L_RYSV
ID L_RYSV Reviewed; 1967 AA.
AC O10378;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 94.
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 Rice yellow stunt virus (RYSV) (Rice transitory yellowing virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Nucleorhabdovirus.
OX NCBI_TaxID=59380;
OH NCBI_TaxID=4530; Oryza sativa (Rice).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12867659; DOI=10.1099/vir.0.19195-0;
RA Huang Y., Zhao H., Luo Z., Chen X., Fang R.X.;
RT "Novel structure of the genome of Rice yellow stunt virus: identification
RT of the gene 6-encoded virion protein.";
RL J. Gen. Virol. 84:2259-2264(2003).
CC -!- FUNCTION: RNA-directed RNA polymerase that catalyzes the transcription
CC of viral mRNAs, their capping and polyadenylation. The template is
CC composed of the viral RNA tightly encapsidated by the nucleoprotein
CC (N). The viral polymerase binds to the genomic RNA at the 3' leader
CC promoter, and transcribes subsequently all viral mRNAs with a
CC decreasing efficiency. The first gene is the most transcribed, and the
CC last the least transcribed. The viral phosphoprotein acts as a
CC processivity factor. Capping is concommitant with initiation of mRNA
CC transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase)
CC adds the cap structure when the nascent RNA chain length has reached
CC few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and
CC facilitates subsequent guanine-N-7 methylation, both activities being
CC carried by the viral polymerase. Polyadenylation of mRNAs occur by a
CC stuttering mechanism at a slipery stop site present at the end viral
CC genes. After finishing transcription of a mRNA, the polymerase can
CC resume transcription of the downstream gene.
CC {ECO:0000250|UniProtKB:P03523}.
CC -!- FUNCTION: RNA-directed RNA polymerase that catalyzes the replication of
CC viral genomic RNA. The template is composed of the viral RNA tightly
CC encapsidated by the nucleoprotein (N). The replicase mode is dependent
CC on intracellular N protein concentration. In this mode, the polymerase
CC replicates the whole viral genome without recognizing transcriptional
CC signals, and the replicated genome is not caped or polyadenylated.
CC {ECO:0000250|UniProtKB:P03523}.
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=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: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=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 -!- SUBUNIT: May form homodimer. Interacts with the P protein.
CC {ECO:0000250|UniProtKB:P03523}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03523}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P03523}. Note=L and P are packaged
CC asymmetrically towards the blunt end of the virus.
CC {ECO:0000250|UniProtKB:P03523}.
CC -!- SIMILARITY: Belongs to the rhabdoviridae protein L family.
CC {ECO:0000305}.
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DR EMBL; AB011257; BAA25160.1; -; Genomic_RNA.
DR RefSeq; NP_620502.1; NC_003746.1.
DR SMR; O10378; -.
DR PRIDE; O10378; -.
DR GeneID; 944307; -.
DR KEGG; vg:944307; -.
DR Proteomes; UP000002325; 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 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.
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..1967
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000297839"
FT DOMAIN 604..790
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ SEQUENCE 1967 AA; 223602 MW; DE70AB80A45FC776 CRC64;
MDDEGHGYWQ DYDEDESWLD AENDVFDDDI FEEAEDNEHL VEGGDFHLKS ALRGEADMLT
NPIYEKEREK LQEDVGDLGV ALGHLNVRPF LEKMGERIST DHTNTPLIEN IKQGGFGAIH
HMKSTARLIV AEAATVTETM LTSGVDTTLA GAYHFFEQNH PHMKCTVNMV LMFLTILNNV
KNIRLNVDLH QILKNNISIK GSTVCMYITV ATVAYFSTDI VVFDIDGQKY NTPKTYFLNA
CDKIQERFNV ILYSYLAEGL SIPGSPPTYI VNRIIDWGDS ILYQMGNDGY DVIALYEATV
VGVILSRDDK DLSPTSGGGD FLENIQQDLG PVQQNHIRYL IALLHDMTPH QLADLHGLYR
IWAHPIIDID GGVKKLQKVT QSLKGDINSK PESQETVRSF RRLFVMDYFV KHQFYPPITL
PEKSNCYIGN CIRTSKKIDE SHINYNFSDW DLVELGGAFS IPYSWNVLHL AKDKAISPTR
SEMYTMLCKT KRVFNAELRR GVLKLMNTTL TPLREFLTEV AEHGLDIDDC IIGLFPKERE
LKIMARFFAL LSFKMRLYFT ATEELLGSKL LRYFPQITMS SNLLDMQEKM SSMSRDLESQ
NKSVTYVINM DFVKWNQQMR ESTCEGFLKN WSKLFGLPGL YSRSHQIFRD SILYIADGTR
DLTPDPDTGI MVDNNVCWID DGAGKEGIRQ KAWTIMTVCD IAAVARHHPG VFHLVGGGDN
QVLTVTYHTN QIDTDGNITE EGKSKIKAKV KKFIEALETH FAARGLPLKT SETWCSTSLF
MYNKFMYYKG VPLRSPLKQV SRLFPYSNNT SMTLQSMAQC LGTGLRSAAQ KEVSHIALLF
MRNIWGSVLG WIILYCHPML PSISSETCNS GVSTIVRGRK AINMKTHRID LVALILKILY
LPGQLGGPGL VNIYQMTMRG FPDPVTEAIC FLRKFKNYLI CVGSSYSSHL ARMAGVSFSA
SRSYEPLIED VCSLNLDTPR SGTGGKREVP RKILLKSRLG GNQHLKELLG IMKGPSEGEF
YRAISSGKVL DVRVMHEITS STLYAVTNTF TSRVDKTATL KRLTFKFSML ESLADAELKY
IRYLSVRDDK THDIMFDGCS RIIADECRTK GWGKPVLGVT VPTPFEYLQI SWTDEHICDN
NHITVRISNQ DRQVTTETLG PCKPYLGAYT KEKFKMTEVA AAYGDEDVLS KSLRILKIIN
WRYQDGSTMS EIIKAPFRAV TDIDPQRMVQ ESTVTKGDYD HRRKMDARVH GGIPNFVTTP
LSHISISTST WYKHARGKNE NIHFQACIIQ TMYQIIIRTM SNIHSQEKLH VHECCQTSIS
EIQEPRANLD LTTPQMIPTF PTLMGNPLVY IPEQSITFDY SRTQEVDYSR RVGSLDCQRS
TDYGWVDAYS SLSWLIMCDV IGWTKMPDSF YIMQQERVDH YLLSMYIISI WKVLKSEFDL
HKTMLDWGPL LKVYSSDTGV QVLSQSMGIV VLGKLEGGLS VNMMDICNSL TGLTSNQIPP
FSVNLALPRI HKQVATWWKL TCSDTMYCIQ CSNILKGYWE GTLINTRIDN DLRCSECADG
GISPRIVNAH ISNLSDHLIK IIPDREEVQL PLLAGGEDLN NLEVVLSLED EWPDSDDITI
LNRIGEMNDI DGRMKNYLEV MALLNPDVVI IRPEILELEI LRRVCEVVRL ASEGKLIIHI
LVEEPSYLES GAIYEMERAF PRHNLFHVQF SFRKPPEGLH KLWLLPQDIT LARADVGDWL
VIPFTQLLDF HDTITPDTRL HHQREAIRQD VFWSTKEQGG LGLVVLQHIC TKTELSYRLD
RSKVDVEINK MMIKDPVMGG KYVILKRRCS WAIFSTKYEL LCSAERIKGN LSADGKKITS
KDFSRTYKED IIIFIISVLM RSLDCDEKRV MTLSYVECLP ELLTLKPRFN KSGVISVRYL
DYFWFFKRVY SYNNPEVAIP YSAVIKGVNL GSPRKEGYSL ASSDGAP
