ID   VP4A_LNYV3              Reviewed;         300 AA.
AC   Q9E7N7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   29-SEP-2021, entry version 53.
DE   RecName: Full=Phosphoprotein;
DE            Short=Protein P;
DE   AltName: Full=Protein 4a;
GN   Name=P;
OS   Lettuce necrotic yellows virus (isolate 318) (LNYV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Betarhabdovirinae;
OC   Cytorhabdovirus.
OX   NCBI_TaxID=928304;
OH   NCBI_TaxID=43191; Embergeria.
OH   NCBI_TaxID=4236; Lactuca sativa (Garden lettuce).
OH   NCBI_TaxID=43208; Reichardia tingitana.
OH   NCBI_TaxID=255580; Sonchus hydrophilus.
OH   NCBI_TaxID=50207; Sonchus oleraceus (Common sowthistle).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA / MRNA].
RX   PubMed=16313992; DOI=10.1016/j.virusres.2005.10.024;
RA   Dietzgen R.G., Callaghan B., Wetzel T., Dale J.L.;
RT   "Completion of the genome sequence of Lettuce necrotic yellows virus, type
RT   species of the genus Cytorhabdovirus.";
RL   Virus Res. 118:16-22(2006).
CC   -!- FUNCTION: Non catalytic polymerase cofactor and regulatory protein that
CC       plays a role in viral transcription and replication. Stabilizes the RNA
CC       polymerase L to the N-RNA template and binds the soluble protein N,
CC       preventing it from encapsidating non-genomic RNA (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer when phosphorylated. This trimer is stabilized by
CC       binding to the L protein. Binds soluble protein N, and ribonucleocapsid
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm {ECO:0000250}.
CC   -!- PTM: Phosphorylated by host kinases. {ECO:0000250}.
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DR   EMBL; AF209035; AAG32648.1; -; mRNA.
DR   EMBL; AJ867584; CAI30422.1; -; Genomic_RNA.
DR   RefSeq; YP_425088.1; NC_007642.1.
DR   PDB; 3T4R; X-ray; 2.00 A; A=230-300.
DR   PDBsum; 3T4R; -.
DR   SMR; Q9E7N7; -.
DR   GeneID; 3844365; -.
DR   KEGG; vg:3844365; -.
DR   Proteomes; UP000008592; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Host cytoplasm; Phosphoprotein;
KW   Reference proteome; Viral RNA replication; Virion.
FT   CHAIN           1..300
FT                   /note="Phosphoprotein"
FT                   /id="PRO_0000299209"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           231..241
FT                   /evidence="ECO:0007829|PDB:3T4R"
FT   HELIX           246..249
FT                   /evidence="ECO:0007829|PDB:3T4R"
FT   HELIX           254..260
FT                   /evidence="ECO:0007829|PDB:3T4R"
FT   HELIX           263..268
FT                   /evidence="ECO:0007829|PDB:3T4R"
FT   TURN            269..271
FT                   /evidence="ECO:0007829|PDB:3T4R"
FT   HELIX           277..300
FT                   /evidence="ECO:0007829|PDB:3T4R"
SQ   SEQUENCE   300 AA;  32499 MW;  C64041C7E1E2FBDA CRC64;
     MDSESLDFSS ADTVILRSPN AGTNPDGHPD TVECPDFDTD IPKTSDDSSK MDNKGSSSSS
     KAVKDLLELA AKSQGIVVTD VMQNTAIALH HNLGLDASSL DWFVAGITFA NNSMIMEKMV
     SAIKELQIEV RNIQVASSGI KGTSEELVSK MKANKNDIVK ELVKTRDSVL SAMGGILSAP
     EIEQQPVKTV TIGASQGRRK STVVPPIEIN PELESPVLSK TVSTATPEER IRHEKEKLLA
     DLDWEIGEIA QYTPLIVDFL VPDDILAMAA DGLTPELKEK IQNEIIENHI ALMALEEYSS