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 16-JUN-2009, entry version 39. DE RecName: Full=Large structural protein; DE Short=Protein L; DE AltName: Full=Transcriptase; DE AltName: Full=Replicase; 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 Rice yellow stunt virus (RYSV) (Rice transitory yellowing virus). OC Viruses; ssRNA negative-strand viruses; Mononegavirales; OC Rhabdoviridae; Nucleorhabdovirus. OX NCBI_TaxID=59380; OH NCBI_TaxID=4530; Oryza sativa (Rice). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX MEDLINE=22749841; 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: RT identification of the gene 6-encoded virion protein."; RL J. Gen. Virol. 84:2259-2264(2003). 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 CC displays a different biochemical reaction than the cellular CC enzyme. The template is composed of the viral RNA tightly CC encapsidated by the nucleoprotein (N). Functions either as CC transcriptase or as replicase. The transcriptase synthesizes CC subsequently five subgenomic RNAs, assuring their capping and CC polyadenylation by a stuttering mechanism. The replicase mode is CC dependent on intracellular N protein concentration. In this mode, CC the polymerase replicates the whole viral genome without CC recognizing the transcriptional signals (By similarity). CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S- CC adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. CC -!- SUBUNIT: Interacts with the P protein (By similarity). CC -!- SUBCELLULAR LOCATION: Virion (Potential). Host cytoplasm (By CC similarity). CC -!- SIMILARITY: Belongs to the rhabdoviridae protein L family. CC -!- SIMILARITY: Contains 1 RdRp catalytic domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB011257; BAA25160.1; -; Genomic_RNA. DR RefSeq; NP_620502.1; -. DR GeneID; 944307; -. DR BRENDA; 2.1.1.56; 305814. DR BRENDA; 2.7.7.48; 305814. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:EC. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0006370; P:mRNA capping; IEA:UniProtKB-KW. DR GO; GO:0006410; P:transcription, RNA-dependent; IEA:UniProtKB-KW. DR InterPro; IPR014023; RNA_pol_cat. DR InterPro; IPR001016; RNA_pol_L_viral. DR Pfam; PF00946; Paramyx_RNA_pol; 1. DR PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Methyltransferase; mRNA capping; KW mRNA processing; Multifunctional enzyme; Nucleotide-binding; KW Nucleotidyltransferase; RNA replication; RNA-directed RNA polymerase; KW S-adenosyl-L-methionine; Transferase; Virion. FT CHAIN 1 1967 Large structural protein. FT /FTId=PRO_0000297839. FT DOMAIN 604 790 RdRp catalytic. 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 //