RDRP_PLRVW
ID RDRP_PLRVW Reviewed; 1062 AA.
AC P11623;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 94.
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/Netherlands/Wageningen/1989) (PLrV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Sobelivirales; Solemoviridae; Polerovirus.
OX NCBI_TaxID=12048;
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2466700; DOI=10.1016/0014-5793(89)80190-5;
RA van der Wilk F., Huisman M.J., Cornelissen B.J.C., Huttinga H.,
RA Goldbach R.W.;
RT "Nucleotide sequence and organization of potato leafroll virus genomic
RT RNA.";
RL FEBS Lett. 245:51-56(1989).
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=P11623-1; Sequence=Displayed;
CC Name=Protein P1;
CC IsoId=P11622-1; 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 487 and 488.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA68796.1; Type=Miscellaneous discrepancy; Note=Ribosomal frameshifting not described. Translation N-terminally extended.; Evidence={ECO:0000305};
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DR EMBL; Y07496; CAA68796.1; ALT_SEQ; Genomic_RNA.
DR PIR; S03548; RRVQWA.
DR PRIDE; P11623; -.
DR Proteomes; UP000000474; 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; Ribosomal frameshifting;
KW RNA-directed RNA polymerase; Serine protease; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Viral RNA replication.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1062
FT /note="Protein P1-P2"
FT /id="PRO_0000222400"
FT CHAIN 205..399
FT /note="Serine protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390907"
FT CHAIN 400..1062
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390908"
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 456..557
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; 118686 MW; 4F664E565A503CB5 CRC64;
MNRFTAYAAL FFIFSLCSTA KEAGFQHPAF NFRGTSTMSA LSGDYSAAPT PLYKSWALPS
SLNLTTQPPP LLTDRSYYEL VQALISKMRL DCQTVGDMTW RHLSEMLFAS WNSVKEVSLK
AASVTLWAII SIWFGLYWTL ARLITLFLWT FSIEALCLIL LGCITSLIYK GALSLSEHLP
VFLFMSPLKI IWRAAFSKRN YKNEKAVEGY KGFSVPQKPP KSAVIELQHE NGSHLGYANC
IRLYSGENAL VTAEHCLEGA FATSLKTGNR IPMSTFFPIF KSARNDISIL VGPPNWEGLL
SVKGAHFITA DKIGKGPASF YTLEKGEWMC HSATIDGAHH QFVSVLCNTG PGYSGTGFWS
SKNLLGVLKG FPLEEECNYN VMSVIPSIPG ITSPNYVFES TAVKGRVFSD ETVKELEREA
SEAVKKLARF KSLTGKNWAN DYDSDEDYGL EKEAATNAPA EKTAQTNSAE KTAPSTSAEK
TAPTNKPFKW ASGTARQNKR QLRHPRRRYK RTTNGQNGRT DHHSYGGENQ SLGDRGEDSE
QGVSESPAEA QTKQTRKTWR EEQAKQFTSY FDAIYKWGAQ EEGCPPGFRK CGNIPGYYHP
RTKGETKWGQ KLCQVHPELA DKTAGFGWPK AGFEAELQSL NLQAARWLQR AESATIPGAE
ARKRVIEKTV EAYRNCITNA PLCSLKSKLD WAGFQQDIRE AVQSLELDAG VGIPYIAYGL
PTHRGWVEDH KLLPVLTQLT FDRLQKMSEA SFEDMSAEEL VQEGLCDPIR LFVKGEPHKQ
SKLDEGRYRL IMSVSLVDQL VARVLFQNQN KREISLWRSV PSKPGFGLST DTQTAEFLEC
LQKVSGAPSV EELCANHKEH TRPTDCSGFD WSVAYWMLED DMEVRNRLTF NNTQLTERLR
AAWLKCIGNS VLCLSDGTLL AQTVPGVQKS GSYNTSSSNS RIRVMAAYHC GADWAMAMGD
DALEAPNSDL EEYKTLGFKV EVGRELEFCS HIFRNPTLAV PVNTNKMLYK LIHGYNPECG
NPEVIQNYLA AVFSVLQELR HDRELVAKLH QWLVPSATTK EH
