PHOSP_PHODV
ID PHOSP_PHODV Reviewed; 507 AA.
AC P35939;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 02-JUN-2021, entry version 72.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
GN Name=P/V;
OS Phocine distemper virus (PDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=11240;
OH NCBI_TaxID=9709; Phocidae (true seals).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Ulster/88;
RX PubMed=1535099; DOI=10.1099/0022-1317-73-6-1587;
RA Curran M.D., Rima B.K.;
RT "The genes encoding the phospho- and matrix proteins of phocine distemper
RT virus.";
RL J. Gen. Virol. 73:1587-1591(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RNA EDITING.
RC STRAIN=Isolate DK88-4A;
RX PubMed=1634877; DOI=10.1099/0022-1317-73-4-885;
RA Blixenkrone-Moeller M., Sharma B., Varsanyi T., Hu A., Norrby E.,
RA Koevamees J.;
RT "Sequence analysis of the genes encoding the nucleocapsid protein and
RT phosphoprotein (P) of phocid distemper virus, and editing of the P gene
RT transcript.";
RL J. Gen. Virol. 73:885-893(1992).
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=231 {ECO:0000269|PubMed:1634877};
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 unedited RNA. The edited RNA version gives
CC rise to the V protein (AC P35941).;
CC -!- SIMILARITY: Belongs to the morbillivirus P protein family.
CC {ECO:0000305}.
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DR EMBL; D10371; BAA01203.1; -; Genomic_RNA.
DR EMBL; X75960; CAA53573.1; -; Genomic_RNA.
DR PIR; JQ1609; JQ1563.
DR SMR; P35939; -.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR InterPro; IPR004897; P/V_Pprotein_paramyxoviral.
DR InterPro; IPR028243; Paramyxo_P/V_N.
DR InterPro; IPR016075; RNA_pol_Pprot-P_XD_paramyxovir.
DR Pfam; PF03210; Paramyx_P_V_C; 1.
DR Pfam; PF13825; Paramyxo_P_V_N; 1.
DR SUPFAM; SSF101089; SSF101089; 1.
PE 3: Inferred from homology;
KW Phosphoprotein; RNA editing; Viral RNA replication.
FT CHAIN 1..507
FT /note="Phosphoprotein"
FT /id="PRO_0000142698"
FT REGION 30..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 192
FT /note="A -> T (in Ref. 2; CAA53573)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="A -> V (in Ref. 2; CAA53573)"
FT /evidence="ECO:0000305"
FT CONFLICT 393..394
FT /note="DV -> EL (in Ref. 2; CAA53573)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 54691 MW; D24BC3F3B86F712E CRC64;
MAEEQAYHVS KGLECIKALR ENPPNMEEIQ EVSNIRDQTY KSSKESGTTG VQEEEITQNI
DESHTPTKRS NSVSDVLQED QRGREDNTAP VEAKDRIEED TQTGPAVRRY YVYDHCGEKV
KGIEDADSLM VPAGPPSNRG FEGREGSLDD SIEDSSEDYS EGNASSNWGY TFGLNPDRAA
DVSMLMEEEL TALLGTGHNA GGQKRDGRTL QFPNSPEGSI GNQACEPIKK GTGEKLASHG
MMTAAGLTNG ATRSAPKSTG GSSGPNASAG SVPQSVTTAK MIQKCKTESG TRPQPEKPNE
IESDGEYDDE LFSEIQEIRS AITKLTEDNQ SILSKLDTLL LLKGEIDSIK KQISKQNIAI
STIEGHLSSI MIAIPGFGKD TGDPTANVDI NPDVRPIIGR DSGRALAEVL KKPASSRGNQ
KDGGLILGSK GQLLKDLQLK PIDKNSSSAI GFKPKDSAPS KAVIASLIRS SKVDQSHKQN
MLSLLKNIKG DDNLNEFYQM IKSISHI