RDRP_PEMVW
ID RDRP_PEMVW Reviewed; 1181 AA.
AC P29154;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 78.
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 Pea enation mosaic virus-1 (strain WSG) (PEMV-1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Sobelivirales; Solemoviridae; Enamovirus.
OX NCBI_TaxID=693989;
OH NCBI_TaxID=3827; Cicer arietinum (Chickpea) (Garbanzo).
OH NCBI_TaxID=3859; Lathyrus odoratus (Sweet pea).
OH NCBI_TaxID=3864; Lens culinaris (Lentil) (Cicer lens).
OH NCBI_TaxID=70936; Medicago arabica.
OH NCBI_TaxID=3888; Pisum sativum (Garden pea).
OH NCBI_TaxID=60916; Trifolium incarnatum (Crimson clover).
OH NCBI_TaxID=3906; Vicia faba (Broad bean) (Faba vulgaris).
OH NCBI_TaxID=3908; Vicia sativa (Spring vetch) (Tare).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1875194; DOI=10.1099/0022-1317-72-8-1819;
RA Demler S.A., de Zoeten G.A.;
RT "The nucleotide sequence and luteovirus-like nature of RNA 1 of an aphid
RT non-transmissible strain of pea enation mosaic virus.";
RL J. Gen. Virol. 72:1819-1834(1991).
CC -!- FUNCTION: RNA-dependent RNA polymerase that plays an essential role in
CC virus replication. {ECO:0000250}.
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=P29154-1; Sequence=Displayed;
CC Name=Protein P1;
CC IsoId=Q84710-1; 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 (By similarity).
CC {ECO:0000250, ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform RNA-directed RNA polymerase]: Produced by -1
CC ribosomal frameshifting between codons 589 and 590.
CC -!- SIMILARITY: Belongs to the luteoviruses RNA polymerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA72297.1; Type=Miscellaneous discrepancy; Note=Ribosomal frameshifting not described. Translation N-terminally extended.; Evidence={ECO:0000305};
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DR EMBL; L04573; AAA72297.1; ALT_SEQ; Genomic_RNA.
DR PIR; JQ1384; RRXBPM.
DR PRIDE; P29154; -.
DR Proteomes; UP000000519; 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 InterPro; IPR043502; DNA/RNA_pol_sf.
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; 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 suppression of termination;
KW RNA-directed RNA polymerase; Serine protease; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Viral RNA replication.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..1181
FT /note="Protein P1-P2"
FT /id="PRO_0000222401"
FT CHAIN 316..515
FT /note="Serine protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390909"
FT CHAIN 516..1181
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390910"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 318..515
FT /note="Peptidase S39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT DOMAIN 979..1094
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 572..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 366
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT ACT_SITE 396
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT ACT_SITE 465
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT VARIANT 648
FT /note="G -> S"
FT VARIANT 660
FT /note="Q -> P"
FT VARIANT 666
FT /note="S -> I"
FT VARIANT 675
FT /note="T -> I"
FT VARIANT 677
FT /note="R -> G"
FT VARIANT 686
FT /note="R -> H"
FT VARIANT 918
FT /note="V -> L"
FT VARIANT 941
FT /note="I -> K"
FT VARIANT 992
FT /note="S -> F"
SQ SEQUENCE 1181 AA; 131890 MW; 0095D0EF73B30DE2 CRC64;
MASFLKPVNS QGLWLSLLLA ITYLFLLPSA GQSLDPSGIG LAAGCSQSQG GISSFAALPR
PCNDSVCTLP DLGWSCQRTA QDTANQQQSP FNHTGHFLTT SGWTWPNWTC SPSQCQLLIH
LPTWQIVKQD FLLLLKEWDL LTMCQRCSDL LTKTPGFILR FAGETLILVA NLIEFVLVSW
SLWLCSVLVY VAQAVPGKFL LYMAAFCTTF WAWPRETASS LIRIVTTPLT LIGFLNKTGI
GLISHCLALT WNMFMTWSLL PWVTLMKMMK ILITSSRVLT RSGRPKRTSS KSLKHKLKIS
RAIQKKQGKK TPVEERTIPG VQIKKLREDP PKGVILRCTD QFGDHVGYAS AVKLEKGQTG
IVLPIHVWTD TVYINGPNGK LKMADFTALY EVTNHDSLIM TSAMAGWGSI LGVRPRPLTT
IDAVKLKNYS LFTERDGKWY VQAAKCIAPA EGMFRVVSDT RPGDSGLPLF DMKMNVVAVH
RGTWPSERFP ENRAFAILPV PDLTSSSSPK FTGCETYSEA ETAYEMADNF SDGEEILIRT
KGQSYRTFIG SNKVALLSIR KLEEELSRGP IGLWADDTED DESAPRRSGK RIIPVDSGET
KSSEDPLPKG RGVSSTPSRS KSRKGKACPS FRNDAGTEES RQPQEEKGQS CQEDSLNSTQ
EIQGQSTHFV PSSGTGRKSC ESSPHRPTTK ITSIFEDFYR WKEPREEAPG FNSVGSCPFT
VYKCPPKGLS SWGERVARTS AFLQACTEKY SWPETGAEAE LSSLRYQAAR RQSAQTTAVI
PPKDVREDLI KRTTEAYRST ALPAPMWAHN FDESHMRFEF WECVRKLKGQ AGSGVPYAAF
SGRKTNDKWV FDHESTEDLW ETVRDRLFRL LNQDFIDPVQ AVKDGLVDPI RLFVKLEPHK
MEKIRNKRYR LIASVSIVDQ LVARMLFRDQ NEEELLQHMA IPSKPGLGFS QDHQVLAFTE
SVAALAGTSA QDLVDNWSRY LTPTDCSGFD WSVPMWLLED DLAVRNELTL GLPHGLRKMR
ETWLKCLGQS VFCLSNGLLL AQTSPGIQKS GSFNTSSTNS RMRYMLALYA GASWAVTMGD
DALESVGSDL SQYARLGIKC ERAEEFDFCS HLFRAPDVVI PKNLEKMVYG LLSGTSPESP
LLADRFSWLS ALQSILEEMR HMPQDFVNML IEHLGVGDLV E
