ID POL2_CPMVS Reviewed; 1046 AA. AC P03599; Q66170; Q84103; Q9WJE1; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 27-MAR-2024, entry version 133. DE RecName: Full=RNA2 polyprotein; DE AltName: Full=Genome polyprotein M; DE AltName: Full=M RNA polyprotein; DE AltName: Full=Middle component RNA polyprotein; DE AltName: Full=P2; DE Contains: DE RecName: Full=VP58; DE AltName: Full=P58; DE Contains: DE RecName: Full=Movement protein; DE Short=MP; DE AltName: Full=48 kDa protein; DE Contains: DE RecName: Full=Large capsid protein; DE Short=LCP; DE AltName: Full=Coat protein VP37; DE AltName: Full=L subunit; DE AltName: Full=Large coat protein; DE Contains: DE RecName: Full=Small capsid protein precursor; DE AltName: Full=S subunit; DE Contains: DE RecName: Full=Mature small capsid protein; DE Short=SCP; DE AltName: Full=Coat protein VP23; DE AltName: Full=Small capsid protein, N-terminus part; DE AltName: Full=Small coat protein, N-terminus part; DE Contains: DE RecName: Full=Small capsid protein C-terminus part; DE AltName: Full=Small coat protein C-terminus part; OS Cowpea mosaic virus (strain SB) (CPMV). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Picornavirales; Secoviridae; Comovirinae; Comovirus; Comovirus vignae. OX NCBI_TaxID=928299; OH NCBI_TaxID=3821; Cajanus cajan (Pigeon pea) (Cajanus indicus). OH NCBI_TaxID=3829; Crotalaria juncea (Sunn hemp). OH NCBI_TaxID=3917; Vigna unguiculata (Cowpea). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] (ISOFORM 1), AND ACETYLATION AT MET-460. RC STRAIN=SB; RX PubMed=6641721; DOI=10.1002/j.1460-2075.1983.tb01525.x; RA van Wezenbeek P., Verver J., Harmsen J., Vos P., van Kammen A.; RT "Primary structure and gene organization of the middle-component RNA of RT cowpea mosaic virus."; RL EMBO J. 2:941-946(1983). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1). RC STRAIN=SB; RX PubMed=16453487; DOI=10.1002/j.1460-2075.1983.tb01731.x; RA Lomonossoff G.P., Shanks M.; RT "The nucleotide sequence of cowpea mosaic virus B RNA."; RL EMBO J. 2:2253-2258(1983). RN [3] RP PROTEOLYTIC CLEAVAGE (RNA2 POLYPROTEIN). RX PubMed=16789216; DOI=10.1128/jvi.41.1.8-17.1982; RA Franssen H., Goldbach R., Broekhuijsen M., Moerman M., van Kammen A.; RT "Expression of Middle-Component RNA of Cowpea Mosaic Virus: In Vitro RT Generation of a Precursor to Both Capsid Proteins by a Bottom-Component RT RNA-Encoded Protease from Infected Cells."; RL J. Virol. 41:8-17(1982). RN [4] RP ALTERNATIVE INITIATION. RX PubMed=2773321; DOI=10.1016/0042-6822(89)90133-5; RA Holness C.L., Lomonossoff G.P., Evans D., Maule A.J.; RT "Identification of the initiation codons for translation of cowpea mosaic RT virus middle component RNA using site-directed mutagenesis of an infectious RT cDNA clone."; RL Virology 172:311-320(1989). RN [5] RP ALTERNATIVE INITIATION. RX PubMed=1765773; DOI=10.1099/0022-1317-72-12-3109; RA Belsham G.J., Lomonossoff G.P.; RT "The mechanism of translation of cowpea mosaic virus middle component RNA: RT no evidence for internal initiation from experiments in an animal cell RT transient expression system."; RL J. Gen. Virol. 72:3109-3113(1991). RN [6] RP FUNCTION (MOVEMENT PROTEIN), AND SUBCELLULAR LOCATION (VP58). RX PubMed=8497075; DOI=10.1128/jvi.67.6.3660-3664.1993; RA Wellink J., van Lent J.W., Verver J., Sijen T., Goldbach R.W., RA van Kammen A.; RT "The cowpea mosaic virus M RNA-encoded 48-kilodalton protein is responsible RT for induction of tubular structures in protoplasts."; RL J. Virol. 67:3660-3664(1993). RN [7] RP FUNCTION (MOVEMENT PROTEIN). RX PubMed=9501035; DOI=10.1006/viro.1997.8982; RA Verver J., Wellink J., Van Lent J., Gopinath K., Van Kammen A.; RT "Studies on the movement of cowpea mosaic virus using the jellyfish green RT fluorescent protein."; RL Virology 242:22-27(1998). RN [8] RP MASS SPECTROMETRY, FUNCTION (SMALL CAPSID PROTEIN PRECURSOR), PROTEOLYTIC RP CLEAVAGE (SMALL CAPSID PROTEIN PRECURSOR), AND DOMAIN (SMALL CAPSID PROTEIN RP PRECURSOR). RX PubMed=10049828; DOI=10.1006/viro.1998.9567; RA Taylor K.M., Spall V.E., Butler P.J.G., Lomonossoff G.P.; RT "The cleavable carboxyl-terminus of the small coat protein of cowpea mosaic RT virus is involved in RNA encapsidation."; RL Virology 255:129-137(1999). RN [9] RP LACK OF GLYCOSYLATION (LARGE CAPSID PROTEIN), AND LACK OF GLYCOSYLATION RP (MATURE SMALL CAPSID PROTEIN). RX PubMed=10725439; DOI=10.1099/0022-1317-81-4-1111; RA Altmann F., Lomonossoff G.P.; RT "Glycosylation of the capsid proteins of cowpea mosaic virus: a RT reinvestigation shows the absence of sugar residues."; RL J. Gen. Virol. 81:1111-1114(2000). RN [10] RP MUTAGENESIS OF 126-ILE-PRO-127; 209-PRO-VAL-210; 220-SER-ASP-221; RP 238-ILE-GLU-239; 259-VAL-ASP-260; 279-ARG-GLY-280; 409-LEU-LYS-410 AND RP 448-LEU-ASP-449. RX PubMed=10662615; DOI=10.1006/viro.1999.0087; RA Bertens P., Wellink J., Goldbach R., van Kammen A.; RT "Mutational analysis of the cowpea mosaic virus movement protein."; RL Virology 267:199-208(2000). RN [11] RP SUBCELLULAR LOCATION (MOVEMENT PROTEIN). RX PubMed=10864669; DOI=10.1128/jvi.74.14.6556-6563.2000; RA Carette J.E., Stuiver M., Van Lent J., Wellink J., Van Kammen A.; RT "Cowpea mosaic virus infection induces a massive proliferation of RT endoplasmic reticulum but not Golgi membranes and is dependent on de novo RT membrane synthesis."; RL J. Virol. 74:6556-6563(2000). RN [12] RP DOMAIN (MOVEMENT PROTEIN), AND FUNCTION (MOVEMENT PROTEIN). RX PubMed=12556992; DOI=10.1007/s00705-002-0918-z; RA Bertens P., Heijne W., van der Wel N., Wellink J., van Kammen A.; RT "Studies on the C-terminus of the Cowpea mosaic virus movement protein."; RL Arch. Virol. 148:265-279(2003). RN [13] RP SUBCELLULAR LOCATION (MOVEMENT PROTEIN), AND FUNCTION (MOVEMENT PROTEIN). RX PubMed=14579172; DOI=10.1007/s00705-003-0180-z; RA Gopinath K., Bertens P., Pouwels J., Marks H., Van Lent J., Wellink J., RA Van Kammen A.; RT "Intracellular distribution of cowpea mosaic virus movement protein as RT visualised by green fluorescent protein fusions."; RL Arch. Virol. 148:2099-2114(2003). RN [14] RP DOMAIN (MOVEMENT PROTEIN), INTERACTION WITH THE LARGE CAPSID PROTEIN RP (MOVEMENT PROTEIN), AND INTERACTION WITH THE MOVEMENT PROTEIN (LARGE CAPSID RP PROTEIN). RX PubMed=12867661; DOI=10.1099/vir.0.19101-0; RA Carvalho C.M., Wellink J., Ribeiro S.G., Goldbach R.W., Van Lent J.W.; RT "The C-terminal region of the movement protein of Cowpea mosaic virus is RT involved in binding to the large but not to the small coat protein."; RL J. Gen. Virol. 84:2271-2277(2003). RN [15] RP FUNCTION (SMALL CAPSID PROTEIN C-TERMINUS PART), AND FUNCTION (SMALL CAPSID RP PROTEIN PRECURSOR). RX PubMed=15483261; DOI=10.1099/vir.0.80454-0; RA Canizares M.C., Taylor K.M., Lomonossoff G.P.; RT "Surface-exposed C-terminal amino acids of the small coat protein of Cowpea RT mosaic virus are required for suppression of silencing."; RL J. Gen. Virol. 85:3431-3435(2004). RN [16] RP FUNCTION (SMALL CAPSID PROTEIN C-TERMINUS PART), AND FUNCTION (SMALL CAPSID RP PROTEIN PRECURSOR). RX PubMed=15165817; DOI=10.1016/j.virol.2004.02.013; RA Liu L., Grainger J., Canizares M.C., Angell S.M., Lomonossoff G.P.; RT "Cowpea mosaic virus RNA-1 acts as an amplicon whose effects can be RT counteracted by a RNA-2-encoded suppressor of silencing."; RL Virology 323:37-48(2004). RN [17] RP FUNCTION (MOVEMENT PROTEIN), AND MUTAGENESIS OF VAL-259 AND ASP-260. RX PubMed=14722313; DOI=10.1128/jvi.78.3.1591-1594.2004; RA Carvalho C.M., Pouwels J., van Lent J.W., Bisseling T., Goldbach R.W., RA Wellink J.; RT "The movement protein of cowpea mosaic virus binds GTP and single-stranded RT nucleic acid in vitro."; RL J. Virol. 78:1591-1594(2004). RN [18] RP SUBCELLULAR LOCATION (MOVEMENT PROTEIN). RX PubMed=27339685; DOI=10.1007/s00705-016-2936-2; RA den Hollander P.W., Kieper S.N., Borst J.W., van Lent J.W.; RT "The role of plasmodesma-located proteins in tubule-guided virus transport RT is limited to the plasmodesmata."; RL Arch. Virol. 161:2431-2440(2016). RN [19] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 460-1022, INTERACTION WITH THE RP MATURE SMALL CAPSID PROTEIN (LARGE CAPSID PROTEIN), INTERACTION WITH THE RP LARGE CAPSID PROTEIN (MATURE SMALL CAPSID PROTEIN), FUNCTION (LARGE CAPSID RP PROTEIN), FUNCTION (MATURE SMALL CAPSID PROTEIN), SUBCELLULAR LOCATION RP (LARGE CAPSID PROTEIN), AND SUBCELLULAR LOCATION (MATURE SMALL CAPSID RP PROTEIN). RC STRAIN=Bi1 mutant; RX PubMed=10603314; DOI=10.1006/viro.1999.0038; RA Lin T., Chen Z., Usha R., Stauffacher C.V., Dai J.B., Schmidt T., RA Johnson J.E.; RT "The refined crystal structure of cowpea mosaic virus at 2.8 A RT resolution."; RL Virology 265:20-34(1999). RN [20] {ECO:0007744|PDB:2BFU} RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 460-828 AND 834-1022. RX PubMed=16873025; DOI=10.1016/j.chembiol.2006.05.014; RA Ochoa W.F., Chatterji A., Lin T., Johnson J.E.; RT "Generation and structural analysis of reactive empty particles derived RT from an icosahedral virus."; RL Chem. Biol. 13:771-778(2006). RN [21] {ECO:0007744|PDB:5A32, ECO:0007744|PDB:5A33} RP STRUCTURE BY ELECTRON MICROSCOPY (3.04 ANGSTROMS) OF 460-828 AND 834-1046, RP FUNCTION (SMALL CAPSID PROTEIN PRECURSOR), MUTAGENESIS OF ARG-476; TRP-649; RP VAL-942; GLU-980; PHE-1025; ARG-1026 AND PHE-1027, INTERACTION WITH THE RP MATURE SMALL CAPSID PROTEIN (LARGE CAPSID PROTEIN), INTERACTION WITH THE RP LARGE CAPSID PROTEIN (MATURE SMALL CAPSID PROTEIN), SUBUNIT (LARGE CAPSID RP PROTEIN), FUNCTION (LARGE CAPSID PROTEIN), FUNCTION (MATURE SMALL CAPSID RP PROTEIN), SUBCELLULAR LOCATION (LARGE CAPSID PROTEIN), AND SUBCELLULAR RP LOCATION (MATURE SMALL CAPSID PROTEIN). RX PubMed=26657148; DOI=10.1038/ncomms10113; RA Hesketh E.L., Meshcheriakova Y., Dent K.C., Saxena P., Thompson R.F., RA Cockburn J.J., Lomonossoff G.P., Ranson N.A.; RT "Mechanisms of assembly and genome packaging in an RNA virus revealed by RT high-resolution cryo-EM."; RL Nat. Commun. 6:10113-10113(2015). RN [22] {ECO:0007744|PDB:5FMO} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 460-833 AND 834-1046, INTERACTION RP WITH THE MATURE SMALL CAPSID PROTEIN (LARGE CAPSID PROTEIN), INTERACTION RP WITH THE LARGE CAPSID PROTEIN (MATURE SMALL CAPSID PROTEIN), SUBUNIT (LARGE RP CAPSID PROTEIN), PROTEOLYTIC CLEAVAGE (SMALL CAPSID PROTEIN PRECURSOR), RP FUNCTION (LARGE CAPSID PROTEIN), FUNCTION (MATURE SMALL CAPSID PROTEIN), RP SUBCELLULAR LOCATION (LARGE CAPSID PROTEIN), AND SUBCELLULAR LOCATION RP (MATURE SMALL CAPSID PROTEIN). RX PubMed=27021160; DOI=10.1016/j.str.2016.02.011; RA Huynh N.T., Hesketh E.L., Saxena P., Meshcheriakova Y., Ku Y.C., RA Hoang L.T., Johnson J.E., Ranson N.A., Lomonossoff G.P., Reddy V.S.; RT "Crystal Structure and Proteomics Analysis of Empty Virus-like Particles of RT Cowpea Mosaic Virus."; RL Structure 24:567-575(2016). RN [23] RP STRUCTURE BY ELECTRON MICROSCOPY (4.25 ANGSTROMS) OF 460-828 AND 834-1046, RP MUTAGENESIS OF ASN-633, INTERACTION WITH THE MATURE SMALL CAPSID PROTEIN RP (LARGE CAPSID PROTEIN), INTERACTION WITH THE LARGE CAPSID PROTEIN (MATURE RP SMALL CAPSID PROTEIN), SUBUNIT (LARGE CAPSID PROTEIN), FUNCTION (LARGE RP CAPSID PROTEIN), FUNCTION (MATURE SMALL CAPSID PROTEIN), SUBCELLULAR RP LOCATION (LARGE CAPSID PROTEIN), SUBCELLULAR LOCATION (MATURE SMALL CAPSID RP PROTEIN), DOMAIN (MATURE SMALL CAPSID PROTEIN), AND DOMAIN (LARGE CAPSID RP PROTEIN). RX PubMed=28373698; DOI=10.1038/s41598-017-00533-w; RA Hesketh E.L., Meshcheriakova Y., Thompson R.F., Lomonossoff G.P., RA Ranson N.A.; RT "The structures of a naturally empty cowpea mosaic virus particle and its RT genome-containing counterpart by cryo-electron microscopy."; RL Sci. Rep. 7:539-539(2017). CC -!- FUNCTION: [VP58]: Responsible for viral RNA2 accumulation. May function CC by recruiting the RNA1-encoded polyprotein that contains the CC replication protein to RNA2 and enable its replication. CC {ECO:0000250|UniProtKB:P23009}. CC -!- FUNCTION: [Movement protein]: Transports the viral genome to CC neighboring plant cells directly through plasmosdesmata, without any CC budding (PubMed:9501035). The movement protein allows efficient cell to CC cell propagation, by bypassing the host cell wall barrier. Acts by CC forming a tubular structure at the host plasmodesmata, enlarging it CC enough to allow free passage of virion capsids (PubMed:12556992, CC PubMed:14579172) (Probable). Binds to GTP and to single-stranded RNA CC and single-stranded DNA in a non-sequence-specific manner CC (PubMed:14722313). {ECO:0000269|PubMed:12556992, CC ECO:0000269|PubMed:14579172, ECO:0000269|PubMed:14722313, CC ECO:0000269|PubMed:9501035, ECO:0000305|PubMed:8497075}. CC -!- FUNCTION: [Large capsid protein]: Together with the mature small capsid CC protein, forms an icosahedral capsid (T=3) enclosing the viral positive CC strand RNA genome, with a diameter of approximately 300 Angstroms CC (PubMed:28373698, PubMed:10603314, PubMed:26657148, PubMed:27021160). CC The capsid is formed from 60 copies each of the large and the small CC capsid protein (PubMed:28373698, PubMed:10603314, PubMed:26657148, CC PubMed:27021160). The large capsid protein interacts with the viral RNA CC (PubMed:28373698, PubMed:26657148). {ECO:0000269|PubMed:10603314, CC ECO:0000269|PubMed:26657148, ECO:0000269|PubMed:27021160, CC ECO:0000269|PubMed:28373698}. CC -!- FUNCTION: [Mature small capsid protein]: Together with the large capsid CC protein, forms an icosahedral capsid (T=3) enclosing the viral positive CC strand RNA genome, with a diameter of approximately 300 Angstroms. The CC capsid is formed from 60 copies each of the large and the small capsid CC protein. The mature small capsid protein forms the turrets at the CC fivefold axes of the viral particle. {ECO:0000269|PubMed:10603314, CC ECO:0000269|PubMed:26657148, ECO:0000269|PubMed:27021160, CC ECO:0000269|PubMed:28373698}. CC -!- FUNCTION: [Small capsid protein precursor]: The cleavable C-terminus of CC small capsid protein seems to be involved in viral assembly and RNA CC packaging (PubMed:10049828). After virus assembly, these amino acids CC are cleaved off during the normal maturation of the virus CC (PubMed:26657148, PubMed:10049828). Also seems to act as suppressor of CC post-transcriptional gene silencing (PTGS), a mechanism of plant viral CC defense that limits the accumulation of viral RNAs (PubMed:15483261, CC PubMed:15165817). {ECO:0000269|PubMed:10049828, CC ECO:0000269|PubMed:15165817, ECO:0000269|PubMed:15483261, CC ECO:0000269|PubMed:26657148}. CC -!- FUNCTION: [Small capsid protein C-terminus part]: Acts as a suppressor CC of RNA-mediated gene silencing, also known as post-transcriptional gene CC silencing (PTGS), a mechanism of plant viral defense that limits the CC accumulation of viral RNAs. {ECO:0000269|PubMed:15165817, CC ECO:0000269|PubMed:15483261}. CC -!- SUBUNIT: [Mature small capsid protein]: Interacts with the large capsid CC protein (PubMed:26657148, PubMed:10603314). CC {ECO:0000269|PubMed:10603314, ECO:0000269|PubMed:26657148}. CC -!- SUBUNIT: [Large capsid protein]: Interacts with the mature small capsid CC protein (PubMed:26657148, PubMed:27021160, PubMed:28373698, CC PubMed:10603314). Homomultimer; assembles as pentons (PubMed:26657148, CC PubMed:27021160, PubMed:28373698). Interacts with the movement protein CC (via C-terminus) (PubMed:12867661). {ECO:0000269|PubMed:12867661, CC ECO:0000269|PubMed:26657148, ECO:0000269|PubMed:27021160, CC ECO:0000269|PubMed:28373698}. CC -!- SUBUNIT: [Movement protein]: Interacts (via C-terminus) with the large CC capsid protein (PubMed:12867661). {ECO:0000269|PubMed:12867661}. CC -!- SUBCELLULAR LOCATION: [VP58]: Host nucleus CC {ECO:0000269|PubMed:8497075}. CC -!- SUBCELLULAR LOCATION: [Movement protein]: Host cell junction, host CC plasmodesma {ECO:0000269|PubMed:14579172, ECO:0000269|PubMed:27339685}. CC Note=Assembles in tubules that are embedded within modified CC plasmodesmata. {ECO:0000269|PubMed:10864669, CC ECO:0000269|PubMed:14579172, ECO:0000269|PubMed:27339685}. CC -!- SUBCELLULAR LOCATION: [Large capsid protein]: Virion CC {ECO:0000269|PubMed:10603314, ECO:0000269|PubMed:26657148, CC ECO:0000269|PubMed:27021160, ECO:0000269|PubMed:28373698}. CC -!- SUBCELLULAR LOCATION: [Mature small capsid protein]: Virion CC {ECO:0000269|PubMed:10603314, ECO:0000269|PubMed:26657148, CC ECO:0000269|PubMed:27021160, ECO:0000269|PubMed:28373698}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=1; Synonyms=RNA2 polyprotein; CC IsoId=P03599-1; Sequence=Displayed; CC Name=2; CC IsoId=P03599-2; Sequence=VSP_059978; CC -!- DOMAIN: [Small capsid protein precursor]: The C-terminus is required CC for efficient assembly and RNA packaging. CC {ECO:0000269|PubMed:10049828}. CC -!- DOMAIN: [Large capsid protein]: Contains a beta-sheet structure called CC beta-barrel jelly roll. {ECO:0000269|PubMed:28373698}. CC -!- DOMAIN: [Mature small capsid protein]: Contains a beta-sheet structure CC called beta-barrel jelly roll. {ECO:0000269|PubMed:28373698}. CC -!- DOMAIN: [Movement protein]: The C-terminus is involved in binding to CC the large capsid protein, and hence to the virion. CC {ECO:0000269|PubMed:12556992, ECO:0000269|PubMed:12867661}. CC -!- PTM: [RNA2 polyprotein]: Specific enzymatic cleavages by picornain 3C- CC like protease in vivo yield mature proteins. CC {ECO:0000269|PubMed:16789216}. CC -!- PTM: [Small capsid protein precursor]: The C-terminal 24 amino acids of CC the small capsid protein are specifically cleaved by the RNA1 encoded CC picornain 3C-like protease during maturation. CC {ECO:0000269|PubMed:10049828, ECO:0000269|PubMed:27021160}. CC -!- PTM: [Large capsid protein]: Not glycosylated. CC {ECO:0000269|PubMed:10725439}. CC -!- PTM: [Mature small capsid protein]: Not glycosylated. CC {ECO:0000269|PubMed:10725439}. CC -!- MASS SPECTROMETRY: [Mature small capsid protein]: Mass=21121.8; CC Method=Electrospray; Evidence={ECO:0000269|PubMed:10049828}; CC -!- MISCELLANEOUS: [Isoform 2]: The 2 isoforms probably arise from CC alternative initiation (leaky scanning). {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-118 is the initiator. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid CC structure; CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1ny7"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X00729; CAA25314.1; -; Genomic_RNA. DR EMBL; X00729; CAA25315.1; -; Genomic_RNA. DR EMBL; X00729; CAA25317.1; -; Genomic_RNA. DR RefSeq; NP_613285.1; NC_003550.1. DR PDB; 1NY7; X-ray; 3.00 A; 1=834-1022, 2=460-828. DR PDB; 2BFU; X-ray; 4.00 A; L=460-828, S=834-1022. DR PDB; 5A32; EM; 3.44 A; A=834-1022, B=460-828. DR PDB; 5A33; EM; 3.04 A; A=834-1046, B=460-828. DR PDB; 5FMO; X-ray; 2.30 A; L=460-833, S=834-1046. DR PDBsum; 1NY7; -. DR PDBsum; 2BFU; -. DR PDBsum; 5A32; -. DR PDBsum; 5A33; -. DR PDBsum; 5FMO; -. DR SMR; P03599; -. DR iPTMnet; P03599; -. DR GeneID; 956626; -. DR KEGG; vg:956626; -. DR EvolutionaryTrace; P03599; -. DR Proteomes; UP000008589; Genome. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell. DR GO; GO:0039617; C:T=3 icosahedral viral capsid; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. 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; IPR003181; Como_LCP. DR InterPro; IPR003182; RNA2_polyprotein. DR InterPro; IPR029053; Viral_coat. DR Pfam; PF02247; Como_LCP; 1. DR Pfam; PF02248; Como_SCP; 1. DR SUPFAM; SSF88633; Positive stranded ssRNA viruses; 3. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative initiation; Capsid protein; KW DNA-binding; GTP-binding; Host cell junction; Host nucleus; KW Host-virus interaction; Inhibition of host innate immune response by virus; KW Nucleotide-binding; Reference proteome; RNA-binding; KW Suppressor of RNA silencing; T=3 icosahedral capsid protein; Transport; KW Viral immunoevasion; Viral movement protein; Virion. FT CHAIN 1..1046 FT /note="RNA2 polyprotein" FT /id="PRO_0000445839" FT CHAIN 1..459 FT /note="VP58" FT /id="PRO_0000037024" FT CHAIN 118..459 FT /note="Movement protein" FT /id="PRO_0000445840" FT CHAIN 460..833 FT /note="Large capsid protein" FT /id="PRO_0000037025" FT CHAIN 834..1046 FT /note="Small capsid protein precursor" FT /id="PRO_0000445841" FT CHAIN 834..1022 FT /note="Mature small capsid protein" FT /id="PRO_0000037026" FT CHAIN 1023..1046 FT /note="Small capsid protein C-terminus part" FT /id="PRO_0000037027" FT REGION 62..84 FT /note="Hydrophobic" FT /evidence="ECO:0000255" FT REGION 409..415 FT /note="Involved in tubule formation by the movement FT protein" FT /evidence="ECO:0000269|PubMed:12556992" FT SITE 459..460 FT /note="Cleavage; by viral protease" FT /evidence="ECO:0000269|PubMed:10049828" FT SITE 476 FT /note="Interaction with the viral RNA" FT /evidence="ECO:0000269|PubMed:26657148" FT SITE 633 FT /note="Interaction with the viral RNA; probable role in FT viral RNA packaging" FT /evidence="ECO:0000269|PubMed:28373698" FT SITE 649 FT /note="Interaction with the viral RNA; probable role in FT viral RNA packaging" FT /evidence="ECO:0000269|PubMed:26657148, FT ECO:0000269|PubMed:28373698" FT SITE 833..834 FT /note="Cleavage; by viral protease" FT /evidence="ECO:0000269|PubMed:10049828" FT SITE 1022..1023 FT /note="Cleavage" FT /evidence="ECO:0000269|PubMed:27021160" FT SITE 1025 FT /note="Involved in viral capsid assembly and RNA binding" FT /evidence="ECO:0000269|PubMed:26657148" FT MOD_RES 460 FT /note="N-acetylmethionine; by host" FT /evidence="ECO:0000269|PubMed:6641721" FT VAR_SEQ 1..117 FT /note="Missing (in isoform 2)" FT /id="VSP_059978" FT MUTAGEN 126..127 FT /note="IP->AA: No effect on the formation of tubules FT induced by the movement protein; No effect on infectivity." FT /evidence="ECO:0000269|PubMed:10662615" FT MUTAGEN 209..210 FT /note="PV->AA: Strong decrease in the formation of tubules FT induced by the movement protein; complete loss of FT infectivity." FT /evidence="ECO:0000269|PubMed:10662615" FT MUTAGEN 220..221 FT /note="SD->AA: No effect on the formation of tubules FT induced by the movement protein; No effect on infectivity." FT /evidence="ECO:0000269|PubMed:10662615" FT MUTAGEN 238..239 FT /note="IE->AA: Complete loss of formation of tubules FT induced by the movement protein; No effect on infectivity." FT /evidence="ECO:0000269|PubMed:10662615" FT MUTAGEN 259..260 FT /note="VD->AA: Complete loss of formation of tubules FT induced by the movement protein and complete loss of GTP FT binding; No effect on infectivity." FT /evidence="ECO:0000269|PubMed:10662615, FT ECO:0000269|PubMed:14722313" FT MUTAGEN 259 FT /note="V->A: Complete loss of GTP binding; when associated FT with A-260." FT /evidence="ECO:0000269|PubMed:14722313" FT MUTAGEN 260 FT /note="D->A: Complete loss of GTP binding; when associated FT with A-259." FT /evidence="ECO:0000269|PubMed:14722313" FT MUTAGEN 279..280 FT /note="RG->AA: Complete loss of formation of tubules FT induced by the movement protein; No effect on infectivity." FT /evidence="ECO:0000269|PubMed:10662615" FT MUTAGEN 409..410 FT /note="LK->AA: No effect on the formation of tubules FT induced by the movement protein; No effect on infectivity." FT /evidence="ECO:0000269|PubMed:10662615" FT MUTAGEN 448..449 FT /note="LD->AA: No effect on the formation of tubules FT induced by the movement protein; No effect on infectivity." FT /evidence="ECO:0000269|PubMed:10662615" FT MUTAGEN 476 FT /note="R->D,E: Complete loss of RNA packaging and decreased FT capsid assembly." FT /evidence="ECO:0000269|PubMed:26657148" FT MUTAGEN 476 FT /note="R->G,K,W: No effect on viral yield and virus FT systemic transport." FT /evidence="ECO:0000269|PubMed:26657148" FT MUTAGEN 633 FT /note="N->A: Loss of hability to cause a systemic infection FT in the host plant; no effect on encapsidation." FT /evidence="ECO:0000269|PubMed:28373698" FT MUTAGEN 633 FT /note="N->D: Markedly reduced viral yield and loss of FT hability to cause a systemic infection in the host plant FT probably due to reduced RNA encapsidation." FT /evidence="ECO:0000269|PubMed:28373698" FT MUTAGEN 649 FT /note="W->A,D: No effect." FT /evidence="ECO:0000269|PubMed:26657148" FT MUTAGEN 649 FT /note="W->F: Complete loss of viral RNA binding and capsid FT assembly." FT /evidence="ECO:0000269|PubMed:26657148" FT MUTAGEN 942 FT /note="V->W: Loss of capsid assembly." FT /evidence="ECO:0000269|PubMed:26657148" FT MUTAGEN 980 FT /note="E->R: Complete loss of capsid assembly." FT /evidence="ECO:0000269|PubMed:26657148" FT MUTAGEN 1025 FT /note="F->W: Strongly reduces the efficiency of RNA FT packaging. No effect on particle assembly." FT /evidence="ECO:0000269|PubMed:26657148" FT MUTAGEN 1026 FT /note="R->D: Complete loss of capsid assembly." FT /evidence="ECO:0000269|PubMed:26657148" FT MUTAGEN 1027 FT /note="F->W: Slightly reduced viral particle yield." FT /evidence="ECO:0000269|PubMed:26657148" FT STRAND 465..467 FT /evidence="ECO:0007829|PDB:5FMO" FT HELIX 468..470 FT /evidence="ECO:0007829|PDB:1NY7" FT TURN 479..481 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 482..491 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 499..505 FT /evidence="ECO:0007829|PDB:5FMO" FT HELIX 506..510 FT /evidence="ECO:0007829|PDB:5FMO" FT HELIX 518..522 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 525..527 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 529..536 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 546..555 FT /evidence="ECO:0007829|PDB:5FMO" FT HELIX 563..566 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 569..574 FT /evidence="ECO:0007829|PDB:5FMO" FT TURN 576..578 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 579..586 FT /evidence="ECO:0007829|PDB:5FMO" FT HELIX 597..602 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 606..613 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 623..635 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 645..661 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 663..665 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 669..674 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 680..682 FT /evidence="ECO:0007829|PDB:1NY7" FT STRAND 685..687 FT /evidence="ECO:0007829|PDB:5FMO" FT HELIX 690..695 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 698..711 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 721..726 FT /evidence="ECO:0007829|PDB:5FMO" FT HELIX 736..739 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 742..745 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 753..758 FT /evidence="ECO:0007829|PDB:5FMO" FT HELIX 760..762 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 767..770 FT /evidence="ECO:0007829|PDB:5FMO" FT TURN 777..779 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 784..791 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 796..798 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 801..818 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 846..851 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 861..866 FT /evidence="ECO:0007829|PDB:5FMO" FT TURN 867..869 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 872..877 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 881..884 FT /evidence="ECO:0007829|PDB:5FMO" FT HELIX 888..895 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 896..911 FT /evidence="ECO:0007829|PDB:5FMO" FT HELIX 916..918 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 923..929 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 932..935 FT /evidence="ECO:0007829|PDB:5A32" FT STRAND 938..943 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 949..957 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 960..963 FT /evidence="ECO:0007829|PDB:5FMO" FT TURN 970..973 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 978..984 FT /evidence="ECO:0007829|PDB:5FMO" FT TURN 986..988 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 989..998 FT /evidence="ECO:0007829|PDB:5FMO" FT STRAND 1003..1009 FT /evidence="ECO:0007829|PDB:5FMO" FT HELIX 1027..1032 FT /evidence="ECO:0007829|PDB:5A33" SQ SEQUENCE 1046 AA; 116218 MW; 350EBECBF6558A1E CRC64; MFSFTEAKSK ISLWTRSAAP LNNVYLSYSC RCGLGKRKLA GGCCSAPYIT CYDSADFRRV QYLYFCLTRY CCLYFFLLLL ADWFYKKSSI FFETEFSRGF RTWRKIVKLL YILPKFEMES IMSRGIPSGI LEEKAIQFKR AKEGNKPLKD EIPKPEDMYV SHTSKWNVLR KMSQKTVDLS KAAAGMGFIN KHMLTGNILA QPTTVLDIPV TKDKTLAMAS DFIRKENLKT SAIHIGAIEI IIQSFASPES DLMGGFLLVD SLHTDTANAI RSIFVAPMRG GRPVRVVTFP NTLAPVSCDL NNRFKLICSL PNCDIVQGSQ VAEVSVNVAG CATSIEKSHT PSQLYTEEFE KEGAVVVEYL GRQTYCAQPS NLPTEEKLRS LKFDFHVEQP SVLKLSNSCN AHFVKGESLK YSISGKEAEN HAVHATVVSR EGASAAPKQY DPILGRVLDP RNGNVAFPQM EQNLFALSLD DTSSVRGSLL DTKFAQTRVL LSKAMAGGDV LLDEYLYDVV NGQDFRATVA FLRTHVITGK IKVTATTNIS DNSGCCLMLA INSGVRGKYS TDVYTICSQD SMTWNPGCKK NFSFTFNPNP CGDSWSAEMI SRSRVRMTVI CVSGWTLSPT TDVIAKLDWS IVNEKCEPTI YHLADCQNWL PLNRWMGKLT FPQGVTSEVR RMPLSIGGGA GATQAFLANM PNSWISMWRY FRGELHFEVT KMSSPYIKAT VTFLIAFGNL SDAFGFYESF PHRIVQFAEV EEKCTLVFSQ QEFVTAWSTQ VNPRTTLEAD GCPYLYAIIH DSTTGTISGD FNLGVKLVGI KDFCGIGSNP GIDGSRLLGA IAQGPVCAEA SDVYSPCMIA STPPAPFSDV TAVTFDLING KITPVGDDNW NTHIYNPPIM NVLRTAAWKS GTIHVQLNVR GAGVKRADWD GQVFVYLRQS MNPESYDART FVISQPGSAM LNFSFDIIGP NSGFEFAESP WANQTTWYLE CVATNPRQIQ QFEVNMRFDP NFRVAGNILM PPFPLSTETP PLLKFRFRDI ERSKRSVMVG HTATAA //