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Database: UniProt
Entry: C7SW01_9SECO
LinkDB: C7SW01_9SECO
Original site: C7SW01_9SECO 
ID   C7SW01_9SECO            Unreviewed;      1095 AA.
AC   C7SW01;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=RNA2 polyprotein {ECO:0000256|ARBA:ARBA00022361};
DE   AltName: Full=Genome polyprotein M {ECO:0000256|ARBA:ARBA00032125};
DE   AltName: Full=M RNA polyprotein {ECO:0000256|ARBA:ARBA00033402};
DE   AltName: Full=Middle component RNA polyprotein {ECO:0000256|ARBA:ARBA00030233};
DE   AltName: Full=P2 {ECO:0000256|ARBA:ARBA00031918};
OS   Turnip ringspot virus.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Secoviridae; Comovirinae; Comovirus.
OX   NCBI_TaxID=392504 {ECO:0000313|EMBL:ACV41392.1, ECO:0000313|Proteomes:UP000202412};
RN   [1] {ECO:0000313|EMBL:ACV41392.1, ECO:0000313|Proteomes:UP000202412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Toledo {ECO:0000313|EMBL:ACV41392.1};
RX   PubMed=19838619; DOI=10.1007/s00705-009-0523-5;
RA   Khandekar S., He J., Leisner S.;
RT   "Complete nucleotide sequence of the Toledo isolate of turnip ringspot
RT   virus.";
RL   Arch. Virol. 154:1917-1922(2009).
CC   -!- FUNCTION: Responsible for viral RNA2 accumulation. May function by
CC       recruiting the RNA1-encoded polyprotein that contains the replication
CC       protein to RNA2 and enable its replication.
CC       {ECO:0000256|ARBA:ARBA00003642}.
CC   -!- SUBCELLULAR LOCATION: Host cell junction, host plasmodesma
CC       {ECO:0000256|ARBA:ARBA00004621}.
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DR   EMBL; FJ712027; ACV41392.1; -; Genomic_RNA.
DR   RefSeq; YP_003193666.1; NC_013219.1.
DR   GeneID; 11187370; -.
DR   KEGG; vg:11187370; -.
DR   Proteomes; UP000202412; Genome.
DR   GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   4: Predicted;
KW   Capsid protein {ECO:0000256|ARBA:ARBA00023060};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Host cell junction {ECO:0000256|ARBA:ARBA00023081};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022463};
KW   Inhibition of host innate immune response by virus
KW   {ECO:0000256|ARBA:ARBA00022463}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Suppressor of RNA silencing {ECO:0000256|ARBA:ARBA00022463};
KW   T=3 icosahedral capsid protein {ECO:0000256|ARBA:ARBA00023060};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00023031};
KW   Viral immunoevasion {ECO:0000256|ARBA:ARBA00022463};
KW   Viral movement protein {ECO:0000256|ARBA:ARBA00023031};
KW   Virion {ECO:0000256|ARBA:ARBA00023060}.
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1045..1095
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1056..1087
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1095 AA;  122063 MW;  D43F0D71C28ADBB3 CRC64;
     MNNIKGRHHC IDNLIPQFAG EPARDFSDKP QEKYVKFLKV SPFSFLCFLI VCHIVTYCET
     VFKVCFYFNS WTGTKLRDWL LSITRDANVE YKRLEAISSW SAGHQVVIQH SFSAKKMETV
     MERGIAAKAL ELRNDSAMNK GKRFVGLKDH IPAGKDLYVH KQKLFEMLKG SKRSREVDIS
     RIKGCEVVEM KHIDVGTLSP GENQIINVKI VKDDMLPQPV QSDYAMVTHS NESKYANAMH
     VGAIEVIFNS YASPTSDIVG GMILVDTCHK SVANAVRSVF VTGLAGGKLI RVLMYPNTLV
     EIGPKMNDRF KLVCTTSNSD ISEGFNLASV KVNVVGCTQS LMTQYVPQPL LDNLLNKEQG
     TVVEYLGQLS YVMHHSNHIT EEFLANQTME FDLGKKLQLT PSGSGASLAK STSMRYVVGP
     KQRLLNAEED DGASSFDKRR DAARKIVGMR ADATYVDPVF GMTQRAFGQA STTQSLLNKF
     ANTRQMEGTP IETKIARTKI ILTKVMAGGN ILYTERLSDV LSNVEQRAAI AFQRTHVQHK
     KLVALATINV PENTGCALMM CYNSGIRGKA VVDAYTASAE ASTIWNPACQ QQARLEINVN
     PCKSAWSYQF LRQSKGVFNV VCISGWTTTP STDLSLTIDW YLSDKDAEPE TYCAVGINPK
     IVLNRWMGKL SFPQGTDVTL RRMPLAIGGG AGGTGLVYMN MPNALCSLWR YMRGGMSFEV
     IKLSSPYIKA TIAFFIAFTD VDATVPNLEA YPHKLVQFSE IQERVTISFD KEDFVMAWST
     QVHNSVPLSE DGCPYLYAVV HDSVGSTISG DFNIGVVLKE MNEVESIGRH PGWKGARPLA
     VSPQGLRKSP SGVWNELFMV RGPPEAKSTD VVQFAIDLVG VGIATKNPGA WSIETNNSPM
     NNLMRTATWK SGTFHFQVLM EGNPLIKRGD WSSYCEVSLT QSTKVSTMSS RNWVMKDPSS
     WELEFDIKIE GPNDGFENWE SHFSNQTSWF LVFSVFNPDQ STVFVVNGMI DDDCWFAGNT
     LMPPFLEPGS VSSRHSFLSS VQFDYGTTPS RRAPSSPADN EDDDGRRSER IRQLERYRER
     DDQNRGNLAT YMRRS
//
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