VSR_BSMV
ID VSR_BSMV Reviewed; 153 AA.
AC Q80874; Q07118;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Suppressor of RNA silencing;
DE AltName: Full=Gamma-B protein;
DE AltName: Full=Gammab protein {ECO:0000303|PubMed:28388677};
OS Barley stripe mosaic virus (BSMV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Virgaviridae; Hordeivirus.
OX NCBI_TaxID=12327;
OH NCBI_TaxID=4513; Hordeum vulgare (Barley).
OH NCBI_TaxID=4565; Triticum aestivum (Wheat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3590624; DOI=10.1016/0042-6822(87)90211-x;
RA Gustafson G., Hunter B., Hanau R., Armour S.L., Jackson A.O.;
RT "Nucleotide sequence and genetic organization of barley stripe mosaic virus
RT RNA gamma.";
RL Virology 158:394-406(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2586501;
RA Kozlov Y.V., Afanasiev B.N., Rupasov V.V., Golova I.B., Kulaeva O.I.,
RA Dolia V.V., Atabekov I.G., Baev A.A.;
RT "Primary structure of RNA 3 of barley stripe mosaic virus and its
RT variability.";
RL Mol. Biol. (Mosk.) 23:1080-1090(1989).
RN [3]
RP FUNCTION.
RC STRAIN=ND18;
RX PubMed=12438624; DOI=10.1128/jvi.76.24.12981-12991.2002;
RA Yelina N.E., Savenkov E.I., Solovyev A.G., Morozov S.Y., Valkonen J.P.T.;
RT "Long-distance movement, virulence, and RNA silencing suppression
RT controlled by a single protein in hordei- and potyviruses: complementary
RT functions between virus families.";
RL J. Virol. 76:12981-12991(2002).
RN [4]
RP ZINC-BINDING DOMAINS, AND MUTAGENESIS OF CYS-7; CYS-9; CYS-10; CYS-19;
RP CYS-23; ARG-25; LYS-26; ARG-33; LYS-35; ARG-36; CYS-60; CYS-64; CYS-71;
RP CYS-81 AND HIS-85.
RX PubMed=15220411; DOI=10.1128/jvi.78.14.7379-7391.2004;
RA Bragg J.N., Lawrence D.M., Jackson A.O.;
RT "The N-terminal 85 amino acids of the barley stripe mosaic virus gammab
RT pathogenesis protein contain three zinc-binding motifs.";
RL J. Virol. 78:7379-7391(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH APLHA-A PROTEIN.
RX PubMed=28388677; DOI=10.1371/journal.ppat.1006319;
RA Zhang K., Zhang Y., Yang M., Liu S., Li Z., Wang X., Han C., Yu J., Li D.;
RT "The Barley stripe mosaic virus gammab protein promotes chloroplast-
RT targeted replication by enhancing unwinding of RNA duplexes.";
RL PLoS Pathog. 13:e1006319-e1006319(2017).
RN [6]
RP PHOSPHORYLATION AT SER-96, MUTAGENESIS OF SER-96, AND SUBUNIT.
RX PubMed=29453938; DOI=10.1111/nph.15065;
RA Zhang X., Dong K., Xu K., Zhang K., Jin X., Yang M., Zhang Y., Wang X.,
RA Han C., Yu J., Li D.;
RT "Barley stripe mosaic virus infection requires PKA-mediated phosphorylation
RT of gammab for suppression of both RNA silencing and the host cell death
RT response.";
RL New Phytol. 218:1570-1585(2018).
RN [7]
RP INTERACTION WITH HOST ATG7, AND FUNCTION.
RX PubMed=29848767; DOI=10.1105/tpc.18.00122;
RA Yang M., Zhang Y., Xie X., Yue N., Li J., Wang X.B., Han C., Yu J., Liu Y.,
RA Li D.;
RT "Barley stripe mosaic virus gammab Protein Subverts Autophagy to Promote
RT Viral Infection by Disrupting the ATG7-ATG8 Interaction.";
RL Plant Cell 30:1582-1595(2018).
RN [8]
RP INTERACTION WITH TGB1, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=32730331; DOI=10.1371/journal.ppat.1008709;
RA Jiang Z., Zhang K., Li Z., Li Z., Yang M., Jin X., Cao Q., Wang X., Yue N.,
RA Li D., Zhang Y.;
RT "The Barley stripe mosaic virus gammab protein promotes viral cell-to-cell
RT movement by enhancing ATPase-mediated assembly of ribonucleoprotein
RT movement complexes.";
RL PLoS Pathog. 16:e1008709-e1008709(2020).
RN [9]
RP INTERACTION WITH HOST STY46, AND PHOSPHORYLATION AT SERINES.
RX PubMed=33576790; DOI=10.1093/plphys/kiab056;
RA Zhang X., Wang X., Xu K., Jiang Z., Dong K., Xie X., Zhang H., Yue N.,
RA Zhang Y., Wang X.B., Han C., Yu J., Li D.;
RT "The serine/threonine/tyrosine kinase STY46 defends against hordeivirus
RT infection by phosphorylating gammab protein.";
RL Plant Physiol. 186:715-730(2021).
CC -!- FUNCTION: Suppressor of RNA-mediated gene silencing, also known as
CC post-transcriptional gene silencing (PTGS), a mechanism of plant viral
CC defense that limits the accumulation of viral RNAs (PubMed:12438624).
CC Promotes viral cell-to-cell long distance movement by enhancing the
CC ATPase activity of TGB1 (PubMed:12438624, PubMed:32730331). Enhances
CC RNA helicase activity of replication protein alpha-A (PubMed:28388677).
CC Suppresses autophagy induced by the host as a defense mechanism against
CC viral infection (PubMed:29848767). {ECO:0000269|PubMed:12438624,
CC ECO:0000269|PubMed:28388677, ECO:0000269|PubMed:29848767,
CC ECO:0000269|PubMed:32730331}.
CC -!- SUBUNIT: Homooligomer (PubMed:29453938). Interacts (via C-terminus)
CC with replication protein alpha-A (PubMed:28388677). Interacts (via N-
CC terminus) with the movement protein TGB1; this interaction targets
CC gammab-TGB1 at the periphery of chloroplasts and plasmodesmata
CC (PubMed:32730331). Interacts with host autophagy protein ATG7; this
CC interaction disrupts the host ATG7-ATG8 interaction to promote viral
CC infection (PubMed:29848767). Interacts (via BM region) with host STY46;
CC this interaction inhibits the viral infection (PubMed:33576790).
CC {ECO:0000269|PubMed:28388677, ECO:0000269|PubMed:29453938,
CC ECO:0000269|PubMed:29848767, ECO:0000269|PubMed:32730331,
CC ECO:0000269|PubMed:33576790}.
CC -!- SUBCELLULAR LOCATION: Host chloroplast envelope
CC {ECO:0000269|PubMed:28388677}. Host endoplasmic reticulum
CC {ECO:0000269|PubMed:32730331}. Host cell junction, host plasmodesma
CC {ECO:0000269|PubMed:32730331}. Note=Recruited by the replication
CC protein alpha-A to viral replication sites at the host chloroplast
CC membrane. {ECO:0000269|PubMed:28388677}.
CC -!- DOMAIN: The three domains C1, BM and C2 are involved in zinc-binding.
CC Zinc-binding of each of the motifs is critical for the biological
CC activity. {ECO:0000269|PubMed:15220411}.
CC -!- DOMAIN: The coiled coil domain is probably involved in
CC homooligomerization. {ECO:0000269|PubMed:29453938}.
CC -!- PTM: Phosphorylated at Ser-96 by a host PKA-like kinase; the
CC phosphorylation at this site seems to suppress host cell death.
CC {ECO:0000269|PubMed:29453938}.
CC -!- PTM: Serine-phosphorylated by host STY46 kinase.
CC {ECO:0000269|PubMed:33576790}.
CC -!- MISCELLANEOUS: The genome of this virus consists of three linear,
CC positive, single-stranded RNAs encapsidated in separate virions
CC designated RNA-alpha, RNA-beta and RNA-gamma. Three proteins (alpha-A,
CC beta-A and gamma-A) are translated directly from these genomic RNAs and
CC the remaining proteins encoded on RNA-beta (beta-B, beta-C and beta-D)
CC and RNA-gamma (gamma-B) are expressed via three subgenomic messenger
CC RNAs. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the virgaviridae suppressor of RNA silencing
CC family. {ECO:0000305}.
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DR EMBL; M16576; AAA66601.1; -; Genomic_RNA.
DR EMBL; X52774; CAA36984.1; -; Genomic_RNA.
DR PIR; PN0103; PN0103.
DR RefSeq; NP_604482.1; NC_003478.1.
DR GeneID; 962674; -.
DR KEGG; vg:962674; -.
DR Proteomes; UP000001667; Genome.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0039521; P:suppression by virus of host autophagy; IDA:UniProtKB.
DR GO; GO:0140533; P:suppression of host RNAi-mediated antiviral immune response; IDA:UniProtKB.
DR InterPro; IPR007609; Viral_P18.
DR Pfam; PF04521; Viral_P18; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Host cell junction; Host endoplasmic reticulum;
KW Host-virus interaction; Inhibition of host autophagy by virus;
KW Metal-binding; Phosphoprotein; Reference proteome;
KW Suppressor of RNA silencing; Virulence; Zinc.
FT CHAIN 1..153
FT /note="Suppressor of RNA silencing"
FT /id="PRO_0000222494"
FT REGION 1..85
FT /note="Interaction with TGB1"
FT /evidence="ECO:0000269|PubMed:32730331"
FT REGION 1..23
FT /note="C-1"
FT REGION 19..47
FT /note="Basic motif (BM)"
FT REGION 60..85
FT /note="C-2"
FT REGION 86..127
FT /note="Interaction with replication protein alpha-A"
FT /evidence="ECO:0000269|PubMed:28388677"
FT COILED 92..132
FT /evidence="ECO:0000255"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:29453938"
FT MUTAGEN 7
FT /note="C->S: Complete loss of C1 zinc-binding activity;
FT when associated with S-9; S-10; S-19 and S-23."
FT /evidence="ECO:0000269|PubMed:15220411"
FT MUTAGEN 9
FT /note="C->S: Complete loss of C1 zinc-binding activity;
FT when associated with S-7; S-10; S-19 and S-23."
FT /evidence="ECO:0000269|PubMed:15220411"
FT MUTAGEN 10
FT /note="C->S: Complete loss of C1 zinc-binding activity;
FT when associated with S-7; S-9; S-19 and S-23."
FT /evidence="ECO:0000269|PubMed:15220411"
FT MUTAGEN 19
FT /note="C->S: Complete loss of C1 zinc-binding activity;
FT when associated with S-7; S-9; S-10 and S-23."
FT /evidence="ECO:0000269|PubMed:15220411"
FT MUTAGEN 23
FT /note="C->S: Complete loss of C1 zinc-binding activity;
FT when associated with S-7; S-9; S-10 and S-19."
FT /evidence="ECO:0000269|PubMed:15220411"
FT MUTAGEN 25
FT /note="R->N: Complete loss of BM zinc-binding activity;
FT when associated with K-26; E-33; K-35 and E-36."
FT /evidence="ECO:0000269|PubMed:15220411"
FT MUTAGEN 26
FT /note="K->Q: Complete loss of BM zinc-binding activity;
FT when associated with E-25; E-33; K-35 and E-36."
FT /evidence="ECO:0000269|PubMed:15220411"
FT MUTAGEN 33
FT /note="R->Q: Complete loss of BM zinc-binding activity;
FT when associated with E-25; K-26; K-35 and E-36."
FT /evidence="ECO:0000269|PubMed:15220411"
FT MUTAGEN 35
FT /note="K->N: Complete loss of BM zinc-binding activity;
FT when associated with E-25; K-26; E-33 and E-36."
FT /evidence="ECO:0000269|PubMed:15220411"
FT MUTAGEN 36
FT /note="R->Q: Complete loss of BM zinc-binding activity;
FT when associated with E-25; K-26; E-33 and K-35."
FT /evidence="ECO:0000269|PubMed:15220411"
FT MUTAGEN 60
FT /note="C->S: Complete loss of C2 zinc-binding activity;
FT when associated with S-64; S-71; S-81 and S-85."
FT /evidence="ECO:0000269|PubMed:15220411"
FT MUTAGEN 64
FT /note="C->S: Complete loss of C2 zinc-binding activity;
FT when associated with S-60; S-71; S-81 and S-85."
FT /evidence="ECO:0000269|PubMed:15220411"
FT MUTAGEN 71
FT /note="C->S: Complete loss of C2 zinc-binding activity;
FT when associated with S-60; S-64; S-81 and S-85."
FT /evidence="ECO:0000269|PubMed:15220411"
FT MUTAGEN 81
FT /note="C->S: Complete loss of C2 zinc-binding activity;
FT when associated with S-60; S-64; S-71 and S-85."
FT /evidence="ECO:0000269|PubMed:15220411"
FT MUTAGEN 85
FT /note="H->S: Complete loss of C2 zinc-binding activity;
FT when associated with S-60; S-64; S-71 and S-81."
FT /evidence="ECO:0000269|PubMed:15220411"
FT MUTAGEN 96
FT /note="S->A,R: Reduced viral accumulation."
FT /evidence="ECO:0000269|PubMed:29453938"
FT MUTAGEN 96
FT /note="S->D: No effect on viral accumulation."
FT /evidence="ECO:0000269|PubMed:29453938"
FT CONFLICT 54
FT /note="G -> E (in Ref. 2; CAA36984)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="P -> L (in Ref. 2; CAA36984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 153 AA; 17160 MW; 979B4CC3F451EA97 CRC64;
MMATFSCVCC GTSTTSTYCG KRCERKHVYS ETRNKRLELY KKYLLEPQKC ALNGIVGHSC
GMPCSIAEEA CDQLPIVSRF CGQKHADLYD SLLKRSEQEL LLEFLQKKMQ ELKLSHIVKM
AKLESEVNAI RKSVASSFED SVGCDDSSSV SKL
