POL_MLVMS
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 03-AUG-2022, entry version 189.
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).
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;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
CC Note=The RT polymerase active site binds 2 magnesium ions.
CC {ECO:0000255|PROSITE-ProRule:PRU00405};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC Note=Binds 1 magnesium ion for ribonuclease H (RNase H) activity.
CC {ECO:0000269|PubMed:16912289};
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).
CC {ECO:0000269|PubMed:14599799}.
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}.
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DR EMBL; AF033811; AAC82568.1; 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 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 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; Genome.
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; IDA:UniProtKB.
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:0039705; P:viral translational readthrough; IMP:UniProtKB.
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 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 Membrane; Metal-binding; Multifunctional enzyme; Myristate; Nuclease;
KW Nucleotidyltransferase; Phosphoprotein; Protease; Reference proteome;
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: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 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 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 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 1221
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 1242
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 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="3"
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="3"
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
