ID   RDRP_TYYVF              Reviewed;        1035 AA.
AC   P09507;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2002, sequence version 2.
DT   04-NOV-2026, entry version 131.
DE   RecName: Full=Protein P1-P2;
DE   Contains:
DE     RecName: Full=Serine protease;
DE              EC=3.4.21.-;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48;
DE   Flags: Precursor;
GN   ORFNames=ORF1/ORF2;
OS   Turnip yellows virus (isolate FL-1) (TuYV) (BWYV-FL1).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Sobelivirales; Solemoviridae; Polerovirus; Polerovirus BWYV;
OC   Beet western yellows virus.
OX   NCBI_TaxID=12043;
OH   NCBI_TaxID=161934; Beta vulgaris (Sugar beet).
OH   NCBI_TaxID=3709; Brassica napus subsp. rapifera (rutabaga).
OH   NCBI_TaxID=138011; Brassica napus var. napus (canola).
OH   NCBI_TaxID=3710; Brassica nigra (Black mustard) (Sinapis nigra).
OH   NCBI_TaxID=3715; Brassica oleracea var. botrytis (Cauliflower).
OH   NCBI_TaxID=3716; Brassica oleracea var. capitata (Cabbage).
OH   NCBI_TaxID=51350; Brassica rapa subsp. rapa (Turnip).
OH   NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
OH   NCBI_TaxID=3827; Cicer arietinum (Chickpea) (Garbanzo).
OH   NCBI_TaxID=3654; Citrullus lanatus (Watermelon) (Citrullus vulgaris).
OH   NCBI_TaxID=3721; Crambe hispanica subsp. abyssinica (Abyssinian kale) (Crambe abyssinica).
OH   NCBI_TaxID=3659; Cucumis sativus (Cucumber).
OH   NCBI_TaxID=3663; Cucurbita pepo (Vegetable marrow) (Summer squash).
OH   NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH   NCBI_TaxID=4232; Helianthus annuus (Common sunflower).
OH   NCBI_TaxID=4236; Lactuca sativa (Garden lettuce).
OH   NCBI_TaxID=103529; Phlox drummondii (Annual phlox).
OH   NCBI_TaxID=3888; Pisum sativum (Garden pea) (Lathyrus oleraceus).
OH   NCBI_TaxID=3726; Raphanus sativus (Radish) (Raphanus raphanistrum var. sativus).
OH   NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH   NCBI_TaxID=3562; Spinacia oleracea (Spinach).
OH   NCBI_TaxID=3900; Trifolium subterraneum (Subterranean clover).
OH   NCBI_TaxID=3906; Vicia faba (Broad bean) (Faba vulgaris).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3194229; DOI=10.1093/nar/16.21.9917;
RA   Veidt I., Lot H., Leiser M., Scheidecker D., Guilley H., Richards K.E.,
RA   Jonard G.;
RT   "Nucleotide sequence of beet western yellows virus RNA.";
RL   Nucleic Acids Res. 16:9917-9932(1988).
RN   [2]
RP   SEQUENCE REVISION.
RA   Veidt I., Lot H., Leiser M., Scheidecker D., Guilley H., Richards K.E.,
RA   Jonard G.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Precursor from which the RNA-dependent RNA polymerase (RdRp)
CC       is probably released. RNA-dependent RNA polymerase plays an essential
CC       role in virus replication (Potential). {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC         diphosphate; Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC   -!- SUBCELLULAR LOCATION: [Protein P1-P2]: Membrane {ECO:0000305}; Multi-
CC       pass membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=RNA-directed RNA polymerase;
CC         IsoId=P09507-1; Sequence=Displayed;
CC       Name=Protein P1;
CC         IsoId=P09506-1; Sequence=External;
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC       protease probably cleaves itself and releases the RdRp (Potential).
CC       Cleavages have been shown in the P1 protein, but since the N-terminus
CC       containing the serine protease is shared between P1 and P1-P2,
CC       cleavages should also occur within the P1-P2 protein. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform RNA-directed RNA polymerase]: Produced by -1
CC       ribosomal frameshifting between codons 461 and 462.
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DR   EMBL; X13063; CAA31464.2; -; Genomic_RNA.
DR   PIR; S01940; RRVQFL.
DR   RefSeq; NP_620485.2; NC_003743.1.
DR   MEROPS; S39.002; -.
DR   GeneID; 940481; -.
DR   KEGG; vg:940481; -.
DR   CDD; cd23180; ps-ssRNAv_Solemoviridae_RdRp; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR000382; Peptidase_S39B_luteovirus.
DR   InterPro; IPR001795; RNA-dir_pol_orthornavirus.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   Pfam; PF02122; Peptidase_S39; 1.
DR   Pfam; PF02123; RdRP_4; 1.
DR   PRINTS; PR00914; LVIRUSRNAPOL.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51868; PEPTIDASE_S39; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0075523; P:viral translational frameshifting; IEA:UniProtKB-KW.
DR   Proteomes; UP000007545; Segment.
PE   3: Inferred from homology;
KW   Hydrolase; Membrane; Multifunctional enzyme; Nucleotide-binding;
KW   Nucleotidyltransferase; Protease; Reference proteome;
KW   Ribosomal frameshifting; RNA-directed RNA polymerase; Serine protease;
KW   Signal; Transferase; Transmembrane; Transmembrane helix;
KW   Viral RNA replication.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..1035
FT                   /note="Protein P1-P2"
FT                   /id="PRO_0000222398"
FT   CHAIN           204..400
FT                   /note="Serine protease"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000390903"
FT   CHAIN           401..1035
FT                   /note="RNA-directed RNA polymerase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000390904"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          206..400
FT                   /note="Peptidase S39"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT   DOMAIN          829..944
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          455..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..477
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..488
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..519
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        254
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT   ACT_SITE        289
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT   ACT_SITE        357
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT   SITE            203..204
FT                   /note="Cleavage; by viral serine protease"
FT                   /evidence="ECO:0000255"
FT   SITE            400..401
FT                   /note="Cleavage; by viral serine protease"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1035 AA;  115871 MW;  54642FEC88E6F66F CRC64;
     MYSKLMFFFA LCSISFLFTS EAASTMLLES SYLPLNQSYA PGFLYKRDML PPPLQAVLTY
     TCPEPRPLAE ESYNDLLRAI SQKSSSDFQN AYSLALSFSS DFYQHGLKTL KDVSFLAVEK
     FLWGLTRLWS SLILASFSAL WWLVSNFTTP VFCLALLYTV TKYMVKTVSF LFGGLPIWII
     SIAFSLLKKS FSALRSTPKC LYEKAIDGFK SFTIPQSPPK SCVIPITHAS GNHAGYASCI
     KLYNGENALM TATHVLRDCP NAVAVSAKGL KTRIPLAEFK TIAKSDKGDV TLLRGPPNWE
     GLLGCKAANV ITAANLAKCK ASIYSFDRDG WVSSYAEIVG SEGTDVMVLS HTEGGHSGSP
     YFNGKTILGV HSGASATGNY NLMAPIPSLP GLTSPTYVFE TTAPQGRVFA QEDIAEIEGL
     YAQVMKRVQQ AEDFKPKTGK YWGDMEDDED IFFESKEDLS GKRSARHRPR NKRRRQLHPK
     DKQRRWERDD GENNLISSGK DKSREHREES DRGDLRESDE NSEIPPQKSP KETAGEFERY
     FSSLYNWEVP TSPREVPGFR HCGKLPQYYH PKQKEESSWG KTLVGNHPAL GEKTSGFGWP
     KFGPEAELKS LRLQASRWLE RAQSAEIPSD AERERVIQKT ADVYHPCQTN GPAATRGGTL
     TWNNFMIDFK QAVFSLEFDA GIELPYIAYG KPTHRGWVED QKLLPILAQL TFFRLQKMLE
     VNFEDMGPEE LVRNGLCDPI RLFVKGEPHK QAKLDEGRYR LIMSVSLVDQ LVARVLFQNQ
     NKREIALWRA IPSKPGFGLS TDEQVLDFVE SLARQVGTTT TEVVANWKNY LTPTDCSGFD
     WSVADWMLHD DMIVRNRLTI DLNPATERLR SCWLRCISNS VLCLSDGTLL AQIHPGVQKS
     GSYNTSSSNS RIRVMAAFHT GAIWAMAMGD DALESNPADL AAYKKLGFKV EVSGQLEFCS
     HIFRAPDLAL PVNENKMIYK LIYGYNPGSG NAEVVSNYLA ACFSVLNELR HDPASVELLY
     SWLVDPVLPQ KIPGE
//