POL_SRV2
ID POL_SRV2 Reviewed; 1768 AA.
AC P51517;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Gag-Pro-Pol polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p10;
DE Contains:
DE RecName: Full=Phosphorylated protein pp24;
DE Contains:
DE RecName: Full=Phosphorylated protein pp18;
DE Contains:
DE RecName: Full=p12;
DE Contains:
DE RecName: Full=Capsid protein p27;
DE Contains:
DE RecName: Full=Nucleocapsid protein-dUTPase;
DE Short=NC-dUTPase;
DE EC=3.6.1.23 {ECO:0000250|UniProtKB: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 Simian retrovirus SRV-2.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=39068;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2435057; DOI=10.1016/0042-6822(87)90274-1;
RA Thayer R.M., Power M.D., Bryant M.L., Gardner M.B., Barr P.J., Luciw P.A.;
RT "Sequence relationships of type D retroviruses which cause simian acquired
RT immunodeficiency syndrome.";
RL Virology 157:317-329(1987).
RN [2]
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 [3]
RP REVIEW (INTEGRASE).
RX PubMed=28458055; DOI=10.1016/j.sbi.2017.04.005;
RA Engelman A.N., Cherepanov P.;
RT "Retroviral intasomes arising.";
RL Curr. Opin. Struct. Biol. 47:23-29(2017).
CC -!- FUNCTION: [Matrix protein p10]: Matrix protein.
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:0000250|UniProtKB:P07570}.
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: [Nucleocapsid protein-dUTPase]: Homotrimer.
CC {ECO:0000250|UniProtKB:P07570}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protease 13 kDa]: Virion
CC {ECO: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=P51517-1; Sequence=Displayed;
CC Name=Gag-Pro polyprotein;
CC IsoId=P51518-1; Sequence=External;
CC Name=Gag polyprotein;
CC IsoId=P51516-1; 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 Phosphorylated protein pp24 and phosphorylated protein pp18 contains
CC one L domain: a PPXY motif which binds to the WW domains of the
CC ubiquitin ligase NEDD4. {ECO:0000250|UniProtKB:P07572}.
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: [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 -!- 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: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 -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC {ECO:0000305}.
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DR EMBL; M16605; AAA47562.1; -; Genomic_RNA.
DR SMR; P51517; -.
DR PRIDE; P51517; -.
DR Proteomes; UP000007229; Genome.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR CDD; cd05482; HIV_retropepsin_like; 1.
DR CDD; cd07557; trimeric_dUTPase; 1.
DR Gene3D; 1.10.10.200; -; 1.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.490; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR Gene3D; 2.30.30.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 2.70.40.10; -; 1.
DR Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.270; -; 2.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR003322; B_retro_matrix.
DR InterPro; IPR038124; B_retro_matrix_sf.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR000721; Gag_p24_N.
DR InterPro; IPR017856; Integrase-like_N.
DR InterPro; IPR036862; Integrase_C_dom_sf_retrovir.
DR InterPro; IPR001037; Integrase_C_retrovir.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR003308; Integrase_Zn-bd_dom_N.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR034170; Retropepsin-like_cat_dom.
DR InterPro; IPR018061; Retropepsins.
DR InterPro; IPR008916; Retrov_capsid_C.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR010661; RVT_thumb.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00692; dUTPase; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF02337; Gag_p10; 1.
DR Pfam; PF00607; Gag_p24; 1.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF00552; IN_DBD_C; 1.
DR Pfam; PF02022; Integrase_Zn; 1.
DR Pfam; PF00075; RNase_H; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF06817; RVT_thumb; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF46919; SSF46919; 1.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF50122; SSF50122; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF51283; SSF51283; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF57756; SSF57756; 2.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS51027; INTEGRASE_DBD; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
DR PROSITE; PS50876; ZF_INTEGRASE; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Coiled coil; DNA integration; DNA recombination;
KW DNA-binding; DNA-directed DNA polymerase; Endonuclease; Hydrolase;
KW Lipoprotein; Magnesium; Metal-binding; Multifunctional enzyme; Myristate;
KW Nuclease; Nucleotidyltransferase; Protease; Repeat;
KW Ribosomal frameshifting; RNA-binding; RNA-directed DNA polymerase;
KW Transferase; Viral genome integration; Viral matrix protein;
KW Viral nucleoprotein; Virion; Virus entry into host cell; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT CHAIN 2..1768
FT /note="Gag-Pro-Pol polyprotein"
FT /id="PRO_0000125499"
FT CHAIN 2..100
FT /note="Matrix protein p10"
FT /id="PRO_0000443169"
FT CHAIN 101..214
FT /note="Phosphorylated protein pp24"
FT /id="PRO_0000443170"
FT PROPEP 101..159
FT /evidence="ECO:0000305"
FT /id="PRO_0000443171"
FT CHAIN 160..214
FT /note="Phosphorylated protein pp18"
FT /id="PRO_0000443172"
FT CHAIN 215..297
FT /note="p12"
FT /id="PRO_0000443173"
FT CHAIN 298..523
FT /note="Capsid protein p27"
FT /id="PRO_0000443174"
FT CHAIN 524..756
FT /note="Nucleocapsid protein-dUTPase"
FT /id="PRO_0000443175"
FT CHAIN 757..908
FT /note="Protease 17 kDa"
FT /id="PRO_0000443176"
FT CHAIN 757..874
FT /note="Protease 13 kDa"
FT /id="PRO_0000443177"
FT PEPTIDE 875..908
FT /note="G-patch peptide"
FT /id="PRO_0000443178"
FT CHAIN 909..1493
FT /note="Reverse transcriptase/ribonuclease H"
FT /id="PRO_0000443179"
FT CHAIN 1494..1768
FT /note="Integrase"
FT /id="PRO_0000443180"
FT DOMAIN 777..853
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 864..910
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT DOMAIN 956..1144
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 1358..1489
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 1547..1708
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 544..561
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 1493..1534
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT DNA_BIND 1713..1762
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT REGION 132..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 215..251
FT /evidence="ECO:0000255"
FT MOTIF 200..203
FT /note="PPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P07572"
FT ACT_SITE 782
FT /note="Protease; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT BINDING 1021
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 1096
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 1097
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 1367
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 1396
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 1417
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 1481
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 1502
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1506
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1530
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1533
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1558
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 1615
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 1651
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000250|UniProtKB:P03354"
FT SITE 100..101
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 159..160
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 214..215
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 297..298
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 523..524
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 756..757
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07572"
FT SITE 874..875
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07572"
FT SITE 908..909
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07572"
FT SITE 1493..1494
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03365"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:P11283"
SQ SEQUENCE 1768 AA; 197910 MW; E8FC5408EA62444A CRC64;
MGQELSQHEL YVEQLKKALK TRGVKVKGND LLKFFDFVKD TCPWFPQEGT IDIKRWRRVG
DCFQDYYNTF GPEKIPVTAF SYWNLIKDLI DKKEADPQVM AAVTQTEKIL KVSSQTDLRD
NSHNKDMDLI SLESDDEEAK APSEKMTMSN KSPKKYPAML ASQNNNTDKD PDLSEVDWDG
LEDEAAKYHN PDWPPFLSRP PPYNRTAATA PAVMAVVNPK EELKEKISQL EEQIKLEELH
QSLIIRLQKL KTGNERVTSS GNIESHSRTP KWPGQCLPKG KYLINKNTEE YPPKDIFPVT
ETMDGQGQAW RHHNGFDFTV IKELKTAVSQ YGATAPYTLA IVESIADNWL TPTDWNTLVR
AVLSGGDHLI WKSEFFENCR DTAKRNQQAG NGWDFDMLTG SGNYANTDAQ MQYDPGLFAQ
IQAAATNAWR KLPVKGDPGA SLTGVKQGPD EPFADFVHRL ITTAGRIFGN AEAGVDYVKQ
LAYENANPAC QAAIRPYRKK TDLTGYIRLC SDIGPSYQQG LAMAAAFSGQ TVKDLLNNKN
KDRGGCFKCG KKGHFAKDCR DHSNKNPESK VPGLCPRCKR GKHWANECKS KTDSQGNPLP
PHQGNRDEGP APGPEASLWG SQLCSSQQQQ SISKLNRASP GSAGLDLCST THTVLTPEMG
PQTLATGVYG PLPPNTFGLI LGRGSTTVKG LQIYPGVIDN DYTGEFKIMA RAISSIITIP
QGERIAQLVL LPLLRTAHKI QHPYRGDKNF GSSDIFWVQP ITHQKPSLVL WLDGKAFTGL
IDTGADVTII KQEDWPSHWP TTETLTNLRG IGQSNNPRQS SKYLTWKDKE NNSGLIKPFV
IPNLPVNLWG RDLLSQMKIM MCSPNDIVTA QMLAQGYSPG KGLGKREDGI LQPIPNSGQL
DRKGFGNFLA TAVDILAPQR YADPITWKSD EPVWVDQWPL TQEKLAAAQQ LVQEQLQAGH
IIESNSPWNT PIFVIKKKSG KWRLLQDLRA VNATMVLMGA LQPGLPSPVA IPQGYFKIVI
DLKDCFFTIP LQPVDQKRFA FSLPSTNFKQ PMKRYQWKVL PQGMANSPTL CQKYVAAAIE
PVRKSWAQMY IIHYMDDILI AGKLGEQVLQ CFAQLKQALT TTGLQIAPEK VQLQDPYTYL
GFQINGPKIT NQKAVIRRDK LQTLNDFQKL LGDINWLRPY LHLTTGDLKP LFDILKGDSN
PNSPRSLSEA ALASLQKVET AIAEQFVTQI DYTQPLTFLI FNTTLTPTGL FWQNNPVMWV
HLPASPKKVL LPYYDAIADL IILGRDNSKK YFGLEPSTII QPYSKSQIHW LMQNTETWPI
ACASYAGNID NHYPPNKLIQ FCKLHAVVFP RIISKTPLDN ALLVFTDGSS TGIAAYTFEK
TTVRFKTSHT SAQLVELQAL IAVLSAFPHR ALNVYTDSAY LAHSIPLLET VSHIKHISDT
AKFFLQCQQL IYNRSIPFYL GHIRAHSGLP GPLSQGNHIT DLATKVVATT LTTNLTEAQT
AHALHHLNAQ SLRLMFKITR EQARQIVKQC PTCVTYLPIP HFGVNPKGLV PNMLWQMDVT
HYSEFGKLKY VHVSIDTFSG FLVATLQTGE ATKHVIAHLL HCFSIIGQPI HIKTDNGPGY
TSSNFRAFCS KLHIKHTFGI PYNPQGQGIV ERAHLSLKNT LEKIKKGEWY PTQGSPRNIL
NHALFILNFL NLDAQNKSAA DRFWHTSSKK EYAMVKWKDP LDNTWHGPDP VLIWGRGSVC
VYSQTHDAAR WLPERLVRQV SNVTQSRE
