POL2_SDVS5
ID POL2_SDVS5 Reviewed; 1574 AA.
AC Q9WAL9;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 23-FEB-2022, entry version 60.
DE RecName: Full=RNA2 polyprotein;
DE AltName: Full=P2;
DE Contains:
DE RecName: Full=Movement protein;
DE Short=MP;
DE Contains:
DE RecName: Full=Large capsid protein;
DE Short=LCP;
DE Contains:
DE RecName: Full=Small capsid protein;
DE Short=SCP;
OS Satsuma dwarf virus (isolate Satsuma mandarin/Japan/S-58/1977) (SDV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Sadwavirus; Satsumavirus.
OX NCBI_TaxID=650481;
OH NCBI_TaxID=55188; Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10092021; DOI=10.1099/0022-1317-80-3-793;
RA Iwanami T., Kondo Y., Karasev A.V.;
RT "Nucleotide sequences and taxonomy of satsuma dwarf virus.";
RL J. Gen. Virol. 80:793-797(1999).
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 form a capsid enclosing the viral positive
CC strand RNA genome. Together they form an icosahedral capsid pseudo T=3
CC with a diameter of approximately 30 nm (Potential). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Movement protein]: Host cell junction, host
CC plasmodesma {ECO:0000250}. Note=Assembles in tubules that are embedded
CC within modified plasmodesmata. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Large capsid protein]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Small capsid protein]: Virion {ECO:0000305}.
CC -!- PTM: Specific enzymatic cleavages by RNA1 encoded picornain 3C-like
CC protease in vivo yield mature proteins. {ECO:0000250}.
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DR EMBL; AB009959; BAA76747.1; -; Genomic_RNA.
DR RefSeq; NP_620567.1; NC_003786.2.
DR GeneID; 993328; -.
DR KEGG; vg:993328; -.
DR Proteomes; UP000000675; 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; -; 1.
DR InterPro; IPR005306; Nepo_coat_N.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF03689; Nepo_coat_N; 1.
PE 3: Inferred from homology;
KW Capsid protein; Coiled coil; Host cell junction; Reference proteome;
KW Transport; Viral movement protein; Virion.
FT CHAIN 1..1574
FT /note="RNA2 polyprotein"
FT /id="PRO_0000402776"
FT CHAIN 1..913
FT /note="Movement protein"
FT /id="PRO_0000402777"
FT CHAIN 914..1357
FT /note="Large capsid protein"
FT /id="PRO_0000402778"
FT CHAIN 1358..1574
FT /note="Small capsid protein"
FT /id="PRO_0000402779"
FT REGION 557..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 361..422
FT /evidence="ECO:0000255"
FT COMPBIAS 868..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 913..914
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 1357..1358
FT /note="Cleavage"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1574 AA; 174410 MW; 923BB7BDB7311C28 CRC64;
MEIYGFSPLS FQDTESWKNS AFAACRGCKT YPIEEVGTDG SVRIRELPVG LVLKGVMAQY
RSILWTQFVA DPATTTVDRK SFDFWLFCRR AEAAQERAFR ARQSKRAAKA AALDAEGLID
RSYKGRTYKV SVRGLSWKSV RAAQKAARKA AKNFGFTISE NPFSALPSEG RSAFSAGETP
APPACALPNI CWAARRASAK SASPADVESL PFLGLLPESP RLRNEGLLSL LRAKLADFKA
ARAPLVPIAK RVVKTPSEDS IWESVEKNAP IVGCVINGMV GIPKNPIIQR LLPERKYIAR
KCVRAFVPQV MCSSRHKHDF AQLRNPDKWI VFPSVIRIST VDAYATARRL GLINDCSSAL
ERVKAFSSHH LDLEKEVSRL EREACAAPRK TIVARVFKFF FEEYALAYDE VVERLRAAKE
DRRREHLAFL RNIKRQAHEL ELKERQSFLV AIEEARIKSL ELKAKIEEGP PPQILYTPEW
HVVQRAKAYA DVTMSPSERD IAHLAYENKY VNARAYPNTD VAAKFRARCD AHFERIFGYA
VHRGTRTETL TQVAESPPPI ITAPVGQRVG GNPPTETPGA AAVRAAMRRA VERNRPGPGE
SSAMPAREPL LSHRGQYYAR SLSDRYNNIC SRNNAYDLMR ETDVPIMEFT FGQQQDIAIP
LSSRFGNHQS LHVGELEIAV QSSVLTGVDT AMAIMVSDAS HDRLEEGFLS LTILRLGAGW
MRHTIPIGIT VFPTDPLVDR FLRLSVLTGG SPMADGRQVA RLHYGLLGQA YTGAGEQRLT
QYATRRINVR QTHVTQFLEG NHIHIARSED RQQPLPHMSL EFRPLSGSTR YVARPGGYQA
IESGRQSVDI TQNFIRMPTH LTRSATDREE TPAPNNPNEQ NVGRSEINAE IPTNSAEEEE
RRRRTPHGSA IHRGYTEFSE RNENLIEHLY VPSMHGLSLK EDIHLFTKNL EIPSTADFCK
ELARYSGLTE AMSYRGASYY SRLLSGVAIL RPHFKFTFRL VTPILESIPL FVVWDDLGQL
NTKVSLLSSA FQVIDSDHTR AAVYEVRPSG PTDLLTPSKA NYGVGGDLVI FSGGYGSLSL
SSPLRLKIEA CLLKDTSLGS GEIALPQGPS SMLSFHYLNE VDLGDVNMHI FLGSCKYKSS
STVGGRKYIS VCPAAGLVHK GGKAAYLGLG ASLFSLYNFW KGSYVLKVDV LSKGSCAGAI
SIYIPPPGSS ADHYSQSQLD TLPRYELPWR GSGSARFEVE NFSWIGWHLT KPQRYITNED
WFSLNAGLLV VLNQPPTTRT GGSSDIRVIF RIVKFKNLTL KERSTTCDIF AGIKDSEYTD
PLVDVLDENI TAPSASSLTT VQDPDLGLET TSSAQTSGLT TTRSFGAYYA YLLGGESAGN
RWHSYVLPIT MGHHREMIGA SKTGYLNTQL DETIRIRYSL RNPLHILCSA GAYYAVDLLF
TLVVDGDHGA ERAYTQLGLI QTPLMEYFDG YSASRNLSSE GGYSNQLGVG KSYVQLIVPR
RNYRARSITT NTGALFFETI GSLTVKFAVS AKIKGVHLYV EPVGPIDVDG YGRGADISLT
NENFVLMPSL RTAA