P21_BYVU
ID P21_BYVU Reviewed; 177 AA.
AC Q08545;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 02-JUN-2021, entry version 71.
DE RecName: Full=RNA silencing suppressor;
DE AltName: Full=21 kDa protein;
DE AltName: Full=p21;
GN ORFNames=ORF8;
OS Beet yellows virus (isolate Ukraine) (BYV) (Sugar beet yellows virus).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Closteroviridae; Closterovirus.
OX NCBI_TaxID=478555;
OH NCBI_TaxID=161934; Beta vulgaris (Sugar beet).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1990061; DOI=10.1099/0022-1317-72-1-15;
RA Agranovsky A.A., Boyko V.P., Karasev A.V., Lunina N.A., Koonin E.V.,
RA Dolja V.V.;
RT "Nucleotide sequence of the 3'-terminal half of beet yellows closterovirus
RT RNA genome: unique arrangement of eight virus genes.";
RL J. Gen. Virol. 72:15-23(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8259666; DOI=10.1006/viro.1994.1034;
RA Agranovsky A.A., Koonin E.V., Boyko V.P., Maiss E., Froetschl R.,
RA Lunina N.A., Atabekov J.G.;
RT "Beet yellows closterovirus: complete genome structure and identification
RT of a leader papain-like thiol protease.";
RL Virology 198:311-324(1994).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12642093; DOI=10.1016/s0042-6822(02)00051-x;
RA Reed J.C., Kasschau K.D., Prokhnevsky A.I., Gopinath K., Pogue G.P.,
RA Carrington J.C., Dolja V.V.;
RT "Suppressor of RNA silencing encoded by Beet yellows virus.";
RL Virology 306:203-209(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
RX PubMed=16154094; DOI=10.1016/j.str.2005.06.017;
RA Ye K., Patel D.J.;
RT "RNA silencing suppressor p21 of Beet yellows virus forms an RNA binding
RT octameric ring structure.";
RL Structure 13:1375-1384(2005).
CC -!- FUNCTION: Acts as suppressor of RNA-mediated gene silencing, also known
CC as post-transcriptional gene silencing (PTGS), a mechanism of plant
CC viral defense that limits the accumulation of viral RNAs. Binds to
CC ssRNAs and dsRNAs in vitro. Also functions as replication enhancer.
CC {ECO:0000269|PubMed:12642093}.
CC -!- SUBUNIT: Homooctamer. The eight monomers assemble into a closed ring
CC that binds RNA.
CC -!- INTERACTION:
CC Q08545; Q08545: ORF8; NbExp=2; IntAct=EBI-15556683, EBI-15556683;
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:12642093}.
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DR EMBL; X53462; CAA37556.1; -; Genomic_RNA.
DR EMBL; X73476; CAA51870.1; -; Genomic_RNA.
DR PIR; S28717; S28717.
DR RefSeq; NP_041877.1; NC_001598.1.
DR PDB; 2CWO; X-ray; 3.30 A; A/B/C/D=1-177.
DR PDBsum; 2CWO; -.
DR SMR; Q08545; -.
DR GeneID; 1724788; -.
DR KEGG; vg:1724788; -.
DR EvolutionaryTrace; Q08545; -.
DR Proteomes; UP000000359; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR021742; RSS_P20_N.
DR InterPro; IPR021575; Suppressor_P21_C.
DR Pfam; PF11757; RSS_P20; 1.
DR Pfam; PF11479; Suppressor_P21; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Reference proteome; RNA-binding;
KW Suppressor of RNA silencing.
FT CHAIN 1..177
FT /note="RNA silencing suppressor"
FT /id="PRO_0000312570"
FT HELIX 10..24
FT /evidence="ECO:0007829|PDB:2CWO"
FT HELIX 33..61
FT /evidence="ECO:0007829|PDB:2CWO"
FT HELIX 78..89
FT /evidence="ECO:0007829|PDB:2CWO"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2CWO"
FT HELIX 102..117
FT /evidence="ECO:0007829|PDB:2CWO"
FT HELIX 121..126
FT /evidence="ECO:0007829|PDB:2CWO"
FT HELIX 129..144
FT /evidence="ECO:0007829|PDB:2CWO"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2CWO"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:2CWO"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:2CWO"
SQ SEQUENCE 177 AA; 20558 MW; DFD0D072DF993A76 CRC64;
MKFFLKDGET SRALSRSESL LRRVKELGTN SQQSEISECV DEFNELASFN HLLVTVEHRE
WMEQHPNQSS KLRVPSRIGE MLKEIRAFLK VRVVTPMHKE TASDTLNAFL EEYCRITGLA
REDALREKMR KVKSVVLFHH SELLKFEVTE NMFSYTELLK LNLSLRVISS QILGMAI