L_MILVL
ID L_MILVL Reviewed; 2280 AA.
AC Q8BCV9;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 29-SEP-2021, entry version 68.
DE RecName: Full=RNA-directed RNA polymerase L;
DE Short=Protein L;
DE AltName: Full=Large structural protein;
DE AltName: Full=Replicase;
DE AltName: Full=Transcriptase;
DE Includes:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE Includes:
DE RecName: Full=mRNA (guanine-N(7))-methyltransferase;
DE EC=2.1.1.56;
DE Includes:
DE RecName: Full=mRNA guanylyltransferase;
DE EC=2.7.7.-;
GN Name=L;
OS Mirafiori lettuce virus (isolate Lettuce/Netherlands/LS301-O) (MiLV)
OS (Mirafiori lettuce big-vein virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Milneviricetes; Serpentovirales; Aspiviridae; Ophiovirus.
OX NCBI_TaxID=652964;
OH NCBI_TaxID=4236; Lactuca sativa (Garden lettuce).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12388823; DOI=10.1099/0022-1317-83-11-2869;
RA Van Der Wilk F., Dullemans A.M., Verbeek M., Van Den Heuvel J.F.J.M.;
RT "Nucleotide sequence and genomic organization of an ophiovirus associated
RT with lettuce big-vein disease.";
RL J. Gen. Virol. 83:2869-2877(2002).
CC -!- FUNCTION: Displays RNA-directed RNA polymerase, mRNA guanylyl
CC transferase, mRNA (guanine-N(7)-)-methyltransferase and poly(A)
CC synthetase activities. The viral mRNA guanylyl transferase displays a
CC different biochemical reaction than the cellular enzyme. The template
CC is composed of the viral RNA tightly encapsidated by the nucleoprotein
CC (N). Functions either as transcriptase or as replicase (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; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC ChEBI:CHEBI:167617; EC=2.1.1.56;
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DR EMBL; AF525933; AAN60447.1; -; Genomic_RNA.
DR PRIDE; Q8BCV9; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR InterPro; IPR014023; Mononeg_RNA_pol_cat.
DR PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
PE 3: Inferred from homology;
KW ATP-binding; Methyltransferase; mRNA capping; mRNA processing;
KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW RNA-directed RNA polymerase; S-adenosyl-L-methionine; Transferase;
KW Viral RNA replication.
FT CHAIN 1..2280
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000391501"
FT DOMAIN 638..804
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ SEQUENCE 2280 AA; 262635 MW; E2FF37747BDC256C CRC64;
MDDFMKEKKI NYLKTPYLRT LLESYKEDYV SLKSTIEAEK KKEAREIDVN YPHILTDLIE
RDRDEVVSLE KIGTPSVISK INSPYTEISE ENLNMIKGAL YPEKWNRKAH LELLLFREFF
LSRLDKESEI SYDLSQDGSI ELVKRLYNGG YASPESNVVY KFANTLVSHE LSKIEMNMLG
TQEMKFNEDE ISLDSAKKYW VLDVLEHLNK NIMMKASARE NKRDAPDSID FYEGKRIKTN
YFGVGSSISR IEFENSLPPL VIFLSSTICG YYFEGEAKCF IGKAEMMNYS MYLADNLLTL
SLIRTKLSTE EKKFMDYYVS LLDQPLKTRV GMGALYETTC LLMSDQKTLS SSMPILDNLI
ESIEVSTEQT EIIVEVCISV GPETCIKMSS LGKTLILAST NPSKGLSKYT QRTNRDNPVN
INTIRRLRSL FRQRVIISYI EKHGRVPNLI SVPEDLGAQL EMKAAGGNYL GHMISEISRY
DSVRLGKFLD TGKEMNLQSR IIDKACTKDS YDSENNSEKE IQYYISNDMK EVFKDPIAID
RDQYKSKERL VKVVHRKEPL MMPMKKYLNV RLSAKEKEQK TAARFYGIAS FKLKLWISST
MEMIKRAMKL LPGQMMTMTD DERRLIMFKM SEKLLSKNSY SLFLDYSGHN TSQRPENTNF
ILEEIANMYG YYEGTPEFNE LTSLSYVFSN INIIVEDSWS DYVYISQGQL GAIEGWLGSL
WGIQSQLMIE DMFMQLGMND YIGTTYSDDS CGVFTQSSLD VHKLNGIIKN VQRYGEDMGL
IVKLSQTQVT NGRCSMLKEH YYRGKPMDMS IKKMMSISPN GPKLLGDELE SATLIDSGYT
SSCTRASEIG IQTLLRNFRI VKLLSNSTRK LIEDIDNDIL DERYLSSKNN YEISMKIAAK
NLSKNRLSSY IPAPRSRVIE FYQFHVTNEK VLDLYLMIMY SPYTLYGYAL TPMPDVLISG
YSLSNVKRLA YLQGILGKEA LIVLSKLINL SGNALSYIDN PFPFVGGRKD TKLLIKPIIV
KQLPKRVRNP ELLKLLSLQK DKEEINFKTK IVEVFENCFS SRIASKFYEC SIYSYISGVI
SKVDNSTTMK MLLGGRKMMS LINDAWMRNH KLRIRLNDKG IMNYNELLFA RNQKVLKYKN
DEEIKLNFLE IEEIPIMGKV KYSEYRNMMQ PIFKGSTKLT EQGKKNVPPQ KTFFNIAKFD
RELGVDGMFE HKLIFQAYDL VRYVKWLMME QERFSKKMNE KDELNLTKLC NMTLHTFTDA
SYHDLQEHVV CPKGGRYFHR ALTSGFNPKT GDLSSNIYSS SYDITGIDQL LAKTGGADNN
LNIQYLLIYV RICLSLLRPS PNKLRSLTLT NDIYFNIKDV TFSLENLNDP GSSETLYEVA
SRDKIQSRGK LYYNYSTYIE MDEDLENKFI DHVSTTRQEF IEKESAFRSV HSYMLDQMII
SPELISDLIL EGLIGKKMIS KGRERFFDQF YKYYKSLNVI GAETPARSVI RGLLYEELFK
VNPKSKKGEL WSTEIIKHGY SSGFKDSLMK LFILSTSLSY RMLDKQNGKM KLIVNLNRTV
QNSKSNFERI RKGECQFYIK DKRITEMILN SFPTLGYTYS DVHQAATDVC CEISDMEFEQ
VRLGSYYLKL HKAETNKIEG MVYGYVNFSE LEINYQDLLD NLGLESALKG FETACSLMVS
PEQLSSPTLS AVYPSAKGLL DSLIGNGFIK NSDTIIELCG GRGDFHLAMM EKEIKHTTLS
REDGYNLAMR IPGMTSKKVS FNCFRQSDYI PYFDHSIILL DISHITEKKD CLSGILGDCI
TSKKKVILRL NGLNKFLNYE ILQELKMYEM KAYLPVLESP GYVYLTIDAS KKLEEEKQLD
RKIFTDQLGY SRSILTCSLI NSISIVNLQG VISVPPKRVQ DQTMEVISDE VLTEMILEED
PEYVHVNPEI KTQVKTADDF KDNLYVYISE KLSIKYKNKL KFLEERLITK GKIEKSENKP
KNLIELARKI RRKESDTIEV DYRMLINSKV NIISGVTGMD HNELVEVLND AMSVKFNKRM
SFECWKLILN LSANEKLIDS DLIVETINIQ KFRKDVDRTI NSSFEIASKA VISFKTGRIV
EGLLAVARLD NVRRKSILNH KDKTTRNNIL HYKLYMNRIM IISQSMYVEP QFPGISDSKF
GKIWRSLGSI ESDIDIERAN AALDSIESLN KFFKEMNDEY FSFLNNFDLS VDNMTERIKE
ECQPIDALVD TLTTFGLEVT EEDIARNKEL DTWEKVQEYC GEEELFDAWA QEDIGDWGDE
