PHOSP_MEASI
ID PHOSP_MEASI Reviewed; 507 AA.
AC P26033;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 02-JUN-2021, entry version 75.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
GN Name=P/V;
OS Measles virus (strain IP-3-Ca) (MeV) (Subacute sclerose panencephalitis
OS virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=11237;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1585658; DOI=10.1016/0042-6822(92)90552-z;
RA Schmid A., Spielhofer P., Cattaneo R., Baczko K., Ter Meulen V.,
RA Billeter M.A.;
RT "Subacute sclerosing panencephalitis is typically characterized by
RT alterations in the fusion protein cytoplasmic domain of the persisting
RT measles virus.";
RL Virology 188:910-915(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:0000250}; Note=Partially
CC edited. RNA editing at this position consists of an insertion of one
CC guanine nucleotide. The sequence displayed here is the P protein,
CC derived from the unedited RNA. The edited RNA gives rise to the V
CC protein (AC P26036) (By similarity). {ECO:0000250};
CC -!- SIMILARITY: Belongs to the morbillivirus P protein family.
CC {ECO:0000305}.
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DR EMBL; X16566; CAA34564.1; -; Genomic_RNA.
DR SMR; P26033; -.
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_0000142691"
FT REGION 40..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 53885 MW; DF955AA9A9812440 CRC64;
MAEEQARHVK NGLECIRALK AEPIGSLAIG EAMAAWSEIS DNPGQEQATC KEEEAGASGL
SKPCLSAIGS TEGGAPRIRG QGSGESDDDT ETLGFPSRNL QASSTGLQCY YVYDHSGEAV
KGIQDADSIM VQSGLDGDST LSGGDNESEN SDVDIGEPDT EGYAITDRGP APISMGFRAS
DVETAEGGEI HELLRLQSRG NNFPKLGKTL NVPPPPDPGR ASTSETPIKK GTDARLASFG
TEIASLLTDG ATQCARKSPS EPSGPGAPAG NVPECVSNAA LTQEWTPESG TTISPRSQNK
GKGGDYYDDE LFSDVQDIKT ALAKIHEDNQ KVISKLESLL LLKGEVESIK KQINKQNISI
STLEGHLSSI MIAIPGLGKD PNDPTADVEI NPDLKPIIGR DSGRALAEVL KKPVASRQLQ
GMTNGRTSSR GQLLKEFQLK PIGKKMSSAV GFVPDTGPAS RSVIRSIIKS SRIEEDRKRY
LMTLLDDIKG ANDLAKFHQM LMKIIMK