ID POL_HTLV2 Reviewed; 1461 AA.
AC P03363;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 27-MAR-2024, entry version 165.
DE RecName: Full=Gag-Pro-Pol polyprotein;
DE AltName: Full=Pr160Gag-Pro-Pol;
DE Contains:
DE RecName: Full=Matrix protein p19;
DE Short=MA;
DE Contains:
DE RecName: Full=Capsid protein p24;
DE Short=CA;
DE Contains:
DE RecName: Full=Nucleocapsid protein p15-pro;
DE Short=NC';
DE Short=NC-pro;
DE Contains:
DE RecName: Full=Protease;
DE Short=PR;
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
DE Contains:
DE RecName: Full=p1;
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:8623556};
DE EC=3.1.-.- {ECO:0000305|PubMed:8623556};
GN Name=gag-pro-pol;
OS Human T-cell leukemia virus 2 (HTLV-2).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus;
OC Primate T-lymphotropic virus 2.
OX NCBI_TaxID=11909;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2582407; DOI=10.1073/pnas.82.10.3101;
RA Shimotohno K., Takahashi Y., Shimizu N., Gojobori T., Golde D.W.,
RA Chen I.S.Y., Miwa M., Sugimura T.;
RT "Complete nucleotide sequence of an infectious clone of human T-cell
RT leukemia virus type II: an open reading frame for the protease gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:3101-3105(1985).
RN [2]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=2467996; DOI=10.1128/jvi.63.5.2400-2404.1989;
RA Mador N., Panet A., Honigman A.;
RT "Translation of gag, pro, and pol gene products of human T-cell leukemia
RT virus type 2.";
RL J. Virol. 63:2400-2404(1989).
RN [3]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=8371359; DOI=10.1128/jvi.67.10.6273-6277.1993;
RA Falk H., Mador N., Udi R., Panet A., Honigman A.;
RT "Two cis-acting signals control ribosomal frameshift between human T-cell
RT leukemia virus type II gag and pro genes.";
RL J. Virol. 67:6273-6277(1993).
RN [4]
RP FUNCTION (INTEGRASE).
RX PubMed=8623556; DOI=10.1006/viro.1996.0224;
RA Balakrishnan M., Zastrow D., Jonsson C.B.;
RT "Catalytic activities of the human T-cell leukemia virus type II
RT integrase.";
RL Virology 219:77-86(1996).
RN [5]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=11222762; DOI=10.1093/nar/29.5.1125;
RA Kim Y.-G., Maas S., Rich A.;
RT "Comparative mutational analysis of cis-acting RNA signals for
RT translational frameshifting in HIV-1 and HTLV-2.";
RL Nucleic Acids Res. 29:1125-1131(2001).
RN [6]
RP STRUCTURE BY NMR OF 1-136.
RX PubMed=9000634; DOI=10.1006/jmbi.1996.0700;
RA Christensen A.M., Massiah M.A., Turner B.G., Sundquist W.I., Summers M.F.;
RT "Three-dimensional structure of the HTLV-II matrix protein and comparative
RT analysis of matrix proteins from the different classes of pathogenic human
RT retroviruses.";
RL J. Mol. Biol. 264:1117-1131(1996).
CC -!- FUNCTION: [Gag-Pro-Pol polyprotein]: The matrix domain targets Gag,
CC Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a
CC multipartite membrane binding signal, that includes its myristoylated
CC N-terminus. {ECO:0000250|UniProtKB:P03345}.
CC -!- FUNCTION: [Matrix protein p19]: Matrix protein.
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- FUNCTION: [Capsid protein p24]: Forms the spherical core of the virus
CC that encapsulates the genomic RNA-nucleocapsid complex.
CC {ECO:0000250|UniProtKB:P03362}.
CC -!- FUNCTION: [Nucleocapsid protein p15-pro]: Binds strongly to viral
CC nucleic acids and promote their aggregation. Also destabilizes the
CC nucleic acids duplexes via highly structured zinc-binding motifs.
CC {ECO:0000250|UniProtKB:P03345}.
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 (Potential). Cleaves the
CC translation initiation factor eIF4G leading to the inhibition of host
CC cap-dependent translation (By similarity).
CC {ECO:0000250|UniProtKB:P03362, ECO:0000255|PROSITE-ProRule:PRU00275}.
CC -!- FUNCTION: [Reverse transcriptase/ribonuclease H]: RT is a
CC multifunctional enzyme that converts the viral RNA genome into dsDNA in
CC the cytoplasm, shortly after virus entry into the cell. This enzyme
CC displays a DNA polymerase activity that can copy either DNA or RNA
CC templates, and a ribonuclease H (RNase H) activity that cleaves the RNA
CC 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-Pro binds to the primer-binding site (PBS) situated
CC at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer
CC to perform a short round of RNA-dependent minus-strand DNA synthesis.
CC The reading proceeds through the U5 region and ends after the repeated
CC (R) region which is present at both ends of viral RNA. The portion of
CC the RNA-DNA heteroduplex is digested by the RNase H, resulting in a
CC ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes
CC with 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 perform 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 primer. PPT and tRNA primers are then removed by RNase H. The 3' and 5'
CC 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 (By similarity). {ECO:0000250}.
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:8623556}.
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=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 -!- 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; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity.
CC {ECO:0000250};
CC -!- SUBUNIT: [Gag-Pro-Pol polyprotein]: Homodimer; the homodimers are part
CC of the immature particles. Interacts with human TSG101 and NEDD4; these
CC interactions are essential for budding and release of viral particles.
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- SUBUNIT: [Matrix protein p19]: Homodimer; further assembles as
CC homohexamers. {ECO:0000250|UniProtKB:P03345}.
CC -!- INTERACTION:
CC P03363; O14770: MEIS2; Xeno; NbExp=3; IntAct=EBI-9676133, EBI-2804934;
CC -!- SUBCELLULAR LOCATION: [Matrix protein p19]: Virion
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p24]: Virion
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p15-pro]: Virion
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Comment=This strategy of translation probably allows the virus to
CC modulate the quantity of each viral protein. {ECO:0000305};
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P03363-1; Sequence=Displayed;
CC Name=Gag-Pro polyprotein;
CC IsoId=P03353-1; Sequence=External;
CC Name=Gag polyprotein;
CC IsoId=P03346-1; Sequence=External;
CC -!- DOMAIN: Gag polyprotein: Late-budding domains (L domains) are short
CC sequence motifs essential for viral particle release. They can occur
CC individually or in close proximity within structural proteins. They
CC interacts with sorting cellular proteins of the multivesicular body
CC (MVB) pathway. Most of these proteins are class E vacuolar protein
CC sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes.
CC Matrix protein p19 contains two L domains: a PTAP/PSAP motif which
CC interacts with the UEV domain of TSG101, and a PPXY motif which binds
CC to the WW domains of the ubiquitin ligase NEDD4.
CC {ECO:0000250|UniProtKB:P03345}.
CC -!- DOMAIN: [Capsid protein p24]: The capsid protein N-terminus seems to be
CC involved in Gag-Gag interactions. {ECO:0000250|UniProtKB:P03362}.
CC -!- PTM: [Matrix protein p19]: Phosphorylation of the matrix protein p19 by
CC MAPK1 seems to play a role in budding. {ECO:0000250|UniProtKB:P03345}.
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:P03345}.
CC -!- PTM: [Gag-Pro-Pol polyprotein]: Specific enzymatic cleavages by the
CC viral protease yield mature proteins. The polyprotein is cleaved during
CC and after budding, this process is termed maturation. The protease is
CC autoproteolytically processed at its N- and C-termini.
CC {ECO:0000250|UniProtKB:P03362}.
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 frameshifting at the gag-pol genes boundary.
CC {ECO:0000269|PubMed:11222762, ECO:0000269|PubMed:2467996,
CC ECO:0000269|PubMed:8371359}.
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DR EMBL; M10060; AAB59885.1; ALT_SEQ; Genomic_DNA.
DR PIR; A03962; GNLJH2.
DR RefSeq; NP_041003.3; NC_001488.1.
DR PDB; 1JVR; NMR; -; A=1-136.
DR PDB; 6QBT; X-ray; 2.29 A; A=1217-1385.
DR PDB; 6QBV; X-ray; 2.45 A; A/B/C/D=1217-1380.
DR PDB; 6QBW; X-ray; 2.40 A; A=1217-1385.
DR PDBsum; 1JVR; -.
DR PDBsum; 6QBT; -.
DR PDBsum; 6QBV; -.
DR PDBsum; 6QBW; -.
DR SMR; P03363; -.
DR IntAct; P03363; 8.
DR MINT; P03363; -.
DR GeneID; 1491941; -.
DR KEGG; vg:1491941; -.
DR EvolutionaryTrace; P03363; -.
DR Proteomes; UP000009254; 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-EC.
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:0005198; F:structural molecule activity; IEA:InterPro.
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:0039657; P:suppression by virus of host gene expression; 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 Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR Gene3D; 1.10.185.10; Delta-retroviral matrix; 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; 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; IPR003139; D_retro_matrix.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR045345; Gag_p24_C.
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; 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; 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; PF02228; Gag_p19; 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; PF00098; zf-CCHC; 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; 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; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Capsid protein; DNA integration;
KW DNA recombination; DNA-binding; Endonuclease;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus;
KW Host gene expression shutoff by virus; Host-virus interaction; Hydrolase;
KW Lipoprotein; Magnesium; Metal-binding; Multifunctional enzyme; Myristate;
KW Nuclease; Nucleotidyltransferase; Protease; Reference proteome; Repeat;
KW Ribosomal frameshifting; RNA-directed DNA polymerase; Transferase;
KW Viral genome integration; 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..1461
FT /note="Gag-Pro-Pol polyprotein"
FT /id="PRO_0000085472"
FT CHAIN 2..136
FT /note="Matrix protein p19"
FT /id="PRO_0000259946"
FT CHAIN 137..350
FT /note="Capsid protein p24"
FT /id="PRO_0000259947"
FT CHAIN 351..446
FT /note="Nucleocapsid protein p15-pro"
FT /id="PRO_0000259948"
FT CHAIN 447..571
FT /note="Protease"
FT /id="PRO_0000261318"
FT PEPTIDE 572..579
FT /note="p1"
FT /id="PRO_0000259949"
FT CHAIN 580..1166
FT /note="Reverse transcriptase/ribonuclease H"
FT /id="PRO_0000259950"
FT CHAIN 1167..1461
FT /note="Integrase"
FT /id="PRO_0000259951"
FT DOMAIN 473..551
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 612..802
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 1029..1164
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 1218..1387
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 361..378
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 384..401
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT DNA_BIND 1392..1441
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT REGION 94..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 94..97
FT /note="PTAP/PSAP motif"
FT MOTIF 124..127
FT /note="PPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P03345"
FT MOTIF 130..133
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000250|UniProtKB:P03345"
FT COMPBIAS 97..121
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 478
FT /note="For protease activity; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT BINDING 678
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 753
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 754
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 1038
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 1073
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 1095
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 1156
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 1229
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 1286
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 SITE 136..137
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03362"
FT SITE 350..351
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03362"
FT SITE 446..447
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03362"
FT SITE 571..572
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03362"
FT SITE 579..580
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03362"
FT SITE 1019..1020
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03362"
FT SITE 1166..1167
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03362"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1JVR"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:1JVR"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1JVR"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:1JVR"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:1JVR"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:1JVR"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:1JVR"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:1JVR"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:1JVR"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1JVR"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1JVR"
FT STRAND 1224..1235
FT /evidence="ECO:0007829|PDB:6QBT"
FT STRAND 1238..1247
FT /evidence="ECO:0007829|PDB:6QBT"
FT TURN 1248..1250
FT /evidence="ECO:0007829|PDB:6QBT"
FT STRAND 1253..1259
FT /evidence="ECO:0007829|PDB:6QBT"
FT HELIX 1263..1277
FT /evidence="ECO:0007829|PDB:6QBT"
FT STRAND 1281..1284
FT /evidence="ECO:0007829|PDB:6QBT"
FT HELIX 1289..1292
FT /evidence="ECO:0007829|PDB:6QBT"
FT HELIX 1294..1302
FT /evidence="ECO:0007829|PDB:6QBT"
FT STRAND 1306..1308
FT /evidence="ECO:0007829|PDB:6QBT"
FT HELIX 1320..1338
FT /evidence="ECO:0007829|PDB:6QBT"
FT STRAND 1339..1342
FT /evidence="ECO:0007829|PDB:6QBT"
FT HELIX 1344..1357
FT /evidence="ECO:0007829|PDB:6QBT"
FT TURN 1362..1364
FT /evidence="ECO:0007829|PDB:6QBT"
FT HELIX 1368..1372
FT /evidence="ECO:0007829|PDB:6QBT"
SQ SEQUENCE 1461 AA; 162402 MW; 2D2911076BDD1002 CRC64;
MGQIHGLSPT PIPKAPRGLS THHWLNFLQA AYRLQPRPSD FDFQQLRRFL KLALKTPIWL
NPIDYSLLAS LIPKGYPGRV VEIINILVKN QVSPSAPAAP VPTPICPTTT PPPPPPPSPE
AHVPPPYVEP TTTQCFPILH PPGAPSAHRP WQMKDLQAIK QEVSSSALGS PQFMQTLRLA
VQQFDPTAKD LQDLLQYLCS SLVVSLHHQQ LNTLITEAET RGMTGYNPMA GPLRMQANNP
AQQGLRREYQ NLWLAAFSTL PGNTRDPSWA AILQGLEEPY CAFVERLNVA LDNGLPEGTP
KEPILRSLAY SNANKECQKI LQARGHTNSP LGEMLRTCQA WTPKDKTKVL VVQPRRPPPT
QPCFRCGKVG HWSRDCTQPR PPPGPCPLCQ DPSHWKRDCP QLKPPQEEGE PLLLDLPSTS
GTTEEKNLLK GGDLISPHPD QDISILPLIP LRQQQQPILG VRISVMGQTP QPTQALLDTG
ADLTVIPQTL VPGPVKLHDT LILGASGQTN TQFKLLQTPL HIFLPFRRSP VILSSCLLDT
HNKWTIIGRD ALQQCQGLLY LPDDPSPHQL LPIATPNTIG LEHLPPPPQV DQFPLNLPER
LQALNDLVSK ALEAGHIEPY SGPGNNPVFP VKKPNGKWRF IHDLRATNAI TTTLTSPSPG
PPDLTSLPTA LPHLQTIDLT DAFFQIPLPK QYQPYFAFTI PQPCNYGPGT RYAWTVLPQG
FKNSPTLFEQ QLAAVLNPMR KMFPTSTIVQ YMDDILLASP TNEELQQLSQ LTLQALTTHG
LPISQEKTQQ TPGQIRFLGQ VISPNHITYE STPTIPIKSQ WTLTELQVIL GEIQWVSKGT
PILRKHLQSL YSALHGYRDP RACITLTPQQ LHALHAIQQA LQHNCRGRLN PALPLLGLIS
LSTSGTTSVI FQPKQNWPLA WLHTPHPPTS LCPWGHLLAC TILTLDKYTL QHYGQLCQSF
HHNMSKQALC DFLRNSPHPS VGILIHHMGR FHNLGSQPSG PWKTLLHLPT LLQEPRLLRP
IFTLSPVVLD TAPCLFSDGS PQKAAYVLWD QTILQQDITP LPSHETHSAQ KGELLALICG
LRAAKPWPSL NIFLDSKYLI KYLHSLAIGA FLGTSAHQTL QAALPPLLQG KTIYLHHVRS
HTNLPDPIST FNEYTDSLIL APLVPLTPQG LHGLTHCNQR ALVSFGATPR EAKSLVQTCH
TCQTINSQHH MPRGYIRRGL LPNHIWQGDV THYKYKKYKY CLHVWVDTFS GAVSVSCKKK
ETSCETISAV LQAISLLGKP LHINTDNGPA FLSQEFQEFC TSYRIKHSTH IPYNPTSSGL
VERTNGVIKN LLNKYLLDCP NLPLDNAIHK ALWTLNQLNV MNPSGKTRWQ IHHSPPLPPI
PEASTPPKPP PKWFYYKLPG LTNQRWKGPL QSLQEAAGAA LLSIDGSPRW IPWRFLKKAA
CPRPDASELA EHAATDHQHH G
//
