TGB1_FXMV
ID TGB1_FXMV Reviewed; 236 AA.
AC P22169; B1NLP5;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 07-OCT-2020, entry version 75.
DE RecName: Full=Movement and silencing protein TGBp1;
DE AltName: Full=25 kDa protein;
DE AltName: Full=Silencing suppressor P25;
DE AltName: Full=Triple gene block 1 protein;
DE Short=TGBp1;
GN ORFNames=ORF2;
OS Foxtail mosaic virus.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Alphaflexiviridae; Potexvirus.
OX NCBI_TaxID=12179;
OH NCBI_TaxID=4555; Setaria italica (Foxtail millet) (Panicum italicum).
OH NCBI_TaxID=4556; Setaria viridis (Green bristlegrass) (Setaria italica subsp. viridis).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1840610; DOI=10.1099/0022-1317-72-9-2173;
RA Bancroft J.B., Rouleau M., Johnston R., Prins L., Mackie G.A.;
RT "The entire nucleotide sequence of foxtail mosaic virus RNA.";
RL J. Gen. Virol. 72:2173-2181(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=17955161; DOI=10.1007/s00705-007-1057-3;
RA Bruun-Rasmussen M., Madsen C.T., Johansen E., Albrechtsen M.;
RT "Revised sequence of foxtail mosaic virus reveals a triple gene block
RT structure similar to potato virus X.";
RL Arch. Virol. 153:223-226(2008).
RN [3]
RP REVIEW.
RX PubMed=15828680; DOI=10.1094/mpmi-18-0283;
RA Verchot-Lubicz J.;
RT "A new cell-to-cell transport model for Potexviruses.";
RL Mol. Plant Microbe Interact. 18:283-290(2005).
CC -!- FUNCTION: Transports viral genome to neighboring plant cells directly
CC through plasmosdesmata, without any budding. The movement protein
CC allows efficient cell to cell propagation, by bypassing the host cell
CC wall barrier. Increases plasmodesma size exclusion limit. Acts as a
CC suppressor of RNA-mediated gene silencing, also known as post-
CC transcriptional gene silencing (PTGS), a mechanism of plant viral
CC defense that limits the accumulation of viral RNAs (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer and homooligomer. Interacts with capsid protein.
CC Interacts with host AGO1; this interaction targets the host protein for
CC degradation, thereby suppressing the antiviral RNA silencing (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: TGBp1, TGBp2 and TGBp3 seem to act together for cell-to-
CC cell propagation. TGBp1 is the main movement protein that physically
CC cross the plasmodesma with the viral genome. TGBp2 and TGBp3 would
CC facilitate TGBp1 function.
CC -!- SIMILARITY: Belongs to the Tymovirales TGBp1 protein family.
CC {ECO:0000305}.
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DR EMBL; M62730; AAA43827.1; -; Genomic_RNA.
DR EMBL; EF630359; ABW25049.1; -; Genomic_RNA.
DR PIR; JQ1259; JQ1259.
DR RefSeq; NP_040989.1; NC_001483.1.
DR GeneID; 1494010; -.
DR KEGG; vg:1494010; -.
DR Proteomes; UP000008623; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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 InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01443; Viral_helicase1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
PE 3: Inferred from homology;
KW Host cytoplasm; Host-virus interaction; Reference proteome; RNA-binding;
KW Suppressor of RNA silencing; Transport; Viral movement protein.
FT CHAIN 1..236
FT /note="Movement and silencing protein TGBp1"
FT /id="PRO_0000222565"
FT DOMAIN 1..117
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 118..236
FT /note="(+)RNA virus helicase C-terminal"
FT CONFLICT 111
FT /note="A -> R (in Ref. 1; AAA43827)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 236 AA; 26313 MW; 7259026D4743F1D1 CRC64;
MDSEIVERLT KLGFVKTSHT HIAGEPLVIH AVAGAGKTTL LRSLLELPGV EVFTGGEHDP
PNLSGKYIRC AAPPVAGAYN ILDEYPAYPN WRSQPWNVLI ADNLQYKEPT ARAHYTCNRT
HRLGQLTVDA LRRVGFDITF AGTQTEDYGF QEGHLYTSQF YGQVISLDTQ AHKIAVRHGL
APLSALETRG LEFDETTVIT TKTSLEEVKD RHMVYVALTR HRRTCHLYTA HFAPSA