RDRP_PNLV
ID RDRP_PNLV Reviewed; 1100 AA.
AC Q5NDM9;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Protein P2-P3;
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=ORF2/ORF3;
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 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 -!- FUNCTION: RNA-dependent RNA polymerase replicates the viral genome.
CC {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: Host membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Protein P2-P3;
CC IsoId=Q5NDM9-1; Sequence=Displayed;
CC Name=Genome-linked protein precursor;
CC IsoId=Q5NDN0-1; Sequence=External;
CC -!- MISCELLANEOUS: [Isoform Protein P2-P3]: Produced by -1 ribosomal
CC frameshifting between codons 541 and 542.
CC -!- SIMILARITY: Belongs to the ssRNA positive-strand viruses RNA-directed
CC RNA polymerase family. {ECO:0000305}.
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DR EMBL; AJ867490; CAI34771.1; ALT_SEQ; Genomic_RNA.
DR RefSeq; YP_002308462.1; NC_011543.1.
DR PRIDE; Q5NDM9; -.
DR GeneID; 7040108; -.
DR KEGG; vg:7040108; -.
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: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 Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
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; 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 Host membrane; Hydrolase; Membrane; 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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1100
FT /note="Protein P2-P3"
FT /id="PRO_0000402480"
FT CHAIN 222..416
FT /note="Serine protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000402481"
FT CHAIN 417..1100
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000402482"
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 DOMAIN 897..1012
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 463..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..601
FT /note="Basic and acidic 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 1100 AA; 122814 MW; 9376D2EACDD5DA54 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
GKRSSGFGHG KNRKGTNHPM RRGYNFRNCK KGGGQDESES HREISGRDPG RESNDKSPQG
EAEEFERYFS SFYSWKLHNS GEANSGFRPC GKIPKFYRPR KRRVSEWGQN LARKHSSLGE
ITQGFGWPEA GAEAELRSLR LQAQRWLERS KSSVIPSAIE REIVISRLVE SYKICRSEAP
LCSSGSDLSW KGFLEDFREA VSSLELDAGI GVPYIGYGYP THRGWVENPR LLPVLSRLVY
ARLQRLATLS VDGKTPEELV RDGLVDPVRV FVKGEPHKQS KLDEGRYRLI MSVSLIDQLV
ARVLFQKQNK LELLLWRSIP SKPGFGLSTV EQVEEFIDHL ARVVDVKSDD LLENWRELMV
PTDCSGFDWS VSDWMLKDEM EVRNRLTINC NDLTRRLRNS WLYCLSNSDL ALSDGSLLAQ
EVPGVQKSGS YNTSSTNSRI RVMAAYFAGA SWAVAIGDDA LESIDTTLAV YKSLGFKVEV
SEDLEFCSHI FKTRSLAIPV NTSKMLYRLI YGYEPECGNL DVLRNYLCAL ASVLHELRHD
QDLVQNLSKW LIPDGSQKIS
