RA Bauerova-Zabranska H., Stokrova J., Strisovsky K., Hunter E., Ruml T.,
RA Pichova I.;
RT "The RNA binding G-patch domain in retroviral protease is important for
RT infectivity and D-type morphogenesis of Mason-Pfizer monkey virus.";
RL J. Biol. Chem. 280:42106-42112(2005).
RN [6]
RP DOMAIN (PROTEASE 17 KDA), CATALYTIC ACTIVITY (REVERSE
RP TRANSCRIPTASE/RIBONUCLEASE H), MUTAGENESIS OF GLY-879; TYR-880; GLY-883;
RP GLY-885; LEU-886; GLY-887; GLY-892 AND GLY-907, FUNCTION (G-PATCH PEPTIDE),
RP INTERACTION WITH THE REVERSE TRANSCRIPTASE/RIBONUCLEASE H (G-PATCH
RP PEPTIDE), AND INTERACTION WITH THE G-PATCH PEPTIDE (REVERSE
RP TRANSCRIPTASE/RIBONUCLEASE H).
RX PubMed=22171253; DOI=10.1128/jvi.06638-11;
RA Krizova I., Hadravova R., Stokrova J., Guenterova J., Dolezal M., Ruml T.,
RA Rumlova M., Pichova I.;
RT "The G-patch domain of Mason-Pfizer monkey virus is a part of reverse
RT transcriptase.";
RL J. Virol. 86:1988-1998(2012).
RN [7]
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 [8]
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: Nucleocapsid protein.
CC {ECO:0000305}.
CC -!- FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}.
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. {ECO:0000255|PROSITE-
CC ProRule:PRU00275, ECO:0000269|PubMed:9636364}.
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. {ECO:0000255|PROSITE-
CC ProRule:PRU00275, ECO:0000269|PubMed:9636364}.
CC -!- FUNCTION: [G-patch peptide]: Enhances the activity of the reverse
CC transcriptase. May be part of the mature RT.
CC {ECO:0000269|PubMed:22171253}.
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, ECO:0000269|PubMed:22171253};
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, ECO:0000269|PubMed:22171253};
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 (By similarity).
CC {ECO:0000250|UniProtKB:P07570}.
CC -!- SUBUNIT: [Reverse transcriptase/ribonuclease H]: Interacts with the G-
CC patch peptide (PubMed:22171253). {ECO:0000269|PubMed:22171253}.
CC -!- SUBUNIT: [G-patch peptide]: Interacts with the reverse
CC transcriptase/ribonuclease H (PubMed:22171253).
CC {ECO:0000269|PubMed:22171253}.
CC -!- SUBUNIT: [Nucleocapsid protein-dUTPase]: Homotrimer (By similarity).
CC {ECO:0000250|UniProtKB:P07570}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protease 13 kDa]: Virion
CC {ECO:0000269|PubMed:9636364}.
CC -!- SUBCELLULAR LOCATION: [Protease 17 kDa]: Virion
CC {ECO:0000269|PubMed:9636364}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P07572-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P07567-1; Sequence=External;
CC Name=Gag-Pro polyprotein;
CC IsoId=P07570-1; 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 Phosphorylated protein pp24 and phosphorylated protein pp18 contains
CC two L domains: a PTAP/PSAP motif which interacts with the UEV domain of
CC TSG101, and a PPXY motif which binds to the WW domains of the ubiquitin
CC ligase NEDD4. Both motifs contribute to viral release. The PSAP motif
CC acts as an additional L domain and promotes the efficient release of
CC the virions but requires an intact PPPY motif to perform its function.
CC {ECO:0000269|PubMed:12915562}.
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:0000269|PubMed:16257973,
CC ECO:0000269|PubMed:22171253}.
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:0000269|PubMed:16257973, ECO:0000269|PubMed:9636364}.
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:0000269|PubMed:9636364}.
CC -!- MISCELLANEOUS: The reverse transcriptase is an error-prone enzyme that
CC lacks a proof-reading function. High mutations rate is a direct
CC consequence of this characteristic. RT also displays frequent template
CC swiching leading to high recombination rate. Recombination mostly
CC occurs between homologous regions of the two copackaged RNA genomes. If
CC these two RNA molecules derive from different viral strains, reverse
CC transcription will give rise to highly recombinated proviral DNAs.
CC {ECO:0000255|PROSITE-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:2421920, ECO:0000305|PubMed:24298557}.
CC -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA47711.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M12349; AAA47711.1; ALT_SEQ; Genomic_RNA.
DR EMBL; AF033815; AAC82576.1; -; Genomic_RNA.
DR PIR; C25839; GNLJMP.
DR RefSeq; NP_056891.1; NC_001550.1. [P07572-1]
DR PDB; 6HWI; EM; 7.20 A; A/B/C=317-516.
DR PDB; 6S1U; X-ray; 1.90 A; A/B=760-873.
DR PDB; 6S1V; X-ray; 1.64 A; A/B=760-873.
DR PDB; 6S1W; X-ray; 1.98 A; A/B=760-873.
DR PDB; 7BGT; X-ray; 1.93 A; A/B/C/D=760-873.
DR PDB; 7BGU; X-ray; 2.43 A; A/B/C/D=760-873.
DR PDBsum; 6HWI; -.
DR PDBsum; 6S1U; -.
DR PDBsum; 6S1V; -.
DR PDBsum; 6S1W; -.
DR PDBsum; 7BGT; -.
DR PDBsum; 7BGU; -.
DR SMR; P07572; -.
DR MEROPS; A02.009; -.
DR GeneID; 2746973; -.
DR KEGG; vg:2746973; -.
DR Proteomes; UP000008870; Genome.
DR Proteomes; UP000105838; 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 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; 1.
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; 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 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Coiled coil; 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; Repeat;
KW 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:0000305"
FT CHAIN 2..1771
FT /note="Gag-Pro-Pol polyprotein"
FT /id="PRO_0000125494"
FT CHAIN 2..100
FT /note="Matrix protein p10"
FT /id="PRO_0000443138"
FT CHAIN 101..216
FT /note="Phosphorylated protein pp24"
FT /id="PRO_0000443139"
FT PROPEP 101..161
FT /evidence="ECO:0000305"
FT /id="PRO_0000443140"
FT CHAIN 162..216
FT /note="Phosphorylated protein pp18"
FT /id="PRO_0000443141"
FT CHAIN 217..299
FT /note="p12"
FT /id="PRO_0000443142"
FT CHAIN 300..525
FT /note="Capsid protein p27"
FT /id="PRO_0000443143"
FT CHAIN 526..759
FT /note="Nucleocapsid protein-dUTPase"
FT /id="PRO_0000443144"
FT CHAIN 760..911
FT /note="Protease 17 kDa"
FT /id="PRO_0000443145"
FT CHAIN 760..873
FT /note="Protease 13 kDa"
FT /id="PRO_0000443146"
FT PEPTIDE 874..911
FT /note="G-patch peptide"
FT /id="PRO_0000443147"
FT CHAIN 912..1496
FT /note="Reverse transcriptase/ribonuclease H"
FT /id="PRO_0000434773"
FT CHAIN 1497..1771
FT /note="Integrase"
FT /id="PRO_0000434774"
FT DOMAIN 780..856
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 867..913
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092,
FT ECO:0000269|PubMed:22171253"
FT DOMAIN 959..1147
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 1361..1492
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 1550..1719
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 547..564
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 576..593
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 1496..1537
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT DNA_BIND 1716..1765
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT REGION 113..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 216..257
FT /evidence="ECO:0000255"
FT MOTIF 202..205
FT /note="PPXY motif"
FT /evidence="ECO:0000269|PubMed:12915562"
FT MOTIF 210..213
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000269|PubMed:12915562"
FT MOTIF 335..338
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000250|UniProtKB:P03365"
FT COMPBIAS 113..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 785
FT /note="Protease; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT BINDING 1024
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 1099
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 1100
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 1370
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 1399
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 1420
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 1484
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 1505
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1509
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1533
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1536
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1561
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 1618
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 1654
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 100..101
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 161..162
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 216..217
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 299..300
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 525..526
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 759..760
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:9636364"
FT SITE 873..874
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:16257973"
FT SITE 911..912
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:9636364"
FT SITE 1496..1497
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"
FT MUTAGEN 203..205
FT /note="PPY->GAA: 80% loss of virus release."
FT /evidence="ECO:0000269|PubMed:12915562"
FT MUTAGEN 210..211
FT /note="PS->AG: 30% loss of virus release."
FT /evidence="ECO:0000269|PubMed:12915562"
FT MUTAGEN 868
FT /note="N->I: Accelerated processing of the protease C-
FT terminus."
FT /evidence="ECO:0000269|PubMed:16257973"
FT MUTAGEN 873
FT /note="A->R: 30% loss of infectivity."
FT /evidence="ECO:0000269|PubMed:16257973"
FT MUTAGEN 874
FT /note="Q->I: Accelerated processing of the protease C-
FT terminus. 50% loss of RT activity."
FT /evidence="ECO:0000269|PubMed:16257973"
FT MUTAGEN 879
FT /note="G->A: 85% loss of infectivity and 65% loss of RT
FT activity."
FT /evidence="ECO:0000269|PubMed:22171253"
FT MUTAGEN 880
FT /note="Y->A: 90% loss of infectivity and 65% loss of RT
FT activity."
FT /evidence="ECO:0000269|PubMed:22171253"
FT MUTAGEN 880
FT /note="Y->S: Defective in nucleic acid binding. 80% loss of
FT infectivity. 50% loss of RT activity."
FT /evidence="ECO:0000269|PubMed:16257973"
FT MUTAGEN 883
FT /note="G->A: 90% loss of infectivity and 55% loss of RT
FT activity."
FT /evidence="ECO:0000269|PubMed:22171253"
FT MUTAGEN 885
FT /note="G->A: 70% loss of infectivity and 60% loss of RT
FT activity."
FT /evidence="ECO:0000269|PubMed:22171253"
FT MUTAGEN 886
FT /note="L->A: 85% loss of infectivity and 60% loss of RT
FT activity."
FT /evidence="ECO:0000269|PubMed:22171253"
FT MUTAGEN 887
FT /note="G->A: 95% loss of infectivity and 95% loss of RT
FT activity."
FT /evidence="ECO:0000269|PubMed:22171253"
FT MUTAGEN 892
FT /note="G->A: 85% loss of infectivity and 60% loss of RT
FT activity."
FT /evidence="ECO:0000269|PubMed:22171253"
FT MUTAGEN 907
FT /note="G->A: 60% loss of infectivity and 35% loss of RT
FT activity."
FT /evidence="ECO:0000269|PubMed:22171253"
FT STRAND 761..763
FT /evidence="ECO:0007829|PDB:6S1V"
FT STRAND 770..775
FT /evidence="ECO:0007829|PDB:6S1V"
FT STRAND 778..784
FT /evidence="ECO:0007829|PDB:6S1V"
FT STRAND 788..790
FT /evidence="ECO:0007829|PDB:6S1V"
FT STRAND 792..794
FT /evidence="ECO:0007829|PDB:6S1V"
FT HELIX 795..797
FT /evidence="ECO:0007829|PDB:6S1V"
FT STRAND 804..806
FT /evidence="ECO:0007829|PDB:7BGT"
FT HELIX 812..814
FT /evidence="ECO:0007829|PDB:6S1W"
FT STRAND 821..825
FT /evidence="ECO:0007829|PDB:6S1V"
FT STRAND 827..830
FT /evidence="ECO:0007829|PDB:6S1V"
FT STRAND 836..839
FT /evidence="ECO:0007829|PDB:6S1V"
FT STRAND 842..846
FT /evidence="ECO:0007829|PDB:6S1V"
FT STRAND 848..852
FT /evidence="ECO:0007829|PDB:6S1U"
FT HELIX 854..859
FT /evidence="ECO:0007829|PDB:6S1V"
FT STRAND 863..865
FT /evidence="ECO:0007829|PDB:6S1V"
SQ SEQUENCE 1771 AA; 198014 MW; BE8BEAB195B4E833 CRC64;
MGQELSQHER YVEQLKQALK TRGVKVKYAD LLKFFDFVKD TCPWFPQEGT IDIKRWRRVG
DCFQDYYNTF GPEKVPVTAF SYWNLIKELI DKKEVNPQVM AAVAQTEEIL KSNSQTDLTK
TSQNPDLDLI SLDSDDEGAK SSSLQDKGLS STKKPKRFPV LLTAQTSKDP EDPNPSEVDW
DGLEDEAAKY HNPDWPPFLT RPPPYNKATP SAPTVMAVVN PKEELKEKIA QLEEQIKLEE
LHQALISKLQ KLKTGNETVT HPDTAGGLSR TPHWPGQHIP KGKCCASREK EEQIPKDIFP
VTETVDGQGQ AWRHHNGFDF AVIKELKTAA SQYGATAPYT LAIVESVADN WLTPTDWNTL
VRAVLSGGDH LLWKSEFFEN CRDTAKRNQQ AGNGWDFDML TGSGNYSSTD AQMQYDPGLF
AQIQAAATKA WRKLPVKGDP GASLTGVKQG PDEPFADFVH RLITTAGRIF GSAEAGVDYV
KQLAYENANP ACQAAIRPYR KKTDLTGYIR LCSDIGPSYQ QGLAMAAAFS GQTVKDFLNN
KNKEKGGCCF KCGKKGHFAK NCHEHAHNNA EPKVPGLCPR CKRGKHWANE CKSKTDNQGN
PIPPHQGNRV EGPAPGPETS LWGSQLCSSQ QKQPISKLTR ATPGSAGLDL CSTSHTVLTP
EMGPQALSTG IYGPLPPNTF GLILGRSSIT MKGLQVYPGV IDNDYTGEIK IMAKAVNNIV
TVSQGNRIAQ LILLPLIETD NKVQQPYRGQ GSFGSSDIYW VQPITCQKPS LTLWLDDKMF
TGLIDTGADV TIIKLEDWPP NWPITDTLTN LRGIGQSNNP KQSSKYLTWR DKENNSGLIK
PFVIPNLPVN LWGRDLLSQM KIMMCSPNDI VTAQMLAQGY SPGKGLGKKE NGILHPIPNQ
GQSNKKGFGN FLTAAIDILA PQQCAEPITW KSDEPVWVDQ WPLTNDKLAA AQQLVQEQLE
AGHITESSSP WNTPIFVIKK KSGKWRLLQD LRAVNATMVL MGALQPGLPS PVAIPQGYLK
IIIDLKDCFF SIPLHPSDQK RFAFSLPSTN FKEPMQRFQW KVLPQGMANS PTLCQKYVAT
AIHKVRHAWK QMYIIHYMDD ILIAGKDGQQ VLQCFDQLKQ ELTAAGLHIA PEKVQLQDPY
TYLGFELNGP KITNQKAVIR KDKLQTLNDF QKLLGDINWL RPYLKLTTGD LKPLFDTLKG
DSDPNSHRSL SKEALASLEK VETAIAEQFV THINYSLPLI FLIFNTALTP TGLFWQDNPI
MWIHLPASPK KVLLPYYDAI ADLIILGRDH SKKYFGIEPS TIIQPYSKSQ IDWLMQNTEM
WPIACASFVG ILDNHYPPNK LIQFCKLHTF VFPQIISKTP LNNALLVFTD GSSTGMAAYT
LTDTTIKFQT NLNSAQLVEL QALIAVLSAF PNQPLNIYTD SAYLAHSIPL LETVAQIKHI
SETAKLFLQC QQLIYNRSIP FYIGHVRAHS GLPGPIAQGN QRADLATKIV ASNINTNLES
AQNAHTLHHL NAQTLRLMFN IPREQARQIV KQCPICVTYL PVPHLGVNPR GLFPNMIWQM
DVTHYSEFGN LKYIHVSIDT FSGFLLATLQ TGETTKHVIT HLLHCFSIIG LPKQIKTDNG
PGYTSKNFQE FCSTLQIKHI TGIPYNPQGQ GIVERAHLSL KTTIEKIKKG EWYPRKGTPR
NILNHALFIL NFLNLDDQNK SAADRFWHNN PKKQFAMVKW KDPLDNTWHG PDPVLIWGRG
SVCVYSQTYD AARWLPERLV RQVSNNNQSR E
