ID L_TAVCV Reviewed; 1928 AA. AC Q5GA85; DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 16-JUN-2009, entry version 21. 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 Taro vein chlorosis virus (TAVCV). OC Viruses; ssRNA negative-strand viruses; Mononegavirales; OC Rhabdoviridae; Nucleorhabdovirus; unclassified Nucleorhabdovirus. OX NCBI_TaxID=303300; OH NCBI_TaxID=4460; Colocasia esculenta (Elephant's ear) (Taro). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=15659770; DOI=10.1099/vir.0.80591-0; RA Revill P., Trinh X., Dale J., Harding R.; RT "Taro vein chlorosis virus: characterization and variability of a new RT nucleorhabdovirus."; RL J. Gen. Virol. 86:491-499(2005). 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; AY674964; AAV92087.1; -; Genomic_RNA. DR RefSeq; YP_224083.1; -. DR GeneID; 5076497; -. 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 1928 Large structural protein. FT /FTId=PRO_0000297841. FT DOMAIN 596 782 RdRp catalytic. SQ SEQUENCE 1928 AA; 217363 MW; 042E4E6FBC396429 CRC64; MDSDYPDLDP EALTVLDSIR EGIQDEEEED NNDKILSGTG DYHLKSALRT LDDMTRHPIF NKEYQKAVRH FGISPTMMMT PTAVLKLTVS QTKINKAVGF LFGDILVRLD SLPWAVDCYD SIQAEIKTMH SHMMIFATPS WVEDVHNKVS SLVEYDHDAT LIWATVITLK NYLPAWREKG ASLLDWRSVQ YDPESEYLVM KVDRDFIIYV GSDICVMEIG KQTLWAPVPY ILNGADKVAE RYNVKYYCAL CDELDIPDRI SLEKLNQIIE VGDDCLQALG NKGYDIIGSY EALLAGIIQA RDNPQVIPDR ELLQRTTLND PGNTIGVTFL KRWDALMEDL NPEQIACAHG LYRIWGHPAV DILGGINKMR EVASIVKLPS SKILTDIGRQ FKEMFFTSYH SVHKHYPKHL IREYKSDSYI HECLKDNRTL NSKVLSYHFP DWDSVALEKN FEVPYSWNLV HNLKDKAISP SRSELYETLS TRNSIFGASN RRGILKSLTM ETVQLRAFLQ DVNDKGLPDN DKIIGVYPKE RELKIKARLF SLMSFKLRLY FVSTEALLGD KILKYFPQIT MSLDMLSMIK KMFRVSGQTT RGDDSVTVIF NLDFVKWNLQ MRKIICSPVF TQLGALFGMP NLFDITHDLF RESVIYLCSG EGDLRGDPVF GVAPDGVWSW TGDESGKEGL RQKGWTILTV VTIMLIAKRH HVDVSLMGGG DNQVLGITIG GMVRDSVGEL TQDSCKLAQC TIKRFTQDLI TTFGDLGLPL KASETWVSDS LFMYNKHMFY KGMPLRSPLK AVSRIFPLAN DSIMTLDNMI NNISSGVKAA CMKERHGIPL VFIKTMAYRR VAELSLIMHP LTVCFKKPEL PDHGIVARSG KKLKIPVTSK NLRQYFSLCT LGSSTMGHPG TLHLPDIIMR GFPDPLTSHL SFISEMRRYI VDPGLASVVD KLSHLSTSPT TEYAKLVEDP TSINHDAPTH GLNEIRQMSR DFLMSTTLAT NPHLKSLFSL LDRGTEKDFY DALCSAQELD VKVLHEIAGA TLYGYTNGIA SRIDQTGTVR ALNENIDVLR RLALAETRYI GYLMARDTRE HDLKPSSCSR ITAQQYRDLS WRKPILGVTV PHPMEMCQIM SSTETIYHDA VVCWSDRVSG SEIYQSMGQG KIYQGSYTKE RFKATDIAAA YGNEDILVKA VRLQKLINWR YDEGSNFAKI ISLTLEAITD ANTEGFHRSK EEIKGEFDHR RGVTGDISGG IPNFLVTPTS HFSSTTSSWV SHSRGGKNEN IHFQSVLINL LYRAMVYRGS VPGLPEMIWY SKEKCSDCIT EIKDPDPIKT TPSLHTLPSA KGNPFAYIES VNVKLDYHHQ IEITKGMEEE YLINSLWDGQ NVSGEEESGL LLYLMLIGSR QISESFILLM RERINAATAL QYMLNRVILA RKLGLDSQFP IRSTSCVNLL LGTDDNILSC RDRFNIELLS GSWESGVSCD MSVLYRDDLL TASELHVNVY LQNVPLQLAL SRAASSTQLQ SCLECQAIVL DRPSQRELMR YLHWCCPYHT ANAPPRILRI HSEKLIKGIE LRTDNPLLVP YVCNPVTLER VEKVPVMVDS WELPVHMHST WDSILPQLYL TLKSLLSQVT ISSLIVDDDI TLINLAASVM LDLRRELPVY INVKGFSGTE INNKFDNLKL LPPNIRSSVS VYHENRSLIE ASAAVWLPEP SSVESVGADW LVLWGDTWRM GAGVPGHVLV TESKLSTGMA WVLHRDPLAS QSVLELCGAV QIWEKKALDW DMREGHCVPI QMNRTLACSR LGSRGVRWTM WSTAAGLDKV TRILRSKLLS LSGNPGSSYH WRKGCQKILK AYVLSLYAHC VDNMLEASGR LVGVSVHGSL SGIVPICDMH SSDRIQRAQY LFLKERCQGG PFILRNRLER RINLLSPVHD LLDGPSQS //