ID L_EBORR Reviewed; 2212 AA. AC Q8JPX5; Q5UAK4; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 30. 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 Reston ebolavirus (strain Reston-89) (REBOV) (Reston Ebola virus). OC Viruses; ssRNA negative-strand viruses; Mononegavirales; Filoviridae; OC Ebola-like viruses. OX NCBI_TaxID=386032; OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=77231; Epomops franqueti (Franquet's epauleted bat). OH NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX MEDLINE=22180312; PubMed=12191779; DOI=10.1016/S0168-1702(02)00087-4; RA Groseth A., Stroeher U., Theriault S., Feldmann H.; RT "Molecular characterization of an isolate from the 1989/90 epizootic RT of Ebola virus Reston among macaques imported into the United RT States."; RL Virus Res. 87:155-163(2002). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate Pennsylvania-89; RX PubMed=15661171; DOI=10.1016/j.virol.2004.11.018; RA Boehmann Y., Enterlein S., Randolf A., Muehlberger E.I.; RT "A reconstituted replication and transcription system for Ebola virus RT Reston and comparison with Ebola virus Zaire."; RL Virology 332:406-417(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 subgenomic RNAs, assuring their capping and CC polyadenylation by a stuttering mechanism. The transcriptase CC stutters on a specific sequence, resulting on a cotranscriptional CC editing of the glycoprotein (GP) mRNA. 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 -!- SUBCELLULAR LOCATION: Host cytoplasm. Virion (By similarity). 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; AF522874; AAN04454.1; -; Genomic_RNA. DR EMBL; AY769362; AAV48581.1; -; Genomic_RNA. DR RefSeq; NP_690587.1; -. DR GeneID; 955191; -. 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; IPR017235; RNA-dir_RNA_pol_filovir. DR InterPro; IPR014023; RNA_pol_cat. DR InterPro; IPR001016; RNA_pol_L_viral. DR Pfam; PF00946; Paramyx_RNA_pol; 1. DR PIRSF; PIRSF037548; RNA_pol_Filoviridae; 1. DR PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Methyltransferase; KW mRNA capping; mRNA processing; Multifunctional enzyme; KW Nucleotide-binding; Nucleotidyltransferase; RNA replication; KW RNA-directed RNA polymerase; S-adenosyl-L-methionine; Transferase; KW Virion. FT CHAIN 1 2212 Large structural protein. FT /FTId=PRO_0000245048. FT DOMAIN 625 809 RdRp catalytic. FT VARIANT 192 192 K -> R (in strain: Isolate Pennsylvania- FT 89). FT VARIANT 324 324 H -> R (in strain: Isolate Pennsylvania- FT 89). FT VARIANT 442 442 F -> V (in strain: Isolate Pennsylvania- FT 89). FT VARIANT 600 600 E -> G (in strain: Isolate Pennsylvania- FT 89). FT VARIANT 755 755 K -> E (in strain: Isolate Pennsylvania- FT 89). FT VARIANT 1374 1374 D -> G (in strain: Isolate Pennsylvania- FT 89). FT VARIANT 1487 1487 E -> D (in strain: Isolate Pennsylvania- FT 89). FT VARIANT 1679 1679 E -> A (in strain: Isolate Pennsylvania- FT 89). FT VARIANT 1896 1898 ASQ -> SSH (in strain: Isolate FT Pennsylvania-89). FT VARIANT 1909 1909 S -> SS (in strain: Isolate Pennsylvania- FT 89). SQ SEQUENCE 2212 AA; 252549 MW; C28CE580881136E3 CRC64; MATQHTQYPD ARLSSPIVLD QCDLVTRACG LYSSYSLNPQ LRQCKLPKHI YRLKFDTIVS KFLSDTPVAT LPIDYLVPIL LRSLTGHGDR PLTPTCNQFL DEIINYTLHD AAFLDYYLKA TGAQDHLTNI ATREKLKNEI LNNDYVHQLF FWHDLSILAR RGRLNRGNNR STWFVHDEFI DILGYGDYIF WKIPLSLLPV TIDGVPHAAT DWYQPTLFKE SILGHSQILS VSTAEILIMC KDIITCRFNT SLIASIAKLE DVDVSDYPDP SDILKIYNAG DYVISILGSE GYKIIKYLEP LCLAKIQLCS KFTERKGRFL TQMHLSVIND LRELISNRRL KDYQQEKIRD FHKILLQLQL SPQQFCELFS VQKHWGHPIL HSEKAIQKVK RHATILKALR PNVIFETYCV FKYNIAKHYF DSQGTWYSVI SDRNLTPGLN SFIKRNHFPS LPMIKDLLWE FYHLNHPPLF STKVISDLSI FIKDRATAVE QTCWDAVFEP NVLGYNPPNK FSTKRVPEQF LEQEDFSIES VLNYAQELHY LLPQNRNFSF SLKEKELNIG RTFGKLPYLT RNVQTLCEAL LADGLAKAFP SNMMVVTERE QKESLLHQAS WHHTSDDFGE NATVRGSSFV TDLEKYNLAF RYEFTAPFIE YCNHCYGVRN VFNWMHYLIP QCYMHVSDYY NPPHNVNLSN REYPPEGPSS YRGHLGGIEG LQQKLWTSIS CAQISLVEIK TGFKLRSAVM GDNQCITVLS VFPLKTDPEE QEQSAEDNAA RVAASLAKVT SACGIFLKPD ETFVHSGFIY FGKKQYLNGV QLPQSLKTAA RMAPLSDAIF DDLQGTLASI GTAFERAISE TRHILPCRIV AAFHTYFAVR ILQYHHLGFN KGIDLGQLSL SKPLDYGTIT LTLAVPQVLG GLSFLNPEKC FYRNFGDPVT SGLFQLRVYL EMVNMKDLFC PLISKNPGNC SAIDFVLNPS GLNVPGSQDL TSFLRQIVRR SITLTARNKL INTLFHASAD LEDEMVCKWL LSSNPVMSRF AADIFSRTPS GKRLQILGYL EGTRTLLASK IINNNSETPV LDKLRKITLQ RWNLWFSYLD HCDQLLADAL QKISCTVDLA QILREYTWSH ILEGRSLIGA TLPCMVEQFK VKWLGQYEPC PECLNKKGSN AYVSVAVKDQ VVSAWPNTSR ISWTIGSGVP YIGSRTEDKI GQPAIKPRCP SSALKEAIEL ASRLTWVTQG GSNSEQLIRP FLEARVNLSV SEVLQMTPSH YSGNIVHRYN DQYSPHSFMA NRMSNTATRL IVSTNTLGEF SGGGQAARDS NIIFQNVINL AVALYDIRFR NTNTSDIRHN RAHLHLTECC TKEVPAQYLT YTSALNLDLS RYRDNELIYD SNPLKGGLNC NLTIDSPLVK GPRLNMIEDD LLRFPHLSGW ELAKTVVQSI ISDNSNSSTD PISSGETRSF TTHFLTYPQI GLLYSFGAVL CFYLGNTILW TKKLDYEQFL YYLHNQLHNL PHRALRVFKP TFKHASVMSR LMEIDSNFSI YIGGTSGDRG LSDAARLFLR TAIASFLQFL KSWIIDRQKT IPLWIVYPLE GQQPESINEF LHKILGLLKQ GPKSIPKEVS IQNDGHLDLA ENNYVYNSKS TASNFFHASL AYWRSRKSRK TQDHNDFSRG DGTLTEPVRK FSSNHQSDEK YYNVTCGKSP KPQERKDFSQ YRLSNNGQTM SNHRKKGKFH KWNPCKMLME SQRGTVLTEG DYFQNNTPPT DDVSSPHRLI LPFFKLGNHN HAHDQDAQEL MNQNIKQYLH QLRSMLDTTI YCRFTGIVSS MHYKLDEVLL EYNSFDSAIT LAEGEGSGAL LLLQKYSTRL LFLNTLATEH SIESEVVSGF STPRMLLPIM QKVHEGQVTV ILNNSASQIT DITSSMWLSN QKYNLPCQVE IIMMDAETTE NLNRSQLYRA VYNLILDHID PQYLKVVVLK VFLSDIEGIL WINDYLAPLF GAGYLIKPIT SSARSSEWYL CLSNLISTNR RSAHQTHKAC LGVIRDALQA QVQRGVYWLS HIAQYATKNL HCEYIGLGFP SLEKVLYHRY NLVDTGLGPL SSVIRHLTNL QAEIRDLVLD YNLMRESRTQ TYHFIKTAKG RITKLVNDFL KFSLIVQALK NNSSWYTELK KLPEVINVCN RFYHTHNCEC QEKFFVQTLY LQRLRDAEIK LIERLTGLMR FYPEGLIYSN HT //