ID   RDRP_PMV                Reviewed;        1547 AA.
AC   P20951;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=RNA replication protein;
DE   AltName: Full=176 kDa protein;
DE   AltName: Full=ORF1 protein;
DE   Includes:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48;
DE   Includes:
DE     RecName: Full=Helicase;
DE              EC=3.6.4.13;
OS   Papaya mosaic potexvirus (PMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Tymovirales; Alphaflexiviridae; Potexvirus.
OX   NCBI_TaxID=12181;
OH   NCBI_TaxID=3649; Carica papaya (Papaya).
OH   NCBI_TaxID=108055; Ullucus tuberosus (Olluco).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2778435; DOI=10.1099/0022-1317-70-9-2325;
RA   Sit T.L., Abouhaidar M.G., Holy S.;
RT   "Nucleotide sequence of papaya mosaic virus RNA.";
RL   J. Gen. Virol. 70:2325-2331(1989).
CC   -!- FUNCTION: RNA replication. The central part of this protein possibly
CC       functions as an ATP-binding helicase (Probable). {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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SIMILARITY: Belongs to the potexvirus/carlavirus RNA replication
CC       protein family. {ECO:0000305}.
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DR   EMBL; D13957; BAA03050.1; -; Genomic_RNA.
DR   PIR; JQ0096; JQ0096.
DR   RefSeq; NP_044330.1; NC_001748.1.
DR   GeneID; 1494026; -.
DR   KEGG; vg:1494026; -.
DR   Proteomes; UP000000477; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   Gene3D; 2.60.120.590; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR   InterPro; IPR037151; AlkB-like_sf.
DR   InterPro; IPR002588; Alphavirus-like_MT_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR   Pfam; PF00978; RdRP_2; 1.
DR   Pfam; PF01443; Viral_helicase1; 1.
DR   Pfam; PF01660; Vmethyltransf; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   RNA-directed RNA polymerase; Transferase; Viral RNA replication.
FT   CHAIN           1..1547
FT                   /note="RNA replication protein"
FT                   /id="PRO_0000222552"
FT   DOMAIN          59..227
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          599..690
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   DOMAIN          793..948
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          949..1082
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          1324..1431
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          477..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..522
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         822..829
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1547 AA;  176321 MW;  6CA4282C6A082622 CRC64;
     MANLRSVFEQ LNDVSLRAVI QEEAYRDIKL TIKETKTYNP YAHPVAVADS LEKLGIETNP
     FAVKAHTHAA AKTIELDMYK IVSFYLPKEN PTTFMFMKRS KLQYFRRGPQ QKDVFLNAHI
     EPKDVARYDV DTLFDKNVTP QITTNTAFMG DTLHFLPLTA IERIFKSSPK LQTLYATMVL
     PPEALHRLHS LHPGIYELEF HQEHFIYKPG GHAGAAYIHK YEQLEWIKVG RFKWADEKGL
     THMVTSQILE TKGANHLFIF QRGRFLTPEL RCFSTETKYV TMPPIFLPKQ FNARLPIKKT
     TAQQLFLYVK SVKNVTERDI WAKMRQLLKT SELQDYNPRE VTLLVNYFLL IARLRSETCF
     DNVLSGGMFK KLFKPFIAWW EIQKHKIFGN EEFEQLMEAL EWVDVTLTYP TKTFDNRGWV
     VKLEARRGYE WFADEMHKPK GPELNLEEKK TDPDAASYEK YLKALSLLQK EPEVMEAKEA
     EATDEPQRPE VKEEQAEAST SGRAEEIQED PATKKGKEEP NPNRDLLCPC GLHLKIKNAE
     FPELPVLDHP DHLTGRKAWF FSKDGKPYSY TGGSHASRGW PNWLEKILAA IEIKEPLPEF
     NQCLVQQFKL QAAIPFHRDD EPCYPKGHQV LTINHSGECL TQIACQKGKA SITMGFGDYY
     LSPVGFQESH KHAVSNTTGG RVSLTFRCTV QQNKFNDDGS MEALDNLPWK AWIPKLQNLG
     FQGRQLQYDP NGALISPIEE IRSMPKCKPE GVPEVVYKTL DGLARAPTPY SPNPIRARAY
     TSDVKNCRIG ALLRQQGKEW GCRFDALVEA GKRELAISVI HGAGGSGKSQ ALQTLIKDNP
     ELDITVVLPT NELRLDWLRK LPKAPQEKFK TFEKALLAPP TPIVIFDDYG KLPAGYVEAF
     CLYFSTVQLI ILTGDCKQSV HHESNENATT SSIEPLVKEA SELCRYYINA THRNKKDLAN
     KLGVYSEKTG LTEVTHGTTP IPGLHMLVPS LYKKQAFSEM GHKVSTYAGC QGITAPKIQI
     LLTEETSLCS REVLYTALSR AVHSIHFVNA SPNNQAFWKK LECTPYLKAF LSTLREEVAQ
     PIEEKKAEPT PVEPPRTHIA KEDAMVEYEN VIEKMPEKHE REIFSEKHGH SNCVQTEDPF
     IQMFSHQQAK DDTLLWATIE ARLVISNPKA NWQEYLEKRP VGEVLFESYK RAMHLPKMPI
     PFEEDLWNSS MHEVQKTYLS KPENMIKNGM ARQSPDYDPN VISLFLKSQW VKKMEKLGAI
     KIKPGQTIAS FHQATVMLFG TMARYMRRMR EVFQPAHIRI NCEMTPEDLS SWAAGEGGHW
     KFKGPSLAND FTAFDQSQDG AMLQFEILKA RHHSIPEDIL DAYLTIKTNS KIFLGTLAIM
     RLTGEGPTFD ANTECNIAFT HTKFNIPEGT AQLYAGDDSA IDGLPALRPS FKMIEQKLTL
     RSKPQVALQQ KGDWAEFCGF RITPKGLIKD PKKLHASWML EKKKGNVKNV LRSYELDLAL
     AYQHKDSLHE LLSEEELKYH YETVRSIVKS GGGGVLNTYI SKDESLY