TGB1_PMTVS
ID TGB1_PMTVS Reviewed; 463 AA.
AC Q9IV54;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Movement protein TGB1;
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P04867};
DE AltName: Full=P51;
DE AltName: Full=Triple gene block 1 protein;
DE Short=TGBp1;
OS Potato mop-top virus (isolate Potato/Sweden/Sw) (PMTV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Virgaviridae; Pomovirus.
OX NCBI_TaxID=652839;
OH NCBI_TaxID=4112; Solanum nigrum (Black nightshade).
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12655103; DOI=10.1099/vir.0.18813-0;
RA Savenkov E.I., Germundsson A., Zamyatnin A.A. Jr., Sandgren M.,
RA Valkonen J.P.;
RT "Potato mop-top virus: the coat protein-encoding RNA and the gene for
RT cysteine-rich protein are dispensable for systemic virus movement in
RT Nicotiana benthamiana.";
RL J. Gen. Virol. 84:1001-1005(2003).
RN [2]
RP RNA-BINDING, SUBUNIT, AND FUNCTION.
RX PubMed=12093178; DOI=10.1006/viro.2002.1435;
RA Cowan G.H., Lioliopoulou F., Ziegler A., Torrance L.;
RT "Subcellular localisation, protein interactions, and RNA binding of Potato
RT mop-top virus triple gene block proteins.";
RL Virology 298:106-115(2002).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20923354; DOI=10.1094/mpmi-05-10-0105;
RA Wright K.M., Cowan G.H., Lukhovitskaya N.I., Tilsner J., Roberts A.G.,
RA Savenkov E.I., Torrance L.;
RT "The N-terminal domain of PMTV TGB1 movement protein is required for
RT nucleolar localization, microtubule association, and long-distance
RT movement.";
RL Mol. Plant Microbe Interact. 23:1486-1497(2010).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21660184; DOI=10.2174/1874357901105010001;
RA Shemyakina E.A., Solovyev A.G., Leonova O.G., Popenko V.I., Schiemann J.,
RA Morozov S.Y.;
RT "The Role of Microtubule Association in Plasmodesmal Targeting of Potato
RT mop-top virus Movement Protein TGBp1.";
RL Open Virol. J. 5:1-11(2011).
RN [5]
RP SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION WITH HOST IMPORTIN SUBUNIT
RP ALPHA.
RX PubMed=25576325; DOI=10.1104/pp.114.254938;
RA Lukhovitskaya N.I., Cowan G.H., Vetukuri R.R., Tilsner J., Torrance L.,
RA Savenkov E.I.;
RT "Importin-alpha-mediated nucleolar localization of potato mop-top virus
RT TRIPLE GENE BLOCK1 (TGB1) protein facilitates virus systemic movement,
RT whereas TGB1 self-interaction is required for cell-to-cell movement in
RT Nicotiana benthamiana.";
RL Plant Physiol. 167:738-752(2015).
CC -!- FUNCTION: Participates in the transport of viral genome to neighboring
CC plant cells directly through plasmodesmata, without any budding
CC (PubMed:20923354, PubMed:12093178, PubMed:12655103, PubMed:21660184).
CC Multifunctional movement protein with RNA-binding, ATPase and helicase
CC activities (By similarity). Engages in homologous interactions leading
CC to the formation of a ribonucleoprotein complex containing plus-sense
CC viral RNAs (vRNPs) (By similarity). ATPase activity is probably
CC required for vRNPs movement complex assembly (By similarity).
CC Intracellular delivery of TGBp1-containing vRNPs to plasmodesmata is
CC facilitated by TGBp2 and TGBp3 (PubMed:12093178).
CC {ECO:0000250|UniProtKB:P04867, ECO:0000269|PubMed:12093178,
CC ECO:0000269|PubMed:12655103, ECO:0000269|PubMed:20923354,
CC ECO:0000269|PubMed:21660184}.
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:0000250|UniProtKB:P04867};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P04867};
CC -!- SUBUNIT: Homooligomer (Probable) (PubMed:25576325). TGB1-TGB3-TGB2
CC complex formation is enhanced by ATP hydrolysis (By similarity).
CC Interacts with the suppressor of RNA silencing (via N-terminus) (By
CC similarity). Interacts (via N-terminus) with host importin IMPA1
CC (PubMed:25576325). {ECO:0000250|UniProtKB:P04867,
CC ECO:0000269|PubMed:25576325, ECO:0000305|PubMed:12093178}.
CC -!- SUBCELLULAR LOCATION: Host cell junction, host plasmodesma
CC {ECO:0000269|PubMed:20923354}. Host nucleus
CC {ECO:0000269|PubMed:20923354}. Host cytoplasm
CC {ECO:0000269|PubMed:20923354}. Host nucleus, host nucleolus
CC {ECO:0000269|PubMed:20923354, ECO:0000269|PubMed:25576325}. Host
CC cytoplasm, host cytoskeleton {ECO:0000269|PubMed:20923354,
CC ECO:0000269|PubMed:21660184}. Note=TGB1 nuclear-cytoplasmic trafficking
CC is required for cell-to-cell movement and systemic infection (By
CC similarity). Associates with host microtubules (PubMed:20923354).
CC {ECO:0000250|UniProtKB:P04867, ECO:0000269|PubMed:20923354}.
CC -!- DOMAIN: The N-terminal 84 amino acids contain a nucleolar localization
CC signal. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the virgaviridae/benyvirus TGB1 movement protein
CC family. {ECO:0000305}.
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DR EMBL; AJ277556; CAB91101.1; -; Genomic_RNA.
DR RefSeq; NP_620438.1; NC_003725.1.
DR TCDB; 9.B.308.6.1; the lettuce infectious yellows virus p5 (liyv-p5) family.
DR PRIDE; Q9IV54; -.
DR GeneID; 991174; -.
DR KEGG; vg:991174; -.
DR Proteomes; UP000006715; 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:0016787; F:hydrolase activity; 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; -; 1.
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 1: Evidence at protein level;
KW ATP-binding; Host cell junction; Host cytoplasm; Host cytoskeleton;
KW Host nucleus; Hydrolase; Nucleotide-binding; Reference proteome; Transport;
KW Viral movement protein.
FT CHAIN 1..463
FT /note="Movement protein TGB1"
FT /id="PRO_0000410609"
FT DOMAIN 185..326
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 327..463
FT /note="(+)RNA virus helicase C-terminal"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 11..16
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000269|PubMed:25576325"
FT REGION 37..52
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000269|PubMed:25576325"
FT COMPBIAS 22..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 215..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 463 AA; 51188 MW; 9DB2947C17C6F9F2 CRC64;
MESGFNGSRP HRVKKDLPDR VNPVNTQGSS GTTGNAFRKN NNNKTQNWKP RSGPGNRNEG
DQTKNNKSDL QQPSEVHPEN QVRPESSTGE SVKQQSEPHR VLEDKKQSGK TAGSSVRIPE
EGGGGLGSAN YLGKRQLDFV AKLCVESGFK STGKPLKRYP AEFFKSSGLL EKFVKYLSSR
LDKGCNLSQR ESEVVLKNLR SKRAEQSFLA GAVTGVPGSG KTTLLRKVQC EGGFNSIVIL
GNPRSKTEFS NLPSCYTAKE ILLLGIAIKC EVLLIDEYTL LTSGEILLLQ KITNSRIVIL
FGDRAQGSSN TLCSPEWLQV PVIFQSLTSR RFGKATANLC RRQGFDFEGG EHEDKVVESP
YEGSSPATDI NIVFSESTRE DLLECGIEST LVSDVQGKEY NTVTLFIPDE DREYLTNAHL
RSVAFSRHKF ALEIRCNPEL FMQLINGELA SKQQPQTDRY GPE
