ID   POL2_TOTV               Reviewed;        1198 AA.
AC   A1XIQ1;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=RNA2 polyprotein;
DE   Contains:
DE     RecName: Full=Movement protein;
DE   Contains:
DE     RecName: Full=Capsid protein VP35;
DE   Contains:
DE     RecName: Full=Capsid protein VP26;
DE   Contains:
DE     RecName: Full=Capsid protein VP23;
OS   Tomato torrado virus (isolate Solanum lycopersicum/Spain/PRIToTV0301/-)
OS   (ToTV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Secoviridae; Torradovirus.
OX   NCBI_TaxID=686948;
OH   NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
OH   NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
OH   NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH   NCBI_TaxID=4111; Solanum melongena (Eggplant) (Aubergine).
OH   NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=17226066; DOI=10.1007/s00705-006-0917-6;
RA   Verbeek M., Dullemans A.M., van den Heuvel J.F., Maris P.C.,
RA   van der Vlugt R.A.;
RT   "Identification and characterisation of tomato torrado virus, a new plant
RT   picorna-like virus from tomato.";
RL   Arch. Virol. 152:881-890(2007).
CC   -!- FUNCTION: [Movement protein]: Transports viral genome to neighboring
CC       plant cells directly through plasmosdesmata, without any budding. The
CC       movement protein allows efficient cell to cell propagation, by
CC       bypassing the host cell wall barrier. Acts by forming a tubular
CC       structure at the host plasmodesmata, enlarging it enough to allow free
CC       passage of virion capsids (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Capsid proteins VP35, VP26, and VP23 form a capsid enclosing
CC       the viral positive strand RNA genome. Together they form an icosahedral
CC       capsid pseudo T=3 with a diameter of approximately 30 nm (Potential).
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Movement protein]: Host cell junction. Host cell
CC       junction, host plasmodesma.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP35]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP26]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP23]: Virion {ECO:0000305}.
CC   -!- PTM: Specific enzymatic cleavages in vivo by the P1 encoded 3C-like
CC       protease yield mature proteins. {ECO:0000250}.
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DR   EMBL; DQ388880; ABD38936.1; -; Genomic_RNA.
DR   RefSeq; YP_001040018.1; NC_009032.1.
DR   SMR; A1XIQ1; -.
DR   PRIDE; A1XIQ1; -.
DR   GeneID; 5130565; -.
DR   KEGG; vg:5130565; -.
DR   Proteomes; UP000000825; Genome.
DR   GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0046740; P:transport of virus in host, cell to cell; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.20; -; 2.
DR   InterPro; IPR000603; MPV.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF00803; 3A; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Host cell junction; Reference proteome; Transport;
KW   Viral movement protein; Virion.
FT   CHAIN           1..?449
FT                   /note="Movement protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000214035"
FT   CHAIN           ?450..?732
FT                   /note="Capsid protein VP35"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000214036"
FT   CHAIN           ?733..?974
FT                   /note="Capsid protein VP26"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000214037"
FT   CHAIN           ?975..1198
FT                   /note="Capsid protein VP23"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000214038"
SQ   SEQUENCE   1198 AA;  133709 MW;  DC45AD813FD20C73 CRC64;
     MMMSSVAGQR KGPSDKSAAV SEQLIAQITA AVEAGNKNLL RKLGMGSYGI LYGAQEKKAM
     ELFDPEDVHN ITSLWSSFKK TFTSSRDHGN LFFHLYGVMF FMVPHVHGGE GSVKISLCSS
     NDPTNPVLQE KVLYFSGGAQ AVLMSPTITL PFVKRGPMFY YTMECLGTRA QIPCSVVAIW
     KQKIDIRSAI YSKQETMSWA IEALHRPQFF QDRQEAAQYI SSVYSNATSS ATDSVLPFVG
     AQLGDTKMNV PSEARMIRSS SLRVPMLKVQ SKRFSSMEIP STSTAHLLGT TRDETVIQEE
     SRYEEEGDDG VLFPVKKAQG LNYSHVWDNL GIESFVDVEL PENWDELSVR QQVAAAMIAF
     ANKGVCLVPK HIINRDKHNI HLENITEHNY LVILERYGIV NAGSLARTEN WYNLTLAQRV
     EELIYQRDDA YFMFGDNTNP YPPFDCYDGL TLKVRSELER VAKEQARQRF YKEAARAQVK
     NKVAQTSVEE IPSTSFATKV AMESGSVDSM KIAIQAEAAN EAVRPNEVMF EFGQEMNNEG
     ATELELQQPA CVASNSFFNV GVFEFAWKKS SSVAAEVLSL ALPAALFGKS KEMSMGSQML
     RYYDAALIMY KVILYISGMG AISGQLALVW DECNVLNRKK EFINIASLYA SKHRLVSASE
     QSSGEFCFTP TGIGKFVPLD PASGAYDLGS IRVFVTHPLA SATELESIPC HIHLQCKVLS
     TNIMQPPRLR AQAQFGMKPD QTHFPRFPTN QVLLHYNWGV AASMGTTLVS IFSPSGIYES
     DGTLQPSLLG NIARNCKWWT GTCVFEICIE KTQFHSGSLA IGLGTLNTSM STPHDILNMP
     HVICNLEMGR KFYFRCTITN WNGKNLLTTG RKSSLPRPKH MSHMRLFATV LKPLVSTSIH
     LDTVGVTVQL KCIEDLVLGG TVSVKPIYGH WTKGKNAVDF LFSEMDLSQR KEIEKLRKEN
     VETFDEKGKK QPQVQVPLRD KFSYGAVQYF VMNWKDEERL LVLPCAPWSV RFPQGALVQE
     AITCPFIDWC SSFCYWSGSL EYTIIVHRVQ TSNNIGGVLN ITLDSSGYPF PLGISKGTYV
     VSAGGGAKWA FTYGMSDNIF SFVVHDDEFF PRRHTKARAI DPNASRIMTL QDRLGNLIIN
     LPAKDVISSL EILVKPGPDF KLQLAQAPSA NHEKHLGDMQ THTYLYTPDF SELRSFEN