RDRP_BOTVX
ID RDRP_BOTVX Reviewed; 1413 AA.
AC Q6YNQ7;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
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;
OS Botrytis virus X (isolate Botrytis cinerea/New Zealand/Howitt/2006)
OS (BOTV-X).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Alphaflexiviridae; Botrexvirus.
OX NCBI_TaxID=686947;
OH NCBI_TaxID=40559; Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16172841; DOI=10.1007/s00705-005-0621-y;
RA Howitt R.L., Beever R.E., Pearson M.N., Forster R.L.;
RT "Genome characterization of a flexuous rod-shaped mycovirus, Botrytis virus
RT X, reveals high amino acid identity to genes from plant 'potex-like'
RT viruses.";
RL Arch. Virol. 151:563-579(2006).
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=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};
CC -!- SIMILARITY: Belongs to the potexviruses/carlaviruses RNA replication
CC protein family. {ECO:0000305}.
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DR EMBL; AY055762; AAL17722.1; -; Genomic_RNA.
DR RefSeq; NP_932306.1; NC_005132.1.
DR GeneID; 2943228; -.
DR KEGG; vg:2943228; -.
DR Proteomes; UP000001664; 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; 3.40.50.300; -; 2.
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; 2.
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 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..1413
FT /note="RNA replication protein"
FT /id="PRO_0000401067"
FT DOMAIN 59..226
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 614..771
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 772..905
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1143..1249
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 413..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..436
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 643..650
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1413 AA; 158250 MW; A60AB3DA931DED2E CRC64;
MSALRSLASD LSDPTTKAAA NEIAFKHFSD GIKSTKLSFP YKVDESTAIL LEKEGVLTNP
FSTTLHTHAA EKMLENRTLN EVGKKLKVHT GPFTFIQFKT GKLGHVGRGH NQGDQIINYA
REAKDLSRFE TLDTAVVPPV HNRVALLHDT LHFLSPRQLA QLFHHNPNLH LLYATLVLPV
EALHNLPSLN PHAYTLEYFS NGDFAYMPGG HAGSGYYHSA ETLHWLRAGQ IKLGHFSLSL
NKEDSFGAHH IFTVTRQFIP PAPRYLYAET ELVTLHDIFY PADSNVQRPY PATLINRMEL
YCRSVKAVSL RDIFAKFRQV TETAQLRHMR ISDVIRLANY FLFSASLSGT NDYPSLVGHG
LFKKMRVSFQ ERVKEVLAPL VGHTQYRTLM SFVQPKPFTF SLTPVTFHAA QGRKWSNPLG
PMDPPPPGPA GPDEPSDPLI GPTLSLLALG IPDDDLDADL DKIAKRNTRK DELLAELTQT
PTKVEVPPAP EDAAGPQNPT TTTPTAADPP TTPADEPTPE APKHHPTLTA VDIQLLNDLR
FTDLDIQHGI DGPILPLHRN PAELTPTLIA DINCAPFVEM LSARHIPIIS RPVNNARAHA
LASDVKNAKI GKLLTKQPQD WLKSWDARCS TSELQLNVAV IHGAGGSGKS YSIQETLRNK
RETLEHTTIV TPTVELRNDW SGKIPRMAPD RIKTYEKAML QPGTATVILD DYGKLPPGYL
DSYAVLHPNV ELFILTGDHR QTTYHVSDPE ANTFHLTSEI QEFRPLCAYY INATHRQPRR
LANVLGTHSS KTSGGAVLEA DMIPDDATVL VPSRVEQAKL IDLNRRAMTY AGCQGLTAKN
VTIVLDRDTP LCTDETMYTA LSRASESITF VNTYSKEPGF LAKLDCAPYL KTMLTGVHEE
EYQPDDTPAN DNPTEPELTK THLPVENDNV FFEPLVEQCT DKDTRELFTA EHGKTNLAQT
SSLEVQLFPH QQAKDDALMT ETMKARITTS TRDANLRELH DTNALSGLLF EFYADFMKVP
KDPMPFNPTL WAESRARAER TYLSKTAAQI LNGANRQDPD FPDNFVALFL KSQWVKKLEK
VGMQFKAGQT ISSFKQQVVL LTTTLALYLR ACRNSHQPDN VFIMCEKTSN QFNDFVKDWN
FERDNYTSDY TQYDKSQDGL FLNFELRKAR HFGVPQAVLD AYTAIKTDAK VFADTLKIMR
LSGEGPTFDA NTECNIAYDA ARFQLSDVKA CYAGDDLARD RNCPERASWK YISHQFTLQA
KPLVTRKPDF CGWSLTKHGI VKNPKQLWQS MQLGLKLDKL KDIVPSYSLD FHHAYALGDK
VYDIFTEEEM AYHQATVRLM HKMGVHPKIA GDHLPVFHIT SDRLLKETKP IPALVPTISI
TPPATPPPEA EVELTTFTTH IPDSRPIRNV HFD
