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PHOSP_PI3B
ID   PHOSP_PI3B              Reviewed;         596 AA.
AC   P06163;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   02-JUN-2021, entry version 81.
DE   RecName: Full=Phosphoprotein;
DE            Short=Protein P;
GN   Name=P/V/D;
OS   Bovine parainfluenza 3 virus (BPIV-3).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Respirovirus.
OX   NCBI_TaxID=11215;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=910N;
RX   PubMed=3031614; DOI=10.1093/nar/15.7.2927;
RA   Sakai Y., Suzu S., Shioda T., Shibuta H.;
RT   "Nucleotide sequence of the bovine parainfluenza 3 virus genome: its 3' end
RT   and the genes of NP, P, C and M proteins.";
RL   Nucleic Acids Res. 15:2927-2944(1987).
RN   [2]
RP   RNA EDITING.
RX   PubMed=1846805; DOI=10.1002/j.1460-2075.1991.tb07966.x;
RA   Pelet T., Curran J., Kolakofsky D.;
RT   "The P gene of bovine parainfluenza virus 3 expresses all three reading
RT   frames from a single mRNA editing site.";
RL   EMBO J. 10:443-448(1991).
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=Undetermined; Note=Partially edited.
CC       RNA editing consists of an insertion of one to six guanine nucleotides.
CC       The sequence displayed here is the P protein, derived from the unedited
CC       RNA. The edited RNA versions give rise to the V protein and the D
CC       protein depending on the number of inserted nucleotides.
CC       {ECO:0000269|PubMed:1846805};
CC   -!- SIMILARITY: Belongs to the respirovirus P protein family.
CC       {ECO:0000305}.
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DR   EMBL; Y00114; CAA68294.1; -; Genomic_RNA.
DR   EMBL; D84095; BAA12214.1; -; Genomic_RNA.
DR   SMR; P06163; -.
DR   Proteomes; UP000133413; Genome.
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; IPR002693; Paramyxo_PProtein_C.
DR   InterPro; IPR016075; RNA_pol_Pprot-P_XD_paramyxovir.
DR   Pfam; PF01806; Paramyxo_P; 1.
DR   SUPFAM; SSF101089; SSF101089; 1.
PE   3: Inferred from homology;
KW   Phosphoprotein; RNA editing; Viral RNA replication.
FT   CHAIN           1..596
FT                   /note="Phosphoprotein"
FT                   /id="PRO_0000142705"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          38..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          220..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..246
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..333
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   596 AA;  66409 MW;  656F4EE535E318F9 CRC64;
     MENNAKDNQI MDSWEEGSGD KSSDISSALD IIEFILSTDS QENTADSNEV NTGNKRLSTT
     IYQLESKTTE TSKENSGSVN ENRQLGASHE RATETKNRNV NQETIQGGNR GRSSSDSRAE
     IMVTRGISRS SPDPNNGTQI QESIDYNEVG EMDKDSAKRE MRQSKDVPVK VSRSDAIPPT
     KQDGNGDDGR SMESISTFDS GYTSIVTAAT LDDEEELLMK NTRPKRYQST PQEDDKGIKK
     GVGKPEDTNK QSPILDYELN SKGSKRNQKT LKISTTTGES TRPQSGSQGK RITSWNILNS
     ESGSRTESTS QNSQIPTSGK SNTVGPGRTT LESRIKTQKT DGKEREDTEE STRFTERAIT
     LLQNLGVIQS AAKLDLYQDK RVVCVANVLN NADTASKIDF LAGLMIGVSM DHDTKLNQIQ
     NEILSLKTDL KKMDESHRRL IENQKEQLSL ITSLISNLKI MTERGGKKDQ PENSGRTPMI
     KTKAKEEKIK KVRFDPLMET QGIEKNIPDL YRSIEKTPEN DIQIKSDINR SNDESNATRL
     VPKRTSNTMR SLIIIINNSN LSSRAKQSYI NELKLCKSDE EVSELMDMFN EDVSSQ
 
 
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