ID   PHOSP_ISFV              Reviewed;         289 AA.
AC   Q5K2K6;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Phosphoprotein;
DE            Short=Protein P;
DE   AltName: Full=Protein M1;
GN   Name=P;
OS   Isfahan virus (ISFV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Vesiculovirus.
OX   NCBI_TaxID=290008;
OH   NCBI_TaxID=10045; Gerbillinae (gerbils).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=29031; Phlebotomus papatasi (Sandfly).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15614433; DOI=10.1007/s00705-004-0452-2;
RA   Marriott A.C.;
RT   "Complete genome sequences of Chandipura and Isfahan vesiculoviruses.";
RL   Arch. Virol. 150:671-680(2005).
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; AJ810084; CAH17545.1; -; Genomic_RNA.
DR   RefSeq; YP_007641383.1; NC_020806.1.
DR   SMR; Q5K2K6; -.
DR   GeneID; 14857916; -.
DR   KEGG; vg:14857916; -.
DR   Proteomes; UP000204017; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR   Gene3D; 1.10.8.440; -; 1.
DR   InterPro; IPR043036; Phosphoprotein_C_viral.
DR   InterPro; IPR037263; Phosphoprotein_central.
DR   SUPFAM; SSF160892; SSF160892; 1.
PE   3: Inferred from homology;
KW   Chaperone; Host cytoplasm; Phosphoprotein; Viral RNA replication; Virion.
FT   CHAIN           1..289
FT                   /note="Phosphoprotein"
FT                   /id="PRO_0000292949"
FT   REGION          170..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         246
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   289 AA;  32250 MW;  EC6F8AE3726A6D2B CRC64;
     MSRLNQILKD YPLLEATTSE IESMESSLAD DVITSNDDEI QSVSPQYYLR DMFKASITEG
     PDDDFPPVPE VENDIILDDD EEYDGYKVDF AEARPWTALT QKNIDGRMNL ELMAPENLTD
     AQYKQWVESV SSIMTISRQI RLHQAEIMDT SSGLLIIENM IPSIGRTSEF KSIPEHIPPS
     PTSDHTTPPS SLRSDTPSQT SSSSMGLPDV SSASDWSGMI NKKIRIPPVV SSKSPYEFTL
     SDLYGSNQAA LDYLSGSGMD LRTAVCSGLK QRGIYNRIRI QYKITPEFV