ID   PHOSP_SVCV              Reviewed;         309 AA.
AC   Q91DS2;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   29-SEP-2021, entry version 62.
DE   RecName: Full=Phosphoprotein;
DE            Short=P protein;
DE            Short=Protein P;
DE   AltName: Full=Protein M1;
GN   Name=P;
OS   Spring viremia of carp virus (Rhabdovirus carpia).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Sprivivirus.
OX   NCBI_TaxID=696863;
OH   NCBI_TaxID=7962; Cyprinus carpio (Common carp).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Fijan reference;
RX   PubMed=11900842; DOI=10.1016/s0168-1702(01)00441-5;
RA   Hoffmann B., Schutze H., Mettenleiter T.C.;
RT   "Determination of the complete genomic sequence and analysis of the gene
RT   products of the virus of Spring Viremia of Carp, a fish rhabdovirus.";
RL   Virus Res. 84:89-100(2002).
RN   [2]
RP   INTERACTION WITH HOST REF(2)P.
RX   PubMed=7684462; DOI=10.1128/jvi.67.6.3208-3216.1993;
RA   Wyers F., Dru P., Simonet B., Contamine D.;
RT   "Immunological cross-reactions and interactions between the Drosophila
RT   melanogaster ref(2)P protein and sigma rhabdovirus proteins.";
RL   J. Virol. 67:3208-3216(1993).
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. {ECO:0000250|UniProtKB:P03520}.
CC   -!- SUBUNIT: Homotrimer. This trimer is stabilized by binding to the L
CC       protein. Binds N(0), and N in ribonucleocapsid (By similarity). May
CC       bind to host ref(2)P (PubMed:7684462). {ECO:0000250|UniProtKB:P03520,
CC       ECO:0000269|PubMed:7684462}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03520}. Host
CC       cytoplasm {ECO:0000250|UniProtKB:P03520}.
CC   -!- PTM: Phosphorylated by host kinases. Phosphorylation play an important
CC       role in facilitating trimerization and possibly P-L complex formation.
CC       {ECO:0000250|UniProtKB:P03520}.
CC   -!- SIMILARITY: Belongs to the vesiculovirus protein P family.
CC       {ECO:0000305}.
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DR   EMBL; AJ318079; CAC51334.1; -; Genomic_RNA.
DR   SMR; Q91DS2; -.
DR   Proteomes; UP000007541; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.440; -; 1.
DR   InterPro; IPR043036; Phosphoprotein_C_viral.
PE   1: Evidence at protein level;
KW   Chaperone; Host cytoplasm; Phosphoprotein; Reference proteome;
KW   Viral RNA replication; Viral transcription; Virion.
FT   CHAIN           1..309
FT                   /note="Phosphoprotein"
FT                   /id="PRO_0000287351"
FT   REGION          38..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..67
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         14
FT                   /note="Phosphotyrosine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03520"
FT   MOD_RES         272
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03520"
SQ   SEQUENCE   309 AA;  35513 MW;  1D0E682F23E8E8DA CRC64;
     MSLHSKLSES LKAYADLDKT VKEIEEQVSS MEEPVPKTVK YVTFEENLSE EEWESDSGDD
     DEDSIDDSLI PDYLRESSSI TVDEDEEDQK EDMEEHLPTV SWEEEPTGID IGFGPGIVMP
     SVSNHEGGTY VRYNGLGGVD PNCKDLISKM MRSLIGQIGN KYGYDIDLFD YQGDFLEVFL
     PHKPSKEDVR PDIRIGKKNE EGTSKQVSKP RGKEKIVLKT GDECGRFPMN KEAKKREPEG
     LWEVMKVLSV QFDPWKEDEP PLSLTIRDLF ISESEFRLHC NHSQTEREMA LVGIKLRRLY
     NKLYQKYRL