P1_PLRVW
ID P1_PLRVW Reviewed; 639 AA.
AC P11622;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Protein P1;
DE AltName: Full=69.7 kDa protein;
DE AltName: Full=Genome-linked protein precursor;
DE AltName: Full=Protein ORF1;
DE Contains:
DE RecName: Full=Serine protease;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=VPg/P1-C25;
DE Flags: Precursor;
GN ORFNames=ORF1;
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).
RN [2]
RP FUNCTION.
RX PubMed=18573562; DOI=10.1016/j.virusres.2008.05.001;
RA Nickel H., Kawchuk L., Twyman R.M., Zimmermann S., Junghans H., Winter S.,
RA Fischer R., Prufer D.;
RT "Plantibody-mediated inhibition of the Potato leafroll virus P1 protein
RT reduces virus accumulation.";
RL Virus Res. 136:140-145(2008).
CC -!- FUNCTION: Precursor from which the VPg molecule is probably released at
CC the onset of the RNA synthesis. Essential for virus replication.
CC {ECO:0000269|PubMed:18573562}.
CC -!- SUBCELLULAR LOCATION: [Protein P1]: Membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Protein P1;
CC IsoId=P11622-1; Sequence=Displayed;
CC Name=RNA-directed RNA polymerase;
CC IsoId=P11623-1; Sequence=External;
CC -!- DOMAIN: The C-terminus part of VPg/P1-C25 displays RNA-binding
CC properties. {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC protease probably cleaves itself and releases the VPg protein. The VPg
CC protein is probably further cleaved in its C-terminus (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Protein P1]: Produced by conventional
CC translation.
CC -!- SIMILARITY: Belongs to the peptidase S39B family. {ECO:0000305}.
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DR EMBL; Y07496; CAA68795.1; -; Genomic_RNA.
DR PIR; S03547; S03547.
DR MEROPS; S39.002; -.
DR Proteomes; UP000000474; Genome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; 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:0016032; P:viral process; IEA:InterPro.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR018019; Luteovirus_Orf2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000382; Peptidase_S39B_luteovirus.
DR Pfam; PF02122; Peptidase_S39; 1.
DR PRINTS; PR00913; LVIRUSORF2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS51868; PEPTIDASE_S39; 1.
PE 3: Inferred from homology;
KW Hydrolase; Membrane; Protease; Ribosomal frameshifting; RNA-binding;
KW Serine protease; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..639
FT /note="Protein P1"
FT /id="PRO_0000222397"
FT CHAIN 205..399
FT /note="Serine protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390901"
FT CHAIN 400..639
FT /note="VPg/P1-C25"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390902"
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 REGION 456..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..631
FT /note="Polar 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 639 AA; 69677 MW; 92E1473FE3FEF148 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
TAPTNKPLNG RAAPPAKTNG NSDIPDAAIS APPMDKMVEQ IITAMVGRIN LSEIEEKIVS
RVSQKALQKP KQNKRGRRGG KNKQNNLPPT STQSISGAPK KKAVPQASGS AGISPATTTP
APKEKPSGGK NSAKFIPSWR IKQQDSAGQK PDLKLNSKA
