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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
 
 
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