ID   PHOSP_PIRYV             Reviewed;         327 AA.
AC   Q01769;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   23-FEB-2022, entry version 73.
DE   RecName: Full=Phosphoprotein;
DE            Short=Protein P;
DE   AltName: Full=Protein M1;
GN   Name=P;
OS   Piry virus (PIRYV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Vesiculovirus.
OX   NCBI_TaxID=11274;
OH   NCBI_TaxID=126289; Gracilinanus microtarsus (Brazilian gracile mouse opossum).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1454546; DOI=10.1093/nar/20.21.5843;
RA   Barik S.;
RT   "The phosphoprotein (P) gene of the rhabdovirus Piry: its cloning,
RT   sequencing, and expression in Escherichia coli.";
RL   Nucleic Acids Res. 20:5843-5843(1992).
CC   -!- FUNCTION: Essential component of the RNA polymerase transcription and
CC       replication complex. Binds the viral ribonucleocapsid and positions the
CC       L polymerase on the template. May act as a chaperone for newly
CC       synthesized free N protein, so-called N(0). Plays a role in virion
CC       assembly (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer when phosphorylated in domain I. This trimer is
CC       stabilized by binding to the L protein. Binds N(0), and N in
CC       ribonucleocapsid (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm {ECO:0000250}.
CC   -!- PTM: Phosphorylated by host kinases. Phosphorylation play an important
CC       role in facilitating trimerization and possibly P-L complex formation
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the vesiculovirus protein P family.
CC       {ECO:0000305}.
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DR   EMBL; D26175; BAA05161.1; -; Genomic_RNA.
DR   EMBL; Z15093; CAA78805.1; -; Genomic_RNA.
DR   PIR; S26647; S26647.
DR   SMR; Q01769; -.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.10.8.440; -; 1.
DR   InterPro; IPR043036; Phosphoprotein_C_viral.
PE   3: Inferred from homology;
KW   Chaperone; Host cytoplasm; Phosphoprotein; Viral RNA replication; Virion.
FT   CHAIN           1..327
FT                   /note="Phosphoprotein"
FT                   /id="PRO_0000222826"
FT   REGION          28..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..77
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..243
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         284
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   327 AA;  35734 MW;  21B3C25C453B4C5E CRC64;
     MSSRGRAIQK ALANYPDFNQ TLSALNEMEE QTEKSFSTFT TLSASNGSSP EYFLGSMLKE
     SDESESVDDD ESVNDDLSPE NAVEPYKGSE GEDSFGDKDE TVFFEEDLPW SAMVQKTVNG
     KLVAELSAPQ GLTPKQLSQW TDSVLALMDL SKNIRLSSAK IDYLASGLKI TEHMSSCFSS
     TAPPLLKEFQ PVTLSHRDTS PERGPSSRPS RPTVMPPART LILENTPSTP TPESTSSASG
     SPLNLPEIKP PKDWASIAIR EFSLNPLSGD GPQYKGTLAR LFGSLESALQ YANGGNPSTK
     DMLIAGLRRK GIFNKIRIKY FLDPIYD