RDRP_PLRV1
ID RDRP_PLRV1 Reviewed; 1062 AA.
AC P17520;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 88.
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 AltName: Full=69.6 kDa protein;
DE Flags: Precursor;
GN ORFNames=ORF1/ORF2;
OS Potato leafroll virus (strain Potato/Scotland/strain 1/1984) (PLrV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Sobelivirales; Solemoviridae; Polerovirus.
OX NCBI_TaxID=12046;
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2732710; DOI=10.1099/0022-1317-70-5-1037;
RA Mayo M.A., Robinson D.J., Jolly C.A., Hyman L.;
RT "Nucleotide sequence of potato leafroll luteovirus RNA.";
RL J. Gen. Virol. 70:1037-1051(1989).
RN [2]
RP RIBOSOMAL FRAMESHIFTING.
RX PubMed=1547775; DOI=10.1002/j.1460-2075.1992.tb05151.x;
RA Prufer D., Tacke E., Schmitz J., Kull B., Kaufmann A., Rohde W.;
RT "Ribosomal frameshifting in plants: a novel signal directs the -1
RT frameshift in the synthesis of the putative viral replicase of potato
RT leafroll luteovirus.";
RL EMBO J. 11:1111-1117(1992).
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 Comment=The isoform P1 is produced by conventional translation,
CC whereas the isoform RNA-directed RNA polymerase is produced by -1
CC ribosomal frameshifting between codons 487 and 488. {ECO:0000305};
CC Name=RNA-directed RNA polymerase;
CC IsoId=P17520-1; Sequence=Displayed;
CC Name=Protein P1;
CC IsoId=P17519-1; 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 -!- SEQUENCE CAUTION:
CC Sequence=BAA00418.1; Type=Miscellaneous discrepancy; Note=Ribosomal frameshifting not described. Translation N-terminally extended.; Evidence={ECO:0000305};
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DR EMBL; D00530; BAA00418.1; ALT_SEQ; Genomic_RNA.
DR PIR; JA0119; RRVQLL.
DR Proteomes; UP000006723; 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:0070008; F:serine-type exopeptidase 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 InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR018019; Luteovirus_Orf2.
DR InterPro; IPR009003; Peptidase_S1_PA.
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; PR00913; LVIRUSORF2.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1062
FT /note="Protein P1-P2"
FT /id="PRO_0000222399"
FT CHAIN 205..399
FT /note="Serine protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390905"
FT CHAIN 400..1062
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390906"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 207..399
FT /note="Peptidase S39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT DOMAIN 859..974
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 455..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..513
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 255
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT ACT_SITE 286
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT ACT_SITE 354
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT SITE 204..205
FT /note="Cleavage; by viral serine protease"
FT /evidence="ECO:0000255"
FT SITE 399..400
FT /note="Cleavage; by viral serine protease"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1062 AA; 118730 MW; 842C778B71EFDBA5 CRC64;
MNRFTAYAAL FFMFSLCSTA KEAGFLHPAF NFRGTSTMSA SSGDYSAAPT PLYKSWALPS
SLNLTTQPPP PLTDRSYYEL VQALTSKMRL DCQTVGDMTW RHLSEMLFAS WNSVKEVSLK
AASVTLWAII NIWFGLYWTL ARLITLFLWT FSIEALCLIL LGCITSLIYK GALSLSEHLP
VFLFMSPLKI IWRAAFSKRN YKNERAVEGY KGFSVPQKPP KSAVIELQHE NGSHLGYANC
IRLYSGENAL VTAEHCLEGA FATSLKTGNR IPMSTFFPIF KSARNDISIL VGPPNWEGLL
SVKGAHFITA DKIGKGPASF YTLEKGEWMC HSATIDGAHH QFVSVLCNTG PGYSGTGFWS
SKNLLGVLKG FPLEEECNYN VMSVIPSIPG ITSPNYVFES TAVKGRVFSD EAVKELEREA
SEAVKKLARF KSLTDKNWAD DYDSDEDYGL EREAATNAPA EKTAQTNSAE KTAPSTSAEK
TALTNKPFKW ASGTVRQNKR QLRHPRRRYK RTTNGQNGRT DHHSYGGENQ SLGDRGEDSE
QGVSESPAEA QTKEARKAWR EEQAKQFTSY FNAIYKWGAQ EGGCPPGFRK CGHIPRYYHP
RTRGETQWGQ KLCQVHPELA DKTAGFGWPK AGSEAELQSL NLQAARWLQR AESATIPGAE
ARKRVIEKTV EAYRNCVTNA PLCSLKSKLD WAGFQQDIRE AVQSLELDAG VGIPYIAYGL
PAHRGWVEDH KLLPVLTQLT FDRLQKMSEA SFEDMSAEEL VQEGLCDPIR LFVKGEPHKQ
SKLDEGRYRL IMSVSLVDQL VARVLFQNQN KREISLWRSV PSKPGFGLST DTQTAEFLEC
LQKVSGAPSV EELCANHKEY TRPTDCSGFD WSVAYWMLED DMEVRNRLTF NNTQLTKRLR
AAWLKCIGNS VLCLSDGTLL AQTVPGVQKS GSYNTSSSNS RIRVMAAYHC GADWAMAMGD
DALEAPNSDL EEYKTLGFKV EVGRELEFCS HIFRNPTLAV PVNTNKMLYK LIHGYNPECG
NPEVIQNYLA AVFSVLQELR HDRELVAKLH QWLVPSATTK EH
