L_LBVAV
ID L_LBVAV Reviewed; 2040 AA.
AC Q8B0U2;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 29-SEP-2021, entry version 80.
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 {ECO:0000250|UniProtKB:P28887};
DE Includes:
DE RecName: Full=GTP phosphohydrolase {ECO:0000250|UniProtKB:P03523};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:P03523};
DE Includes:
DE RecName: Full=GDP polyribonucleotidyltransferase {ECO:0000305};
DE EC=2.7.7.88 {ECO:0000250|UniProtKB:P03523};
DE AltName: Full=PRNTase {ECO:0000305};
DE Includes:
DE RecName: Full=mRNA cap methyltransferase {ECO:0000305};
DE EC=2.1.1.375 {ECO:0000250|UniProtKB:P03523};
DE AltName: Full=mRNA (guanine-N(7)-)-methyltransferase {ECO:0000250|UniProtKB:P03523};
DE Short=G-N7-MTase {ECO:0000250|UniProtKB:P03523};
DE AltName: Full=mRNA (nucleoside-2'-O-)-methyltransferase {ECO:0000250|UniProtKB:P03523};
DE Short=N1-2'-O-MTase {ECO:0000250|UniProtKB:P03523};
GN Name=L;
OS Lettuce big-vein associated virus (isolate Japan/Kagawa) (LBVaV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Betarhabdovirinae;
OC Varicosavirus.
OX NCBI_TaxID=652962;
OH NCBI_TaxID=4236; Lactuca sativa (Garden lettuce).
OH NCBI_TaxID=50193; Sonchus asper (Spiny sowthistle) (Sonchus oleraceus var. asper).
OH NCBI_TaxID=50207; Sonchus oleraceus (Common sowthistle).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12083827; DOI=10.1006/viro.2002.1420;
RA Sasaya T., Ishikawa K., Koganezawa H.;
RT "The nucleotide sequence of RNA1 of Lettuce big-vein virus, genus
RT Varicosavirus, reveals its relation to nonsegmented negative-strand RNA
RT viruses.";
RL Virology 297:289-297(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. The
CC transcriptase synthesizes subsequently subgenomic RNAs, assuring their
CC capping and polyadenylation by a stuttering mechanism (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)-adenylyl-adenylyl-cytidylyl-
CC adenosine in mRNA + 2 S-adenosyl-L-methionine = a 5'-end (N(7)-methyl
CC 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-
CC adenosine in mRNA + H(+) + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:65376, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16798,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:156483, ChEBI:CHEBI:156484; EC=2.1.1.375;
CC Evidence={ECO:0000250|UniProtKB:P03523};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-
CC adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (5'-
CC triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-
CC adenosine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:65380, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16801,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:156482, ChEBI:CHEBI:156484;
CC Evidence={ECO:0000250|UniProtKB:P03523};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:P28887};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-
CC adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a
CC 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-
CC adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:65440, Rhea:RHEA-COMP:16798, Rhea:RHEA-COMP:16801,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156482,
CC ChEBI:CHEBI:156483; Evidence={ECO:0000250|UniProtKB:P03523};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end triphospho-adenylyl-adenylyl-cytidylyl-adenosine in
CC mRNA + GDP + H(+) = a 5'-end (5'-triphosphoguanosine)-adenylyl-
CC adenylyl-cytidylyl-adenosine in mRNA + diphosphate;
CC Xref=Rhea:RHEA:65436, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16799,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:156484, ChEBI:CHEBI:156503; EC=2.7.7.88;
CC Evidence={ECO:0000250|UniProtKB:P03523};
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the varicosavirus protein L family.
CC {ECO:0000305}.
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DR EMBL; AB075039; BAC16226.1; -; Genomic_RNA.
DR SMR; Q8B0U2; -.
DR Proteomes; UP000008154; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR InterPro; IPR039736; L_poly_C.
DR InterPro; IPR026890; Mononeg_mRNAcap.
DR InterPro; IPR014023; Mononeg_RNA_pol_cat.
DR InterPro; IPR025786; Mononega_L_MeTrfase.
DR Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 1.
DR TIGRFAMs; TIGR04198; paramyx_RNAcap; 1.
DR PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
DR PROSITE; PS51590; SAM_MT_MNV_L; 1.
PE 3: Inferred from homology;
KW ATP-binding; Host cytoplasm; Hydrolase; Methyltransferase; mRNA capping;
KW mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; RNA-directed RNA polymerase;
KW S-adenosyl-L-methionine; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..2040
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000391473"
FT DOMAIN 583..768
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1632..1811
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
SQ SEQUENCE 2040 AA; 232113 MW; 4E2F2A4815417BF7 CRC64;
MSLASRMTSV GGADNYGESD YGWDETVLGD MHLNSAINLD LFKEFLHIDP PVYKVKENHR
LTEELRELQS LARKGSKIEI GFQRLFARMF PRDGNLIPMD STMTRMIMKI IRDSGTKYKL
GIPLLGISEE MIKKGAMVPS NLVYSFNCFL NIIYGRSEWI RSEGIAIRFK MYEHGRFIRR
DLTISEKEYN FIVGKEVVEI RASRRKERFI ADYNSLLLLL DVAGQRICAH LCSQLGEISG
VPGSLSRYHL ETLCTAGDRM IERCGNKAYE VLGMYEALCV GRLLENNPDG ITDHTQFSAN
CEEELQELIA GSVEPAFMKS QVDLIKTTLE KMKNQDISNA FCLYRVWGHP TVDIYEGMKK
VHTIGTKVKV IPPNLGTIMV CQFRKMFMST FFKKHHRYPP ITGTPGEYLE RCLKDNVAIR
IEHLAYNLRD FEFIRIGETY SVPDTFDMCH VLNDKAVSPD MSELLESIKN GKGTSCGAKR
RGMLRWMEGD SLNCKSFLSD IDEKGLSEED LLIGMYEKER EIKVAARMYS LMTERMRYYF
VLTEGLIADY ILPHFPEITM KDSLNVLLKK MWESGGQRSI GSMDVNINID FSKWNTNMRE
GPTSDTFREM DGIFGFKRLI ARTHEIFNAS LVYSASGKYL PTIEDGRILD DPPMCYRGHL
GGFEGLRQKG WTVATVCLLA YLSEQNKIQM KLMGQGDNQI IRLRMPTSYW DSLRLTEEMK
KKEARILSDK FVHEMDIIFT GVGLPIKVRE TWKSTRLFMY GKVMLLDGRQ LPQWYKKTLR
SYALSNEGTL TISGVIGTIA TNMCAAGGGS EVPCVMYLFF LLLAEWSLEF MFRYHPFTRV
GIKDGSSMEF RLNEKGGYVH KQTRKTNNLW LKSLLVLVPT AVGGSVTIPL TGFIMRGFPD
KASEGYAWLK FLGSSKSPIQ GFLKNFYTFL PNDTVEADML VQSPFSLNHK RPPTPGLQTK
ENIREWLLST PRFQQNRFIR SMQVLLSGFD KKSVCRELLT ERMNPLISHE VYETFGHVYC
EGIVARVENT RTIRTLHLSR EDRKPIVAKL MTDEMAYIAY MWWRGNTKGE VFEECATKQA
RKGRNVGWKR EIMGITTPHP LEVLFQSVCR PGDQCQRSDD YITSKLVDDG KFPPFLGSKI
KNKVYSLQDE EARREPLIKT GARLARQFNW IGMGENMRGL VLKNVGSICD VSVFDKFVDD
DPSDNLYTGS LMHRFTPSSV SEGCFINYAP QVGHKVFMSS DTLPSLSRGQ TNYTFHFQAM
YCFLQYSISK SGNEGSYHHH IMCQDCVVPV EDEFDDIPNE TPSIVKAQEE QYVSIIRTTL
GYIHTKPRSA MVLEDKSPIG RYIEDVEGHE KELYSGVVEL LCWKSALEIL GRTRDTHATV
GTEDLQGWPR IYAYKVSRRH IIGKVTSFIL YILAVQIGEL PLPYSMERVS RRAIDVVSRV
GLEGFSAVAS LCLGRDIPMV NDVVTIVDGF AYPETVSVCL RSIKASILMT IGKVIRVDGF
MSRRSVYPTE SMTSDDFLRI LGFKAVIFYG CTKIHEKCQL KGLDQVTYAE MMCHHRCLEK
LLSSNLLTHM TMDRAMKYLP IKITKILPKI SSTRPNTIAV TREVETENRE FSDTFPIDER
VTYPEMDLKT NQMIQYPTSS IYKWSDILLG IEHYDHVVVM GDGTGGTSMV AAHMFPNSTI
YPMALLESKN LIPQDMESLA PPMSRKLTNV DSSLLIDLPD DIRKPTFRTR MLERVSLMRG
NILIISDIEG TGTLFRDIVS TCLYMPTSTD VLMKTHLADL CGSYYMMKGA GRIRLRGSRL
ANLRYGEVFV SFRVTGGNIR PNRRGLGNCI QEVMIGLMNT QIETATGMLS QIESMFPLAA
DMSMNIAMMK MASWGGSFSR KVLGEDGLKL MGYVYQYINT HYHFASSSYR PGDNRTVTPR
RKEDLTKLLC SIMLGVYGED TETIEEVSKY TLIGSKKGVP GKSYFKVLMW KTGTKRALEH
DEYMVGRAIR NYRTRILEAK KLDGPIGLPF HSGSLRKIAT WGYKIPISAS GGWIDNHLQI
