PHOSP_RYSV
ID PHOSP_RYSV Reviewed; 322 AA.
AC O70790; Q86522;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 29-SEP-2021, entry version 49.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
DE AltName: Full=Protein M1;
GN Name=P;
OS Rice yellow stunt virus (RYSV) (Rice transitory yellowing virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Nucleorhabdovirus.
OX NCBI_TaxID=59380;
OH NCBI_TaxID=4530; Oryza sativa (Rice).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Zhu H.T., Fang R.X., Chen X.Y.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12867659; DOI=10.1099/vir.0.19195-0;
RA Huang Y., Zhao H., Luo Z., Chen X., Fang R.X.;
RT "Novel structure of the genome of Rice yellow stunt virus: identification
RT of the gene 6-encoded virion protein.";
RL J. Gen. Virol. 84:2259-2264(2003).
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; U47053; AAA92922.1; -; Genomic_RNA.
DR EMBL; AB011257; BAA25155.1; -; Genomic_RNA.
DR RefSeq; NP_620497.1; NC_003746.1.
DR GeneID; 944312; -.
DR KEGG; vg:944312; -.
DR Proteomes; UP000002325; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
PE 3: Inferred from homology;
KW Chaperone; Host cytoplasm; Phosphoprotein; Reference proteome;
KW Viral RNA replication; Virion.
FT CHAIN 1..322
FT /note="Phosphoprotein"
FT /id="PRO_0000299227"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 4
FT /note="S -> D (in Ref. 1; AAA92922)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 35499 MW; 403119618524986E CRC64;
MSGSGSEQTP RLTRSSSRST LTGVASGRVE KIRSSPKSLD RIAKKYKDFD PETAKIIRAD
LEETQADKTM EVGGSTQESA QQITGAKRPN EEDQGGAQEA AKRVNRSNKV NSLLTSNGVT
DPAKSKISNY IVGRLNANNI EADSVMVAEC TNIAIHAWKE GKKYLDDKII SQATTTIPTL
ITNLVSNANT LSNVIASLNN VPDKLVSDIR TQVENVSNQT GQKAAKRDVL LKSSESIYNN
AVKESKVDFI NNYLTSSGVN VDELRKDSHH YRTVVSRIEK KYTVLVMMPE HEEHHTLKEK
VATNRTFVKE SAQTLSQKYV TQ