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PHOSP_MEASY
ID   PHOSP_MEASY             Reviewed;         507 AA.
AC   Q00793;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   02-JUN-2021, entry version 69.
DE   RecName: Full=Phosphoprotein;
DE            Short=Protein P;
GN   Name=P/V;
OS   Measles virus (strain Yamagata-1) (MeV) (Subacute sclerose panencephalitis
OS   virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus.
OX   NCBI_TaxID=11239;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RX   PubMed=1536889; DOI=10.1016/0167-4781(92)90515-2;
RA   Komase K., Haga T., Yoshikawa Y., Yamanouchi K.;
RT   "Complete nucleotide sequence of the phosphoprotein of the Yamagata-1
RT   strain of a defective subacute sclerosing panencephalitis (SSPE) virus.";
RL   Biochim. Biophys. Acta 1129:342-344(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:1536889};
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 gives rise to
CC       the V protein (AC P60168) (Probable). {ECO:0000305};
CC   -!- SIMILARITY: Belongs to the morbillivirus P protein family.
CC       {ECO:0000305}.
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DR   EMBL; D10635; BAA01483.1; -; mRNA.
DR   PIR; S20828; S20828.
DR   SMR; Q00793; -.
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   2: Evidence at transcript level;
KW   Phosphoprotein; RNA editing; Viral RNA replication.
FT   CHAIN           1..507
FT                   /note="Phosphoprotein"
FT                   /id="PRO_0000142692"
FT   REGION          42..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..156
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..300
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   507 AA;  54019 MW;  6AC7C921EDD75B91 CRC64;
     MAEEQARHVK NGLECIRALK AEPIGSLAIG EAMAAWSEIS DNPGQERATY KEEKAGGSGL
     SKPCLSAIGS TEGGAPRIRG QGSGESDDDT ETLGIPSRNL QASSTGLQCH YVYDHSGEAV
     KGIQDADSIM VQSGLDGDST LSEGDNESEN SDVDIGEPDT EGYAITDRGS APISMGFRAS
     DVETAEGGEI HELLRLQSRG NNFPKLGKTL NVPPPPDPGR ASTSETPIKK GTDARLASFG
     TEIASLLTGG ATQCARKSPS EPSGPGAPAG NVPECVSNAA LIQEWTPESG TTISPRSQNN
     KEGGDHYDDE LFSDIQDIKT ALAKIHEDNQ KIISKLESLL LLKGEVESIK KQINKQNISI
     STLEGHLSSI MIAIPGLGKD PNDPTADVEI NPDLKPIIGR DSGRALAEVL KKPVASRQLQ
     GMTNGRTSSR GQLLKEFQLK PIGKKMSSAV GFVPDTGPVS RSVIRSIIKS SRIEEDRKRY
     LMTLLDDIKG ANDLSKFHQM LMKIIMK
 
 
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