ID   RDRP_SCVLB              Reviewed;        1512 AA.
AC   P23172; Q87027;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   29-SEP-2021, entry version 60.
DE   RecName: Full=Probable RNA-directed RNA polymerase;
DE            EC=2.7.7.48;
DE   AltName: Full=Gag-Pol protein;
GN   Name=gag-pol;
OS   Saccharomyces cerevisiae virus L-BC (ScV-L-BC) (ScVLa).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Chrymotiviricetes;
OC   Ghabrivirales; Totiviridae; Totivirus.
OX   NCBI_TaxID=42478;
OH   NCBI_TaxID=4932; Saccharomyces cerevisiae (Baker's yeast).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 622-863.
RC   STRAIN=LO14;
RX   PubMed=2014162; DOI=10.1093/nar/19.2.217;
RA   Bruenn J.A.;
RT   "Relationships among the positive strand and double-strand RNA viruses as
RT   viewed through their RNA-dependent RNA polymerases.";
RL   Nucleic Acids Res. 19:217-226(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8607277; DOI=10.1006/viro.1996.0083;
RA   Park C.M., Lopinski J.D., Masuda J., Tzeng T.H., Bruenn J.A.;
RT   "A second double-stranded RNA virus from yeast.";
RL   Virology 216:451-454(1996).
CC   -!- FUNCTION: RNA-dependent RNA polymerase which replicates the viral
CC       genome. Catalyzes the transcription of fully conservative plus-strand
CC       genomic RNAs that are extruded from the virion into the cytoplasm where
CC       they function as mRNAs for translation of viral proteins and also as
CC       substrates for encapsidation to form new virions. Once encapsidated,
CC       the positive strand is converted to dsRNA by the RNA-directed RNA
CC       polymerase (By similarity). {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;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=RNA-directed RNA polymerase; Synonyms=Pol protein;
CC         IsoId=P23172-1; Sequence=Displayed;
CC       Name=Major capsid protein; Synonyms=Gag protein;
CC         IsoId=Q87026-1; Sequence=External;
CC   -!- MISCELLANEOUS: One molecule or two of Gag capsid protein is replaced in
CC       the virion by Gag-Pol because the fusion protein is essential for RNA
CC       encapsidation and replication. {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform RNA-directed RNA polymerase]: Produced by -1
CC       ribosomal frameshifting.
CC   -!- SIMILARITY: Belongs to the totiviridae RNA-directed RNA polymerase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB02146.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X54405; CAA38271.1; -; mRNA.
DR   EMBL; U01060; AAB02146.1; ALT_SEQ; Genomic_RNA.
DR   PIR; S72354; S72354.
DR   RefSeq; NP_042581.1; NC_001641.1.
DR   PRIDE; P23172; -.
DR   GeneID; 1403712; -.
DR   KEGG; vg:1403712; -.
DR   Proteomes; UP000207604; Genome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.90.1840.10; -; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR015302; Major_coat_LA-virus.
DR   InterPro; IPR036332; Major_coat_LA-virus_sf.
DR   InterPro; IPR001795; RNA-dir_pol_luteovirus.
DR   Pfam; PF09220; LA-virus_coat; 1.
DR   Pfam; PF02123; RdRP_4; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   SUPFAM; SSF82856; SSF82856; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   Ribosomal frameshifting; RNA-binding; RNA-directed RNA polymerase;
KW   Transferase; Viral RNA replication.
FT   CHAIN           1..1512
FT                   /note="Probable RNA-directed RNA polymerase"
FT                   /id="PRO_0000222992"
SQ   SEQUENCE   1512 AA;  171449 MW;  E1CFE4289C72D4C2 CRC64;
     MSSLLNSLLP EYFKPKTNLN INSSRVQYGF NARIDMQYED DSGTRKGSRP NAFMSNTVAF
     IGNYEGIIVD DIPILDGLRA DIFDTHGDLD MGLVEDALSK STMIRRNVPT YTAYASELLY
     KRNLTSLFYN MLRLYYIKKW GSIKYEKDAI FYDNGHACLL NRQLFPKSRD ASLESSLSLP
     EAEIAMLDPG LEFPEEDVPA ILWHGRVSSR ATCILGQACS EFAPLAPFSI AHYSPQLTRK
     LFVNAPAGIE PSSGRYTHED VKDAITILVS ANQAYTDFEA AYLMLAQTLV SPVPRTAEAS
     AWFINAGMVN MPTLSCANGY YPALTNVNPY HRLDTWKDTL NHWVAYPDML FYHSVAMIES
     CYVELGNVAR VSDSDAINKY TFTELSVQGR PVMNRGIIVD LTLVAMRTGR EISLPYPVSC
     GLTRTDALLQ GTEIHVPVVV KDIDMPQYYN AIDKDVIEGQ ETVIKVKQLP PAMYPIYTYG
     INTTEFYSDH FEDQVQVEMA PIDNGKAVFN DARKFSKFMS IMRMMGNDVT ATDLVTGRKV
     SNWADNSSGR FLYTDVKYEG QTAFLVDMDT VKARDHCWVS IVDPNGTMNL SYKMTNFRAA
     MFSRNKPLYM TGGSVRTIAT GNYRDAAERL RAMDETLRLK PFKITEKLDF SCSSLRDTKF
     VGQQYAILTP SGTTTDIRSG RGTNQSYRRG RTSTGYRIGV EDDEDLDIGT VKYIVPLYLN
     GDNVAQNCLE ATHVLIKACS IANRIVDDGE GHCFTQQGLA QQWIFHRGEM IFVKAVRIGQ
     LNAYYVDYKN VTNYSLKTAA QVGATISNNL RHGFVDNQQD AYTRLVANYS DTRKWIRDNF
     TYNYNMEKEK YRITQYHHTH VRLKDLFPSR KIVKLEGYEA LLAMMLDRFN NIESTHVTFF
     TYLRALPDRE KEVFISLVLN YNGLGREWLK SEGVRAKQAQ GTVKYDMSKL FELNVLENGV
     DEEVDWEKEK RNRSDIKTVN ISYAKVLEHC RELFIMARAE GKRPMRMKWQ EYWRQRAVIM
     PGGSVHSQHP VEQDVIRVLP REIRSKKGVA SVMPYKEQKY FTSRRPEIHA YTSTKYEWGK
     VRALYGCDFS SHTMADFGLL QCEDTFPGFV PTGSYANEDY VRTRIAGTHS LIPFCYDFDD
     FNSQHSKEAM QAVIDAWISV YHDKLTDDQI EAAKWTRNSV DRMVAHQPNT GETYDVKGTL
     FSGWRLTTFF NTALNYCYLA NAGINSLVPT SLHNGDDVFA GIRTIADGIS LIKNAAATGV
     RANTTKMNIG TIAEFLRVDM RAKNSTGSQY LTRGIATFTH SRVESDAPLT LRNLVSAYKT
     RYDEILARGA SIDNMKPLYR KQLFFARKLF NVEKDIVDNL ITMDISCGGL QEKGRVSEMV
     LQEVDIENID SYRKTRMIAK LIDKGVGDYT AFLKTNFSEI ADAITRETRV ESVTKAYNVK
     KKTVVRAFRD LSAAYHERAV RHAWKGMSGL HIVNRIRMGV SNLVMVVSKI NPAKANVLAK
     SGDPTKWLAV LT