NCAP_HRSVA
ID NCAP_HRSVA Reviewed; 391 AA.
AC P03418; P88810;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Nucleoprotein;
DE Short=Protein N;
DE AltName: Full=Nucleocapsid protein;
GN Name=N;
OS Human respiratory syncytial virus A (strain A2).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=11259;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3839952; DOI=10.1016/0042-6822(85)90053-4;
RA Collins P.L., Anderson K., Langer S.J., Wertz G.W.;
RT "Correct sequence for the major nucleocapsid protein mRNA of respiratory
RT syncytial virus.";
RL Virology 146:69-77(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6310521; DOI=10.1093/nar/11.17.5941;
RA Elango N., Venkatesan S.;
RT "Amino acid sequence of human respiratory syncytial virus nucleocapsid
RT protein.";
RL Nucleic Acids Res. 11:5941-5951(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Cold-passage attenuated;
RX PubMed=7747420; DOI=10.1006/viro.1995.1178;
RA Connors M., Crowe J.E. Jr., Firestone C.Y., Murphy B.R., Collins P.L.;
RT "A cold-passaged, attenuated strain of human respiratory syncytial virus
RT contains mutations in the F and L genes.";
RL Virology 208:478-484(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Cold-passage attenuated;
RX PubMed=9035372; DOI=10.1007/bf00366988;
RA Crowe J.E. Jr., Firestone C.Y., Whitehead S.S., Collins P.L., Murphy B.R.;
RT "Acquisition of the ts phenotype by a chemically mutagenized cold-passaged
RT human respiratory syncytial virus vaccine candidate results from the
RT acquisition of a single mutation in the polymerase (L) gene.";
RL Virus Genes 13:269-273(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Cold-passage attenuated;
RX PubMed=8918930; DOI=10.1006/viro.1996.0618;
RA Firestone C.Y., Whitehead S.S., Collins P.L., Murphy B.R., Crowe J.E. Jr.;
RT "Nucleotide sequence analysis of the respiratory syncytial virus subgroup A
RT cold-passaged (cp) temperature sensitive (ts) cpts-248/404 live attenuated
RT virus vaccine candidate.";
RL Virology 225:419-422(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Cold-passage attenuated;
RX PubMed=9557743; DOI=10.1128/jvi.72.5.4467-4471.1998;
RA Whitehead S.S., Juhasz K., Firestone C.Y., Collins P.L., Murphy B.R.;
RT "Recombinant respiratory syncytial virus (RSV) bearing a set of mutations
RT from cold-passaged RSV is attenuated in chimpanzees.";
RL J. Virol. 72:4467-4471(1998).
RN [7]
RP FUNCTION.
RX PubMed=9299631; DOI=10.1006/viro.1997.8734;
RA Fearns R., Peeples M.E., Collins P.L.;
RT "Increased expression of the N protein of respiratory syncytial virus
RT stimulates minigenome replication but does not alter the balance between
RT the synthesis of mRNA and antigenome.";
RL Virology 236:188-201(1997).
RN [8]
RP INTERACTION WITH PROTEIN M2-1.
RX PubMed=10846068; DOI=10.1128/jvi.74.13.5880-5885.2000;
RA Hardy R.W., Wertz G.W.;
RT "The Cys(3)-His(1) motif of the respiratory syncytial virus M2-1 protein is
RT essential for protein function.";
RL J. Virol. 74:5880-5885(2000).
RN [9]
RP INTERACTION WITH THE PHOSPHOPROTEIN.
RX PubMed=11861854; DOI=10.1128/jvi.76.6.2871-2880.2002;
RA Lu B., Brazas R., Ma C.H., Kristoff T., Cheng X., Jin H.;
RT "Identification of temperature-sensitive mutations in the phosphoprotein of
RT respiratory syncytial virus that are likely involved in its interaction
RT with the nucleoprotein.";
RL J. Virol. 76:2871-2880(2002).
RN [10]
RP INTERACTION WITH THE PHOSPHOPROTEIN.
RX PubMed=12368320; DOI=10.1128/jvi.76.21.10776-10784.2002;
RA Lu B., Ma C.H., Brazas R., Jin H.;
RT "The major phosphorylation sites of the respiratory syncytial virus
RT phosphoprotein are dispensable for virus replication in vitro.";
RL J. Virol. 76:10776-10784(2002).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=17703289; DOI=10.1007/s00705-007-1048-4;
RA Carromeu C., Simabuco F.M., Tamura R.E., Farinha Arcieri L.E.,
RA Ventura A.M.;
RT "Intracellular localization of human respiratory syncytial virus L
RT protein.";
RL Arch. Virol. 152:2259-2263(2007).
RN [12]
RP INTERACTION WITH THE PHOSPHOPROTEIN.
RX PubMed=17170452; DOI=10.1099/vir.0.82282-0;
RA Tran T.L., Castagne N., Bhella D., Varela P.F., Bernard J., Chilmonczyk S.,
RA Berkenkamp S., Benhamo V., Grznarova K., Grosclaude J., Nespoulos C.,
RA Rey F.A., Eleouet J.F.;
RT "The nine C-terminal amino acids of the respiratory syncytial virus protein
RT P are necessary and sufficient for binding to ribonucleoprotein complexes
RT in which six ribonucleotides are contacted per N protein protomer.";
RL J. Gen. Virol. 88:196-206(2007).
RN [13]
RP INTERACTION WITH HOST EIF2AK2.
RX PubMed=20519500; DOI=10.1074/jbc.m109.077321;
RA Groskreutz D.J., Babor E.C., Monick M.M., Varga S.M., Hunninghake G.W.;
RT "Respiratory syncytial virus limits alpha subunit of eukaryotic translation
RT initiation factor 2 (eIF2alpha) phosphorylation to maintain translation and
RT viral replication.";
RL J. Biol. Chem. 285:24023-24031(2010).
RN [14]
RP PHOSPHORYLATION AT TYR-38, AND MUTAGENESIS OF TYR-23; TYR-38 AND TYR-69.
RX PubMed=22019509; DOI=10.1016/j.virusres.2011.10.004;
RA Asenjo A., Cuesta I., Vivo A., Villanueva N.;
RT "Phosphorylation of the human respiratory syncytial virus N protein
RT provokes a decrease in viral RNA synthesis.";
RL Virus Res. 163:396-400(2012).
RN [15]
RP FUNCTION.
RX PubMed=22623778; DOI=10.1128/jvi.00215-12;
RA Lifland A.W., Jung J., Alonas E., Zurla C., Crowe J.E. Jr.,
RA Santangelo P.J.;
RT "Human respiratory syncytial virus nucleoprotein and inclusion bodies
RT antagonize the innate immune response mediated by MDA5 and MAVS.";
RL J. Virol. 86:8245-8258(2012).
RN [16]
RP INTERACTION WITH THE PHOSPHOPROTEIN, MUTAGENESIS OF ARG-132, AND FUNCTION.
RX PubMed=22623798; DOI=10.1128/jvi.00058-12;
RA Galloux M., Tarus B., Blazevic I., Fix J., Duquerroy S., Eleouet J.F.;
RT "Characterization of a viral phosphoprotein binding site on the surface of
RT the respiratory syncytial nucleoprotein.";
RL J. Virol. 86:8375-8387(2012).
RN [17]
RP INTERACTION WITH THE PHOSPHOPROTEIN.
RX PubMed=25407889; DOI=10.1186/s12985-014-0191-2;
RA Shapiro A.B., Gao N., O'Connell N., Hu J., Thresher J., Gu R.F.,
RA Overman R., Hardern I.M., Sproat G.G.;
RT "Quantitative investigation of the affinity of human respiratory syncytial
RT virus phosphoprotein C-terminus binding to nucleocapsid protein.";
RL Virol. J. 11:191-191(2014).
RN [18]
RP INTERACTION WITH HOST EIF1AX.
RX PubMed=25479059; DOI=10.1371/journal.pone.0114447;
RA Wei T., Li D., Marcial D., Khan M., Lin M.H., Snape N., Ghildyal R.,
RA Harrich D., Spann K.;
RT "The eukaryotic elongation factor 1A is critical for genome replication of
RT the paramyxovirus respiratory syncytial virus.";
RL PLoS ONE 9:e114447-e114447(2014).
RN [19]
RP INTERACTION WITH THE PHOSPHOPROTEIN.
RX PubMed=25568210; DOI=10.1128/jvi.03666-14;
RA Galloux M., Gabiane G., Sourimant J., Richard C.A., England P., Moudjou M.,
RA Aumont-Nicaise M., Fix J., Rameix-Welti M.A., Eleouet J.F.;
RT "Identification and characterization of the binding site of the respiratory
RT syncytial virus phosphoprotein to RNA-free nucleoprotein.";
RL J. Virol. 89:3484-3496(2015).
RN [20]
RP INTERACTION WITH THE PHOSPHOPROTEIN.
RX PubMed=26474524; DOI=10.1016/j.virusres.2015.10.011;
RA Asenjo A., Villanueva N.;
RT "Phosphorylation of the human respiratory syncytial virus P protein
RT mediates M2-2 regulation of viral RNA synthesis, a process that involves
RT two P proteins.";
RL Virus Res. 211:117-125(2016).
RN [21]
RP INTERACTION WITH THE PHOSPHOPROTEIN.
RX PubMed=28031463; DOI=10.1074/jbc.m116.765958;
RA Pereira N., Cardone C., Lassoued S., Galloux M., Fix J., Assrir N.,
RA Lescop E., Bontems F., Eleouet J.F., Sizun C.;
RT "New Insights into Structural Disorder in Human Respiratory Syncytial Virus
RT Phosphoprotein and Implications for Binding of Protein Partners.";
RL J. Biol. Chem. 292:2120-2131(2017).
RN [22]
RP INTERACTION WITH THE PHOSPHOPROTEIN.
RX PubMed=30626736; DOI=10.1074/jbc.ra118.006453;
RA Esneau C., Raynal B., Roblin P., Brule S., Richard C.A., Fix J.,
RA Eleouet J.F., Galloux M.;
RT "Biochemical characterization of the respiratory syncytial virus N0-P
RT complex in solution.";
RL J. Biol. Chem. 294:3647-3660(2019).
RN [23]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=32878896; DOI=10.1128/jvi.01380-20;
RA Jobe F., Simpson J., Hawes P., Guzman E., Bailey D.;
RT "Respiratory syncytial virus sequesters NF-kappaB subunit p65 to
RT cytoplasmic inclusion bodies to inhibit innate immune signalling.";
RL J. Virol. 0:0-0(2020).
RN [24] {ECO:0007744|PDB:2WJ8}
RP X-RAY CRYSTALLOGRAPHY (3.29 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=19965480; DOI=10.1126/science.1177634;
RA Tawar R.G., Duquerroy S., Vonrhein C., Varela P.F., Damier-Piolle L.,
RA Castagne N., MacLellan K., Bedouelle H., Bricogne G., Bhella D.,
RA Eleouet J.F., Rey F.A.;
RT "Crystal structure of a nucleocapsid-like nucleoprotein-RNA complex of
RT respiratory syncytial virus.";
RL Science 326:1279-1283(2009).
RN [25] {ECO:0007744|PDB:2YHM}
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 1-375.
RX PubMed=22102022; DOI=10.1107/s1744309111029228;
RA El Omari K., Dhaliwal B., Ren J., Abrescia N.G., Lockyer M., Powell K.L.,
RA Hawkins A.R., Stammers D.K.;
RT "Structures of respiratory syncytial virus nucleocapsid protein from two
RT crystal forms: details of potential packing interactions in the native
RT helical form.";
RL Acta Crystallogr. F 67:1179-1183(2011).
RN [26] {ECO:0007744|PDB:4BKK}
RP STRUCTURE BY NMR, FUNCTION, AND SUBUNIT.
RX PubMed=23677789; DOI=10.1099/vir.0.053025-0;
RA Bakker S.E., Duquerroy S., Galloux M., Loney C., Conner E., Eleouet J.F.,
RA Rey F.A., Bhella D.;
RT "The respiratory syncytial virus nucleoprotein-RNA complex forms a left-
RT handed helical nucleocapsid.";
RL J. Gen. Virol. 94:1734-1738(2013).
RN [27] {ECO:0007744|PDB:4UC6, ECO:0007744|PDB:4UC7, ECO:0007744|PDB:4UC8, ECO:0007744|PDB:4UC9, ECO:0007744|PDB:4UCA, ECO:0007744|PDB:4UCB, ECO:0007744|PDB:4UCC, ECO:0007744|PDB:4UCD, ECO:0007744|PDB:4UCE}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 31-252.
RX PubMed=26246564; DOI=10.1128/jvi.01612-15;
RA Ouizougun-Oubari M., Pereira N., Tarus B., Galloux M., Lassoued S., Fix J.,
RA Tortorici M.A., Hoos S., Baron B., England P., Desmaele D., Couvreur P.,
RA Bontems F., Rey F.A., Eleouet J.F., Sizun C., Slama-Schwok A.,
RA Duquerroy S.;
RT "A Druggable Pocket at the Nucleocapsid/Phosphoprotein Interaction Site of
RT Human Respiratory Syncytial Virus.";
RL J. Virol. 89:11129-11143(2015).
RN [28]
RP RNA-BINDING, AND FUNCTION.
RX PubMed=31229488; DOI=10.1016/j.abb.2019.06.005;
RA Alvarez Paggi D., Esperante S.A., Salgueiro M., Camporeale G.,
RA de Oliveira G.A.P., Prat Gay G.;
RT "A conformational switch balances viral RNA accessibility and protection in
RT a nucleocapsid ring model.";
RL Arch. Biochem. Biophys. 671:77-86(2019).
CC -!- FUNCTION: Encapsidates the viral RNA genome by forming a left-handed
CC helical nucleocapsid that protects the RNA from nucleases
CC (PubMed:23677789, PubMed:19965480, PubMed:31229488). RNA replication
CC depends on the availability of soluble nucleoprotein (PubMed:9299631,
CC PubMed:22623798). The encapsidated genomic RNA is termed the NC and
CC serves as template for transcription and replication (PubMed:22623798).
CC Together with the phosphoprotein, sequesters host NF-kappa-B in
CC inclusion bodies (IBs) thereby inhibiting this host defense pathway
CC (PubMed:32878896). May also act as a modulator of the innate immune
CC response by sequestration of host IFIH1/MDA5 and MAVS into IBs
CC (PubMed:22623778). {ECO:0000269|PubMed:19965480,
CC ECO:0000269|PubMed:22623778, ECO:0000269|PubMed:22623798,
CC ECO:0000269|PubMed:23677789, ECO:0000269|PubMed:31229488,
CC ECO:0000269|PubMed:32878896, ECO:0000269|PubMed:9299631}.
CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid (PubMed:23677789,
CC PubMed:19965480). Binds to viral genomic RNA. Interacts (via N-
CC terminus) with the phosphoprotein P (via C-terminus); the
CC phosphorylated phosphoprotein P binds to N-RNA complex
CC (PubMed:26474524, PubMed:17170452, PubMed:22623798, PubMed:25407889,
CC PubMed:11861854, PubMed:12368320, PubMed:28031463). When in a monomeric
CC RNA-free form, interacts with the phosphoprotein (via N-terminus)
CC (PubMed:25568210, PubMed:30626736). Interacts with protein M2-1; this
CC interaction allows the association of nucleocapsid with the matrix
CC protein (PubMed:10846068). Interacts with host EIF2AK2/PKR; this
CC interaction inhibits EIF2AK2 phosphorylation of EIF2S1 and blocks
CC EIF2AK2-mediated translation shutoff (PubMed:20519500). Interacts with
CC host EIF1AX; this interaction recruits EIF1AX to the viral replication
CC complex to facilitate viral genomic RNA synthesis and virus production
CC (PubMed:25479059). Interacts with host NF-kappa-B; this interaction
CC sequesters NF-kappa-B in inclusion bodies (By similarity).
CC {ECO:0000250|UniProtKB:P22677, ECO:0000269|PubMed:10846068,
CC ECO:0000269|PubMed:11861854, ECO:0000269|PubMed:12368320,
CC ECO:0000269|PubMed:17170452, ECO:0000269|PubMed:19965480,
CC ECO:0000269|PubMed:20519500, ECO:0000269|PubMed:22623798,
CC ECO:0000269|PubMed:23677789, ECO:0000269|PubMed:25407889,
CC ECO:0000269|PubMed:25479059, ECO:0000269|PubMed:25568210,
CC ECO:0000269|PubMed:26474524, ECO:0000269|PubMed:28031463,
CC ECO:0000269|PubMed:30626736}.
CC -!- INTERACTION:
CC P03418; O14744: PRMT5; Xeno; NbExp=2; IntAct=EBI-6930799, EBI-351098;
CC P03418; Q9BQA1: WDR77; Xeno; NbExp=3; IntAct=EBI-6930799, EBI-1237307;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm
CC {ECO:0000269|PubMed:17703289, ECO:0000269|PubMed:32878896}.
CC Note=Localizes in cytoplasmic inclusion bodies.
CC {ECO:0000269|PubMed:17703289, ECO:0000269|PubMed:32878896}.
CC -!- PTM: Tyrosine phosphorylation modulates viral transcription and
CC replication. {ECO:0000269|PubMed:22019509}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA24906.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M11486; AAB59852.1; -; Genomic_RNA.
DR EMBL; X00001; CAA24906.1; ALT_FRAME; Genomic_RNA.
DR EMBL; U50362; AAB86658.1; -; Genomic_RNA.
DR EMBL; U50363; AAB86670.1; -; Genomic_RNA.
DR EMBL; U63644; AAC55964.1; -; Genomic_RNA.
DR EMBL; AF035006; AAC14896.1; -; Genomic_RNA.
DR PIR; A04026; VHNZ.
DR PIR; A23316; VHNZ1.
DR PDB; 2WJ8; X-ray; 3.29 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-391.
DR PDB; 2YHM; X-ray; 3.60 A; A/B/C/D/E/F/G/H/I/J=1-375.
DR PDB; 4BKK; EM; -; B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-391.
DR PDB; 4UC6; X-ray; 2.10 A; A/B=31-252.
DR PDB; 4UC7; X-ray; 2.45 A; A/B=31-252.
DR PDB; 4UC8; X-ray; 2.00 A; A/B=31-252.
DR PDB; 4UC9; X-ray; 2.40 A; A/B/C/D=31-252.
DR PDB; 4UCA; X-ray; 3.22 A; A/B=31-252.
DR PDB; 4UCB; X-ray; 2.79 A; A/B=31-252.
DR PDB; 4UCC; X-ray; 2.05 A; A/B=31-252.
DR PDB; 4UCD; X-ray; 2.66 A; A/B=31-252.
DR PDB; 4UCE; X-ray; 2.95 A; A/B=31-252.
DR PDB; 6YJL; NMR; -; A=361-391.
DR PDBsum; 2WJ8; -.
DR PDBsum; 2YHM; -.
DR PDBsum; 4BKK; -.
DR PDBsum; 4UC6; -.
DR PDBsum; 4UC7; -.
DR PDBsum; 4UC8; -.
DR PDBsum; 4UC9; -.
DR PDBsum; 4UCA; -.
DR PDBsum; 4UCB; -.
DR PDBsum; 4UCC; -.
DR PDBsum; 4UCD; -.
DR PDBsum; 4UCE; -.
DR PDBsum; 6YJL; -.
DR SMR; P03418; -.
DR IntAct; P03418; 8.
DR BindingDB; P03418; -.
DR ChEMBL; CHEMBL4105793; -.
DR PRIDE; P03418; -.
DR EvolutionaryTrace; P03418; -.
DR Proteomes; UP000007678; Genome.
DR Proteomes; UP000134464; Genome.
DR Proteomes; UP000181145; Genome.
DR Proteomes; UP000181262; Genome.
DR Proteomes; UP000181559; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0039644; P:suppression by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR GO; GO:0039580; P:suppression by virus of host PKR signaling; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0039554; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host MDA-5 activity; IEA:UniProtKB-KW.
DR GO; GO:0039545; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; IEA:UniProtKB-KW.
DR InterPro; IPR004930; Pneumo_ncap.
DR Pfam; PF03246; Pneumo_ncap; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Helical capsid protein; Host cytoplasm;
KW Host-virus interaction; Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host MAVS by virus; Inhibition of host MDA5 by virus;
KW Inhibition of host NF-kappa-B by virus; Inhibition of host PKR by virus;
KW Inhibition of host RLR pathway by virus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Viral immunoevasion;
KW Viral nucleoprotein; Virion.
FT CHAIN 1..391
FT /note="Nucleoprotein"
FT /id="PRO_0000142652"
FT REGION 31..252
FT /note="Interaction with the phosphoprotein"
FT /evidence="ECO:0000269|PubMed:22623798"
FT REGION 244..290
FT /note="Interaction with the phosphoprotein"
FT /evidence="ECO:0000250|UniProtKB:P22677"
FT REGION 338..364
FT /note="Interaction with the phosphoprotein"
FT /evidence="ECO:0000250|UniProtKB:P22677"
FT MOD_RES 38
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:22019509"
FT VARIANT 267
FT /note="V -> I (in strain: Cold-passage attenuated)"
FT MUTAGEN 23
FT /note="Y->D,F: 65% loss of transcription but no effect on
FT replication."
FT /evidence="ECO:0000269|PubMed:22019509"
FT MUTAGEN 38
FT /note="Y->D,F: 45% loss of transcription but no effect on
FT replication."
FT /evidence="ECO:0000269|PubMed:22019509"
FT MUTAGEN 69
FT /note="Y->F: Increased transcription and 50% loss of
FT replication."
FT /evidence="ECO:0000269|PubMed:22019509"
FT MUTAGEN 132
FT /note="R->A: Almost complete loss of viral RNA synthesis."
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:2WJ8"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:4UC6"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:4UC8"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:4UC8"
FT HELIX 62..74
FT /evidence="ECO:0007829|PDB:4UC8"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:4UC8"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4UC6"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:4UC8"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:4UC8"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:4UC8"
FT HELIX 121..142
FT /evidence="ECO:0007829|PDB:4UC8"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:4UC8"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:4UC8"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:4UC8"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:4UC8"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:4UC8"
FT HELIX 202..215
FT /evidence="ECO:0007829|PDB:4UC8"
FT HELIX 218..230
FT /evidence="ECO:0007829|PDB:4UC8"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:4UC9"
FT HELIX 238..249
FT /evidence="ECO:0007829|PDB:4UC8"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:4UC7"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:2WJ8"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:2WJ8"
FT HELIX 275..294
FT /evidence="ECO:0007829|PDB:2WJ8"
FT HELIX 295..300
FT /evidence="ECO:0007829|PDB:2WJ8"
FT TURN 301..305
FT /evidence="ECO:0007829|PDB:2WJ8"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:2WJ8"
FT HELIX 318..330
FT /evidence="ECO:0007829|PDB:2WJ8"
FT HELIX 344..357
FT /evidence="ECO:0007829|PDB:2WJ8"
FT HELIX 372..380
FT /evidence="ECO:0007829|PDB:6YJL"
SQ SEQUENCE 391 AA; 43451 MW; D06E84F4F88D382B CRC64;
MALSKVKLND TLNKDQLLSS SKYTIQRSTG DSIDTPNYDV QKHINKLCGM LLITEDANHK
FTGLIGMLYA MSRLGREDTI KILRDAGYHV KANGVDVTTH RQDINGKEMK FEVLTLASLT
TEIQINIEIE SRKSYKKMLK EMGEVAPEYR HDSPDCGMII LCIAALVITK LAAGDRSGLT
AVIRRANNVL KNEMKRYKGL LPKDIANSFY EVFEKHPHFI DVFVHFGIAQ SSTRGGSRVE
GIFAGLFMNA YGAGQVMLRW GVLAKSVKNI MLGHASVQAE MEQVVEVYEY AQKLGGEAGF
YHILNNPKAS LLSLTQFPHF SSVVLGNAAG LGIMGEYRGT PRNQDLYDAA KAYAEQLKEN
GVINYSVLDL TAEELEAIKH QLNPKDNDVE L
