ID   RDRP_MYRV9              Reviewed;        1354 AA.
AC   Q7TDB6;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   29-SEP-2021, entry version 41.
DE   RecName: Full=RNA-directed RNA polymerase VP1;
DE            EC=2.7.7.48;
OS   Cryphonectria parasitica mycoreovirus 1 (strain 9B21) (CpMYRV-1).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Spinareovirinae; Mycoreovirus.
OX   NCBI_TaxID=230407;
OH   NCBI_TaxID=5116; Cryphonectria parasitica (Chestnut blight fungus) (Endothia parasitica).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=14694120; DOI=10.1128/jvi.78.2.892-898.2004;
RA   Hillman B.I., Supyani S., Kondo H., Suzuki N.;
RT   "A reovirus of the fungus Cryphonectria parasitica that is infectious as
RT   particles and related to the coltivirus genus of animal pathogens.";
RL   J. Virol. 78:892-898(2004).
CC   -!- FUNCTION: RNA-directed RNA polymerase that is involved in transcription
CC       and genome replication. Following infection, it catalyzes the synthesis
CC       of fully conservative plus strands. After core assembly, which consists
CC       in recruitment of one capped plus-strand for each genomic segments and
CC       polymerase complexes, the polymerase switches mode and catalyzes the
CC       synthesis of complementary minus-strands (By similarity).
CC       {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;
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DR   EMBL; AY277888; AAP45577.1; -; Genomic_RNA.
DR   RefSeq; YP_001936004.1; NC_010743.1.
DR   PRIDE; Q7TDB6; -.
DR   GeneID; 6336086; -.
DR   KEGG; vg:6336086; -.
DR   Proteomes; UP000006719; Genome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Hydrolase; Nucleotidyltransferase; Reference proteome;
KW   RNA-directed RNA polymerase; Transferase; Viral RNA replication.
FT   CHAIN           1..1354
FT                   /note="RNA-directed RNA polymerase VP1"
FT                   /id="PRO_0000403423"
SQ   SEQUENCE   1354 AA;  151783 MW;  424FADC9EC936667 CRC64;
     MSLTSRYTHF VPDSTITEIL NDSNTPQILL HYANIVNGST PVHFTSHHDN QVNWTVATLT
     RMSQYMIPDF MKLFPPLEPT LSLQPDCHCS FINLPRPEIK IPIEILSPPK PNYAKYHYDA
     TTSRVFVNSK HEMYMDNFDV SQLIRDVAAI KTDSPSGNIT KGLLKTFHDS IKLRALSPIM
     SMFHSLLSYR CPCCTSLNGM KKLNHLCFQY SSIYAFLCDM VRPYMCVPFF VDRLGVQILP
     GFKVSSQYPL LFFEAIELMH TVGLGNLSDS LSGWCFYTWL DRARIGVFRE MFNRRGSITM
     LKSRVVSTGT IFRFSQREFV IESITEQRST DISPTFEECS FSDSQYIQDN CYKPIYDITT
     TLDDVKCRWL DVALNYFYGA VLYVTGPVSL ALEQSGMGRP GSLNLQFGGT TDVYVEGRWI
     TIDVEPVSPF VSRIKQLADR ELAKTKVNGD SLEHGFFEAQ TTNSAGNTKE TLAGLRSEII
     EQHDSPQEGR LLASMAGIRV IDAMRRFNTT FRDHTEFLNE VRRPTKAGMR YQQQRRPRVI
     QMTGTEAQLG GWLLLNVYEP TYKRLGYTSS GKNIGDIRDM QAVLEASGQN GINSSVDIIG
     MDASTQNTHV TLLGSAAIKA YNPERIGFPK MFFQSTHNGG DANSRVLPTR VTRDGQTIPK
     DDDVKYNLPQ LAIIYSLHGM HGPTILYDGY FAPAVLTSQT VFRSGWYNTS SQHTMLGSLV
     LLSLEEDIRN GYKNPYDGAP ERSLIAKHWH SIRIIGRVLG DDILLKAFGP PTLTPDELRE
     VTAEVCAEFE HRMELLGFLC ERAFSDVMCE FLKQKGFGGA PHMFPDRLVL YTSERGNQAM
     TNPTTMYRVC DALIIEFNSR SRNIFNTCVS RRVLQTVCST FALRMTSSGH LVRRSYASRK
     PYSRVAKVSD GILSELHNHK TVFRIIDYNV LGDHIAMIFL PMLWATNHIL GCPPPAIVSI
     SGANIPAASP LTYPSAAITT FWLTATSRRK IDFDSSATAY KKSMSDISNL TAVPLDIIFS
     FSNAMELSPL SINLDKDYDI DTLRTFGFIV GIMSDSLFPT PSATRAKIKS PVVDDWSRYA
     DSLLNPTRVR SSHHGSEILA ESNVVVPYEL RYAHRGTAKV RQSMYELPVT DLEYGENTMT
     TLTQLSESLK VKPGTSKLLR DAMLAGEVFV IPTTHPVTLP CPSFDAHGYG HIIPPNSLQS
     LLLTHLGLPV SSASYTSSFA KTILSDGKLP GSAEAYLSLY QETYKKGPSA VAYLKDAIGF
     SDSSMSALER LASNGLYGIS GASFAYNPRG GFFFRFDQDN ADRFGTSLSP SPTIRRLDIV
     HMMFTMLMYP TTMVSQNQWM MVRFGRSFSR LARR