PRO_MPMV
ID PRO_MPMV Reviewed; 911 AA.
AC P07570; O92810;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Gag-Pro polyprotein;
DE AltName: Full=Pr95 {ECO:0000312|EMBL:AAC82574.1};
DE Contains:
DE RecName: Full=Matrix protein p10;
DE Contains:
DE RecName: Full=Phosphorylated protein pp24;
DE Contains:
DE RecName: Full=Phosphorylated protein pp18;
DE Contains:
DE RecName: Full=p12;
DE Contains:
DE RecName: Full=Capsid protein p27;
DE Contains:
DE RecName: Full=Nucleocapsid protein-dUTPase;
DE Short=NC-dUTPase;
DE EC=3.6.1.23 {ECO:0000269|PubMed:17169987};
DE Contains:
DE RecName: Full=Protease 17 kDa {ECO:0000303|PubMed:16257973};
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275, ECO:0000269|PubMed:9636364};
DE Contains:
DE RecName: Full=Protease 13 kDa {ECO:0000303|PubMed:16257973};
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275, ECO:0000269|PubMed:9636364};
DE Contains:
DE RecName: Full=G-patch peptide {ECO:0000303|PubMed:22171253};
GN Name=gag-pro;
OS Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=11855;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RIBOSOMAL FRAMESHIFT.
RC STRAIN=Clone 6A;
RX PubMed=2421920; DOI=10.1016/0092-8674(86)90323-5;
RA Sonigo P., Barker C., Hunter E., Wain-Hobson S.;
RT "Nucleotide sequence of Mason-Pfizer monkey virus: an immunosuppressive D-
RT type retrovirus.";
RL Cell 45:375-385(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Chappey C.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEOLYTIC CLEAVAGE (PROTEASE 17 KDA), CATALYTIC ACTIVITY (PROTEASE 17
RP KDA), FUNCTION (PROTEASE 17 KDA), PROTEOLYTIC CLEAVAGE (GAG-PRO
RP POLYPROTEIN), SUBCELLULAR LOCATION (PROTEASE 17 KDA), SUBCELLULAR LOCATION
RP (PROTEASE 13 KDA), CATALYTIC ACTIVITY (PROTEASE 13 KDA), AND FUNCTION
RP (PROTEASE 13 KDA).
RX PubMed=9636364; DOI=10.1006/viro.1998.9173;
RA Zabransky A., Andreansky M., Hruskova-Heidingsfeldova O., Havlicek V.,
RA Hunter E., Ruml T., Pichova I.;
RT "Three active forms of aspartic proteinase from Mason-Pfizer monkey
RT virus.";
RL Virology 245:250-256(1998).
RN [4]
RP DOMAIN (GAG-PRO POLYPROTEIN), AND MUTAGENESIS OF 203-PRO--TYR-205 AND
RP 210-PRO--PRO-211.
RX PubMed=12915562; DOI=10.1128/jvi.77.17.9474-9485.2003;
RA Gottwein E., Bodem J., Mueller B., Schmechel A., Zentgraf H.,
RA Kraeusslich H.G.;
RT "The Mason-Pfizer monkey virus PPPY and PSAP motifs both contribute to
RT virus release.";
RL J. Virol. 77:9474-9485(2003).
RN [5]
RP PROTEOLYTIC CLEAVAGE (PROTEASE 17 KDA), DOMAIN (PROTEASE 17 KDA), AND
RP MUTAGENESIS OF ASN-868; ALA-873; GLN-874 AND TYR-880.
RX PubMed=16257973; DOI=10.1074/jbc.m508031200;
RA Bauerova-Zabranska H., Stokrova J., Strisovsky K., Hunter E., Ruml T.,
RA Pichova I.;
RT "The RNA binding G-patch domain in retroviral protease is important for
RT infectivity and D-type morphogenesis of Mason-Pfizer monkey virus.";
RL J. Biol. Chem. 280:42106-42112(2005).
RN [6]
RP DOMAIN (PROTEASE 17 KDA), MUTAGENESIS OF GLY-879; TYR-880; GLY-883;
RP GLY-885; LEU-886; GLY-887; GLY-892 AND GLY-907, FUNCTION (G-PATCH PEPTIDE),
RP AND INTERACTION WITH THE REVERSE TRANSCRIPTASE/RIBONUCLEASE H (G-PATCH
RP PEPTIDE).
RX PubMed=22171253; DOI=10.1128/jvi.06638-11;
RA Krizova I., Hadravova R., Stokrova J., Guenterova J., Dolezal M., Ruml T.,
RA Rumlova M., Pichova I.;
RT "The G-patch domain of Mason-Pfizer monkey virus is a part of reverse
RT transcriptase.";
RL J. Virol. 86:1988-1998(2012).
RN [7]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=24298557; DOI=10.1155/2013/984028;
RA Huang X., Cheng Q., Du Z.;
RT "A genome-wide analysis of RNA pseudoknots that stimulate efficient -1
RT ribosomal frameshifting or readthrough in animal viruses.";
RL Biomed. Res. Int. 2013:984028-984028(2013).
RN [8] {ECO:0007744|PDB:1NSO}
RP STRUCTURE BY NMR OF 163-269, AND PROTEOLYTIC CLEAVAGE (PROTEASE 17 KDA).
RX PubMed=14568536; DOI=10.1016/j.jmb.2003.08.049;
RA Veverka V., Bauerova H., Zabransky A., Lang J., Ruml T., Pichova I.,
RA Hrabal R.;
RT "Three-dimensional structure of a monomeric form of a retroviral
RT protease.";
RL J. Mol. Biol. 333:771-780(2003).
RN [9] {ECO:0007744|PDB:2D4L, ECO:0007744|PDB:2D4M, ECO:0007744|PDB:2D4N}
RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 12-162, CATALYTIC ACTIVITY
RP (NUCLEOCAPSID PROTEIN-DUTPASE), AND SUBUNIT (NUCLEOCAPSID PROTEIN-DUTPASE).
RX PubMed=17169987; DOI=10.1093/nar/gkl1074;
RA Nemeth-Pongracz V., Barabas O., Fuxreiter M., Simon I., Pichova I.,
RA Rumlova M., Zabranska H., Svergun D., Petoukhov M., Harmat V., Klement E.,
RA Hunyadi-Gulyas E., Medzihradszky K.F., Konya E., Vertessy B.G.;
RT "Flexible segments modulate co-folding of dUTPase and nucleocapsid
RT proteins.";
RL Nucleic Acids Res. 35:495-505(2007).
CC -!- FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.
CC -!- FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein.
CC {ECO:0000305}.
CC -!- FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}.
CC -!- FUNCTION: [Protease 17 kDa]: The aspartyl protease mediates proteolytic
CC cleavages of Gag and Gag-Pol polyproteins during or shortly after the
CC release of the virion from the plasma membrane. Cleavages take place as
CC an ordered, step-wise cascade to yield mature proteins. This process is
CC called maturation. Displays maximal activity during the budding process
CC just prior to particle release from the cell. {ECO:0000255|PROSITE-
CC ProRule:PRU00275, ECO:0000269|PubMed:9636364}.
CC -!- FUNCTION: [Protease 13 kDa]: The aspartyl protease mediates proteolytic
CC cleavages of Gag and Gag-Pol polyproteins during or shortly after the
CC release of the virion from the plasma membrane. Cleavages take place as
CC an ordered, step-wise cascade to yield mature proteins. This process is
CC called maturation. Displays maximal activity during the budding process
CC just prior to particle release from the cell. {ECO:0000255|PROSITE-
CC ProRule:PRU00275, ECO:0000269|PubMed:9636364}.
CC -!- FUNCTION: [G-patch peptide]: Enhances the activity of the reverse
CC transcriptase. May be part of the mature RT.
CC {ECO:0000269|PubMed:22171253}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;
CC Evidence={ECO:0000269|PubMed:17169987};
CC -!- SUBUNIT: [Protease 17 kDa]: Homodimer (By similarity).
CC {ECO:0000250|UniProtKB:P10271}.
CC -!- SUBUNIT: [G-patch peptide]: Interacts with the reverse
CC transcriptase/ribonuclease H (PubMed:22171253).
CC {ECO:0000269|PubMed:22171253}.
CC -!- SUBUNIT: [Nucleocapsid protein-dUTPase]: Homotrimer (PubMed:17169987).
CC {ECO:0000269|PubMed:17169987}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protease 13 kDa]: Virion
CC {ECO:0000269|PubMed:9636364}.
CC -!- SUBCELLULAR LOCATION: [Protease 17 kDa]: Virion
CC {ECO:0000269|PubMed:9636364}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Gag-Pro polyprotein;
CC IsoId=P07570-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P07567-1; Sequence=External;
CC Name=Gag-Pro-Pol polyprotein;
CC IsoId=P07572-1; Sequence=External;
CC -!- DOMAIN: [Gag-Pro 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 Phosphorylated protein pp24 and phosphorylated protein pp18 contains
CC two L domains: a PTAP/PSAP motif which interacts with the UEV domain of
CC TSG101, and a PPXY motif which binds to the WW domains of the ubiquitin
CC ligase NEDD4. Both motifs contribute to viral release. The PSAP motif
CC acts as an additional L domain and promotes the efficient release of
CC the virions but requires an intact PPPY motif to perform its function.
CC {ECO:0000269|PubMed:12915562}.
CC -!- DOMAIN: [Protease 17 kDa]: The glycine-rich G-patch domain (GPD) is
CC present at the C-terminus of the protease from which it is then
CC detached by the protease itself. {ECO:0000269|PubMed:16257973,
CC ECO:0000269|PubMed:22171253}.
CC -!- PTM: [Protease 17 kDa]: Released by autocatalytic processing. The
CC protease can undergo further autoprocessing to yield 2 shorter but
CC enzymatically active forms of 12 kDa and 13 kDa without the GDP domain.
CC the 12 kDa form is monomeric. {ECO:0000269|PubMed:14568536,
CC ECO:0000269|PubMed:16257973, ECO:0000269|PubMed:9636364}.
CC -!- PTM: [Gag-Pro polyprotein]: Myristoylated. Myristoylation of the matrix
CC (MA) domain mediates the transport and binding of Gag polyproteins to
CC the host plasma membrane and is required for the assembly of viral
CC particles. {ECO:0000250|UniProtKB:P10258}.
CC -!- PTM: [Gag-Pro polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins. {ECO:0000269|PubMed:9636364}.
CC -!- MISCELLANEOUS: [Isoform Gag-Pro polyprotein]: Produced by -1 ribosomal
CC frameshifting between gag-pro. {ECO:0000305|PubMed:2421920,
CC ECO:0000305|PubMed:24298557}.
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DR EMBL; M12349; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AF033815; AAC82574.1; -; Genomic_RNA.
DR PIR; B25839; PRLJMP.
DR RefSeq; NP_056892.1; NC_001550.1. [P07570-1]
DR PDB; 1NSO; NMR; -; A=163-267.
DR PDB; 2D4L; X-ray; 1.70 A; A=11-162.
DR PDB; 2D4M; X-ray; 1.85 A; A=11-162.
DR PDB; 2D4N; X-ray; 1.53 A; A=11-162.
DR PDB; 3SQF; X-ray; 1.63 A; A/B=163-276.
DR PDB; 3TP1; X-ray; 1.60 A; A=11-162.
DR PDB; 3TPN; X-ray; 1.65 A; A=609-759.
DR PDB; 3TPS; X-ray; 1.85 A; A=609-759.
DR PDB; 3TPW; X-ray; 1.65 A; A=11-162.
DR PDB; 3TPY; X-ray; 1.75 A; A=609-759.
DR PDB; 3TQ3; X-ray; 1.85 A; A=609-759.
DR PDB; 3TQ4; X-ray; 1.60 A; A=609-759.
DR PDB; 3TQ5; X-ray; 1.40 A; A=609-759.
DR PDB; 3TRL; X-ray; 1.80 A; A=609-759.
DR PDB; 3TRN; X-ray; 1.83 A; A=609-759.
DR PDB; 3TS6; X-ray; 1.84 A; A=609-759.
DR PDB; 3TSL; X-ray; 2.20 A; A=609-759.
DR PDB; 3TTA; X-ray; 2.00 A; A=609-759.
DR PDBsum; 1NSO; -.
DR PDBsum; 2D4L; -.
DR PDBsum; 2D4M; -.
DR PDBsum; 2D4N; -.
DR PDBsum; 3SQF; -.
DR PDBsum; 3TP1; -.
DR PDBsum; 3TPN; -.
DR PDBsum; 3TPS; -.
DR PDBsum; 3TPW; -.
DR PDBsum; 3TPY; -.
DR PDBsum; 3TQ3; -.
DR PDBsum; 3TQ4; -.
DR PDBsum; 3TQ5; -.
DR PDBsum; 3TRL; -.
DR PDBsum; 3TRN; -.
DR PDBsum; 3TS6; -.
DR PDBsum; 3TSL; -.
DR PDBsum; 3TTA; -.
DR BMRB; P07570; -.
DR SMR; P07570; -.
DR MEROPS; A02.009; -.
DR GeneID; 2746973; -.
DR BRENDA; 3.4.23.B6; 3195.
DR BRENDA; 3.6.1.23; 3195.
DR EvolutionaryTrace; P07570; -.
DR Proteomes; UP000008870; Genome.
DR Proteomes; UP000105838; Genome.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004170; F:dUTP diphosphatase 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:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0016032; P:viral process; IEA:InterPro.
DR CDD; cd05482; HIV_retropepsin_like; 1.
DR CDD; cd07557; trimeric_dUTPase; 1.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.490; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 2.70.40.10; -; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR003322; B_retro_matrix.
DR InterPro; IPR038124; B_retro_matrix_sf.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR000721; Gag_p24_N.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR034170; Retropepsin-like_cat_dom.
DR InterPro; IPR018061; Retropepsins.
DR InterPro; IPR008916; Retrov_capsid_C.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00692; dUTPase; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF02337; Gag_p10; 1.
DR Pfam; PF00607; Gag_p24; 1.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF00077; RVP; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF51283; SSF51283; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Capsid protein; Coiled coil; DNA-binding;
KW Hydrolase; Lipoprotein; Magnesium; Metal-binding; Myristate;
KW Nucleotide metabolism; Protease; Repeat; Ribosomal frameshifting;
KW Viral matrix protein; Viral nucleoprotein; Virion; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000305"
FT CHAIN 2..911
FT /note="Gag-Pro polyprotein"
FT /id="PRO_0000199550"
FT CHAIN 2..100
FT /note="Matrix protein p10"
FT /id="PRO_0000443190"
FT CHAIN 101..216
FT /note="Phosphorylated protein pp24"
FT /id="PRO_0000443191"
FT PROPEP 101..161
FT /evidence="ECO:0000305"
FT /id="PRO_0000443192"
FT CHAIN 162..216
FT /note="Phosphorylated protein pp18"
FT /id="PRO_0000443193"
FT CHAIN 217..299
FT /note="p12"
FT /id="PRO_0000443194"
FT CHAIN 300..525
FT /note="Capsid protein p27"
FT /id="PRO_0000443195"
FT CHAIN 526..759
FT /note="Nucleocapsid protein-dUTPase"
FT /id="PRO_0000443296"
FT CHAIN 760..911
FT /note="Protease 17 kDa"
FT /id="PRO_0000443196"
FT CHAIN 760..873
FT /note="Protease 13 kDa"
FT /id="PRO_0000443197"
FT PEPTIDE 874..911
FT /note="G-patch peptide"
FT /id="PRO_0000443198"
FT DOMAIN 780..856
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 867..911
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092,
FT ECO:0000269|PubMed:22171253"
FT ZN_FING 547..564
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 576..593
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 113..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 216..257
FT /evidence="ECO:0000255"
FT MOTIF 202..205
FT /note="PPXY motif"
FT /evidence="ECO:0000269|PubMed:12915562"
FT MOTIF 210..213
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000269|PubMed:12915562"
FT COMPBIAS 113..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 785
FT /note="Protease; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT SITE 100..101
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 161..162
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 216..217
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 299..300
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 525..526
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P07567"
FT SITE 759..760
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:9636364"
FT SITE 873..874
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:16257973"
FT MUTAGEN 203..205
FT /note="PPY->GAA: 80% loss of virus release."
FT /evidence="ECO:0000269|PubMed:12915562"
FT MUTAGEN 210..211
FT /note="PS->AG: 30% loss of virus release."
FT /evidence="ECO:0000269|PubMed:12915562"
FT MUTAGEN 868
FT /note="N->I: Accelerated processing of the protease C-
FT terminus."
FT /evidence="ECO:0000269|PubMed:16257973"
FT MUTAGEN 873
FT /note="A->R: 30% loss of infectivity."
FT /evidence="ECO:0000269|PubMed:16257973"
FT MUTAGEN 874
FT /note="Q->I: Accelerated processing of the protease C-
FT terminus. 50% loss of RT activity."
FT /evidence="ECO:0000269|PubMed:16257973"
FT MUTAGEN 879
FT /note="G->A: 85% loss of infectivity and 65% loss of RT
FT activity."
FT /evidence="ECO:0000269|PubMed:22171253"
FT MUTAGEN 880
FT /note="Y->A: 90% loss of infectivity and 65% loss of RT
FT activity."
FT /evidence="ECO:0000269|PubMed:22171253"
FT MUTAGEN 880
FT /note="Y->S: Defective in nucleic acid binding. 80% loss of
FT infectivity. 50% loss of RT activity."
FT /evidence="ECO:0000269|PubMed:16257973"
FT MUTAGEN 883
FT /note="G->A: 90% loss of infectivity and 55% loss of RT
FT activity."
FT /evidence="ECO:0000269|PubMed:22171253"
FT MUTAGEN 885
FT /note="G->A: 70% loss of infectivity and 60% loss of RT
FT activity."
FT /evidence="ECO:0000269|PubMed:22171253"
FT MUTAGEN 886
FT /note="L->A: 85% loss of infectivity and 60% loss of RT
FT activity."
FT /evidence="ECO:0000269|PubMed:22171253"
FT MUTAGEN 887
FT /note="G->A: 95% loss of infectivity and 95% loss of RT
FT activity."
FT /evidence="ECO:0000269|PubMed:22171253"
FT MUTAGEN 892
FT /note="G->A: 85% loss of infectivity and 60% loss of RT
FT activity."
FT /evidence="ECO:0000269|PubMed:22171253"
FT MUTAGEN 907
FT /note="G->A: 60% loss of infectivity and 35% loss of RT
FT activity."
FT /evidence="ECO:0000269|PubMed:22171253"
FT HELIX 635..637
FT /evidence="ECO:0007829|PDB:3TQ5"
FT STRAND 646..651
FT /evidence="ECO:0007829|PDB:3TQ5"
FT STRAND 656..658
FT /evidence="ECO:0007829|PDB:3TQ5"
FT HELIX 660..662
FT /evidence="ECO:0007829|PDB:3TQ5"
FT STRAND 665..667
FT /evidence="ECO:0007829|PDB:3TQ5"
FT STRAND 670..672
FT /evidence="ECO:0007829|PDB:3TQ5"
FT STRAND 679..685
FT /evidence="ECO:0007829|PDB:3TQ5"
FT HELIX 687..690
FT /evidence="ECO:0007829|PDB:3TQ5"
FT TURN 691..693
FT /evidence="ECO:0007829|PDB:3TQ5"
FT STRAND 694..696
FT /evidence="ECO:0007829|PDB:3TQ5"
FT STRAND 699..701
FT /evidence="ECO:0007829|PDB:3TQ5"
FT STRAND 711..718
FT /evidence="ECO:0007829|PDB:3TQ5"
FT STRAND 720..722
FT /evidence="ECO:0007829|PDB:3TQ5"
FT STRAND 727..735
FT /evidence="ECO:0007829|PDB:3TQ5"
FT STRAND 766..769
FT /evidence="ECO:0007829|PDB:1NSO"
FT STRAND 770..775
FT /evidence="ECO:0007829|PDB:3SQF"
FT STRAND 778..784
FT /evidence="ECO:0007829|PDB:3SQF"
FT STRAND 792..794
FT /evidence="ECO:0007829|PDB:3SQF"
FT HELIX 795..797
FT /evidence="ECO:0007829|PDB:3SQF"
FT STRAND 804..806
FT /evidence="ECO:0007829|PDB:3SQF"
FT STRAND 808..811
FT /evidence="ECO:0007829|PDB:1NSO"
FT HELIX 816..818
FT /evidence="ECO:0007829|PDB:3SQF"
FT STRAND 821..825
FT /evidence="ECO:0007829|PDB:3SQF"
FT STRAND 827..830
FT /evidence="ECO:0007829|PDB:3SQF"
FT TURN 832..834
FT /evidence="ECO:0007829|PDB:1NSO"
FT STRAND 836..839
FT /evidence="ECO:0007829|PDB:3SQF"
FT STRAND 842..844
FT /evidence="ECO:0007829|PDB:3SQF"
FT HELIX 854..857
FT /evidence="ECO:0007829|PDB:3SQF"
SQ SEQUENCE 911 AA; 100648 MW; D9B65A6070A3CA7D CRC64;
MGQELSQHER YVEQLKQALK TRGVKVKYAD LLKFFDFVKD TCPWFPQEGT IDIKRWRRVG
DCFQDYYNTF GPEKVPVTAF SYWNLIKELI DKKEVNPQVM AAVAQTEEIL KSNSQTDLTK
TSQNPDLDLI SLDSDDEGAK SSSLQDKGLS STKKPKRFPV LLTAQTSKDP EDPNPSEVDW
DGLEDEAAKY HNPDWPPFLT RPPPYNKATP SAPTVMAVVN PKEELKEKIA QLEEQIKLEE
LHQALISKLQ KLKTGNETVT HPDTAGGLSR TPHWPGQHIP KGKCCASREK EEQIPKDIFP
VTETVDGQGQ AWRHHNGFDF AVIKELKTAA SQYGATAPYT LAIVESVADN WLTPTDWNTL
VRAVLSGGDH LLWKSEFFEN CRDTAKRNQQ AGNGWDFDML TGSGNYSSTD AQMQYDPGLF
AQIQAAATKA WRKLPVKGDP GASLTGVKQG PDEPFADFVH RLITTAGRIF GSAEAGVDYV
KQLAYENANP ACQAAIRPYR KKTDLTGYIR LCSDIGPSYQ QGLAMAAAFS GQTVKDFLNN
KNKEKGGCCF KCGKKGHFAK NCHEHAHNNA EPKVPGLCPR CKRGKHWANE CKSKTDNQGN
PIPPHQGNRV EGPAPGPETS LWGSQLCSSQ QKQPISKLTR ATPGSAGLDL CSTSHTVLTP
EMGPQALSTG IYGPLPPNTF GLILGRSSIT MKGLQVYPGV IDNDYTGEIK IMAKAVNNIV
TVSQGNRIAQ LILLPLIETD NKVQQPYRGQ GSFGSSDIYW VQPITCQKPS LTLWLDDKMF
TGLIDTGADV TIIKLEDWPP NWPITDTLTN LRGIGQSNNP KQSSKYLTWR DKENNSGLIK
PFVIPNLPVN LWGRDLLSQM KIMMCSPNDI VTAQMLAQGY SPGKGLGKKE NGILHPIPNQ
GQSNKKGFGN F
