POL_SMRVH
ID POL_SMRVH Reviewed; 1880 AA.
AC P03364;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Gag-Pro-Pol polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p19;
DE Contains:
DE RecName: Full=Core protein p16;
DE Contains:
DE RecName: Full=Capsid protein p35;
DE AltName: Full=Capsid protein p34;
DE Contains:
DE RecName: Full=Probable 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 Squirrel monkey retrovirus (SMRV-H) (SMRV-HLB).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11856;
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEIN SEQUENCE OF 319-346, AND
RP PROTEOLYTIC CLEAVAGE (GAG-PRO-POL POLYPROTEIN).
RX PubMed=3201749; DOI=10.1016/s0042-6822(88)90109-2;
RA Oda T., Ikeda S., Watanabe S., Hatsushika M., Akiyama K., Mitsunobu F.;
RT "Molecular cloning, complete nucleotide sequence, and gene structure of the
RT provirus genome of a retrovirus produced in a human lymphoblastoid cell
RT line.";
RL Virology 167:468-476(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 595-774.
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 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 [4]
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 p19]: Matrix protein.
CC {ECO:0000250|UniProtKB:P07567}.
CC -!- FUNCTION: [Capsid protein p35]: Capsid protein.
CC {ECO:0000250|UniProtKB:P07567}.
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:0000305}.
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: [Probable nucleocapsid protein-dUTPase]: Homotrimer.
CC {ECO:0000250|UniProtKB:P07570}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p35]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Probable nucleocapsid protein-dUTPase]: Virion
CC {ECO:0000305}.
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=P03364-1; Sequence=Displayed;
CC Name=Gag-Pro polyprotein;
CC IsoId=P21407-1; Sequence=External;
CC Name=Gag polyprotein;
CC IsoId=P21411-1; Sequence=External;
CC -!- DOMAIN: [Gag-Pro-Pol polyprotein]: Gag polyprotein: Late-budding
CC domains (L domains) are short sequence motifs essential for viral
CC particle release. They can occur individually or in close proximity
CC within structural proteins. They interacts with sorting cellular
CC proteins of the multivesicular body (MVB) pathway. Most of these
CC proteins are class E vacuolar protein sorting factors belonging to
CC ESCRT-I, ESCRT-II or ESCRT-III complexes. Gag-p35 contains one L
CC domain: a PTAP/PSAP motif, which interacts with the UEV domain of
CC TSG101 (Potential). {ECO:0000305}.
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: [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:0000305|PubMed:3201749}.
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 -!- 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 -!- SEQUENCE CAUTION:
CC Sequence=AAA66453.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; K01706; AAA46815.1; -; Genomic_RNA.
DR EMBL; M23385; AAA66453.1; ALT_INIT; Genomic_RNA.
DR PIR; A05072; A05072.
DR PIR; C31827; GNLJHD.
DR RefSeq; NP_041261.1; NC_001514.1.
DR SMR; P03364; -.
DR GeneID; 1491962; -.
DR KEGG; vg:1491962; -.
DR Proteomes; UP000007223; 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; 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 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; 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; PS50876; ZF_INTEGRASE; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Direct protein sequencing; 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;
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:0000255"
FT CHAIN 2..1880
FT /note="Gag-Pro-Pol polyprotein"
FT /id="PRO_0000125496"
FT CHAIN 2..163
FT /note="Matrix protein p19"
FT /id="PRO_0000443148"
FT CHAIN 164..318
FT /note="Core protein p16"
FT /id="PRO_0000443149"
FT CHAIN 319..585
FT /note="Capsid protein p35"
FT /id="PRO_0000443150"
FT CHAIN 586..842
FT /note="Probable nucleocapsid protein-dUTPase"
FT /id="PRO_0000443151"
FT CHAIN 843..996
FT /note="Protease 17 kDa"
FT /id="PRO_0000443152"
FT CHAIN 843..960
FT /note="Protease 13 kDa"
FT /id="PRO_0000443153"
FT PEPTIDE 961..997
FT /note="G-patch peptide"
FT /id="PRO_0000443154"
FT CHAIN 998..?1589
FT /note="Reverse transcriptase/ribonuclease H"
FT /id="PRO_0000443155"
FT CHAIN ?1590..1880
FT /note="Integrase"
FT /id="PRO_0000443156"
FT DOMAIN 863..939
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 950..996
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT DOMAIN 1044..1232
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 1455..1586
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 1643..1804
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 1589..1630
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT DNA_BIND 1809..1858
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT REGION 115..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1859..1880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..366
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 868
FT /note="Protease; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT BINDING 1109
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 1184
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 1185
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 1464
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 1493
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 1514
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 1578
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 1598
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1602
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1626
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1629
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
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:0000255|PROSITE-ProRule:PRU00457"
FT BINDING 1711
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 1747
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 163..164
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000305|PubMed:3201749"
FT SITE 318..319
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000305|PubMed:3201749"
FT SITE 585..586
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000305|PubMed:3201749"
FT SITE 648..649
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000305|PubMed:3201749"
FT SITE 842..843
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07572"
FT SITE 960..961
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07572"
FT SITE 997..998
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07572"
FT SITE 1589..1590
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:0000255"
SQ SEQUENCE 1880 AA; 207175 MW; 4BB9A4268FF31A88 CRC64;
MGQASSHSEN DLFISHLKES LKVRRIRVRK KDLVSFFSFI FKTCPWFPQE GSIDSRVWGR
VGDCLNDYYR VFGPETIPIT TFNYYNLIRD VLTNQSDSPD IQRLCKEGHK ILISHSRPPS
RQAPVTITTS EKASSRPPSR APSTCPSVAI DIGSHDTGQS SLYPNLATLT DPPIQSPHSR
AHTPPQHLPL LANSKTLHNS GSQDDQLNPA DQADLEEAAA QYNNPDWPQL TNTPALPPFR
PPSYVSTAVP PVAVAAPVLH APTSGVPGSP TAPNLPGVAL AKPSGPIDET VSLLDGVKTL
VTKLSDLALL PPAGVMAFPV TRSQGQVSSN TTGRASPHPD THTIPEEEEA DSGESDSEDD
EEESSEPTEP TYTHSYKRLN LKTIEKIKTA VANYGPTAPF TVALVESLSE RWLTPSDWFF
LSRAALSGGD NILWKSEYED ISKQFAERTR VRPPPKDGPL KIPGASPYQN NDKQAQFPPG
LLTQIQSAGL KAWKRLPQKG AATTSLAKIR QGPDESYSDF VSRLQETADR LFGSGESESS
FVKHLAYENA NPACQSAIRP FRQKELSTMS PLLWYCSAHA VGLAIGAALQ NLAPAQLLEP
RPAFAIIVTN PAIFQETAPK KIQPPTQLPT QPNAPQASLI KNLGPTTKCP RCKKGFHWAS
ECRSRLDING QPIIKQGNLE QGPAPGPHYR DELRGFTVHP PIPPANPCPP SNQPRRYVTD
LWRATAGSAG LDLCTTTDTI LTTQNSPLTL PVGIYGPLPP QTFGLILAEP ALPSKGIQVL
PGILDNDFEG EIHIILSTTK DLVTIPKGTR LAQIVILPLQ QINSNFHKPY RGASAPGSSD
VYWVQQISQQ RPTLKLKLNG KLFSGILDTG ADATVISYTH WPRNWPLTTV ATHLRGIGQA
TNPQQSAQML KWEDSEGNNG HITPYVLPNL PVNLWGRDIL SQMKLVMCSP NDTVMTQMLS
QGYLPGQGLG KNNQGITQPI TITPKKDKTG LGFHQNLPRS RAIDIPVPHA DKISWKITDP
VWVDQWPLTY EKTLAAIALV QEQLAAGHIE PTNSPWNTPI FIIKKKSGSW RLLQDLRAVN
KVMVPMGALQ PGLPSPVAIP LNYHKIVIDL KDCFFTIPLH PEDRPYFAFS VPQINFQSPM
PRYQWKVLPQ GMANSPTLCQ KFVAAAIAPV RSQWPEAYIL HYMDDILLAC DSAEAAKACY
AHIISCLTSY GLKIAPDKVQ VSEPFSYLGF ELHHQQVFTP RVCLKTDHLK TLNDFQKLLG
DIQWLRPYLK LPTSALVPLN NILKGDPNPL SVRALTPEAK QSLALINKAI QNQSVQQISY
NLPLVLLLLP TPHTPTAVFW QPNGTDPTKN GSPLLWLHLP ASPSKVLLTY PSLLAMLIIK
GRYTGRQLFG RDPHSIIIPY TQDQLTWLLQ TSDEWAIALS SFTGDIDNHY PSDPVIQFAK
LHQFIFPKIT KCAPIPQATL VFTDGSSNGI AAYVIDNQPI SIKSPYLSAQ LVELYAILQV
FTVLAHQPFN LYTDSAYIAQ SVPLLETVPF IKSSTNATPL FSKLQQLILN RQHPFFIGHL
RAHLNLPGPL AEGNALADAA TQIFPIISDP IHEATQAHTL HHLNAHTLRL LYKITREQAR
DIVKACKQCV VATPVPHLGV NPRGLVPNAI WQMDVTHFTP FGKQRFVHVT VDTFSGFILA
TPQTGEASKN VISHVIHCLA TIGKPHTIKT DNGPGYTGKN FQDFCQKLQI KHVTGIPYNP
QGQGVVERAH QTLKNALNRL ARSPLGFSMQ QPRNLLSHAL FQLNFLQLDS QGRSAADRLW
HPQTSQQHAT VMWRDPLTSV WKGPDPVLIW GRGSACIYDQ KEDGPRWLPE RLIRHINNQT
APLCDRPSNP NTAPGPKGSP
