RDRP_TYYVF
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 03-AUG-2022, entry version 115.
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.
OX NCBI_TaxID=12043;
OH NCBI_TaxID=161934; Beta vulgaris (Sugar beet).
OH NCBI_TaxID=3709; Brassica napus subsp. rapifera.
OH NCBI_TaxID=138011; Brassica napus var. napus.
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).
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=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); 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 Proteomes; UP000007545; Genome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000382; Peptidase_S39B_luteovirus.
DR InterPro; IPR001795; RNA-dir_pol_luteovirus.
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; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51868; PEPTIDASE_S39; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
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 465..481
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..526
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
