POL1_RRVC
ID POL1_RRVC Reviewed; 2367 AA.
AC Q6W8W4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
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 Raspberry ringspot virus (strain cherry) (RpRSV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Comovirinae; Nepovirus.
OX NCBI_TaxID=281921;
OH NCBI_TaxID=57918; Fragaria vesca (Woodland strawberry) (Potentilla vesca).
OH NCBI_TaxID=39639; Narcissus pseudonarcissus (Daffodil).
OH NCBI_TaxID=32247; Rubus idaeus (Raspberry).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=14602206; DOI=10.1016/j.virusres.2003.08.001;
RA Ebel R., Schnabel A., Reustle G.M., Krczal G., Wetzel T.;
RT "Complete nucleotide sequence of an isolate of the nepovirus raspberry
RT ringspot virus from grapevine.";
RL Virus Res. 97:141-144(2003).
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}.
CC -!- SIMILARITY: Belongs to the nepoviruses RNA1 polyprotein family.
CC {ECO:0000305}.
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DR EMBL; AY303787; AAQ73822.1; -; Genomic_RNA.
DR RefSeq; NP_944487.1; NC_005266.1.
DR PRIDE; Q6W8W4; -.
DR GeneID; 2943113; -.
DR KEGG; vg:2943113; -.
DR Proteomes; UP000007182; 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 Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR027417; P-loop_NTPase.
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 PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF52540; SSF52540; 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 3: Inferred from homology;
KW ATP-binding; Covalent protein-RNA linkage; Helicase;
KW Host endoplasmic reticulum; Host membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Nucleotidyltransferase; Protease; RNA-binding;
KW RNA-directed RNA polymerase; Thiol protease; Transferase; Transmembrane;
KW Transmembrane helix; Viral RNA replication.
FT CHAIN 1..586
FT /note="P1A protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037050"
FT CHAIN 587..1235
FT /note="Putative ATP-dependent helicase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037051"
FT CHAIN 1236..1259
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037052"
FT CHAIN 1260..1472
FT /note="Picornain 3C-like protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037053"
FT CHAIN 1473..2367
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037054"
FT TOPO_DOM 587..1194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1195..1215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1216..1235
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 776..940
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1258..1468
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1832..1957
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ACT_SITE 1302
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1339
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1432
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 804..811
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
SQ SEQUENCE 2367 AA; 263135 MW; 88F2D98418227119 CRC64;
MGWTCPVQGC MYSRSTWSNR GLKEDGLSST MRCPGAMCGA MLVRSEPVQA PKATVVPQTP
VTAVRPKRTV VSATPLRKQD CVVVVEVGFP ALLSLEYPAL AGRARHTGEF DSALLARKPS
NGGTARAPTG WFKPRVVRTQ PAKKALPSWV SEARRLIKGA LEGSNAFGPR YCREKFPKAR
LVWVLGMLSK SSPPSVAIGR QLKKSFLALQ ARIARALAKK QSARAARRQE ACRKIRLALQ
QARGIAALER QQARQLSGAG LYSVRLCTKR ALSPIVEVPK RHKKKAISLP SPVSVQEFPE
GLVGPNFWET SGLLNCVASP QRREDLVFPV YGIDSCRTDP EYFVVGPKSP SKIMGDTKPR
LPTCPAEALN LLWASNLFED WELDIIGQMV SDGLLTSQAF LDGCTLVSYY GQEQMVDSFH
CLLQDPVPAE VAEALAVDVQ ALDFDAVFGC GISDFLRGTR DAMKGWIMDP VIAKSTTWCN
TIIDKVRALF DQYFAPFHKI IDGMSYVNSL WAKCKEWAQS VLKNGSQLFS VMWETHCVSF
VIIITCACTL LVENVLKELR LISRVGTLTS CVISGALGIL GCGYILAKCE DLAVVSASIR
AFLGVLLCPP TMEAVDLNQS LIPEEIQATS WTGVDRVLGA LNAVGSGLTG FNTDTIIYWG
RFAQSFDGMR RGKDAVCALA ACLFEKLGTV YNRVTGKEAA FFHELSSLVS IDVQGWLNSS
RRVMAESIAF AKSDAVAFAT VERLINDGET IQLTAASAPK SHSMQFGQIL AERLRELRTL
RNDMAHAGSF EGRRCVPFWL YIYGPPGVGK TTTMHEFSQA LLTAFEFPSD SLTSKSATDK
YWSLYRRQAL VQIDDLGAIS ESGMEQEMMN IVSSATYNPT MAVANEKTTL FDSKFIVSTS
NNYSAGTDAK IHDRKAFNRR RRVVIKTRGK AGVAFNPHDS TAAAEFCVVE RDDRAETPIW
VQSGEAPDDK ELYWMDFRTT VAYVIEQARI HHNAEDIEQA QYSMKHSRTR QLYQVCENYI
GEVKMSVANF VPGDMLGAWN LEPKGRFFYS CVDGRVYSYD PEQKAHDEGP VDKALDFEQI
CLEKLSYTLQ ADIQGGPKSA TAGIFLRSMV SGECAVESVD KLNRSASREH LIFFKNLSLA
DRVYLRLVQK RILQLAMVGD PLGLRSYTVM MEGFQNSYNY VKENGGRLLL ILCSCMLLGI
ACYTFFNALA ILIGGTSVAA GAAAMVDIGA CGSTSTYASE YGAKMGRRNM PHRSREIPAV
WSEETGHDEK WQLCGLLETC RSDMPAVHVN LVPGNKFAIT KHQAQAIPDG SSVGLSVAGR
SFRTFQWRAS ALTEYAESEI CTYFDSRIPS LGKQAMKMYS DSDLDALNVK YFSTRTLHFR
LVDDQVEKRH WDADACVIST PKTIVSTING VIYRQEIPTA ITYRRESVKH DCGALVFTEV
RGKPKAVGML VGTLGGTTYV CKFPHIEVDA FACVPDIRGF NLEAGVSTLG YSKLGWLDRR
HQPHNSEKTE FVPIPEKYHM DDVPCKIPAV LSAKDPRLAD IPQCMGYDPY KQGMEKFAHP
MQEIDEQLLA TVCDEIAQEF HDVGVRGRMV SMDEAINGHH KYEIPSFYVE GASTRELNEL
RTSCSAEVWC CDPRSDIEFE YPRIIPGPVE SKWKCESTCC GCTFKSGGTE AIISFVKARS
PCCEEIFFDG LDLTTSEGYP LFLDRPAGAK GKERFFEGSE NQKFLIPDCP LDVQLKKGIE
ETHLGTPQLI IKESAKDELL KEGKVLPSEG MPGTRLFSIC PAWYNIVVRQ HFVYIAESVR
KRRRTLSSQV GIVVGSREWD DLAARLRSKK NDKMYCCDYS KFDGLMTPQI VHAITNIYER
MFSGNDGMSQ FRQNLLMGIC NRISICGSQV YRVEAGMPSG FALTVDFNSI FNEILVRCAY
RSLVPEIERP FFSNNVVLIV YGDDNVLGIH PNIESAFNGN AIKAYMKEEL GIKITDGADK
LSPVICARPL EQCEFLKRTW RKDRQYGLYR APLVETSIYS CLRYVRLQNY DWQAPLLQNV
QGSLYEASLH GPDMHARIYK HFATHFPKWV EEHELYTYEQ CRTRFIAAKN GDFNFHPASA
QMGHVFSQQT EIQELSQSQN PKRCFQLHPK IHICGPGHNE QDCFYVDVRV KGKITKGKGF
HHAPVFSAGS GQLGTVKWAS SFRSSSACPM RDLAVDAFKR GECVYFRDNG ELINAWLAAI
NFGMSINADG LDGLLQVYRN QGPTHLDDLS FYFEGGVVGV PAPAHLMVYG TDTSILNRLC
PKTVLESAPP PGRSSNVSER SQVQTFLHMS PKPCFITLKG SGKVCHGLRC NNSCRGHISC
TDVVRNSAAN QRAAMLDVLR RGCYNIQ
