ID   RDRP_PMVK               Reviewed;         992 AA.
AC   P89034; P90334;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   29-SEP-2021, entry version 77.
DE   RecName: Full=RNA-directed RNA polymerase;
DE            EC=2.7.7.48;
DE   AltName: Full=Protein p112;
DE   Contains:
DE     RecName: Full=Protein p48;
GN   ORFNames=ORF1;
OS   Panicum mosaic virus (strain United States/Kansas 109S) (PMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Tolucaviricetes;
OC   Tolivirales; Tombusviridae; Procedovirinae; Panicovirus.
OX   NCBI_TaxID=652599;
OH   NCBI_TaxID=58090; Muhlenbergia.
OH   NCBI_TaxID=38727; Panicum virgatum (Blackwell switchgrass).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=9454725; DOI=10.1006/viro.1997.8939;
RA   Turina M., Maruoka M., Monis J., Jackson A.O., Scholthof K.B.;
RT   "Nucleotide sequence and infectivity of a full-length cDNA clone of panicum
RT   mosaic virus.";
RL   Virology 241:141-155(1998).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16524473; DOI=10.1186/1743-422x-3-12;
RA   Batten J.S., Turina M., Scholthof K.B.;
RT   "Panicovirus accumulation is governed by two membrane-associated proteins
RT   with a newly identified conserved motif that contributes to
RT   pathogenicity.";
RL   Virol. J. 3:12-12(2006).
CC   -!- FUNCTION: RNA-dependent RNA polymerase that plays an essential role in
CC       the virus replication. {ECO:0000305|PubMed:16524473}.
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:0000269|PubMed:16524473}.
CC   -!- MISCELLANEOUS: Readthrough of the terminator UAG occurs at position
CC       426.
CC   -!- SIMILARITY: Belongs to the tombusviridae RNA polymerase family.
CC       {ECO:0000305}.
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DR   EMBL; U55002; AAC97551.1; -; Genomic_RNA.
DR   EMBL; U55002; AAC97552.1; -; Genomic_RNA.
DR   RefSeq; NP_068342.1; NC_002598.1.
DR   RefSeq; NP_068343.1; NC_002598.1.
DR   GeneID; 912246; -.
DR   GeneID; 912248; -.
DR   KEGG; vg:912246; -.
DR   KEGG; vg:912248; -.
DR   Proteomes; UP000001665; Genome.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C: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:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   Gene3D; 3.30.70.270; -; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR002166; RNA_pol_HCV.
DR   Pfam; PF00998; RdRP_3; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   Host membrane; Membrane; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; RNA suppression of termination;
KW   RNA-directed RNA polymerase; Transferase; Viral RNA replication.
FT   CHAIN           1..992
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000399486"
FT   CHAIN           1..425
FT                   /note="Protein p48"
FT                   /id="PRO_0000399487"
FT   DOMAIN          656..772
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          963..984
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        966..982
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   992 AA;  112683 MW;  C54AB9AFA91301A2 CRC64;
     MESLIQHILS ATSSLSMPSV DSDKLQLLLT RFPQATLSWL SGIDGLSVHQ FKVVATHVIK
     ESYSHLSPSV AVLLAKPSDY YKLVVHGLTQ KQWNEFDDKV TDAPRTAISW LYNQILVVGQ
     PWMKSLNEGL KEYLPGWLHT CLRMLANLWF GAERVLHGIS HAVSDITTYQ PWMSCRRCVA
     HSPKESLLGE ATTTSNPRES SWFSWLLCGG VVAATVYGFY KWVTITETID RQDLAKQRPT
     HMQKCYEEVK ARLEEESKGF IHDRMEDELT KIVLEPAEID NDGKVLKSEV AQYLVKNHGR
     FVRSLVTMAK NEFAGVPKPT EANQLAVWRY LYRVCDKKGV NPSDTQKSIS AALPFVFLPS
     AYDQDQAITM NCDDTKKVLE RYADTFRHTT PLQKLVTNPL VGANWTAWAR SIFISDPETG
     LRFAKXGCIE KWQGVQCKRT RVRHPRLRCH FKDRDPKVRS IYRIAGLGDQ YEFGLHNNSA
     ANLERGLAER VYMVKNYKTD FVASLDPAFC PAPEPVRGIF KRLDKYKKEI VRRVGRKSPI
     TDEMFLSYYD GPQLTTYSKA VISLSERPVA VQDSYLKTFI KAEKLNLTLK TDPCPRVIQP
     RHPRYNVELG KYLKHIEHPI YKAIDRIWGG KTIFKGMNVE AMGAEIHKKM CKYSNPCAIG
     FDASRFDQHV SVEALRFEHS IYKSIHGYPE LLSLLLKWQI HNQGTAHTND GFFKYLVDGK
     RMSGDMNTSL GNCILASLIV KDLVDSLGVD AQLVNNGDDN VLICSVDDEE VVVKALYDHW
     MKYGFEVVAE QPVYITEQIE FCQMKPVFDG TQYVLVRNPT VTMSKDACSI TPFYTANSAR
     KWCRAVGEAG LSLTGGMPIK QAYYQCMIRN GINKGNIHKS KEFRYGLSYV LHHGKSDRKA
     RPISAATRYS FYLAFGYTPD EQTALEGYYD SLELEWTESR LGIPARTPEC LLLRLLPKIP
     LQPKSPTKPV QRTASKPDLP DSQWQQALAA PL