TGB1_BSMV
ID TGB1_BSMV Reviewed; 528 AA.
AC P04867;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Movement protein TGB1;
DE EC=3.6.4.- {ECO:0000269|PubMed:12069530, ECO:0000269|PubMed:8995680};
DE AltName: Full=58 kDa protein;
DE AltName: Full=Beta-B protein;
DE AltName: Full=Triple gene block 1 protein;
DE Short=TGBp1;
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].
RC STRAIN=ATCC PV43;
RX PubMed=3754962; DOI=10.1093/nar/14.9.3895;
RA Gustafson G., Armour S.L.;
RT "The complete nucleotide sequence of RNA beta from the type strain of
RT barley stripe mosaic virus.";
RL Nucleic Acids Res. 14:3895-3909(1986).
RN [2]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=8995680; DOI=10.1128/jvi.71.2.1538-1546.1997;
RA Donald R.G., Lawrence D.M., Jackson A.O.;
RT "The barley stripe mosaic virus 58-kilodalton beta(b) protein is a
RT multifunctional RNA binding protein.";
RL J. Virol. 71:1538-1546(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=12069530; DOI=10.1006/viro.2001.1328;
RA Kalinina N.O., Rakitina D.V., Solovyev A.G., Schiemann J., Morozov S.Y.;
RT "RNA helicase activity of the plant virus movement proteins encoded by the
RT first gene of the triple gene block.";
RL Virology 296:321-329(2002).
RN [4]
RP INTERACTION WITH MOVEMENT PROTEIN TGB3, AND FUNCTION.
RX PubMed=18353960; DOI=10.1128/jvi.02586-07;
RA Lim H.S., Bragg J.N., Ganesan U., Lawrence D.M., Yu J., Isogai M.,
RA Hammond J., Jackson A.O.;
RT "Triple gene block protein interactions involved in movement of Barley
RT stripe mosaic virus.";
RL J. Virol. 82:4991-5006(2008).
RN [5]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19570874; DOI=10.1128/jvi.00739-09;
RA Lim H.S., Bragg J.N., Ganesan U., Ruzin S., Schichnes D., Lee M.Y.,
RA Vaira A.M., Ryu K.H., Hammond J., Jackson A.O.;
RT "Subcellular localization of the barley stripe mosaic virus triple gene
RT block proteins.";
RL J. Virol. 83:9432-9448(2009).
RN [6]
RP SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=28872759; DOI=10.1111/mpp.12612;
RA Li Z., Zhang Y., Jiang Z., Jin X., Zhang K., Wang X., Han C., Yu J., Li D.;
RT "Hijacking of the nucleolar protein fibrillarin by TGB1 is required for
RT cell-to-cell movement of Barley stripe mosaic virus.";
RL Mol. Plant Pathol. 19:1222-1237(2018).
RN [7]
RP IDENTIFICATION IN THE TGB1-TGB2-TGB3 COMPLEX, ACTIVITY REGULATION,
RP INTERACTION WITH THE SUPPRESSOR OF RNA SILIECING GAMMA-B, AND FUNCTION.
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).
CC -!- FUNCTION: Participates in the transport of viral genome to neighboring
CC plant cells directly through plasmodesmata, without any budding
CC (PubMed:18353960). Multifunctional movement protein with RNA-binding,
CC ATPase and helicase activities (PubMed:8995680, PubMed:12069530).
CC Engages in homologous interactions leading to the formation of a
CC ribonucleoprotein complex containing plus-sense viral RNAs (vRNPs)
CC (PubMed:18353960). ATPase activity is probably required for vRNPs
CC movement complex assembly (PubMed:32730331). Intracellular delivery of
CC TGBp1-containing vRNPs to plasmodesmata is facilitated by TGBp2 and
CC TGBp3 (By similarity). {ECO:0000250|UniProtKB:Q9IV54,
CC ECO:0000269|PubMed:12069530, ECO:0000269|PubMed:18353960,
CC ECO:0000269|PubMed:32730331, ECO:0000269|PubMed:8995680}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:12069530, ECO:0000269|PubMed:8995680};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12069530};
CC -!- ACTIVITY REGULATION: ATPase activity is enhanced by the suppressor of
CC RNA silencing Gamma-B. {ECO:0000269|PubMed:32730331}.
CC -!- SUBUNIT: Homooligomer (PubMed:19570874). Interacts with movement
CC protein TGB3 (PubMed:18353960). TGB1-TGB3-TGB2 complex formation is
CC enhanced by ATP hydrolysis (PubMed:32730331). Interacts with the
CC suppressor of RNA silencing Gamma-B (via N-terminus) (PubMed:32730331).
CC {ECO:0000269|PubMed:18353960, ECO:0000269|PubMed:19570874,
CC ECO:0000269|PubMed:32730331}.
CC -!- SUBCELLULAR LOCATION: Host cell junction, host plasmodesma
CC {ECO:0000269|PubMed:19570874}. Host nucleus
CC {ECO:0000269|PubMed:28872759}. Host cytoplasm
CC {ECO:0000269|PubMed:28872759}. Host nucleus, host nucleolus
CC {ECO:0000269|PubMed:28872759}. Host cytoplasm, host cytoskeleton
CC {ECO:0000250|UniProtKB:Q9IV54}. Note=TGB1 nuclear-cytoplasmic
CC trafficking is required for cell-to-cell movement and systemic
CC infection (PubMed:28872759). Associates with host microtubules (By
CC similarity). {ECO:0000250|UniProtKB:Q9IV54,
CC ECO:0000269|PubMed:28872759}.
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/benyvirus TGB1 movement protein
CC family. {ECO:0000305}.
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DR EMBL; X03854; CAA27485.1; -; Genomic_RNA.
DR PIR; A04191; WMBV8B.
DR RefSeq; NP_604487.1; NC_003481.1.
DR SMR; P04867; -.
DR PRIDE; P04867; -.
DR GeneID; 962677; -.
DR KEGG; vg:962677; -.
DR Proteomes; UP000001667; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell.
DR GO; GO:0044163; C:host cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046740; P:transport of virus in host, cell to cell; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01443; Viral_helicase1; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Host cell junction; Host cytoplasm;
KW Host cytoskeleton; Host nucleus; Hydrolase; Nucleotide-binding;
KW Reference proteome; Repeat; RNA-binding; Transport; Viral movement protein.
FT CHAIN 1..528
FT /note="Movement protein TGB1"
FT /id="PRO_0000222491"
FT REPEAT 52..77
FT /note="1"
FT REPEAT 78..103
FT /note="2"
FT DOMAIN 236..379
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 380..520
FT /note="(+)RNA virus helicase C-terminal"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..103
FT /note="2 X 26 AA tandem repeats"
FT REGION 75..491
FT /note="Interaction with the suppressor of RNA silencing
FT Gamma-B"
FT /evidence="ECO:0000269|PubMed:32730331"
FT REGION 111..120
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000269|PubMed:28872759"
FT REGION 243..254
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:28872759"
FT REGION 508..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 269..276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 528 AA; 58095 MW; 45CC5A0A80F92091 CRC64;
MDMTKTVEEK KTNGTDSVKG VFENSTIPKV PTGQEMGGDG SSTSKLKETL KVADQTPLSV
DNGAKSKLDS SDRQVPGVAD QTPLSVDNGA KSKLDSSDRQ VPGPELKPNV KKSKKKRIQK
PAQPSGPNDL KGGTKGSSQV GENVSENYTG ISKEAAKQKQ KTPKSVKMQS NLADKFKAND
TRRSELINKF QQFVHETCLK SDFEYTGRQY FRARSNFFEM IKLASLYDKH LKECMARACT
LERERLKRKL LLVRALKPAV DFLTGIISGV PGSGKSTIVR TLLKGEFPAV CALANPALMN
DYSGIEGVYG LDDLLLSAVP ITSDLLIIDE YTLAESAEIL LLQRRLRASM VLLVGDVAQG
KATTASSIEY LTLPVIYRSE TTYRLGQETA SLCSKQGNRM VSKGGRDTVI ITDYDGETDE
TEKNIAFTVD TVRDVKDCGY DCALAIDVQG KEFDSVTLFL RNEDRKALAD KHLRLVALSR
HKSKLIIRAD AEIRQAFLTG DIDLSSKASN SHRYSAKPDE DHSWFKAK
