ID   RDRP_BOTVF              Reviewed;        1896 AA.
AC   Q9DRA1;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=RNA replication 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;
DE   Includes:
DE     RecName: Full=Methyltransferase;
DE              EC=2.1.1.-;
GN   ORFNames=ORF1;
OS   Botrytis virus F (isolate Botrytis cinerea/New Zealand/Howitt/2001)
OS   (BotV-F).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Tymovirales; Gammaflexiviridae; Mycoflexivirus.
OX   NCBI_TaxID=686946;
OH   NCBI_TaxID=40559; Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11125160; DOI=10.1099/0022-1317-82-1-67;
RA   Howitt R.L., Beever R.E., Pearson M.N., Forster R.L.;
RT   "Genome characterization of Botrytis virus F, a flexuous rod-shaped
RT   mycovirus resembling plant 'potex-like' viruses.";
RL   J. Gen. Virol. 82:67-78(2001).
CC   -!- FUNCTION: RNA replication protein replicates the viral genomic RNA. The
CC       central part of this protein possibly functions as an ATP-binding
CC       helicase and/or methyltransferase (Probable). {ECO:0000305}.
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   -!- 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};
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DR   EMBL; AF238884; AAG23416.1; -; Genomic_RNA.
DR   RefSeq; NP_068549.1; NC_002604.1.
DR   PRIDE; Q9DRA1; -.
DR   GeneID; 912251; -.
DR   KEGG; vg:912251; -.
DR   Proteomes; UP000000398; 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   InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR   InterPro; IPR002588; Alphavirus-like_MT_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
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; PS51657; PSRV_HELICASE; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   4: Predicted;
KW   ATP-binding; Helicase; Hydrolase; Methyltransferase;
KW   Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; RNA-directed RNA polymerase; Transferase;
KW   Viral RNA replication.
FT   CHAIN           1..1896
FT                   /note="RNA replication protein"
FT                   /id="PRO_0000402499"
FT   DOMAIN          60..227
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          1025..1194
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          1195..1327
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          1668..1774
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          828..991
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1347..1388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        831..857
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        951..966
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1347..1385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         996..1003
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         1059..1066
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1896 AA;  212378 MW;  EE15A3ED1387B271 CRC64;
     MAVPLERAFA SVTQSFHKDA TQGPTTNEYL VARAETQRYA PYAVRKGPAA LLAQVGINTI
     HDSPLSHSHP ACYALNAFHF LKVIPRYLHG KAEVWGTKDN WFRKLQAQID SQTTTLTHRN
     YAITARDHVR YPGTVVDHPG SCTAGTLFMH DALQYMTPLD VYTLFATSPE MHSLVATAVI
     PPESVDRLPA FWPELYQLAY YEDHLCYAPD GNFADAYNQP LAAHQWMTMK SLHGPDFTLS
     VDVPASRYSH HIFVISKRPG LPDTHRDFMC PDLVELPKDF FPGANKADKL LPRTLVNQMV
     EYAASVKRAT IKDATSRTRA YVKDQKYAAV TPVQQMYLSW FGSGLSQMQF PDRPVTPLDN
     FATALWYRLL PSRLYRLPAT IRNFQLKAFV DQLRTPQYLL HFKLDEYHLS SNDKYSDFYR
     NESRQASSKD MLSAFEAICF GGAPELEKKI LGNNNPAPFA TVPNPPSQTA LGLATITAAI
     AFILPNRAAR LTRLVARYAI RAVKEIVNPS FLTIPRFGLL SHSIASWLQT DGAVITYGLA
     PKIASWSAPI WYNAALLAPT DMRSCQVLVD IANDLRFDYR YGTMRLAVTL GLTLLNPFLR
     RLVLLPFKVL WHSYLPSIKN KLDSMVLMSI STLPDNISVP LLTLRGNLNR QRCPDNKDPT
     PIHESDDNST ADDKCLHCPI HCLKSKLSEP AASPDTVPED NPLQEGDLTE EVYAAALAKK
     DTPPPYPTRN DCLLVALADG LLTKRILWFS CIKMFGNTAC WVIHDTGKAF DWMHLKMLAE
     QLKLNVSIEV AAEHDHHWTG LAKRVGPIDG RKIALRWYPY HWELSDRGRE DYGPPPPPPP
     PSTTEPPPPP NPPAASPYHS PTVEDEPLEE IPLANSNGEF STFAFDDMAA DDLNPAQPLS
     SLDLDEEPSA KQEPLEPAAI KTSEPEPLVP ESEEVFFRPS PTPTPSDATP TPAARAPSSV
     SNENAQRPRH PLPPVPTGGA SAPSNDKLNS AAKQYARLVA GKTRQMTVAQ PRSKAYLRDL
     KRGNIGTIPT AEAEQLDAYI DSWAVNGFNR SVHVIYFCGL PGTGKSRRCM KMTERLLKEN
     KYLAQTVRIV TPTDNLRNSV ARQLKPPTES SYSVQTYETP IRQPSLGPVL IVDEYGKMPA
     GWLETVLFLN PRVQMVIFTA DPTQGIFRTR IPDAYCCRIP SSTEAIASYA HEYRRVSDRP
     APGVARALGL PTTSRRPGQI ETSTELNVDW ITVRPEGERA AWHNTWGGKV YTYATCQGET
     FHRAYQMVIN GNTRFWDDRD LFAALTRGSG TLRLIYETQS SKPLPRSTSK LYNALLDFRT
     DPHKLPLAIE EHVNRYIPSH LRNVNQAVPR RNAASNPDAL PSQRILPGGQ STTAEPXQSQ
     ASALPTGGEA IDVPALDRQD PQRFPQLKVL PHLCGYIGDY SEASYPEPEH PKTQMLDATF
     PTYLARNRGW NDPALTDAVT ANYKAPEHRD IWVEAVGETT RQVHGSGDDR DVFLEHRGDD
     KATANITYAK RLRFSQRAAN ERSIAATKVA GSELFEAFTR AIPLPQETFN DSLLEECRTE
     NDTVHLTSKP LATLINNAER SDPSWSLNMI KLFIKGQTVK KLEKMGSDAT AGQSIASFRA
     EVLLAWGPYA RYIDRRIRAL LPPHVYIHSR RTNEDFEKFV AAHWDHTRES TDGDYTAYDA
     SQDATFVNFE TLLMRRLDFP LDIIEAYVEM KASITSHFGP LAIMRFSGEV WTYLFNTLGN
     IAFTYAKYEV PSVAQVYGGD DKSINSPITV RTGWSQLVGK FNLVEKPVVG YEPTFCGWRI
     VPGGIVKDPQ LLFWRTRYAR IRYDAALWAP GYYDELVLSL KTSDRLMDHM SPNDLAYLQA
     LVRFYTKLSR RLPSLADRRR CNPLPADSPS VVLSRD