ID   PHOSP_TPMV              Reviewed;         527 AA.
AC   Q9WS39;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   02-JUN-2021, entry version 62.
DE   RecName: Full=Phosphoprotein;
DE            Short=Protein P;
GN   Name=P/V;
OS   Tupaia paramyxovirus (TPMV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Narmovirus; Tupaia narmovirus.
OX   NCBI_TaxID=92129;
OH   NCBI_TaxID=37347; Tupaia belangeri (Common tree shrew) (Tupaia glis belangeri).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RNA EDITING.
RX   PubMed=10366580; DOI=10.1006/viro.1999.9693;
RA   Tidona C.A., Kurz H.W., Gelderblom H.R., Darai G.;
RT   "Isolation and molecular characterization of a novel cytopathogenic
RT   paramyxovirus from tree shrews.";
RL   Virology 258:425-434(1999).
CC   -!- FUNCTION: Essential component of the RNA polymerase and the nascent
CC       chain assembly complex. Also required during RNA synthesis.
CC   -!- RNA EDITING: Modified_positions=229 {ECO:0000269|PubMed:10366580};
CC       Note=Partially edited. RNA editing at this position consists of an
CC       insertion of one guanine nucleotide. The sequence displayed here is the
CC       P protein, derived from the edited RNA. The unedited RNA gives rise to
CC       the V protein (AC Q9QM81).;
CC   -!- SIMILARITY: Belongs to the morbillivirus P protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF079780; AAD28695.1; -; Genomic_RNA.
DR   RefSeq; NP_054691.1; NC_002199.1.
DR   SMR; Q9WS39; -.
DR   GeneID; 1452636; -.
DR   KEGG; vg:1452636; -.
DR   Proteomes; UP000136220; Genome.
DR   InterPro; IPR004897; P/V_Pprotein_paramyxoviral.
DR   InterPro; IPR028243; Paramyxo_P/V_N.
DR   Pfam; PF03210; Paramyx_P_V_C; 1.
DR   Pfam; PF13825; Paramyxo_P_V_N; 1.
PE   3: Inferred from homology;
KW   Phosphoprotein; Reference proteome; RNA editing; Viral RNA replication.
FT   CHAIN           1..527
FT                   /note="Phosphoprotein"
FT                   /id="PRO_0000142719"
FT   REGION          29..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..132
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..204
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  57380 MW;  BF21CE37F3224F06 CRC64;
     MNNTEIIENA SKVLEAIDAA KEEELRNLNS LVQPRAPLNA GSTPGEIINE IKHLSTRDQE
     GGTSSKDEEE SGAGRTVAEG AATRDHKYSK SRPKKQPRSG LQSGAAGKNP TPDGEGGDTC
     NRELDQHSDG DGHSNTEGAS SDLASIQPCQ TDDAPCSSTS YLDEEDEPAV RPKTQCKQSG
     LIESKEDEDG MLSELHEQHK GRSKRLSALG RVNSSPIPSP RPDELLKKGI GESIVWSGRM
     TESLLSHGVI QCVPGSDRYQ SGKSVSVADA HLNARSACWT QNKEPQCHIT NSPSDTSTDN
     ASRSELRTIE EEDYLQDDDF EQSIEDRDFD PGDWDPSDKH NDNGLLLQIL KNQEEILNRL
     KTIGSIQESL DSIKRIQSKQ GLALSTLEGL LSSVMIAIPG SGNPGSSVEI NPDLKPMLGR
     NKNRALKEVS DELTPPNQFL QKQGMTIQQA VKPKETMFPP AIKTGESSAK GFHPKENLVS
     RTVINSIITA RVNNPELAAK LKLAVAKAQT KEELERIHKS IIKNLKN