ID   P1_PNLV                 Reviewed;         660 AA.
AC   Q5NDN0;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Genome-linked protein precursor;
DE   Contains:
DE     RecName: Full=Serine protease;
DE              EC=3.4.21.-;
DE   Contains:
DE     RecName: Full=VPg;
DE   Flags: Precursor;
GN   ORFNames=ORF2;
OS   Poinsettia latent virus (isolate Euphorbia pulcherrima/Germany/Siepen/2005)
OS   (PnLV) (Poinsettia cryptic virus).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Sobelivirales; Solemoviridae; Polemovirus.
OX   NCBI_TaxID=686943;
OH   NCBI_TaxID=37495; Euphorbia pulcherrima (Poinsettia) (Poinsettia pulcherrima).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15892965; DOI=10.1016/j.virol.2005.03.020;
RA   Aus dem Siepen M., Pohl J.O., Koo B.J., Wege C., Jeske H.;
RT   "Poinsettia latent virus is not a cryptic virus, but a natural polerovirus-
RT   sobemovirus hybrid.";
RL   Virology 336:240-250(2005).
CC   -!- FUNCTION: Precursor from which the VPg molecule is probably released at
CC       the onset of the RNA synthesis. Essential for virus replication (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Genome-linked protein precursor;
CC         IsoId=Q5NDN0-1; Sequence=Displayed;
CC       Name=Protein P2-P3;
CC         IsoId=Q5NDM9-1; Sequence=External;
CC   -!- MISCELLANEOUS: [Isoform Genome-linked protein precursor]: Produced by
CC       conventional translation.
CC   -!- SIMILARITY: Belongs to the peptidase S39B family. {ECO:0000305}.
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DR   EMBL; AJ867490; CAI34770.1; -; Genomic_RNA.
DR   RefSeq; YP_002308461.1; NC_011543.1.
DR   GeneID; 7040107; -.
DR   KEGG; vg:7040107; -.
DR   Proteomes; UP000001670; Genome.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; 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   Host membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW   Ribosomal frameshifting; Serine protease; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..660
FT                   /note="Genome-linked protein precursor"
FT                   /id="PRO_0000402477"
FT   CHAIN           222..416
FT                   /note="Serine protease"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000402478"
FT   CHAIN           417..660
FT                   /note="VPg"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000402479"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          224..416
FT                   /note="Peptidase S39"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT   REGION          463..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        272
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT   ACT_SITE        304
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT   ACT_SITE        373
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT   SITE            221..222
FT                   /note="Cleavage; by viral serine protease"
FT                   /evidence="ECO:0000255"
FT   SITE            416..417
FT                   /note="Cleavage; by viral serine protease"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   660 AA;  72353 MW;  8A2F19D308D62589 CRC64;
     MALLGIKLMT LVFAAWLSCC HSSSALPSSG LSGPCLNHSC LLRNSLNGAS QWGTILHSPA
     VGSNCPPCPM MSIMGCSPPK PLQSNSYGVL CSTIASKAKQ DLKLCWKEVQ TRSEMYSKRI
     SAALIDSLHQ AVGMLLMIII WIWSSIFLVV YHVLAYMTTY HLSSAVCVGF LIFCTICAFR
     LISWICGDLL AFNVSGLTPI WVNFSESSCP AGLSLRRYKN EKTVEGYKPF IIPQKSPKKS
     VIELSFSNGS HLGYATCVRL WDGSICLMTA KHCLVKEALL KGRVAGHSLP VKNFDLFLTC
     DEIDFSLLRG PKQWEAYLGV KGADLITSNR IGRSPVTFYN LSKDGEWLAN SAQITGRHGK
     LCSVLSNTSP GDSGTPYYSG KNVVGIHKGT SELENYNLMI PIPNIPGLTS PDFKFETTNV
     RGNLYNDEGF RLSVGEDDKA EHWTDRLMKS ITFKTKRWAD WAEEESESDD ERGKVVPPAK
     PSNYGEGCPP EHNQYLSDVG DLLTKVIGPE QNEKCVDILM GIMGVDKNEV APHKEEKAEK
     GNEAVVSATV KTVKEPTTQC DEDIISEIVK RVVDKMNLKA IEKSVVEILA EKAMTKAPRG
     KRKNSKDTSR PSTPGSYIIP AKRTPDSGPV EKSLNSTGRA KEESPSGART LPGNIPAWVR