POL_RSVSB
ID POL_RSVSB Reviewed; 1603 AA.
AC O92956;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Gag-Pol polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p19;
DE Contains:
DE RecName: Full=p2A;
DE Contains:
DE RecName: Full=p2B;
DE Contains:
DE RecName: Full=p10;
DE Contains:
DE RecName: Full=Capsid protein p27, alternate cleaved 1;
DE Contains:
DE RecName: Full=Capsid protein p27, alternate cleaved 2;
DE Contains:
DE RecName: Full=p3;
DE Contains:
DE RecName: Full=Nucleocapsid protein p12;
DE Contains:
DE RecName: Full=Protease p15;
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
DE Contains:
DE RecName: Full=Reverse transcriptase beta-subunit;
DE Short=RT-beta;
DE Contains:
DE RecName: Full=Reverse transcriptase alpha-subunit;
DE Short=RT-alpha;
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:0000269|PubMed:9218451};
DE EC=3.1.-.- {ECO:0000269|PubMed:9218451};
DE AltName: Full=pp32;
DE Contains:
DE RecName: Full=p4;
GN Name=gag-pol;
OS Rous sarcoma virus (strain Schmidt-Ruppin B) (RSV-SRB).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX NCBI_TaxID=269447;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bouck J., Skalka A.M., Katz R.A.;
RT "Complete nucleotide sequence of avian sarcoma virus.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP REVIEW (INTEGRASE).
RX PubMed=28458055; DOI=10.1016/j.sbi.2017.04.005;
RA Engelman A.N., Cherepanov P.;
RT "Retroviral intasomes arising.";
RL Curr. Opin. Struct. Biol. 47:23-29(2017).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1332-1487.
RX PubMed=7563093; DOI=10.1006/jmbi.1995.0556;
RA Bujacz G., Jaskolski M., Alexandratos J., Wlodawer A., Merkel G.,
RA Katz R.A., Skalka A.M.;
RT "High-resolution structure of the catalytic domain of avian sarcoma virus
RT integrase.";
RL J. Mol. Biol. 253:333-346(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1334-1477.
RX PubMed=8805516; DOI=10.1016/s0969-2126(96)00012-3;
RA Bujacz G., Jaskolski M., Alexandratos J., Wlodawer A., Merkel G.,
RA Katz R.A., Skalka A.M.;
RT "The catalytic domain of avian sarcoma virus integrase: conformation of the
RT active-site residues in the presence of divalent cations.";
RL Structure 4:89-96(1996).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1334-1479, ACTIVE SITE
RP (INTEGRASE), AND FUNCTION (INTEGRASE).
RX PubMed=9218451; DOI=10.1074/jbc.272.29.18161;
RA Bujacz G., Alexandratos J., Wlodawer A., Merkel G., Andrake M., Katz R.A.,
RA Skalka A.M.;
RT "Binding of different divalent cations to the active site of avian sarcoma
RT virus integrase and their effects on enzymatic activity.";
RL J. Biol. Chem. 272:18161-18168(1997).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1332-1487 IN COMPLEX WITH A HIV-1
RP INTEGRASE-TARGETED INHIBITOR.
RX PubMed=9560188; DOI=10.1073/pnas.95.9.4831;
RA Lubkowski J., Yang F., Alexandratos J., Wlodawer A., Zhao H.,
RA Burke T.R. Jr., Neamati N., Pommier Y., Merkel G., Skalka A.M.;
RT "Structure of the catalytic domain of avian sarcoma virus integrase with a
RT bound HIV-1 integrase-targeted inhibitor.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4831-4836(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1334-1479, AND MUTAGENESIS OF
RP ASP-1344.
RX PubMed=9830010; DOI=10.1074/jbc.273.49.32685;
RA Lubkowski J., Yang F., Alexandratos J., Merkel G., Katz R.A., Gravuer K.,
RA Skalka A.M., Wlodawer A.;
RT "Structural basis for inactivating mutations and pH-dependent activity of
RT avian sarcoma virus integrase.";
RL J. Biol. Chem. 273:32685-32689(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.02 ANGSTROMS) OF 1333-1487.
RX PubMed=10521258; DOI=10.1021/bi991362q;
RA Lubkowski J., Dauter Z., Yang F., Alexandratos J., Merkel G., Skalka A.M.,
RA Wlodawer A.;
RT "Atomic resolution structures of the core domain of avian sarcoma virus
RT integrase and its D64N mutant.";
RL Biochemistry 38:13512-13522(1999).
CC -!- FUNCTION: Capsid protein p27: Self-associates to form the irregular
CC polyhedron core composed of hexamers and pentamers, that encapsulates
CC the genomic RNA-nucleocapsid complex. Assembles as a tube in vitro.
CC {ECO:0000250|UniProtKB:P03322}.
CC -!- FUNCTION: Spacer peptide: Plays a role in the oligomerization of the
CC Gag polyprotein and in the stabilization of the immature particle.
CC Essential layering element during tube assembly.
CC {ECO:0000250|UniProtKB:P03322}.
CC -!- FUNCTION: [Nucleocapsid protein p12]: 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: [Protease p15]: 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: [Integrase]: Catalyzes viral DNA integration into the host
CC chromosome, by performing a series of DNA cutting and joining reactions
CC (PubMed:9218451). This recombination event is an essential step in the
CC viral replication cycle. Has a strong preference for using the 3'-OH at
CC the viral DNA end as a nucleophile. {ECO:0000250|UniProtKB:P03354,
CC ECO:0000269|PubMed:9218451}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
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 Substrate-binding is a precondition for magnesium binding.
CC {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P03354};
CC Note=Binds 8 Mg(2+) ions per integrase homotetramer. {ECO:0000250};
CC -!- SUBUNIT: [Protease p15]: Active as a homodimer.
CC {ECO:0000250|UniProtKB:P03322}.
CC -!- SUBUNIT: [Integrase]: Homodimer; further associates as a homooctamer.
CC {ECO:0000250|UniProtKB:P03322, ECO:0000303|PubMed:28458055,
CC ECO:0000303|PubMed:9218451}.
CC -!- SUBUNIT: [Reverse transcriptase beta-subunit]: Heterodimer of alpha and
CC beta subunits. Three forms of RT exist: alpha-alpha (alpha-Pol), beta-
CC beta (beta-Pol), and alpha-beta, with the major form being the
CC heterodimer. Both the polymerase and RNase H active sites are located
CC in the alpha subunit of heterodimeric RT alpha-beta.
CC {ECO:0000250|UniProtKB:P03354}.
CC -!- SUBUNIT: [Reverse transcriptase alpha-subunit]: Heterodimer of alpha
CC and beta subunits. Three forms of RT exist: alpha-alpha (alpha-Pol),
CC beta-beta (beta-Pol), and alpha-beta, with the major form being the
CC heterodimer. Both the polymerase and RNase H active sites are located
CC in the alpha subunit of heterodimeric RT alpha-beta.
CC {ECO:0000250|UniProtKB:P03354}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p19]: Virion
CC {ECO:0000250|UniProtKB:P03354}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 1]: Virion
CC {ECO:0000250|UniProtKB:P03354}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 2]: Virion
CC {ECO:0000250|UniProtKB:P03354}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p12]: Virion
CC {ECO:0000250|UniProtKB:P03354}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=Translation results in the formation of the Gag polyprotein.
CC Ribosomal frameshifting at the gag/pol genes boundary produces the
CC Gag-Pol polyprotein.;
CC Name=Gag-Pol polyprotein;
CC IsoId=O92956-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=O92954-1; Sequence=External;
CC -!- DOMAIN: [Gag-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 P2B contains two L domain: a PPXY motif which probably binds to the WW
CC domains of HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases
CC and a LYPX(n)L domain which is known to bind the Alix adaptator
CC protein. {ECO:0000250|UniProtKB:P03354}.
CC -!- DOMAIN: [Integrase]: The core domain contains the D-x(n)-D-x(35)-E
CC motif, named for the phylogenetically conserved glutamic acid and
CC aspartic acid residues and the invariant 35 amino acid spacing between
CC the second and third acidic residues. Each acidic residue of the
CC D,D(35)E motif is independently essential for the 3'-processing and
CC strand transfer activities of purified integrase protein (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: [Gag-Pol polyprotein]: Contains a nuclear export signal in p10
CC and a nucleolar localization signal in nucleocapsid protein p12.
CC {ECO:0000250|UniProtKB:P03322}.
CC -!- DOMAIN: Capsid protein p27: Proton-driven dimerization of the C-
CC terminus facilitates capsid assembly. {ECO:0000250|UniProtKB:P03322}.
CC -!- PTM: [Isoform Gag-Pol polyprotein]: Specific enzymatic cleavages in
CC vivo yield mature proteins. {ECO:0000250|UniProtKB:P03354}.
CC -!- PTM: Capsid protein p27: The cleavage at the C-terminus is slowly
CC trimmed by the viral protease, sometimes being cut internally thereby
CC generating the short version of the capsid protein and a capsid protein
CC C-terminally extended by 3 amino acids in a ratio of 2:1.
CC {ECO:0000250|UniProtKB:P03322}.
CC -!- MISCELLANEOUS: Reverse transcriptase: Error-prone enzyme that lacks a
CC proof-reading function. High mutations rate is a direct consequence of
CC this characteristic. RT also displays frequent template switching
CC leading to high recombination rate. Recombination mostly occurs between
CC homologous regions of the two copackaged RNA genomes. If these two RNA
CC molecules derive from different viral strains, reverse transcription
CC will give rise to highly recombinated proviral DNAs.
CC {ECO:0000255|PROSITE-ProRule:PRU00405}.
CC -!- MISCELLANEOUS: [Isoform Gag-Pol polyprotein]: Produced by -1 ribosomal
CC frameshifting.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC08988.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF052428; AAC08988.1; ALT_INIT; Genomic_DNA.
DR PDB; 1A5V; X-ray; 1.90 A; A=1332-1487.
DR PDB; 1A5W; X-ray; 2.00 A; A=1332-1487.
DR PDB; 1A5X; X-ray; 1.90 A; A=1332-1487.
DR PDB; 1ASU; X-ray; 1.70 A; A=1332-1487.
DR PDB; 1ASV; X-ray; 2.20 A; A=1332-1487.
DR PDB; 1ASW; X-ray; 1.80 A; A=1332-1487.
DR PDB; 1CXQ; X-ray; 1.02 A; A=1333-1487.
DR PDB; 1CXU; X-ray; 1.42 A; A=1333-1487.
DR PDB; 1CZ9; X-ray; 1.20 A; A=1333-1487.
DR PDB; 1CZB; X-ray; 1.06 A; A=1333-1487.
DR PDB; 1VSD; X-ray; 1.70 A; A=1335-1479.
DR PDB; 1VSE; X-ray; 2.20 A; A=1335-1479.
DR PDB; 1VSF; X-ray; 2.05 A; A=1335-1479.
DR PDB; 1VSH; X-ray; 1.95 A; A=1335-1479.
DR PDB; 1VSI; X-ray; 2.20 A; A=1335-1479.
DR PDB; 1VSJ; X-ray; 2.10 A; A=1335-1479.
DR PDB; 1VSK; X-ray; 2.20 A; A=1334-1479.
DR PDB; 1VSL; X-ray; 2.20 A; A=1334-1479.
DR PDB; 1VSM; X-ray; 2.15 A; A=1334-1479.
DR PDB; 3O4N; X-ray; 1.80 A; A/B=1333-1479.
DR PDB; 3O4Q; X-ray; 1.55 A; A=1333-1479.
DR PDBsum; 1A5V; -.
DR PDBsum; 1A5W; -.
DR PDBsum; 1A5X; -.
DR PDBsum; 1ASU; -.
DR PDBsum; 1ASV; -.
DR PDBsum; 1ASW; -.
DR PDBsum; 1CXQ; -.
DR PDBsum; 1CXU; -.
DR PDBsum; 1CZ9; -.
DR PDBsum; 1CZB; -.
DR PDBsum; 1VSD; -.
DR PDBsum; 1VSE; -.
DR PDBsum; 1VSF; -.
DR PDBsum; 1VSH; -.
DR PDBsum; 1VSI; -.
DR PDBsum; 1VSJ; -.
DR PDBsum; 1VSK; -.
DR PDBsum; 1VSL; -.
DR PDBsum; 1VSM; -.
DR PDBsum; 3O4N; -.
DR PDBsum; 3O4Q; -.
DR BMRB; O92956; -.
DR SMR; O92956; -.
DR EvolutionaryTrace; O92956; -.
DR Proteomes; UP000159275; Genome.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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:0044823; F:retroviral integrase activity; IDA:UniProtKB.
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: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:InterPro.
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 Gene3D; 1.10.10.200; -; 1.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.90; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR Gene3D; 2.30.30.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.270; -; 2.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR004028; Gag_M.
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; IPR012344; Matrix_HIV/RSV_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; PF00607; Gag_p24; 1.
DR Pfam; PF00552; IN_DBD_C; 1.
DR Pfam; PF02022; Integrase_Zn; 1.
DR Pfam; PF02813; Retro_M; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF06817; RVT_thumb; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF46919; SSF46919; 1.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF50122; SSF50122; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; 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; 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; DNA integration; DNA recombination; DNA-binding;
KW Endonuclease; Hydrolase; Magnesium; Metal-binding; Multifunctional enzyme;
KW Nuclease; Nucleotidyltransferase; Ribosomal frameshifting;
KW RNA-directed DNA polymerase; Transferase; Viral genome integration; Virion;
KW Virus entry into host cell; Zinc; Zinc-finger.
FT CHAIN 1..1603
FT /note="Gag-Pol polyprotein"
FT /id="PRO_0000442480"
FT CHAIN 1..155
FT /note="Matrix protein p19"
FT /id="PRO_0000397058"
FT CHAIN 156..166
FT /note="p2A"
FT /id="PRO_0000397059"
FT CHAIN 167..177
FT /note="p2B"
FT /id="PRO_0000397060"
FT CHAIN 178..239
FT /note="p10"
FT /id="PRO_0000397061"
FT CHAIN 240..479
FT /note="Capsid protein p27, alternate cleaved 2"
FT /id="PRO_0000397062"
FT CHAIN 240..476
FT /note="Capsid protein p27, alternate cleaved 1"
FT /id="PRO_0000442481"
FT CHAIN 480..488
FT /note="p3"
FT /id="PRO_0000397063"
FT CHAIN 489..577
FT /note="Nucleocapsid protein p12"
FT /id="PRO_0000397064"
FT CHAIN 578..708
FT /note="Protease p15"
FT /id="PRO_0000397065"
FT CHAIN 709..1567
FT /note="Reverse transcriptase beta-subunit"
FT /id="PRO_0000397066"
FT CHAIN 709..1280
FT /note="Reverse transcriptase alpha-subunit"
FT /id="PRO_0000040984"
FT CHAIN 1281..1567
FT /note="Integrase"
FT /id="PRO_0000040985"
FT CHAIN 1568..1603
FT /note="p4"
FT /id="PRO_0000397067"
FT DOMAIN 609..690
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 750..938
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 1149..1280
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 1333..1496
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 507..524
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 533..550
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 1280..1321
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT DNA_BIND 1502..1550
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT REGION 128..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1548..1567
FT /note="Involved in homooctamerization"
FT /evidence="ECO:0000250|UniProtKB:P03354"
FT REGION 1549..1603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 172..175
FT /note="PPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT MOTIF 180..184
FT /note="LYPX(n)L motif"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT MOTIF 219..229
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT ACT_SITE 614
FT /note="For protease activity; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT BINDING 815
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 890
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 891
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 1158
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 1192
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 1213
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 1272
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 1289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1344
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 ECO:0000269|PubMed:9218451"
FT BINDING 1401
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 ECO:0000269|PubMed:9218451"
FT BINDING 1437
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 ECO:0000269|PubMed:9218451"
FT SITE 155..156
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 166..167
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 177..178
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 239..240
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 418
FT /note="Involved in capsid protein dimerization upon
FT acidification"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 430
FT /note="Involved in capsid protein dimerization upon
FT acidification"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 476..477
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 479..480
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 488..489
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 577..578
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03322"
FT SITE 708..709
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03354"
FT SITE 1280..1281
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250|UniProtKB:P03354"
FT SITE 1567..1568
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000250"
FT MUTAGEN 1344
FT /note="D->N: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:9830010"
FT CONFLICT 1376
FT /note="V -> A (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 1441
FT /note="R -> K (in Ref. 4)"
FT /evidence="ECO:0000305"
FT STRAND 1331..1333
FT /evidence="ECO:0007829|PDB:1ASU"
FT STRAND 1340..1347
FT /evidence="ECO:0007829|PDB:1CXQ"
FT HELIX 1349..1351
FT /evidence="ECO:0007829|PDB:1CXQ"
FT STRAND 1356..1362
FT /evidence="ECO:0007829|PDB:1CXQ"
FT TURN 1363..1365
FT /evidence="ECO:0007829|PDB:1CXQ"
FT STRAND 1368..1375
FT /evidence="ECO:0007829|PDB:1CXQ"
FT HELIX 1378..1392
FT /evidence="ECO:0007829|PDB:1CXQ"
FT STRAND 1396..1399
FT /evidence="ECO:0007829|PDB:1CXQ"
FT HELIX 1404..1407
FT /evidence="ECO:0007829|PDB:1CXQ"
FT HELIX 1409..1418
FT /evidence="ECO:0007829|PDB:1CXQ"
FT STRAND 1421..1423
FT /evidence="ECO:0007829|PDB:1CXQ"
FT STRAND 1428..1432
FT /evidence="ECO:0007829|PDB:1ASU"
FT HELIX 1434..1453
FT /evidence="ECO:0007829|PDB:1CXQ"
FT STRAND 1457..1459
FT /evidence="ECO:0007829|PDB:1CXQ"
FT HELIX 1462..1477
FT /evidence="ECO:0007829|PDB:1CXQ"
SQ SEQUENCE 1603 AA; 173990 MW; 3BEFAA397C54CDE7 CRC64;
MEAVIKVISS ACKTYCGKTS PSKKEIGAML SLLQKEGLLM SPSDLYSPGS WDPITAALSQ
RAMVLGKSGE LKTWGLVLGA LKAAREEQVT SEQAKFWLGL GGGRVSPPGP ECIEKPATER
RIDKGEEVGE TTVQRDAKMA PEETATPKTV GTSCYHCGTA IGCNCATASA PPPPYVGSGL
YPSLAGVGEQ QGQGGDTPRG AEQPRAEPGH AGLAPGPALT DWARIREELA STGPPVVAMP
VVIKTEGPAW TPLEPKLITR LADTVRTKGL RSPITMAEVE ALMSSPLLPH DVTNLMRVIL
GPAPYALWMD AWGVQLQTVI AAATRDPRHP ANGQGRGERT NLDRLKGLAD GMVGNPQGQA
ALLRPGELVA ITASALQAFR EVARLAEPAG PWADITQGPS ESFVDFANRL IKAVEGSDLP
PSARAPVIID CFRQKSQPDI QQLIRAAPST LTTPGEIIKY VLDRQKIAPL TDQGIAAAMS
SAIQPLVMAV VNRERDGQTG SGGRARRLCY TCGSPGHYQA QCPKKRKSGN SRERCQLCDG
MGHNAKQCRR RDSNQGQRPG RGLSSGPWPV SEQPAVSLAM TMEHKDRPLV RVILTNTGSH
PVKQRSVYIT ALLDSGADIT IISEEDWPTD WPVVDTANPQ IHGIGGGIPM RKSRDMIELG
VINRDGSLER PLLLFPAVAM VRGSILGRDC LQGLGLRLTN LVGRATVLTV ALHLAIPLKW
KPDHTPVWID QWPLPEGKLV ALTQLVEKEL QLGHIEPSLS CWNTPVFVIR KASGSYRLLH
DLRAVNAKLV PFGAVQQGAP VLSALPRGWP LMVLDLKDCF FSIPLAEQDR EAFAFTLPSV
NNQAPARRFQ WKVLPQGMTC SPTICQLVVG QVLEPLRLKH PSLRMLHYMD DLLLAASSHD
GLEAAGEEVI NTLERAGFTI SPDKIQREPG VQYLGYKLGS TYVAPVGLVA EPRIATLWDV
QKLVGSLQWL RPALGIPPRL MGPFYEQLRG SDPNEAREWN LDMKMAWREI VQLSTTAALE
RWDPALPLEG AVVRCEQGAI GVLGQGLSTH PRPCLWLFST QPTKAFTAWL EVLTLLITKL
RASAVRTFGK EVDILLLPAC FREDLPLPEG ILLALRGFAG KIRSSDTPSI FDIARPLHVS
LKVRVTDHPV PGPTVFTDAS SSTHKGVVVW REGPRWEIKE IADLGASVQQ LEARAVAMAL
LLWPTTPTNV VTDSAFVAKM LLKMGQEGVP STAAAFILED ALSQRSAMAA VLHVRSHSEV
PGFFTEGNDV ADSQATFQAY PLREAKDLHT TLHIGPRALS KACNISMQQA REVVQTCPHC
NSAPALEAGV NPRGLGPLQI WQTDFTLEPR MAPRSWLAVT VDTASSAIVV TQHGRVTSVA
AQHHWATAIA VLGRPKAIKT DNGSCFTSKS TREWLARWGI AHTTGIPGNS QGQAMVERAN
RLLKDKIRVL AEGDGFMKRI PASKQGELLA KAMYALNHFE RGENTKTPVQ KHWRPTVLTE
GPPVKIRIET GEWEKGWNVL VWGRGYAAVK NRDTDKVIWV PSRKVKPDIT QKDEVTKKDE
ASPLFAGSSD WIPWGDEQEG LQEEAASNKQ EGPGEDTLAA NES
