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POL2_BBWVS
ID   POL2_BBWVS              Reviewed;        1018 AA.
AC   Q76L39;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   23-FEB-2022, entry version 50.
DE   RecName: Full=RNA2 polyprotein;
DE   AltName: Full=119kDa protein;
DE   AltName: Full=Genome polyprotein M;
DE   Contains:
DE     RecName: Full=VP53;
DE     AltName: Full=53 kDa protein;
DE   Contains:
DE     RecName: Full=Movement protein;
DE              Short=MP;
DE     AltName: Full=37 kDa protein;
DE     AltName: Full=VP37;
DE   Contains:
DE     RecName: Full=Large capsid protein;
DE              Short=LCP;
DE     AltName: Full=44 kDa protein;
DE   Contains:
DE     RecName: Full=Small capsid protein;
DE              Short=SCP;
DE     AltName: Full=22 kDa protein;
OS   Broad bean wilt virus 1 (strain Spinach/United States/ATCC PV-132/1963)
OS   (BBWV-1).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Secoviridae; Comovirinae; Fabavirus.
OX   NCBI_TaxID=649895;
OH   NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
OH   NCBI_TaxID=13163; Myzus.
OH   NCBI_TaxID=4101; Petunia.
OH   NCBI_TaxID=3562; Spinacia oleracea (Spinach).
OH   NCBI_TaxID=3906; Vicia faba (Broad bean) (Faba vulgaris).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Kobayashi Y.O., Kobayashi A., Nakano M., Hagiwara K., Honda Y., Omura T.;
RT   "Analysis of genetic relations between Broad bean wilt virus 1 and Broad
RT   bean wilt virus 2.";
RL   J. Gen. Plant Pathol. 69:320-326(2003).
CC   -!- FUNCTION: [VP53]: Acts as suppressor of post-transcriptional gene
CC       silencing (PTGS), a mechanism of plant viral defense that limits the
CC       accumulation of viral RNAs. Binds ssRNA.
CC       {ECO:0000250|UniProtKB:Q9Q2Q3}.
CC   -!- FUNCTION: [Movement protein]: Transports the viral genome to
CC       neighboring plant cells directly through plasmosdesmata, without any
CC       budding. The movement protein allows efficient cell to cell
CC       propagation, by bypassing the host cell wall barrier. Acts by forming a
CC       tubular structure at the host plasmodesmata, enlarging it enough to
CC       allow free passage of virion capsids. Binds to GTP and to single-
CC       stranded RNA and single-stranded DNA in a non-sequence-specific manner.
CC       Also acts as suppressor of post-transcriptional gene silencing (PTGS),
CC       a mechanism of plant viral defense that limits the accumulation of
CC       viral RNAs. {ECO:0000250|UniProtKB:Q9Q2Q3}.
CC   -!- FUNCTION: [Large capsid protein]: Together with the 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. The
CC       large capsid protein interacts with the viral RNA (By similarity). Also
CC       acts as suppressor of post-transcriptional gene silencing (PTGS), a
CC       mechanism of plant viral defense that limits the accumulation of viral
CC       RNAs. Binds ssRNA (By similarity). {ECO:0000250|UniProtKB:P03599,
CC       ECO:0000250|UniProtKB:Q9Q2Q3}.
CC   -!- FUNCTION: [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 small capsid protein forms the turrets at the fivefold
CC       axes of the viral particle. {ECO:0000250|UniProtKB:P03599}.
CC   -!- SUBUNIT: [Small capsid protein]: Interacts with the large capsid
CC       protein. {ECO:0000250|UniProtKB:P03599}.
CC   -!- SUBUNIT: [Large capsid protein]: Interacts with the small capsid
CC       protein. Homomultimer; assembles as pentons. Interacts with the
CC       movement protein (via C-terminus). {ECO:0000250|UniProtKB:P03599}.
CC   -!- SUBUNIT: [Movement protein]: Interacts (via C-terminus) with the large
CC       capsid protein. {ECO:0000250|UniProtKB:P03599}.
CC   -!- SUBCELLULAR LOCATION: [Movement protein]: Host endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q9Q2Q3}. Host cell junction, host plasmodesma
CC       {ECO:0000250|UniProtKB:Q9Q2Q3}. Note=Assembles in tubules that are
CC       embedded within modified plasmodesmata. {ECO:0000250|UniProtKB:P03599}.
CC   -!- SUBCELLULAR LOCATION: [Large capsid protein]: Virion
CC       {ECO:0000250|UniProtKB:P03599}.
CC   -!- SUBCELLULAR LOCATION: [Small capsid protein]: Virion
CC       {ECO:0000250|UniProtKB:P03599}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=RNA2 polyprotein; Synonyms=119kDa protein;
CC         IsoId=Q76L39-1; Sequence=Displayed;
CC       Name=RNA2 polyprotein 104kDa; Synonyms=104kDa protein;
CC         IsoId=Q76L39-2; Sequence=VSP_059982;
CC   -!- DOMAIN: [Movement protein]: The C-terminus is important for targeting
CC       the movement protein to the plasmodesmata.
CC       {ECO:0000250|UniProtKB:Q9Q2Q3}.
CC   -!- DOMAIN: [VP53]: The N-terminus is involved in ssRNA-binding.
CC       {ECO:0000250|UniProtKB:Q9Q2Q3}.
CC   -!- PTM: [RNA2 polyprotein]: Specific enzymatic cleavages by picornain 3C-
CC       like protease in vivo yield mature proteins.
CC       {ECO:0000250|UniProtKB:P03599}.
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DR   EMBL; AB084451; BAD00184.1; -; Genomic_RNA.
DR   RefSeq; NP_945135.1; NC_005290.1.
DR   SMR; Q76L39; -.
DR   GeneID; 2658943; -.
DR   KEGG; vg:2658943; -.
DR   Proteomes; UP000000409; Genome.
DR   GO; GO:0044165; C:host cell endoplasmic reticulum; 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: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.
PE   3: Inferred from homology;
KW   Alternative initiation; Capsid protein; Host cell junction;
KW   Host endoplasmic reticulum; Reference proteome;
KW   T=3 icosahedral capsid protein; Transport; Viral movement protein; Virion.
FT   CHAIN           1..1018
FT                   /note="RNA2 polyprotein"
FT                   /id="PRO_0000402787"
FT   CHAIN           1..419
FT                   /note="VP53"
FT                   /id="PRO_0000402788"
FT   CHAIN           91..419
FT                   /note="Movement protein"
FT                   /id="PRO_0000445856"
FT   CHAIN           420..821
FT                   /note="Large capsid protein"
FT                   /id="PRO_0000402789"
FT   CHAIN           822..1018
FT                   /note="Small capsid protein"
FT                   /id="PRO_0000402790"
FT   SITE            419..420
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03599"
FT   SITE            821..822
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03599"
FT   VAR_SEQ         1..90
FT                   /note="Missing (in isoform RNA2 polyprotein 104kDa)"
FT                   /id="VSP_059982"
SQ   SEQUENCE   1018 AA;  114253 MW;  99D1B5179D30DEB2 CRC64;
     MPLILLWFCF LCMIYVILKL EYTYVVKPFL KTAFLNTTSH YSDEYLREYS GIRWLHTFKE
     YREHTIFFNF PSFYCSPGSG IKHTLSELIK MEAERVNLTK TETIPKDILL ERAKNYRVAQ
     ESNKSLLPQV EDLYEVSKWK RAISSLQKGE PSFVRTSEVA IGTMSGAGKM RIKVPVVKSY
     EEEVADMRLS QKVRAKADQI VVAAIEIVND GFASVNSDVT LAASLYDKRH KTIASSFKGA
     YASRASGTPS HVVFYPTHRV APGDNPNDTL ELSAVSRDSD FDENFTLANF SVRTVYAKAK
     GPEVIRETQH LLNCKLEDLV KAQQFASDEQ VVLALPRVYP KVNLDNYVMP GPDNVTKQEG
     EYSAKGIHFR KPIFNGSEIV LNATSKLPSS KSRGISKSEK IDDLGCMSDE EGIDYKYGQA
     LMEEDVLEAQ VDMFPLHNVA ETMRLLFSGV STIPMNVVEG TKISVAYLNE LATHPGVHVP
     ILNMLGRIPG SILARVHCEV APTCGIGLAA TYVEGNESAA LGTDLGRLLG IQHVKWNPAI
     EPVKEFRFKP FSCVDWWNMH YLGSSKFSPV LAFVCLSKWI NPPKGECKMS YALYFEPDII
     LPRQIASLNS VPSFMLRKEL GTLSFKQGER RAYAFEVNFG KPQVEGKSVT LNFASAYCGL
     SQYMESDIVI DLTLMSSPMM GGTFTLAYVA GSYLKSIKNM QFLDALPHIT FNFEKGGKST
     RSLRFPSRLF PTYQSLDRWD LNASREDDVS GHFVLYQRDT VSSALEGDLV FRVSARVSGE
     PMMHGVSVGY PTTLTRATTG KMSSRSLGEK VRKPIGLAKG QAHMNLADYK RVFYPMAEWI
     YSSEKYEGRR EDRDILKLLL KMRLDGTKAT EDFRIVHSPL VRVLQNCAWL RGTIHFKIVV
     RANSEMMSYQ RTSQVHVTAH ENSLSSNEFF SGMLTATSGE LEFSKEVVGP VEGFSSMGWN
     VQGNKKFYKL CIALGNVHEY EAVKVMASFG DDVEFAGQQK AGHYALERGV SVFKEFKY
 
 
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