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 02-SEP-2026, entry version 164. 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 Gammaretrovirus murleu; 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:12093170, PubMed:16352559). {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}. 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; 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=351-382. 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 AlphaFoldDB; P03332; -. 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; Segment. DR GO; GO:0030430; C:host cell cytoplasm; EXP:UniProtKB. DR GO; GO:0044185; C:host cell late endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0020002; C:host cell plasma membrane; EXP:UniProtKB. DR GO; GO:0120026; C:host cell uropod; IDA:CACAO. DR GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell. 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:UniProtKB-KW. DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW. DR FunFam; 1.10.150.180:FF:000001; Gag polyprotein; 1. DR Gene3D; 1.10.150.180; Gamma-retroviral matrix domain; 1. DR Gene3D; 1.10.375.10; Human Immunodeficiency Virus Type 1 Capsid Protein; 1. DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 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; IPR050462; Retroviral_Gag-Pol_poly. DR InterPro; IPR010999; Retrovr_matrix. DR InterPro; IPR001878; Znf_CCHC. DR InterPro; IPR036875; Znf_CCHC_sf. DR PANTHER; PTHR33166; GAG_P30 DOMAIN-CONTAINING PROTEIN; 1. 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; 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 PROSITE; PS50158; ZF_CCHC; 1. DR PDBsum; 1A6B; -. DR PDBsum; 1BM4; -. DR PDBsum; 1MN8; -. DR PDBsum; 1U6P; -. DR PDBsum; 1WWD; -. DR PDBsum; 1WWE; -. DR PDBsum; 1WWF; -. DR PDBsum; 1WWG; -. 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..124 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 163..178 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 434..466 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 486..519 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..37 FT /evidence="ECO:0007829|PDB:1MN8" FT HELIX 38..42 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 //