GAG_MLVMS
ID GAG_MLVMS Reviewed; 538 AA.
AC P03332; Q9WJP4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Gag polyprotein;
DE Short=Pr65gag;
DE AltName: Full=Core polyprotein;
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-Gag;
DE Short=NC-gag;
GN Name=gag;
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] (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 SUBCELLULAR LOCATION (GAG POLYPROTEIN).
RX PubMed=8991095; DOI=10.1083/jcb.135.6.1841;
RA Suomalainen M., Hultenby K., Garoff H.;
RT "Targeting of Moloney murine leukemia virus gag precursor to the site of
RT virus budding.";
RL J. Cell Biol. 135:1841-1852(1996).
RN [6]
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 [7]
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 [8]
RP INTERACTION WITH MOUSE NEDD4; TSG101 AND PDCD6IP/ALIX (GAG POLYPROTEIN),
RP 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 [9]
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 [10]
RP PROTEOLYTIC CLEAVAGE (GAG POLYPROTEIN).
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 [11]
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 [12]
RP DOMAIN LATE-BUDDING, FUNCTION (GAG POLYPROTEIN), AND UBIQUITINATION (GAG
RP POLYPROTEIN).
RX PubMed=19864377; DOI=10.1128/jvi.01319-09;
RA Jadwin J.A., Rudd V., Sette P., Challa S., Bouamr F.;
RT "Late domain-independent rescue of a release-deficient Moloney murine
RT leukemia virus by the ubiquitin ligase Itch.";
RL J. Virol. 84:704-715(2010).
RN [13]
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 [14]
RP STRUCTURE BY NMR OF 492-531.
RX PubMed=8019131; DOI=10.1007/bf00175244;
RA Demene H., Jullian N., Morellet N., de Rocquigny H., Cornille F.,
RA Maigret B., Roques B.P.;
RT "Three-dimensional 1H NMR structure of the nucleocapsid protein NCp10 of
RT Moloney murine leukemia virus.";
RL J. Biomol. NMR 4:153-170(1994).
RN [15]
RP STRUCTURE BY NMR OF 352-382.
RX PubMed=9799104; DOI=10.1046/j.1432-1327.1998.2570069.x;
RA Clish C.B., Peyton D.H., Barklis E.;
RT "Solution structures of human immunodeficiency virus type 1 (HIV-1) and
RT moloney murine leukemia virus (MoMLV) capsid protein major-homology-region
RT peptide analogs by NMR spectroscopy.";
RL Eur. J. Biochem. 257:69-77(1998).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 1-99, AND FUNCTION (MATRIX PROTEIN
RP P15).
RX PubMed=12467570; DOI=10.1016/s0969-2126(02)00896-1;
RA Riffel N., Harlos K., Iourin O., Rao Z., Kingsman A., Stuart D., Fry E.;
RT "Atomic resolution structure of Moloney murine leukemia virus matrix
RT protein and its relationship to other retroviral matrix proteins.";
RL Structure 10:1627-1636(2002).
RN [17]
RP STRUCTURE BY NMR OF 479-534, FUNCTION (NUCLEOCAPSID PROTEIN P10-GAG), AND
RP RNA-BINDING (NUCLEOCAPSID PROTEIN P10-GAG).
RX PubMed=15457265; DOI=10.1038/nature02944;
RA D'Souza V., Summers M.F.;
RT "Structural basis for packaging the dimeric genome of Moloney murine
RT leukaemia virus.";
RL Nature 431:586-590(2004).
RN [18]
RP STRUCTURE BY NMR OF 479-534, AND RNA-BINDING (NUCLEOCAPSID PROTEIN
RP P10-GAG).
RX PubMed=15751950; DOI=10.1021/bi047639q;
RA Dey A., York D., Smalls-Mantey A., Summers M.F.;
RT "Composition and sequence-dependent binding of RNA to the nucleocapsid
RT protein of Moloney murine leukemia virus.";
RL Biochemistry 44:3735-3744(2005).
CC -!- FUNCTION: [Gag polyprotein]: Plays a role in budding and is processed
CC by the viral protease during virion maturation outside the cell. During
CC budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-
CC like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to
CC Gag binding host factors. Interaction with HECT ubiquitin ligases
CC probably links the viral protein to the host ESCRT pathway and
CC facilitates release. {ECO:0000269|PubMed:19864377}.
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:0000305|PubMed:12467570}.
CC -!- FUNCTION: [RNA-binding phosphoprotein p12]: Constituent of the pre-
CC integration complex (PIC) which tethers the latter to mitotic
CC chromosomes. {ECO:0000269|PubMed:21085616,
CC 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-Gag]: Involved in the packaging and
CC encapsidation of two copies of the genome. Binds with high affinity to
CC conserved UCUG elements within the packaging signal, located near the
CC 5'-end of the genome. This binding is dependent on genome dimerization.
CC {ECO:0000269|PubMed:15457265}.
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, PubMed:12093170). {ECO:0000250|UniProtKB:P03336,
CC ECO:0000269|PubMed:12093170, ECO:0000269|PubMed:16352559}.
CC -!- SUBUNIT: [Gag polyprotein]: Interacts (via PPXY motif) with host NEDD4
CC (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 -!- INTERACTION:
CC P03332; Q9QZK7: Dok3; Xeno; NbExp=3; IntAct=EBI-935477, EBI-2906753;
CC P03332; Q9JKF1: Iqgap1; Xeno; NbExp=17; IntAct=EBI-935477, EBI-644633;
CC -!- SUBCELLULAR LOCATION: [Gag polyprotein]: Virion {ECO:0000305}. Host
CC cell membrane {ECO:0000269|PubMed:8991095}; Lipid-anchor {ECO:0000305}.
CC Host late endosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
CC Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P26807}.
CC Note=These locations are probably linked to virus assembly sites.
CC {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-Gag]: Virion
CC {ECO:0000305}.
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:23300449}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Pr65gag;
CC IsoId=P03332-1; Sequence=Displayed;
CC Name=Pr80gag; Synonyms=GlycoGag;
CC IsoId=P03332-2; Sequence=Not described;
CC -!- DOMAIN: [Gag polyprotein]: Late-budding domains (L domains) are short
CC sequence motifs essential for viral particle budding. They recruit
CC proteins of the host ESCRT machinery (Endosomal Sorting Complex
CC Required for Transport) or ESCRT-associated proteins. RNA-binding
CC phosphoprotein p12 contains one L domain: a PPXY motif which interacts
CC with the WW domain 3 of NEDD4 E3 ubiquitin ligase. PPXY motif is
CC essential for virus egress. Matrix protein p15 contains one L domain: a
CC PTAP/PSAP motif, which interacts with the UEV domain of TSG101. The
CC junction between the matrix protein p15 and RNA-binding phosphoprotein
CC p12 also contains one L domain: a LYPX(n)L motif which interacts with
CC PDCD6IP. Both PSAP and LYPX(n)L domains might play little to no role in
CC budding and possibly drive residual virus release.
CC {ECO:0000269|PubMed:19864377}.
CC -!- PTM: [Gag 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:0000269|PubMed:19864377}.
CC -!- PTM: [Gag 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; required for virus replication.
CC {ECO:0000269|PubMed:16352559}.
CC -!- PTM: RNA-binding phosphoprotein p12 is phosphorylated on serine
CC residues. {ECO:0000269|PubMed:12525616}.
CC -!- MISCELLANEOUS: [Isoform Pr80gag]: Produced by an upstream CUG
CC initiation codon. {ECO:0000305}.
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DR EMBL; J02255; AAB59942.1; -; Genomic_RNA.
DR EMBL; AF033811; AAC82566.1; -; Genomic_RNA.
DR PIR; A03930; FOMV1M.
DR RefSeq; NP_057934.1; NC_001501.1.
DR PDB; 1A6B; NMR; -; B=492-531.
DR PDB; 1BM4; NMR; -; A=352-382.
DR PDB; 1MN8; X-ray; 1.00 A; A/B/C/D=1-99.
DR PDB; 1U6P; NMR; -; A=479-534.
DR PDB; 1WWD; NMR; -; A=479-534.
DR PDB; 1WWE; NMR; -; A=479-534.
DR PDB; 1WWF; NMR; -; A=479-534.
DR PDB; 1WWG; NMR; -; A=479-534.
DR PDBsum; 1A6B; -.
DR PDBsum; 1BM4; -.
DR PDBsum; 1MN8; -.
DR PDBsum; 1U6P; -.
DR PDBsum; 1WWD; -.
DR PDBsum; 1WWE; -.
DR PDBsum; 1WWF; -.
DR PDBsum; 1WWG; -.
DR BMRB; P03332; -.
DR SMR; P03332; -.
DR IntAct; P03332; 6.
DR MINT; P03332; -.
DR iPTMnet; P03332; -.
DR SwissPalm; P03332; -.
DR GeneID; 1491870; -.
DR KEGG; vg:1491870; -.
DR EvolutionaryTrace; P03332; -.
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:0120026; C:host cell uropod; IDA:CACAO.
DR GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.180; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR InterPro; IPR000840; G_retro_matrix.
DR InterPro; IPR036946; G_retro_matrix_sf.
DR InterPro; IPR002079; Gag_p12.
DR InterPro; IPR003036; Gag_P30.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
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; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Capsid protein; Coiled coil;
KW Direct protein sequencing; Host cell membrane; Host cytoplasm;
KW Host endosome; Host membrane; Host-virus interaction; Lipoprotein;
KW Membrane; Metal-binding; Myristate; Phosphoprotein; Reference proteome;
KW RNA-binding; Ubl conjugation; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral matrix protein;
KW Viral nucleoprotein; Viral release from host cell; Virion; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:6340098"
FT CHAIN 2..538
FT /note="Gag polyprotein"
FT /id="PRO_0000390815"
FT CHAIN 2..131
FT /note="Matrix protein p15"
FT /id="PRO_0000040912"
FT CHAIN 132..215
FT /note="RNA-binding phosphoprotein p12"
FT /id="PRO_0000040913"
FT CHAIN 216..478
FT /note="Capsid protein p30"
FT /id="PRO_0000040914"
FT CHAIN 479..538
FT /note="Nucleocapsid protein p10-Gag"
FT /id="PRO_0000040915"
FT ZN_FING 502..519
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
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:0000269|PubMed:16352559"
FT REGION 430..435
FT /note="Interaction with host UBE2I"
FT /evidence="ECO:0000269|PubMed:16352559"
FT REGION 434..538
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:0000269|PubMed:19864377"
FT MOTIF 130..134
FT /note="LYPX(n)L motif"
FT /evidence="ECO:0000269|PubMed:19864377"
FT MOTIF 162..165
FT /note="PPXY motif"
FT /evidence="ECO:0000269|PubMed:19864377"
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 COMPBIAS 488..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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 HELIX 8..14
FT /evidence="ECO:0007829|PDB:1MN8"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:1MN8"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:1MN8"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:1MN8"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:1MN8"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1MN8"
FT HELIX 80..91
FT /evidence="ECO:0007829|PDB:1MN8"
FT TURN 356..360
FT /evidence="ECO:0007829|PDB:1BM4"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:1BM4"
FT HELIX 364..378
FT /evidence="ECO:0007829|PDB:1BM4"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:1WWD"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:1A6B"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:1A6B"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:1U6P"
FT HELIX 514..516
FT /evidence="ECO:0007829|PDB:1U6P"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:1A6B"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:1WWG"
SQ SEQUENCE 538 AA; 60858 MW; 8A7652439B464495 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 TSLLTLDD
