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POL_XMRV4
ID   POL_XMRV4               Reviewed;        1733 AA.
AC   Q2F7J0;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Gag-Pol polyprotein;
DE            Short=Pr180gag-pol;
DE   Contains:
DE     RecName: Full=Matrix protein p15;
DE              Short=MA;
DE   Contains:
DE     RecName: Full=RNA-binding phosphoprotein p12;
DE     AltName: Full=pp12;
DE   Contains:
DE     RecName: Full=Capsid protein p30;
DE              Short=CA;
DE   Contains:
DE     RecName: Full=Nucleocapsid protein p10;
DE              Short=NC-pol;
DE   Contains:
DE     RecName: Full=Protease p14;
DE              Short=PR;
DE              EC=3.4.23.-;
DE   Contains:
DE     RecName: Full=Reverse transcriptase/ribonuclease H p80;
DE              Short=RT;
DE              EC=2.7.7.49;
DE              EC=2.7.7.7;
DE              EC=3.1.26.4;
DE   Contains:
DE     RecName: Full=Integrase p46;
DE              Short=IN;
DE              EC=2.7.7.- {ECO:0000250|UniProtKB:P03355};
DE              EC=3.1.-.- {ECO:0000250|UniProtKB:P03355};
GN   Name=gag-pol;
OS   Xenotropic MuLV-related virus (isolate VP42) (XMRV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC   unclassified Gammaretrovirus.
OX   NCBI_TaxID=356664;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RETRACTED PAPER.
RX   PubMed=16609730; DOI=10.1371/journal.ppat.0020025;
RA   Urisman A., Molinaro R.J., Fischer N., Plummer S.J., Casey G., Klein E.A.,
RA   Malathi K., Magi-Galluzzi C., Tubbs R.R., Ganem D., Silverman R.H.,
RA   DeRisi J.L.;
RT   "Identification of a novel Gammaretrovirus in prostate tumors of patients
RT   homozygous for R462Q RNASEL variant.";
RL   PLoS Pathog. 2:E25-E25(2006).
RN   [2]
RP   RETRACTION NOTICE OF PUBMED:16609730.
RX   PubMed=23028303;
RX   DOI=10.1371/annotation/7e2efc01-2e9b-4e9b-aef0-87ab0e4e4732;
RA   Urisman A., Molinaro R.J., Fischer N., Plummer S.J., Casey G., Klein E.A.,
RA   Malathi K., Magi-Galluzzi C., Tubbs R.R., Ganem D., Silverman R.H.,
RA   DeRisi J.L.;
RL   PLoS Pathog. 8:0-0(2012).
CC   -!- FUNCTION: Matrix protein p15 targets Gag and gag-pol polyproteins to
CC       the plasma membrane via a multipartite membrane binding signal, that
CC       includes its myristoylated N-terminus. Also mediates nuclear
CC       localization of the preintegration complex (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: Capsid protein p30 forms the spherical core of the virion
CC       that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.
CC   -!- FUNCTION: Nucleocapsid protein p10 is involved in the packaging and
CC       encapsidation of two copies of the genome. Binds with high affinity to
CC       conserved UCUG elements within the packaging signal, located near the
CC       5'-end of the genome. This binding is dependent on genome dimerization
CC       (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: The aspartyl protease mediates proteolytic cleavages of Gag
CC       and Gag-Pol polyproteins during or shortly after the release of the
CC       virion from the plasma membrane. Cleavages take place as an ordered,
CC       step-wise cascade to yield mature proteins. This process is called
CC       maturation. Displays maximal activity during the budding process just
CC       prior to particle release from the cell. {ECO:0000255|PROSITE-
CC       ProRule:PRU00275}.
CC   -!- FUNCTION: Reverse transcriptase/ribonuclease H is a multifunctional
CC       enzyme that converts the viral dimeric RNA genome into dsDNA in the
CC       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 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       perform 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 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       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 (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. This enzyme activity takes place after virion entry into a
CC       cell and reverse transcription of the RNA genome in dsDNA. The first
CC       step in the integration process is 3' processing. This step requires a
CC       complex comprising the viral genome, matrix protein and integrase. This
CC       complex is called the pre-integration complex (PIC). The integrase
CC       protein removes 2 nucleotides from each 3' end of the viral DNA,
CC       leaving recessed CA OH's at the 3' ends. In the second step that
CC       requires cell division, the PIC enters cell nucleus. In the third step,
CC       termed strand transfer, the integrase protein joins the previously
CC       processed 3' ends to the 5' ends of strands of target cellular DNA at
CC       the site of integration. The last step is viral DNA integration into
CC       host chromosome (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Gag-Pol polyprotein plays a role in budding and is processed
CC       by the viral protease during virion maturation outside the cell. During
CC       budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-
CC       like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to
CC       Gag binding host factors. Interaction with HECT ubiquitin ligases
CC       probably link the viral protein to the host ESCRT pathway and
CC       facilitate release (By similarity). {ECO:0000250}.
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=Binds 2 magnesium ions for reverse transcriptase polymerase
CC       activity. {ECO:0000250};
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Magnesium ions are required for integrase activity. Binds at least
CC       1, maybe 2 magnesium ions. {ECO:0000250};
CC   -!- SUBUNIT: Capsid protein p30 is a homohexamer, that further associates
CC       as homomultimer. The virus core is composed of a lattice formed from
CC       hexagonal rings, each containing six capsid monomers. The protease is a
CC       homodimer, whose active site consists of two apposed aspartic acid
CC       residues. The reverse transcriptase is a monomer (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane
CC       {ECO:0000305}; Lipid-anchor {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein p30]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p10]: Virion {ECO:0000305}.
CC   -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC       essential for viral particle release. They can occur individually or in
CC       close proximity within structural proteins. They interacts with sorting
CC       cellular proteins of the multivesicular body (MVB) pathway. Most of
CC       these proteins are class E vacuolar protein sorting factors belonging
CC       to ESCRT-I, ESCRT-II or ESCRT-III complexes. RNA-binding phosphoprotein
CC       p12 contains one L domain: a PPXY motif which potentially interacts
CC       with the WW domain 3 of NEDD4 E3 ubiquitin ligase. PPXY motif is
CC       essential for virus egress. Matrix protein p15 contains one L domain: a
CC       PTAP/PSAP motif, which potentially interacts with the UEV domain of
CC       TSG101. The junction between the matrix protein p15 and RNA-binding
CC       phosphoprotein p12 also contains one L domain: a LYPX(n)L motif which
CC       potentially interacts with PDCD6IP. Both PSAP and LYPX(n)L domains
CC       might play little to no role in budding and possibly drive residual
CC       virus release. contains (By similarity). {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages by the viral protease yield mature
CC       proteins. The protease is released by autocatalytic cleavage. The
CC       polyprotein is cleaved during and after budding, this process is termed
CC       maturation (By similarity). {ECO:0000250}.
CC   -!- PTM: Capsid protein p30 is sumoylated; which is required for virus
CC       replication.
CC   -!- PTM: RNA-binding phosphoprotein p12 is phosphorylated on serine
CC       residues. {ECO:0000250}.
CC   -!- MISCELLANEOUS: This protein is translated as a gag-pol fusion protein
CC       by episodic readthrough of the gag protein termination codon.
CC       Readthrough of the terminator codon TAG occurs between the codons for
CC       536-Asp and 538-Gly (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: The nucleocapsid protein p10 released from Pol
CC       polyprotein (NC-pol) is a few amino acids shorter than the nucleocapsid
CC       protein p10 released from Gag polyprotein (NC-gag). {ECO:0000250}.
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   -!- CAUTION: Originally thought to be characterized from prostate tumors,
CC       the described gammaretrovirus XMRV is in fact laboratory-derived and
CC       there is no association of XMRV with prostate cancer.
CC       {ECO:0000305|PubMed:16609730, ECO:0000305|PubMed:23028303}.
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DR   EMBL; DQ241302; ABB83228.1; -; Genomic_RNA.
DR   MINT; Q2F7J0; -.
DR   PRIDE; Q2F7J0; -.
DR   Proteomes; UP000008602; Genome.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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   GO; GO:0019068; P:virion assembly; IEA:InterPro.
DR   Gene3D; 1.10.150.180; -; 1.
DR   Gene3D; 1.10.375.10; -; 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; IPR000840; G_retro_matrix.
DR   InterPro; IPR036946; G_retro_matrix_sf.
DR   InterPro; IPR039464; Gag-pol_Znf-H3C2.
DR   InterPro; IPR002079; Gag_p12.
DR   InterPro; IPR003036; Gag_P30.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR040643; MLVIN_C.
DR   InterPro; IPR001995; Peptidase_A2_cat.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR018061; Retropepsins.
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; IPR041577; RT_RNaseH_2.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   Pfam; PF01140; Gag_MA; 1.
DR   Pfam; PF01141; Gag_p12; 1.
DR   Pfam; PF02093; Gag_p30; 1.
DR   Pfam; PF18697; MLVIN_C; 1.
DR   Pfam; PF00075; RNase_H; 1.
DR   Pfam; PF17919; RT_RNaseH_2; 1.
DR   Pfam; PF00665; rve; 1.
DR   Pfam; PF00077; RVP; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   Pfam; PF16721; zf-H3C2; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF47836; SSF47836; 1.
DR   SUPFAM; SSF47943; SSF47943; 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; PS50879; RNASE_H_1; 1.
DR   PROSITE; PS50878; RT_POL; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Capsid protein; Coiled coil; DNA integration;
KW   DNA recombination; DNA-binding; DNA-directed DNA polymerase; Endonuclease;
KW   Host cell membrane; Host membrane; Hydrolase; Lipoprotein; Magnesium;
KW   Membrane; Metal-binding; Multifunctional enzyme; Myristate; Nuclease;
KW   Nucleotidyltransferase; Phosphoprotein; Protease;
KW   RNA suppression of termination; RNA-binding; RNA-directed DNA polymerase;
KW   Transferase; Ubl conjugation; Viral genome integration;
KW   Viral matrix protein; Viral nucleoprotein; Virion;
KW   Virus entry into host cell; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..1733
FT                   /note="Gag-Pol polyprotein"
FT                   /id="PRO_0000390860"
FT   CHAIN           2..129
FT                   /note="Matrix protein p15"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000390861"
FT   CHAIN           130..213
FT                   /note="RNA-binding phosphoprotein p12"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000390862"
FT   CHAIN           214..476
FT                   /note="Capsid protein p30"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000390863"
FT   CHAIN           477..532
FT                   /note="Nucleocapsid protein p10"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000390864"
FT   CHAIN           533..657
FT                   /note="Protease p14"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000390865"
FT   CHAIN           658..1328
FT                   /note="Reverse transcriptase/ribonuclease H p80"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000390866"
FT   CHAIN           1329..1733
FT                   /note="Integrase p46"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000390867"
FT   DOMAIN          559..629
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT   DOMAIN          739..930
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   DOMAIN          1172..1318
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   DOMAIN          1442..1600
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   ZN_FING         500..517
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          98..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          436..476
FT                   /evidence="ECO:0000255"
FT   MOTIF           109..112
FT                   /note="PTAP/PSAP motif"
FT   MOTIF           128..132
FT                   /note="LYPX(n)L motif"
FT   MOTIF           161..164
FT                   /note="PPXY motif"
FT   COMPBIAS        98..123
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        564
FT                   /note="Protease; shared with dimeric partner"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT   BINDING         807
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:0000250"
FT   BINDING         881
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:0000250"
FT   BINDING         882
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:0000250"
FT   BINDING         1181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="for RNase H activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         1219
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="for RNase H activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         1240
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="for RNase H activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         1310
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="for RNase H activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         1453
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"
FT   BINDING         1512
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"
FT   SITE            129..130
FT                   /note="Cleavage; by viral protease p14"
FT                   /evidence="ECO:0000250"
FT   SITE            213..214
FT                   /note="Cleavage; by viral protease p14"
FT                   /evidence="ECO:0000250"
FT   SITE            476..477
FT                   /note="Cleavage; by viral protease p14"
FT                   /evidence="ECO:0000250"
FT   SITE            532..533
FT                   /note="Cleavage; by viral protease p14"
FT                   /evidence="ECO:0000250"
FT   SITE            657..658
FT                   /note="Cleavage; by viral protease p14"
FT                   /evidence="ECO:0000250"
FT   SITE            1328..1329
FT                   /note="Cleavage; by viral protease p14"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         190
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1733 AA;  193702 MW;  4208EFFD6F95FA25 CRC64;
     MGQTVTTPLS LTLQHWGDVQ RIASNQSVDV KKRRWVTFCS AEWPTFNVGW PQDGTFNLGI
     ISQVKSRVFC PGPHGHPDQV PYIVTWEALA YDPPPWVKPF VSPKPPPLPT APVLPPGPSA
     QPPSRSALYP ALTPSIKSKP PKPQVLPDSG GPLIDLLTED PPPYGAQPSS SARENNEEEA
     ATTSEVSPPS PMVSRLRGRR DPPAADSTTS QAFPLRMGGD GQLQYWPFSS SDLYNWKNNN
     PSFSEDPGKL TALIESVLIT HQPTWDDCQQ LLGTLLTGEE KQRVLLEARK AVRGNDGRPT
     QLPNEVNAAF PLERPDWGYT TTEGRNHLVL YRQLLLAGLQ NAGRSPTNLA KVKGITQGPN
     ESPSAFLERL KEAYRRYTPY DPEDPGQETN VSMSFIWQSA PDIGRKLERL EDLKSKTLGD
     LVREAEKIFN KRETPEEREE RIRREIEEKE ERRRAEDEQR ERERDRRRHR EMSKLLATVV
     IGQRQDRQGG ERRRPQLDKD QCAYCKEKGH WAKDCPKKPR GPRGPRPQTS LLTLGDXGGQ
     GQEPPPEPRI TLKVGGQPVT FLVDTGAQHS VLTQNPGPLS DKSAWVQGAT GGKRYRWTTD
     RKVHLATGKV THSFLHVPDC PYPLLGRDLL TKLKAQIHFE GSGAQVVGPM GQPLQVLTLN
     IEDEYRLHET SKEPDVPLGS TWLSDFPQAW AETGGMGLAV RQAPLIIPLK ATSTPVSIKQ
     YPMSQEARLG IKPHIQRLLD QGILVPCQSP WNTPLLPVKK PGTNDYRPVQ DLREVNKRVE
     DIHPTVPNPY NLLSGLPPSH QWYTVLDLKD AFFCLRLHPT SQPLFAFEWR DPEMGISGQL
     TWTRLPQGFK NSPTLFDEAL HRDLADFRIQ HPDLILLQYV DDLLLAATSE QDCQRGTRAL
     LQTLGNLGYR ASAKKAQICQ KQVKYLGYLL KEGQRWLTEA RKETVMGQPT PKTPRQLREF
     LGTAGFCRLW IPGFAEMAAP LYPLTKTGTL FNWGPDQQKA YQEIKQALLT APALGLPDLT
     KPFELFVDEK QGYAKGVLTQ KLGPWRRPVA YLSKKLDPVA AGWPPCLRMV AAIAVLTKDA
     GKLTMGQPLV ILAPHAVEAL VKQPPDRWLS NARMTHYQAM LLDTDRVQFG PVVALNPATL
     LPLPEKEAPH DCLEILAETH GTRPDLTDQP IPDADYTWYT DGGSFLQEGQ RRAGAAVTTE
     TEVIWGGVLP AGTSAQRAEL IALTQALKMA EGKKLNVYTD SRYAFATAHV HGEIYRRRGL
     LTSEGREIKN KNEILALLKA LFLPKRLSII HCPGHQKGNS AEARGNRMAD QAAREAAMKA
     VLETSTLLIE DSTPYTPPHF HYTETDLKRL RELGATYNQT KGYWVLQGKP VMPDQSVFEL
     LDSLHRLTHL SPQKMKALLD REESPYYMLN RDRTIQYVTE TCTACAQVNA SKAKIGAGVR
     VRGHRPGTHW EVDFTEVKPG LYGYKYLLVF VDTFSGWVEA FPTKRETAKV VSKKLLEDIF
     PRFGMPQVLG SDNGPAFASQ VSQSVADLLG IDWKLHCAYR PQSSGQVERM NRTIKETLTK
     LTLASGTRDW VLLLPLALYR ARNTPGPHGL TPYEILYGAP PPLVNFHDPE MSKLTNSPSL
     QAHLQALQAV QQEVWKPLAA AYQDQLDQPV IPHPFRVGDA VWVRRHQTKN LEPRWKGPYT
     VLLTTPTALK VDGISAWIHA AHVKAATTPP AGTAWKVQRS QNPLKIRLTR GAP
 
 
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