POL1_GFLV
ID POL1_GFLV Reviewed; 2284 AA.
AC P29149;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=RNA1 polyprotein;
DE AltName: Full=P1;
DE Contains:
DE RecName: Full=P1A protein;
DE Short=1A;
DE AltName: Full=Protease cofactor;
DE Contains:
DE RecName: Full=Putative ATP-dependent helicase;
DE EC=3.6.4.-;
DE AltName: Full=1B;
DE AltName: Full=Membrane-binding protein;
DE AltName: Full=NTP-binding protein;
DE Short=NTB;
DE Contains:
DE RecName: Full=Viral genome-linked protein;
DE AltName: Full=1C-VPg;
DE Contains:
DE RecName: Full=Picornain 3C-like protease;
DE Short=3C-like protease;
DE EC=3.4.22.-;
DE AltName: Full=1D-PRO;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE AltName: Full=1E-POL;
OS Grapevine fanleaf virus (GFLV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Comovirinae; Nepovirus.
OX NCBI_TaxID=12274;
OH NCBI_TaxID=103352; Vitis rupestris.
OH NCBI_TaxID=29760; Vitis vinifera (Grape).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=F13;
RX PubMed=1655953; DOI=10.1099/0022-1317-72-10-2357;
RA Ritzenthaler C., Viry M., Pinck M., Margis R., Fuchs M., Pinck L.;
RT "Complete nucleotide sequence and genetic organization of grapevine fanleaf
RT nepovirus RNA1.";
RL J. Gen. Virol. 72:2357-2365(1991).
RN [2]
RP PROTEIN SEQUENCE OF 1218-1241.
RX PubMed=2060618; DOI=10.1016/0014-5793(91)80775-x;
RA Pinck M., Reinbolt J., Loudes A.-M., Le Ret M., Pinck L.;
RT "Primary structure and location of the genome-linked protein (VPg) of
RT grapevine fanleaf nepovirus.";
RL FEBS Lett. 284:117-119(1991).
CC -!- FUNCTION: Picornain 3C-like protease is a thiol protease that cleaves
CC the P1 and P2 polyproteins. {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: [Viral genome-linked protein]: Host endoplasmic
CC reticulum lumen {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Putative ATP-dependent helicase]: Host
CC endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages by picornain 3C-like protease in vivo
CC yield mature proteins. Picornain 3C-like protease is autocatalytically
CC processed (By similarity). {ECO:0000250}.
CC -!- PTM: VPg is uridylylated by the polymerase and is covalently linked to
CC the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-
CC peptide primer for the polymerase (By similarity). {ECO:0000250}.
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DR EMBL; D00915; BAA00761.1; -; Genomic_RNA.
DR PIR; JQ1373; GNVVGV.
DR RefSeq; NP_619689.1; NC_003615.1.
DR SMR; P29149; -.
DR MEROPS; C03.004; -.
DR PRIDE; P29149; -.
DR GeneID; 1494095; -.
DR KEGG; vg:1494095; -.
DR Proteomes; UP000009160; Genome.
DR GO; GO:0044166; C:host cell endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; 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; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Covalent protein-RNA linkage; Direct protein sequencing;
KW Helicase; Host endoplasmic reticulum; Host membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
KW RNA-binding; RNA-directed RNA polymerase; Thiol protease; Transferase;
KW Transmembrane; Transmembrane helix; Viral RNA replication.
FT CHAIN 1..568
FT /note="P1A protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037045"
FT CHAIN 569..1217
FT /note="Putative ATP-dependent helicase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037046"
FT CHAIN 1218..1241
FT /note="Viral genome-linked protein"
FT /id="PRO_0000037047"
FT CHAIN 1242..1461
FT /note="Picornain 3C-like protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037048"
FT CHAIN 1462..2284
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037049"
FT TOPO_DOM 569..1171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1172..1192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1193..1217
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 751..919
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1243..1458
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1728..1852
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ACT_SITE 1284
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1328
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1420
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 781..788
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT MOD_RES 1218
FT /note="O-(5'-phospho-RNA)-serine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 2284 AA; 252932 MW; 75C6DEE1F45636E9 CRC64;
MWQVPEGSQC CCTGKSFSNA EAKELRYVCS CWMSTRLVKA EAPPQQSRKS GIAPTPLKSK
GTIQVSLPKA TGVKPSIHKS KGASVAPAPL LKQRCEVVVQ YGPPADIELV YPPLVREEEK
SSNIVVLPPT QKVEVRVPVC CAPKWMVAIP KPPVKLAPKA SKLRFPKGAV AYNGVNFIDT
KGKVVLSEGA KRILRGIRVA AKQRLRAARR SAACKKVRAK RALAEFEAIV QSERLDQLKT
GFQVVLPAPK MSCSLKEAAP STTSVVVVKK RKLPRLPKIL PEQDFSCLEG FDWGEKSHPV
EVDIEDDWIL VEKPVLKRQA VQTAQGRATE ALTRFAATSG FSLGAHQKVE DFASSGEAEY
LMAGEFADLC LLSLVYNDAP TLSATIEELR DSKDFLEAIE LLKLELAEIP TDSTTCAPFK
QWASAAKQMA KGVGTMVGDF TRAAGAAVVI SFDMAVEFLQ DKALKFCKRI FDVTMAPYLQ
HLASAHSILK KIWEKLSEWM ESLKSKASLA LEVMRQHAIF ALGAMVIGGV VVLVEKVLIA
AKIIPNCGII LGAFLTLFFA SLGLTALECT AEEIFRMHAC CKSAIYSMYS VAEPTMADEG
ESHTMGATQG LDNAIQALTR VGQSMISFKL GSFSYYAKIA QGFDQLARGK RAIGELTSWL
IDLVGSIYSQ VSGQESTFFD ELSTIVCLDV RAWLLKSKRV RLQVETMAIG DRITLDTIAK
LLEEGHKILV TAAGVPRKTS ADFTMCIKEE VSKLEEVHAR TACAGINEGM RAFPFWVYIF
GASQSGKTTI ANSIIIPALL EEMNLPKSSV YSRPKTGGFW SGYARQACVK VDDFYAIEQT
PSLASSMIDV VNSEPYPLDM AYIHEKGMSM DSPLVVTTAN TAVPPTNSQV VDLPSFYNRR
AAVLEVRRKD GSFFTPRAYD SCIEVRFMHN KCPYVDSAGV PQGPAVNTPM DEGWITPSEA
VAVLKNLLGE HILAEEAKLL EYRERIGNDH PIYNAAKEFI GNMHYPGQWL TAEQKSTYGI
KDDGFSFLAV DGKIYKYNVL GKLNPCESEP PHPNVIPWLE KKTLEIVHWD VHKHIATGPR
NALVACFLQG LVQGQSKVES VERMGKDSSP EQQNFFKRLS LSERIYLRLC QIRIDNIQKE
ELAGSGRGPM AILRECLMKS KQVVVENYSL LLTLVAILLL ISAAYTLLST VVALAGCSSF
AGGMVAVTAV NNASIPCSEP RLEERYSPRN RFVSRISKIR GEGPSKGQGE HEELVTELYY
YCDGVKKLIS TCWFKGRSLL MTRHQALAVP IGNEIEVIYA DGTTKKLVWP GRQEDGNCKG
FVEFPENELV VFEHPHLLTL PIKYEKYFVD DADRQISPNV AVKCCVARLE DGIPQFHFWS
KYATARSEVH TLKDEGGGNV YQNKIRRYIV YAHEAKKYDC GALAVAVIQG IPKVIAMLVS
GNRGVTYSSV IPNYSSSFIR GEVPYVPEDG LVSRGYRKVG YLHASDAPHV PSKTSFMKVP
DELCFPYPDP KQPAILSAED ERLKGTIHEG YTPLRDGMKK FAEPMYLLEE KLLDEVAGDM
VQTWYDPGEF LEDISLDQAI NGDMDEEYFD PLVMDTSEGY PDVLDRKPGE KGKARFFVGE
PGNRAFVAGC NPEKAYYQLE EDSKTKIPSL VSIETPKDER LKRSKIDTPG TRLFSVLPLA
YNLLLRVKFL SFSRLLMKKR GHLPCQVGIN PYSREWTDLY HRLGELSDVG YNCDYKAFDG
LITEQILSTI ADMINAGYRD PVGNRQRKNL LLAICGRLSI CGNQVYATEA GIPSGCALTV
VLNSIFKELL MRYCFKKIVP PVYKECFDRC VVLITYGDDN VFTVAQSVMQ YFTGDALKMQ
MAKLGVTITD GKDKSLSTIP ARPLLELEFL KRGFVRSSGG MINAPLEKLS IMSSLVYIRS
DGSDMLQKLL DNVNTALVEL YLHGDRTYFE SVRAFYFEKL PPGAYKELTT WFQAESFHEC
QKSGESGYKP QGLIEISHGA AFASFTQQAG TELEKHDICP GLSIAGTKYI ATENEIVLSL
SSVLPGDRNV FKLDLPCGDG IGRLPSKCSI LNLRKPGLVM RLCKRAQDEK KTLVIRDERP
YIGAWAVACI CGESFGFGQQ SVLALYANLL GPNQRNGLAS YFSDFESPIH IKKVHAKTNS
YEGGEALKEI FTFCETIFYE ATEMDTRKVM LQNQPDVYPS ISLVGGVCFP NEGGEPGAMY
SETDVTMARE VQGVYVSEAC VKCCRRCVGV ATRVVTDTQL FGNNLLKTHL KALRKIQNHT
CLRK
