ID POL_MLVMS Reviewed; 1738 AA. AC P03355; O92808; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 31-JAN-2018, sequence version 5. DT 27-MAR-2024, entry version 196. 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-Pol; DE Short=NC-pol; DE Contains: DE RecName: Full=Protease; DE Short=PR; DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275, ECO:0000269|PubMed:16603535, ECO:0000269|PubMed:3885215}; DE AltName: Full=p14; 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 AltName: Full=p80; DE Contains: DE RecName: Full=Integrase; DE Short=IN; DE EC=2.7.7.- {ECO:0000305|PubMed:11559787}; DE EC=3.1.-.- {ECO:0000305|PubMed:11559787}; DE AltName: Full=p46; GN Name=gag-pol; OS Moloney murine leukemia virus (isolate Shinnick) (MoMLV). OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus; OC Murine leukemia virus. OX NCBI_TaxID=928306; OH NCBI_TaxID=10090; Mus musculus (Mouse). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Clone PMLV-1; RX PubMed=6169994; DOI=10.1038/293543a0; RA Shinnick T.M., Lerner R.A., Sutcliffe J.G.; RT "Nucleotide sequence of Moloney murine leukaemia virus."; RL Nature 293:543-548(1981). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RA Chappey C.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 2-31, AND MYRISTOYLATION AT GLY-2. RX PubMed=6340098; DOI=10.1073/pnas.80.2.339; RA Henderson L.E., Krutzsch H.C., Oroszlan S.; RT "Myristyl amino-terminal acylation of murine retrovirus proteins: an RT unusual post-translational proteins modification."; RL Proc. Natl. Acad. Sci. U.S.A. 80:339-343(1983). RN [4] RP PROTEIN SEQUENCE OF 479-529. RX PubMed=6267042; DOI=10.1016/s0021-9258(19)68857-5; RA Henderson L.E., Copeland T.D., Sowder R.C., Smythers G.W., Oroszlan S.; RT "Primary structure of the low molecular weight nucleic acid-binding RT proteins of murine leukemia viruses."; RL J. Biol. Chem. 256:8400-8406(1981). RN [5] RP PROTEIN SEQUENCE OF 535-554, CATALYTIC ACTIVITY (PROTEASE), AND READTHROUGH RP OF AMBER CODON. RX PubMed=3885215; DOI=10.1073/pnas.82.6.1618; RA Yoshinaka Y., Katoh I., Copeland T.D., Oroszlan S.; RT "Murine leukemia virus protease is encoded by the gag-pol gene and is RT synthesized through suppression of an amber termination codon."; RL Proc. Natl. Acad. Sci. U.S.A. 82:1618-1622(1985). RN [6] RP FUNCTION (INTEGRASE). RX PubMed=11559787; DOI=10.1128/jvi.75.20.9561-9570.2001; RA Yang F., Roth M.J.; RT "Assembly and catalysis of concerted two-end integration events by Moloney RT murine leukemia virus integrase."; RL J. Virol. 75:9561-9570(2001). RN [7] RP SUBUNIT (CAPSID PROTEIN P30). RX PubMed=12093170; DOI=10.1006/viro.2002.1452; RA Mayo K., McDermott J., Barklis E.; RT "Hexagonal organization of Moloney murine leukemia virus capsid proteins."; RL Virology 298:30-38(2002). RN [8] RP PHOSPHORYLATION AT SER-192, AND MUTAGENESIS OF SER-137; SER-148; SER-150; RP SER-192; SER-196; SER-209 AND SER-212. RX PubMed=12525616; DOI=10.1128/jvi.77.3.1820-1829.2003; RA Yueh A., Goff S.P.; RT "Phosphorylated serine residues and an arginine-rich domain of the moloney RT murine leukemia virus p12 protein are required for early events of viral RT infection."; RL J. Virol. 77:1820-1829(2003). RN [9] RP FUNCTION (PROTEASE). RX PubMed=14610163; DOI=10.1128/jvi.77.23.12392-12400.2003; RA Alvarez E., Menendez-Arias L., Carrasco L.; RT "The eukaryotic translation initiation factor 4GI is cleaved by different RT retroviral proteases."; RL J. Virol. 77:12392-12400(2003). RN [10] RP INTERACTION WITH MOUSE RELEASE FACTOR ETF1 (REVERSE RP TRANSCRIPTASE/RIBONUCLEASE H). RX PubMed=14636559; DOI=10.1016/s0092-8674(03)00805-5; RA Orlova M., Yueh A., Leung J., Goff S.P.; RT "Reverse transcriptase of Moloney murine leukemia virus binds to eukaryotic RT release factor 1 to modulate suppression of translational termination."; RL Cell 115:319-331(2003). RN [11] RP SUBUNIT (INTEGRASE). RX PubMed=14599799; DOI=10.1016/s0042-6822(03)00559-2; RA Villanueva R.A., Jonsson C.B., Jones J., Georgiadis M.M., Roth M.J.; RT "Differential multimerization of Moloney murine leukemia virus integrase RT purified under nondenaturing conditions."; RL Virology 316:146-160(2003). RN [12] RP INTERACTION WITH MOUSE NEDD4; TSG101 AND PDCD6IP/ALIX (GAG-POL RP POLYPROTEIN), AND MUTAGENESIS OF TYR-165. RX PubMed=15908698; DOI=10.1074/jbc.m413735200; RA Segura-Morales C., Pescia C., Chatellard-Causse C., Sadoul R., Bertrand E., RA Basyuk E.; RT "Tsg101 and Alix interact with murine leukemia virus Gag and cooperate with RT Nedd4 ubiquitin ligases during budding."; RL J. Biol. Chem. 280:27004-27012(2005). RN [13] RP INTERACTION WITH UBE2I AND PIAS4 (CAPSID PROTEIN P30), AND SUMOYLATION RP (CAPSID PROTEIN P30). RX PubMed=16352559; DOI=10.1128/jvi.80.1.342-352.2006; RA Yueh A., Leung J., Bhattacharyya S., Perrone L.A., de los Santos K., RA Pu S.-Y., Goff S.P.; RT "Interaction of moloney murine leukemia virus capsid with Ubc9 and PIASy RT mediates SUMO-1 addition required early in infection."; RL J. Virol. 80:342-352(2006). RN [14] RP PROTEOLYTIC CLEAVAGE (GAG-POL POLYPROTEIN), BIOPHYSICOCHEMICAL PROPERTIES RP (PROTEASE), ACTIVITY REGULATION (PROTEASE), CATALYTIC ACTIVITY (PROTEASE), RP CHARACTERIZATION (PROTEASE), AND SUBCELLULAR LOCATION (PROTEASE). RX PubMed=16603535; DOI=10.1099/vir.0.81382-0; RA Feher A., Boross P., Sperka T., Miklossy G., Kadas J., Bagossi P., RA Oroszlan S., Weber I.T., Tozser J.; RT "Characterization of the murine leukemia virus protease and its comparison RT with the human immunodeficiency virus type 1 protease."; RL J. Gen. Virol. 87:1321-1330(2006). RN [15] RP FUNCTION (RNA-BINDING PHOSPHOPROTEIN P12), AND SUBCELLULAR LOCATION RP (RNA-BINDING PHOSPHOPROTEIN P12). RX PubMed=21085616; DOI=10.1371/journal.ppat.1001183; RA Prizan-Ravid A., Elis E., Laham-Karam N., Selig S., Ehrlich M., RA Bacharach E.; RT "The Gag cleavage product, p12, is a functional constituent of the murine RT leukemia virus pre-integration complex."; RL PLoS Pathog. 6:E1001183-E1001183(2010). RN [16] RP FUNCTION (RNA-BINDING PHOSPHOPROTEIN P12), SUBCELLULAR LOCATION RP (RNA-BINDING PHOSPHOPROTEIN P12), AND MUTAGENESIS OF SER-192 AND SER-196. RX PubMed=23300449; DOI=10.1371/journal.ppat.1003103; RA Elis E., Ehrlich M., Prizan-Ravid A., Laham-Karam N., Bacharach E.; RT "p12 tethers the murine leukemia virus pre-integration complex to mitotic RT chromosomes."; RL PLoS Pathog. 8:E1003103-E1003103(2012). RN [17] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 683-937. RX PubMed=8535782; DOI=10.1016/s0969-2126(01)00223-4; RA Georgiadis M.M., Jessen S.M., Ogata C.M., Telesnitsky A., Goff S.P., RA Hendrickson W.A.; RT "Mechanistic implications from the structure of a catalytic fragment of RT Moloney murine leukemia virus reverse transcriptase."; RL Structure 3:879-892(1995). RN [18] {ECO:0007744|PDB:1D0E, ECO:0007744|PDB:1QAI, ECO:0007744|PDB:1QAJ} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 669-933 IN COMPLEX WITH DNA. RX PubMed=10669612; DOI=10.1006/jmbi.1999.3477; RA Najmudin S., Cote M.L., Sun D., Yohannan S., Montano S.P., Gu J., RA Georgiadis M.M.; RT "Crystal structures of an N-terminal fragment from Moloney murine leukemia RT virus reverse transcriptase complexed with nucleic acid: functional RT implications for template-primer binding to the fingers domain."; RL J. Mol. Biol. 296:613-632(2000). RN [19] {ECO:0007744|PDB:1I6J} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 683-937 IN COMPLEX WITH DNA. RX PubMed=11526315; DOI=10.1107/s090744490100943x; RA Cote M.L., Georgiadis M.M.; RT "Structure of a pseudo-16-mer DNA with stacked guanines and two G-A RT mispairs complexed with the N-terminal fragment of Moloney murine leukemia RT virus reverse transcriptase."; RL Acta Crystallogr. D 57:1238-1250(2001). RN [20] {ECO:0007744|PDB:1NND} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 683-937 IN COMPLEX WITH DNA. RX PubMed=15326591; DOI=10.1002/prot.20224; RA Crowther R.L., Remeta D.P., Minetti C.A., Das D., Montano S.P., RA Georgiadis M.M.; RT "Structural and energetic characterization of nucleic acid-binding to the RT fingers domain of Moloney murine leukemia virus reverse transcriptase."; RL Proteins 57:15-26(2004). RN [21] {ECO:0007744|PDB:4MH8} RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 683-1330. RX PubMed=15130474; DOI=10.1016/j.str.2004.02.032; RA Das D., Georgiadis M.M.; RT "The crystal structure of the monomeric reverse transcriptase from Moloney RT murine leukemia virus."; RL Structure 12:819-829(2004). RN [22] {ECO:0007744|PDB:2HB5} RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 1157-1330, COFACTOR (REVERSE RP TRANSCRIPTASE/RIBONUCLEASE H), AND ACTIVE SITE (REVERSE RP TRANSCRIPTASE/RIBONUCLEASE H). RX PubMed=16912289; DOI=10.1128/jvi.00750-06; RA Lim D., Gregorio G.G., Bingman C., Martinez-Hackert E., Hendrickson W.A., RA Goff S.P.; RT "Crystal structure of the moloney murine leukemia virus RNase H domain."; RL J. Virol. 80:8379-8389(2006). RN [23] {ECO:0007744|PDB:2FVP, ECO:0007744|PDB:2FVQ, ECO:0007744|PDB:2FVR, ECO:0007744|PDB:2FVS} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 683-937, AND FUNCTION RP (INTEGRASE). RX PubMed=17003051; DOI=10.1093/nar/gkl693; RA Montano S.P., Cote M.L., Roth M.J., Georgiadis M.M.; RT "Crystal structures of oligonucleotides including the integrase processing RT site of the Moloney murine leukemia virus."; RL Nucleic Acids Res. 34:5353-5360(2006). RN [24] {ECO:0007744|PDB:2MQV, ECO:0007744|PDB:2MS0, ECO:0007744|PDB:2MS1} RP STRUCTURE BY NMR OF 479-534 IN COMPLEX WITH ZINC, AND FUNCTION RP (NUCLEOCAPSID PROTEIN P10-POL). RX PubMed=25209668; DOI=10.1038/nature13709; RA Miller S.B., Yildiz F.Z., Lo J.A., Wang B., D'Souza V.M.; RT "A structure-based mechanism for tRNA and retroviral RNA remodelling during RT primer annealing."; RL Nature 515:591-595(2014). RN [25] {ECO:0007744|PDB:5DMQ, ECO:0007744|PDB:5DMR} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1159-1330 IN COMPLEX WITH ETF1, RP INTERACTION WITH ETF1 (REVERSE TRANSCRIPTASE/RIBONUCLEASE H), MUTAGENESIS RP OF ARG-1244; PHE-1247 AND ALA-1248, AND READTHROUGH OF AMBER CODON. RX PubMed=27329342; DOI=10.1038/ncomms12070; RA Tang X., Zhu Y., Baker S.L., Bowler M.W., Chen B.J., Chen C., Hogg J.R., RA Goff S.P., Song H.; RT "Structural basis of suppression of host translation termination by Moloney RT murine leukemia Virus."; RL Nat. Commun. 7:12070-12070(2016). RN [26] {ECO:0007744|PDB:3NNQ, ECO:0007744|PDB:4NZG} RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1338-1435 IN COMPLEX WITH ZINC. RX PubMed=28066922; DOI=10.1002/prot.25245; RA Guan R., Aiyer S., Cote M.L., Xiao R., Jiang M., Acton T.B., Roth M.J., RA Montelione G.T.; RT "X-ray crystal structure of the N-terminal region of Moloney murine RT leukemia virus integrase and its implications for viral DNA recognition."; RL Proteins 85:647-656(2017). RN [27] {ECO:0007744|PDB:7JQ8} RP STRUCTURE BY NMR OF 1716-1738 IN COMPLEX WITH HOST BRD3, AND INTERACTION RP WITH HOST BRD3. RX PubMed=33592170; DOI=10.1016/j.str.2021.01.010; RA Aiyer S., Swapna G.V.T., Ma L.C., Liu G., Hao J., Chalmers G., Jacobs B.C., RA Montelione G.T., Roth M.J.; RT "A common binding motif in the ET domain of BRD3 forms polymorphic RT structural interfaces with host and viral proteins."; RL Structure 29:886-898(2021). CC -!- FUNCTION: [Gag-Pol polyprotein]: Plays a role in budding and is CC processed by the viral protease during virion maturation outside the CC cell. During budding, it recruits, in a PPXY-dependent or independent CC manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules CC to Gag-Pol, or to Gag-Pol binding host factors. Interaction with HECT CC ubiquitin ligases probably links the viral protein to the host ESCRT CC pathway and facilitates release. {ECO:0000250|UniProtKB:P03332}. 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 pre-integration complex. CC {ECO:0000250|UniProtKB:P03332}. CC -!- FUNCTION: [RNA-binding phosphoprotein p12]: Constituent of the pre- CC integration complex (PIC) which tethers the latter to mitotic CC chromosomes. This allows the integration of the viral genome into the CC host DNA. {ECO:0000269|PubMed:21085616, ECO:0000269|PubMed:23300449}. CC -!- FUNCTION: [Capsid protein p30]: Forms the spherical core of the virion CC that encapsulates the genomic RNA-nucleocapsid complex. CC {ECO:0000250|UniProtKB:P03336}. CC -!- FUNCTION: [Nucleocapsid protein p10-Pol]: Involved in the packaging and CC encapsidation of two copies of the genome (By similarity). Binds with CC high affinity to conserved UCUG elements within the packaging signal, CC located near the 5'-end of the genome (By similarity). This binding is CC dependent on genome dimerization (By similarity). Acts as a nucleic CC acid chaperone which is involved in rearrangement of nucleic acid CC secondary structures during gRNA retrotranscription (PubMed:25209668). CC {ECO:0000250|UniProtKB:P03332, ECO:0000269|PubMed:25209668}. 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 (PubMed:14610163). {ECO:0000255|PROSITE- CC ProRule:PRU00275, ECO:0000269|PubMed:14610163}. 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 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. {ECO:0000255}. 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. {ECO:0000305|PubMed:11559787, CC ECO:0000305|PubMed:17003051}. 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:0000255|PROSITE- CC ProRule:PRU00405}; CC Note=The RT polymerase active site binds 2 magnesium ions. CC {ECO:0000255|PROSITE-ProRule:PRU00405}; CC -!- COFACTOR: [Reverse transcriptase/ribonuclease H]: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:Q2F7J3}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:16912289}; CC Note=Binds 2 Mn(2+)/Mg(2+) ions for ribonuclease H (RNase H) activity. CC {ECO:0000250|UniProtKB:Q2F7J3}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; CC Note=Magnesium ions are required for integrase activity. Binds at least CC 1, maybe 2 magnesium ions. {ECO:0000305}; CC -!- ACTIVITY REGULATION: [Protease]: Most efficiently inhibited by CC Amprenavir, which is able to block Gag-Pol processing in infected CC cells. {ECO:0000269|PubMed:16603535}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 5.0 for protease activity. CC {ECO:0000269|PubMed:16603535}; CC -!- SUBUNIT: [Capsid protein p30]: Homohexamer; further associates as CC homomultimer (By similarity). The virus core is composed of a lattice CC formed from hexagonal rings, each containing six capsid monomers CC (PubMed:12093170). Interacts with mouse UBE2I and mouse PIAS4 CC (PubMed:16352559). {ECO:0000250|UniProtKB:P03336, CC ECO:0000269|PubMed:12093170, ECO:0000269|PubMed:16352559}. CC -!- SUBUNIT: [Gag-Pol polyprotein]: Interacts (via PPXY motif) with host CC NEDD4 (PubMed:15908698). Interacts (via PSAP motif) with host TSG101 CC (PubMed:15908698). Interacts (via LYPX(n)L motif) with host PDCD6IP CC (PubMed:15908698). {ECO:0000269|PubMed:15908698}. CC -!- SUBUNIT: [Reverse transcriptase/ribonuclease H]: The reverse CC transcriptase is a monomer (Potential). Interacts (via RNase domains) CC with host release factor ETF1; this interaction is essential for CC translational readthrough of amber codon between viral gag and pol CC genes, as well as for viral replication (PubMed:14636559, CC PubMed:27329342). {ECO:0000269|PubMed:14636559, CC ECO:0000269|PubMed:27329342}. CC -!- SUBUNIT: [Integrase]: Homodimer (PubMed:14599799). Interacts with host CC BRD3 (via NET domain) (PubMed:33592170). {ECO:0000269|PubMed:14599799, CC ECO:0000269|PubMed:33592170}. CC -!- SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Virion CC {ECO:0000250|UniProtKB:P03332}. Host cell membrane CC {ECO:0000250|UniProtKB:P03332}; Lipid-anchor CC {ECO:0000250|UniProtKB:P03332}. Host late endosome membrane CC {ECO:0000250|UniProtKB:P03332}; Lipid-anchor CC {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular body CC {ECO:0000250|UniProtKB:P26807}. Note=These locations are probably CC linked to virus assembly sites. {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-Pol]: Virion CC {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Protease]: Virion {ECO:0000269|PubMed:16603535}. CC -!- SUBCELLULAR LOCATION: [RNA-binding phosphoprotein p12]: Host cytoplasm CC {ECO:0000269|PubMed:21085616, ECO:0000269|PubMed:23300449}. CC Note=Localizes to the host cytoplasm early in infection and binds to CC the mitotic chromosomes later on. {ECO:0000269|PubMed:21085616, CC ECO:0000269|PubMed:23300449}. 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 RNA-binding phosphoprotein p12 contains one L domain: a PPXY motif CC which potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin CC ligase. PPXY motif is essential for virus egress. Matrix protein p15 CC contains one L domain: a PTAP/PSAP motif, which potentially interacts CC with the UEV domain of TSG101. The junction between the matrix protein CC p15 and RNA-binding phosphoprotein p12 also contains one L domain: a CC LYPX(n)L motif which potentially interacts with PDCD6IP. Both PSAP and CC LYPX(n)L domains might play little to no role in budding and possibly CC drive residual virus release. contains. {ECO:0000250|UniProtKB:P03332}. CC -!- PTM: [Gag-Pol polyprotein]: Ubiquitinated by ITCH. Gag can recruit the CC ubiquitin ligase Itch in an L domain-independent manner to facilitate CC virus release via a mechanism that involves Gag ubiquitination. CC {ECO:0000250|UniProtKB:P03332}. CC -!- PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral CC protease yield mature proteins. The protease is released by CC autocatalytic cleavage. The polyprotein is cleaved during and after CC budding, this process is termed maturation. CC {ECO:0000269|PubMed:16603535}. CC -!- PTM: [Capsid protein p30]: Sumoylated; which is required for virus CC replication. {ECO:0000269|PubMed:16352559}. CC -!- PTM: [RNA-binding phosphoprotein p12]: Phosphorylated on serine CC residues. {ECO:0000269|PubMed:12525616}. CC -!- MISCELLANEOUS: [Gag-Pol polyprotein]: This protein is translated as a CC gag-pol fusion protein by episodic readthrough of the gag protein CC termination codon. Readthrough of the terminator codon TAG occurs CC between the codons for 538-Asp and 540-Gly. CC {ECO:0000269|PubMed:27329342, ECO:0000269|PubMed:3885215}. CC -!- MISCELLANEOUS: [Nucleocapsid protein p10-Pol]: Nucleocapsid protein CC p10-Pol released from Pol polyprotein (NC-pol) is a few amino acids CC shorter than the nucleocapsid protein p10 released from Gag polyprotein CC (NC-gag). {ECO:0000305}. 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 -!- SEQUENCE CAUTION: CC Sequence=AAC82568.2; Type=Miscellaneous discrepancy; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF033811; AAC82568.2; ALT_SEQ; Genomic_RNA. DR EMBL; J02255; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR PIR; A03956; GNMV1M. DR RefSeq; NP_057933.2; NC_001501.1. DR PDB; 1D0E; X-ray; 3.00 A; A/B=683-937. DR PDB; 1D1U; X-ray; 2.30 A; A=683-937. DR PDB; 1I6J; X-ray; 2.00 A; A=683-937. DR PDB; 1MML; X-ray; 1.80 A; A=669-933. DR PDB; 1N4L; X-ray; 2.00 A; A=683-937. DR PDB; 1NND; X-ray; 2.30 A; A=683-937. DR PDB; 1QAI; X-ray; 2.30 A; A/B=669-933. DR PDB; 1QAJ; X-ray; 2.30 A; A/B=683-937. DR PDB; 1ZTT; X-ray; 1.85 A; A=683-937. DR PDB; 1ZTW; X-ray; 1.80 A; A=683-937. DR PDB; 2FJV; X-ray; 2.05 A; A=683-937. DR PDB; 2FJW; X-ray; 1.95 A; A=683-937. DR PDB; 2FJX; X-ray; 1.80 A; A=683-937. DR PDB; 2FVP; X-ray; 2.25 A; A=683-937. DR PDB; 2FVQ; X-ray; 2.30 A; A=683-937. DR PDB; 2FVR; X-ray; 2.20 A; A=683-937. DR PDB; 2FVS; X-ray; 2.35 A; A=683-937. DR PDB; 2HB5; X-ray; 1.59 A; A=1157-1330. DR PDB; 2M9U; NMR; -; A=1659-1738. DR PDB; 2MQV; NMR; -; A=479-534. DR PDB; 2MS0; NMR; -; A/C=479-534. DR PDB; 2MS1; NMR; -; A=479-534. DR PDB; 2R2R; X-ray; 2.10 A; A=683-937. DR PDB; 2R2S; X-ray; 2.80 A; A=683-937. DR PDB; 2R2T; X-ray; 2.00 A; A=683-937. DR PDB; 2R2U; X-ray; 2.30 A; A=683-937. DR PDB; 3FSI; X-ray; 1.75 A; A=683-937. DR PDB; 3NNQ; X-ray; 2.69 A; A/B=1331-1435. DR PDB; 4M94; X-ray; 2.14 A; A=683-937. DR PDB; 4M95; X-ray; 1.72 A; A=683-937. DR PDB; 4MH8; X-ray; 3.00 A; A=683-1330. DR PDB; 4NZG; X-ray; 2.15 A; A/B/C/D=1338-1435. DR PDB; 4XO0; X-ray; 1.70 A; A=683-937. DR PDB; 4XPC; X-ray; 1.68 A; A=683-937. DR PDB; 4XPE; X-ray; 1.78 A; A=683-937. DR PDB; 5DMQ; X-ray; 4.00 A; A=683-1330. DR PDB; 5DMR; X-ray; 2.80 A; A=1159-1330. DR PDB; 5VBS; X-ray; 1.75 A; A=683-937. DR PDB; 6B1Q; X-ray; 1.90 A; A=683-937. DR PDB; 6B1R; X-ray; 1.69 A; A=683-937. DR PDB; 6B1S; X-ray; 2.00 A; A/B=683-937. DR PDB; 6GZA; X-ray; 1.89 A; A/B=347-433. DR PDB; 6MIG; X-ray; 1.70 A; A=683-937. DR PDB; 6MIH; X-ray; 1.60 A; A=683-937. DR PDB; 6MIK; X-ray; 1.70 A; A=683-937. DR PDB; 7JQ8; NMR; -; B=1716-1738. DR PDB; 8DW1; X-ray; 1.85 A; A=683-937. DR PDB; 8DW8; X-ray; 2.58 A; A=683-937. DR PDB; 8DWM; X-ray; 2.99 A; A=683-937. DR PDBsum; 1D0E; -. DR PDBsum; 1D1U; -. DR PDBsum; 1I6J; -. DR PDBsum; 1MML; -. DR PDBsum; 1N4L; -. DR PDBsum; 1NND; -. DR PDBsum; 1QAI; -. DR PDBsum; 1QAJ; -. DR PDBsum; 1ZTT; -. DR PDBsum; 1ZTW; -. DR PDBsum; 2FJV; -. DR PDBsum; 2FJW; -. DR PDBsum; 2FJX; -. DR PDBsum; 2FVP; -. DR PDBsum; 2FVQ; -. DR PDBsum; 2FVR; -. DR PDBsum; 2FVS; -. DR PDBsum; 2HB5; -. DR PDBsum; 2M9U; -. DR PDBsum; 2MQV; -. DR PDBsum; 2MS0; -. DR PDBsum; 2MS1; -. DR PDBsum; 2R2R; -. DR PDBsum; 2R2S; -. DR PDBsum; 2R2T; -. DR PDBsum; 2R2U; -. DR PDBsum; 3FSI; -. DR PDBsum; 3NNQ; -. DR PDBsum; 4M94; -. DR PDBsum; 4M95; -. DR PDBsum; 4MH8; -. DR PDBsum; 4NZG; -. DR PDBsum; 4XO0; -. DR PDBsum; 4XPC; -. DR PDBsum; 4XPE; -. DR PDBsum; 5DMQ; -. DR PDBsum; 5DMR; -. DR PDBsum; 5VBS; -. DR PDBsum; 6B1Q; -. DR PDBsum; 6B1R; -. DR PDBsum; 6B1S; -. DR PDBsum; 6GZA; -. DR PDBsum; 6MIG; -. DR PDBsum; 6MIH; -. DR PDBsum; 6MIK; -. DR PDBsum; 7JQ8; -. DR PDBsum; 8DW1; -. DR PDBsum; 8DW8; -. DR PDBsum; 8DWM; -. DR BMRB; P03355; -. DR SMR; P03355; -. DR ELM; P03355; -. DR ChEMBL; CHEMBL3562; -. DR DrugBank; DB07499; N-(4-{[amino(imino)methyl]amino}butyl)-2,4'-bi-1,3-thiazole-4-carboxamide. DR DrugBank; DB08331; N-1H-imidazol-2-yl-N'-[4-(1H-imidazol-2-ylamino)phenyl]benzene-1,4-diamine. DR MEROPS; A02.008; -. DR iPTMnet; P03355; -. DR PhosphoSitePlus; P03355; -. DR SwissPalm; P03355; -. DR GeneID; 2193424; -. DR KEGG; vg:2193424; -. DR BRENDA; 2.7.7.49; 3393. DR BRENDA; 3.1.13.2; 3393. DR BRENDA; 3.1.26.4; 3393. DR BRENDA; 3.4.23.B5; 3393. DR EvolutionaryTrace; P03355; -. DR PRO; PR:P03355; -. DR Proteomes; UP000006625; Segment. DR Proteomes; UP000180702; Genome. DR GO; GO:0044185; C:host cell late endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0032993; C:protein-DNA complex; IMP:CAFA. 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; IMP:CAFA. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0044824; F:retroviral 3' processing activity; IMP:CAFA. 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:0006308; P:DNA catabolic process; IMP:CAFA. 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; IMP:CAFA. DR GO; GO:0019068; P:virion assembly; IEA:InterPro. DR CDD; cd09273; RNase_HI_RT_Bel; 1. DR CDD; cd06095; RP_RTVL_H_like; 1. DR CDD; cd03715; RT_ZFREV_like; 1. DR Gene3D; 1.10.340.70; -; 1. DR Gene3D; 2.30.30.850; -; 1. DR Gene3D; 3.10.20.370; -; 1. DR Gene3D; 3.30.70.270; -; 2. DR Gene3D; 2.40.70.10; Acid Proteases; 1. DR Gene3D; 1.10.150.180; Gamma-retroviral matrix domain; 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; 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 PANTHER; PTHR33166; GAG_P30 DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR33166:SF8; POM121 TRANSMEMBRANE NUCLEOPORIN LIKE 2; 1. 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; SSF50630; Acid proteases; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF47836; Retroviral matrix proteins; 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; 2. 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 1: Evidence at protein level; KW 3D-structure; Aspartyl protease; Capsid protein; Coiled coil; KW Direct protein sequencing; DNA integration; DNA recombination; DNA-binding; KW DNA-directed DNA polymerase; Endonuclease; KW Eukaryotic host gene expression shutoff by virus; KW Eukaryotic host translation shutoff by virus; Host cell membrane; KW Host cytoplasm; Host endosome; Host gene expression shutoff by virus; KW Host membrane; Host-virus interaction; Hydrolase; Lipoprotein; Magnesium; KW Manganese; Membrane; Metal-binding; Multifunctional enzyme; Myristate; KW Nuclease; Nucleotidyltransferase; Phosphoprotein; Protease; KW Reference proteome; RNA suppression of termination; RNA-binding; KW RNA-directed DNA polymerase; Transferase; Ubl conjugation; KW Viral genome integration; Viral matrix protein; Viral nucleoprotein; KW Virion; Virus entry into host cell; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed; by host" FT /evidence="ECO:0000255, ECO:0000269|PubMed:6340098" FT CHAIN 2..1738 FT /note="Gag-Pol polyprotein" FT /id="PRO_0000390795" FT CHAIN 2..131 FT /note="Matrix protein p15" FT /id="PRO_5000053618" FT CHAIN 132..215 FT /note="RNA-binding phosphoprotein p12" FT /id="PRO_5000053619" FT CHAIN 216..478 FT /note="Capsid protein p30" FT /id="PRO_5000053620" FT CHAIN 479..534 FT /note="Nucleocapsid protein p10-Pol" FT /id="PRO_5000053621" FT CHAIN 535..659 FT /note="Protease" FT /id="PRO_5000053622" FT CHAIN 660..1330 FT /note="Reverse transcriptase/ribonuclease H" FT /id="PRO_5000053623" FT CHAIN 1331..1738 FT /note="Integrase" FT /id="PRO_5000053624" FT DOMAIN 560..631 FT /note="Peptidase A2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275" FT DOMAIN 741..932 FT /note="Reverse transcriptase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405" FT DOMAIN 1174..1320 FT /note="RNase H type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408" FT DOMAIN 1444..1602 FT /note="Integrase catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457" FT ZN_FING 502..519 FT /note="CCHC-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047, FT ECO:0000305|PubMed:25209668" FT ZN_FING 1387..1427 FT /note="HHCC-type" FT /evidence="ECO:0000305|PubMed:28066922" FT REGION 108..220 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 345..393 FT /note="Interaction with host PIAS4" FT /evidence="ECO:0000250|UniProtKB:P03332" FT REGION 430..435 FT /note="Interaction with host UBE2I" FT /evidence="ECO:0000250|UniProtKB:P03332" FT REGION 434..500 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 513..552 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 438..478 FT /evidence="ECO:0000255" FT MOTIF 111..114 FT /note="PTAP/PSAP motif" FT /evidence="ECO:0000250|UniProtKB:P03332" FT MOTIF 130..134 FT /note="LYPX(n)L motif" FT /evidence="ECO:0000250|UniProtKB:P03332" FT MOTIF 162..165 FT /note="PPXY motif" FT /evidence="ECO:0000250|UniProtKB:P03332" FT COMPBIAS 108..127 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 206..220 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 434..476 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 566 FT /note="Protease; shared with dimeric partner" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275" FT BINDING 723 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /ligand_note="RNA template" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 773 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /ligand_note="RNA template" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 775 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /ligand_note="RNA template" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 789 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /ligand_note="RNA template" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 809 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 853 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /ligand_note="RNA template" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 855 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /ligand_note="RNA template" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 883 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 884 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 943 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_note="DNA primer" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 957 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_note="DNA primer" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 960 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_note="DNA primer" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 968 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_note="DNA primer" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 1056 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /ligand_note="RNA template" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 1057 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /ligand_note="RNA template" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 1065 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_note="DNA primer" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 1084 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /ligand_note="RNA template" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 1115 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_note="DNA primer" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 1183 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 ECO:0000269|PubMed:16912289" FT BINDING 1183 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /ligand_note="catalytic; for RNase H activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408, FT ECO:0000269|PubMed:16912289" FT BINDING 1186 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /ligand_note="RNA template" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 1188 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /ligand_note="RNA template" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 1189 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_note="DNA primer" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 1216 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_note="DNA primer" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 1218 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_note="DNA primer" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 1221 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /ligand_note="catalytic; for RNase H activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408, FT ECO:0000269|PubMed:16912289" FT BINDING 1242 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /ligand_note="catalytic; for RNase H activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408, FT ECO:0000269|PubMed:16912289" FT BINDING 1244 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /ligand_note="RNA template" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 1268 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /ligand_note="RNA template" FT /evidence="ECO:0000250|UniProtKB:A1Z651" FT BINDING 1312 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 ECO:0000305|PubMed:16912289" FT BINDING 1455 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /ligand_note="catalytic; for integrase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457" FT BINDING 1514 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /ligand_note="catalytic; for integrase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457" FT SITE 131..132 FT /note="Cleavage; by viral protease" FT /evidence="ECO:0000269|PubMed:16603535" FT SITE 215..216 FT /note="Cleavage; by viral protease" FT /evidence="ECO:0000269|PubMed:16603535" FT SITE 478..479 FT /note="Cleavage; by viral protease" FT /evidence="ECO:0000269|PubMed:16603535" FT SITE 534..535 FT /note="Cleavage; by viral protease" FT /evidence="ECO:0000269|PubMed:16603535" FT SITE 659..660 FT /note="Cleavage; by viral protease" FT /evidence="ECO:0000269|PubMed:16603535" FT SITE 1330..1331 FT /note="Cleavage; by viral protease" FT /evidence="ECO:0000269|PubMed:16603535" FT MOD_RES 192 FT /note="Phosphoserine; by host" FT /evidence="ECO:0000305|PubMed:12525616" FT LIPID 2 FT /note="N-myristoyl glycine; by host" FT /evidence="ECO:0000255, ECO:0000269|PubMed:6340098" FT MUTAGEN 114 FT /note="P->A: Slight reduction in the number of virus-like FT particles produced." FT MUTAGEN 137 FT /note="S->A: No effect on reverse transcription activity." FT /evidence="ECO:0000269|PubMed:12525616" FT MUTAGEN 148 FT /note="S->A: No effect on reverse transcription activity; FT when associated with A-150." FT /evidence="ECO:0000269|PubMed:12525616" FT MUTAGEN 150 FT /note="S->A: No effect on reverse transcription activity; FT when associated with A-148." FT /evidence="ECO:0000269|PubMed:12525616" FT MUTAGEN 165 FT /note="Y->A: Drastic reduction in the number of virus-like FT particles produced." FT /evidence="ECO:0000269|PubMed:15908698" FT MUTAGEN 192 FT /note="S->A: Complete loss of reverse transcription FT activity." FT /evidence="ECO:0000269|PubMed:12525616" FT MUTAGEN 192 FT /note="S->A: Complete loss of stable anchoring of viral PIC FT to mitotic chromosomes; when associated with A-196." FT /evidence="ECO:0000269|PubMed:23300449" FT MUTAGEN 192 FT /note="S->D: Complete loss of reverse transcription FT activity." FT /evidence="ECO:0000269|PubMed:12525616" FT MUTAGEN 196 FT /note="S->A: Complete loss of stable anchoring of viral PIC FT to mitotic chromosomes; when associated with A-192." FT /evidence="ECO:0000269|PubMed:23300449" FT MUTAGEN 196 FT /note="S->A: No effect on reverse transcription activity." FT /evidence="ECO:0000269|PubMed:12525616" FT MUTAGEN 209 FT /note="S->A: Strongly reduced reverse transcription FT activity." FT /evidence="ECO:0000269|PubMed:12525616" FT MUTAGEN 209 FT /note="S->D: Strongly reduced reverse transcription FT activity." FT /evidence="ECO:0000269|PubMed:12525616" FT MUTAGEN 212 FT /note="S->A: No effect on reverse transcription activity." FT /evidence="ECO:0000269|PubMed:12525616" FT MUTAGEN 1244 FT /note="R->A: No effect on readthrough between Gag and Pol." FT /evidence="ECO:0000269|PubMed:27329342" FT MUTAGEN 1247 FT /note="F->A: No effect on readthrough between Gag and Pol." FT /evidence="ECO:0000269|PubMed:27329342" FT MUTAGEN 1248 FT /note="A->K: Almost complete loss of readthrough between FT Gag and Pol." FT /evidence="ECO:0000269|PubMed:27329342" FT HELIX 351..355 FT /evidence="ECO:0007829|PDB:6GZA" FT HELIX 365..379 FT /evidence="ECO:0007829|PDB:6GZA" FT HELIX 387..389 FT /evidence="ECO:0007829|PDB:6GZA" FT HELIX 390..400 FT /evidence="ECO:0007829|PDB:6GZA" FT HELIX 403..410 FT /evidence="ECO:0007829|PDB:6GZA" FT HELIX 415..417 FT /evidence="ECO:0007829|PDB:6GZA" FT HELIX 420..432 FT /evidence="ECO:0007829|PDB:6GZA" FT TURN 488..491 FT /evidence="ECO:0007829|PDB:2MS0" FT HELIX 496..498 FT /evidence="ECO:0007829|PDB:2MQV" FT TURN 505..507 FT /evidence="ECO:0007829|PDB:2MQV" FT STRAND 510..512 FT /evidence="ECO:0007829|PDB:2MQV" FT HELIX 514..516 FT /evidence="ECO:0007829|PDB:2MQV" FT STRAND 520..522 FT /evidence="ECO:0007829|PDB:2MS1" FT STRAND 524..526 FT /evidence="ECO:0007829|PDB:2MQV" FT HELIX 529..532 FT /evidence="ECO:0007829|PDB:2MS0" FT HELIX 684..687 FT /evidence="ECO:0007829|PDB:6MIH" FT TURN 689..691 FT /evidence="ECO:0007829|PDB:6MIH" FT HELIX 693..696 FT /evidence="ECO:0007829|PDB:6MIH" FT STRAND 702..704 FT /evidence="ECO:0007829|PDB:1D0E" FT HELIX 727..742 FT /evidence="ECO:0007829|PDB:6MIH" FT STRAND 745..749 FT /evidence="ECO:0007829|PDB:6MIH" FT STRAND 757..759 FT /evidence="ECO:0007829|PDB:6MIH" FT STRAND 763..766 FT /evidence="ECO:0007829|PDB:1MML" FT STRAND 770..772 FT /evidence="ECO:0007829|PDB:6MIH" FT HELIX 775..778 FT /evidence="ECO:0007829|PDB:6MIH" FT HELIX 791..796 FT /evidence="ECO:0007829|PDB:6MIH" FT STRAND 804..810 FT /evidence="ECO:0007829|PDB:6MIH" FT TURN 811..813 FT /evidence="ECO:0007829|PDB:6MIH" FT HELIX 814..816 FT /evidence="ECO:0007829|PDB:6MIH" FT STRAND 817..819 FT /evidence="ECO:0007829|PDB:6MIH" FT TURN 821..823 FT /evidence="ECO:0007829|PDB:6MIH" FT HELIX 824..827 FT /evidence="ECO:0007829|PDB:6MIH" FT STRAND 829..832 FT /evidence="ECO:0007829|PDB:6MIH" FT TURN 834..836 FT /evidence="ECO:0007829|PDB:6MIH" FT STRAND 839..846 FT /evidence="ECO:0007829|PDB:6MIH" FT HELIX 854..872 FT /evidence="ECO:0007829|PDB:6MIH" FT STRAND 876..881 FT /evidence="ECO:0007829|PDB:6MIH" FT STRAND 884..891 FT /evidence="ECO:0007829|PDB:6MIH" FT HELIX 892..909 FT /evidence="ECO:0007829|PDB:6MIH" FT TURN 915..917 FT /evidence="ECO:0007829|PDB:6MIH" FT STRAND 919..927 FT /evidence="ECO:0007829|PDB:6MIH" FT STRAND 930..933 FT /evidence="ECO:0007829|PDB:6MIH" FT HELIX 941..948 FT /evidence="ECO:0007829|PDB:4MH8" FT HELIX 956..966 FT /evidence="ECO:0007829|PDB:4MH8" FT HELIX 967..969 FT /evidence="ECO:0007829|PDB:4MH8" FT HELIX 976..979 FT /evidence="ECO:0007829|PDB:4MH8" FT TURN 980..985 FT /evidence="ECO:0007829|PDB:4MH8" FT HELIX 997..1011 FT /evidence="ECO:0007829|PDB:4MH8" FT STRAND 1025..1044 FT /evidence="ECO:0007829|PDB:4MH8" FT STRAND 1047..1057 FT /evidence="ECO:0007829|PDB:4MH8" FT HELIX 1060..1063 FT /evidence="ECO:0007829|PDB:4MH8" FT HELIX 1067..1086 FT /evidence="ECO:0007829|PDB:4MH8" FT STRAND 1091..1094 FT /evidence="ECO:0007829|PDB:4MH8" FT TURN 1100..1104 FT /evidence="ECO:0007829|PDB:4MH8" FT HELIX 1116..1123 FT /evidence="ECO:0007829|PDB:4MH8" FT TURN 1126..1128 FT /evidence="ECO:0007829|PDB:4MH8" FT STRAND 1129..1131 FT /evidence="ECO:0007829|PDB:4MH8" FT TURN 1139..1141 FT /evidence="ECO:0007829|PDB:4MH8" FT STRAND 1169..1171 FT /evidence="ECO:0007829|PDB:2HB5" FT STRAND 1177..1189 FT /evidence="ECO:0007829|PDB:2HB5" FT STRAND 1192..1200 FT /evidence="ECO:0007829|PDB:2HB5" FT STRAND 1205..1211 FT /evidence="ECO:0007829|PDB:2HB5" FT HELIX 1217..1231 FT /evidence="ECO:0007829|PDB:2HB5" FT TURN 1232..1234 FT /evidence="ECO:0007829|PDB:2HB5" FT STRAND 1235..1241 FT /evidence="ECO:0007829|PDB:2HB5" FT HELIX 1244..1249 FT /evidence="ECO:0007829|PDB:2HB5" FT HELIX 1273..1282 FT /evidence="ECO:0007829|PDB:2HB5" FT STRAND 1285..1293 FT /evidence="ECO:0007829|PDB:2HB5" FT HELIX 1303..1321 FT /evidence="ECO:0007829|PDB:2HB5" FT HELIX 1346..1355 FT /evidence="ECO:0007829|PDB:4NZG" FT STRAND 1358..1360 FT /evidence="ECO:0007829|PDB:4NZG" FT TURN 1361..1364 FT /evidence="ECO:0007829|PDB:4NZG" FT STRAND 1365..1368 FT /evidence="ECO:0007829|PDB:4NZG" FT STRAND 1371..1374 FT /evidence="ECO:0007829|PDB:4NZG" FT HELIX 1376..1390 FT /evidence="ECO:0007829|PDB:4NZG" FT HELIX 1394..1402 FT /evidence="ECO:0007829|PDB:4NZG" FT TURN 1403..1405 FT /evidence="ECO:0007829|PDB:4NZG" FT STRAND 1407..1410 FT /evidence="ECO:0007829|PDB:4NZG" FT HELIX 1413..1422 FT /evidence="ECO:0007829|PDB:4NZG" FT HELIX 1425..1431 FT /evidence="ECO:0007829|PDB:4NZG" FT STRAND 1661..1667 FT /evidence="ECO:0007829|PDB:2M9U" FT STRAND 1670..1673 FT /evidence="ECO:0007829|PDB:2M9U" FT STRAND 1676..1687 FT /evidence="ECO:0007829|PDB:2M9U" FT STRAND 1690..1693 FT /evidence="ECO:0007829|PDB:2M9U" FT STRAND 1696..1698 FT /evidence="ECO:0007829|PDB:2M9U" FT HELIX 1702..1704 FT /evidence="ECO:0007829|PDB:2M9U" FT STRAND 1705..1707 FT /evidence="ECO:0007829|PDB:2M9U" FT TURN 1714..1716 FT /evidence="ECO:0007829|PDB:2M9U" FT STRAND 1717..1719 FT /evidence="ECO:0007829|PDB:2M9U" FT STRAND 1721..1724 FT /evidence="ECO:0007829|PDB:7JQ8" FT TURN 1726..1728 FT /evidence="ECO:0007829|PDB:2M9U" FT STRAND 1730..1734 FT /evidence="ECO:0007829|PDB:7JQ8" SQ SEQUENCE 1738 AA; 194912 MW; 3DF085F6E5EFCA83 CRC64; MGQTVTTPLS LTLGHWKDVE RIAHNQSVDV KKRRWVTFCS AEWPTFNVGW PRDGTFNRDL ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF VHPKPPPPLP PSAPSLPLEP PRSTPPRSSL YPALTPSLGA KPKPQVLSDS GGPLIDLLTE DPPPYRDPRP PPSDRDGNGG EATPAGEAPD PSPMASRLRG RREPPVADST TSQAFPLRAG GNGQLQYWPF SSSDLYNWKN NNPSFSEDPG KLTALIESVL ITHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGDDGR PTQLPNEVDA AFPLERPDWD YTTQAGRNHL VHYRQLLLAG LQNAGRSPTN LAKVKGITQG PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVSMSFIWQ SAPDIGRKLE RLEDLKNKTL GDLVREAEKI FNKRETPEER EERIRRETEE KEERRRTEDE QKEKERDRRR HREMSKLLAT VVSGQKQDRQ GGERRRSQLD RDQCAYCKEK GHWAKDCPKK PRGPRGPRPQ TSLLTLDDQG GQGQEPPPEP RITLKVGGQP VTFLVDTGAQ HSVLTQNPGP LSDKSAWVQG ATGGKRYRWT TDRKVHLATG KVTHSFLHVP DCPYPLLGRD LLTKLKAQIH FEGSGAQVMG PMGQPLQVLT LNIEDEHRLH ETSKEPDVSL GSTWLSDFPQ AWAETGGMGL AVRQAPLIIP LKATSTPVSI KQYPMSQEAR LGIKPHIQRL LDQGILVPCQ SPWNTPLLPV KKPGTNDYRP VQDLREVNKR VEDIHPTVPN PYNLLSGLPP SHQWYTVLDL KDAFFCLRLH PTSQPLFAFE WRDPEMGISG QLTWTRLPQG FKNSPTLFDE ALHRDLADFR IQHPDLILLQ YVDDLLLAAT SELDCQQGTR ALLQTLGNLG YRASAKKAQI CQKQVKYLGY LLKEGQRWLT EARKETVMGQ PTPKTPRQLR EFLGTAGFCR LWIPGFAEMA APLYPLTKTG TLFNWGPDQQ KAYQEIKQAL LTAPALGLPD LTKPFELFVD EKQGYAKGVL TQKLGPWRRP VAYLSKKLDP VAAGWPPCLR MVAAIAVLTK DAGKLTMGQP LVILAPHAVE ALVKQPPDRW LSNARMTHYQ ALLLDTDRVQ FGPVVALNPA TLLPLPEEGL QHNCLDILAE AHGTRPDLTD QPLPDADHTW YTDGSSLLQE GQRKAGAAVT TETEVIWAKA LPAGTSAQRA ELIALTQALK MAEGKKLNVY TDSRYAFATA HIHGEIYRRR GLLTSEGKEI KNKDEILALL KALFLPKRLS IIHCPGHQKG HSAEARGNRM ADQAARKAAI TETPDTSTLL IENSSPYTSE HFHYTVTDIK DLTKLGAIYD KTKKYWVYQG KPVMPDQFTF ELLDFLHQLT HLSFSKMKAL LERSHSPYYM LNRDRTLKNI TETCKACAQV NASKSAVKQG TRVRGHRPGT HWEIDFTEIK PGLYGYKYLL VFIDTFSGWI EAFPTKKETA KVVTKKLLEE IFPRFGMPQV LGTDNGPAFV SKVSQTVADL LGIDWKLHCA YRPQSSGQVE RMNRTIKETL TKLTLATGSR DWVLLLPLAL YRARNTPGPH GLTPYEILYG APPPLVNFPD PDMTRVTNSP SLQAHLQALY LVQHEVWRPL AAAYQEQLDR PVVPHPYRVG DTVWVRRHQT KNLEPRWKGP YTVLLTTPTA LKVDGIAAWI HAAHVKAADP GGGPSSRLTW RVQRSQNPLK IRLTREAP //