L_EBORE
ID L_EBORE Reviewed; 2212 AA.
AC Q91DD4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 23-FEB-2022, entry version 93.
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 Reston ebolavirus (strain Philippines-96) (REBOV) (Reston Ebola virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX NCBI_TaxID=129003;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9541; Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OH NCBI_TaxID=77225; Pteropodinae.
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11722021; DOI=10.1007/s007050170049;
RA Ikegami T., Calaor A.B., Miranda M.E., Niikura M., Saijo M., Kurane I.,
RA Yoshikawa Y., Morikawa S.;
RT "Genome structure of Ebola virus subtype Reston: differences among Ebola
RT subtypes.";
RL Arch. Virol. 146:2021-2027(2001).
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 -!- SUBCELLULAR LOCATION: Host cytoplasm. Virion {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB050936; BAB69010.1; -; Genomic_RNA.
DR SMR; Q91DD4; -.
DR PRIDE; Q91DD4; -.
DR Proteomes; UP000002322; 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 GO; GO:0039689; P:negative stranded viral RNA replication; ISS:UniProtKB.
DR GO; GO:0039697; P:negative stranded viral RNA transcription; ISS:UniProtKB.
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 InterPro; IPR017235; RNA-dir_pol_L_filovirus.
DR Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 1.
DR PIRSF; PIRSF037548; RNA_pol_Filoviridae; 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; RNA-directed RNA polymerase;
KW S-adenosyl-L-methionine; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..2212
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000245047"
FT DOMAIN 625..809
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1803..2001
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
SQ SEQUENCE 2212 AA; 252708 MW; 82100B1C4BF79DDC CRC64;
MATQHTQYPD ARLSSPIVLD QCDLVTRACG LYSSYSLNPQ LRQCKLPKHI YRLKFDTIVS
KFLSDTPVAT LPIDYLVPIL LRSLTGHGDR PLTPTCNQFL DGIINYTLHD AAFLDYYLKA
TGAQDHLTNI TTREKLKNEI 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 VFPLETDPEE QEQSAEDNAA RVAASLAKVT
SACGIFLKPE ETFVHSGFIY FGKKQYLNGV QLPQSLKTAA RMAPLSDAIF DDLQGTLASI
GTAFERAISE TRHILPCRIV AAFHTYFAVR ILQYHHLGFN KGIDLGQLSL SKPLDYGTIT
LTLAVPQVLG GLSFLNPEKC FYRNFGDPVT SGLFQLRVYL EMVNMKDLFY PLISKNPGNC
SAIDFVLNPS GLNVPGSQDL TSFLRQIVRR SITLTARNKL INTLFHASAD LEDEMVCKWL
LSSNPVMSRF AADIFSRTPS GKRLQILGYL EGTRTLLASK IINNNSETPV LDKLRKITLQ
RWNLWFSYLD HCDQLLADAL QKISCTVDLA QILREYTWSH ILEGRPLIGA TLPCMVEQFK
VKWLRQYEPC PECLNKKGSN AYVSVAVKDQ VVSAWPNTSR ISWTIGSGVP YIGSRTEDKI
GQPAIKPRCP SSALKEAIEL ASRLTWVTQG SSNSEQLIRP FLEARVNLSV SEVLQMTPSH
YSGNIVHRYN DQYSPHSFMA NRMSNTATRL IVSTNTLGEF SGGGQAARDS NIIFQNVINL
AVALYDIRFR NTNTSDIRHN RAHLHLTECC TKEVPAQYLT YTSALNLDLS RYRDNELIYD
SNPLRGGLNC NLTMDSPLVK GPRLNMIEDD LLRFPHLSGW ELAKTVVQSI ISDNSNSSTD
PISSGETRSF TTHFLTYPQI GLLYSFGAVL CFYLGNTILW TKKLDYEQFL YYLHNQLHNL
PHRALRVFKP TFKHASVMSR LMEIDSNFSI YIGGTSGDRG LSDAARLFLR TAIASFLQFL
KSWIIDRQKA IPLWIVYPLE GQQPESINEF LHKIFGLLKQ GPKNIPKEVS IQNDGHLDLA
ENNYVYNSKS TASNFFHASL AYWRSRKSRK TQDHNDFSRG DGTLTEPVCK FSSNHQSDEK
YYNVTCGKSP KPQERKDFSQ YRLSNNGQTM SNHRKKGKFH KWNPCKVLME SQRGTVLKEG
DYFQNNTPPT DDVSSPHRLI LPFFKLGNHN HAHDQDAQEL INQNIKQYLH QLRSMLDTTI
YCRFTGIVSS MHYKLDEVLL EYNSFDSAIT LAEGEGSGAL LLLQKYSTRL LFLNTLATEH
SIESEVVSGF STPRMLLPIM QKVHEGQVTV ILNNSASQIT DITSSMWLSN QKYNLPCQVE
IITMDAETTE NLNRSQLYRA VYNLILDHID PQYLKVVVLK VFLSDIEGIL WINDYLAPLF
GAGYLIKPIT SSARSSEWYL CLSNLISTNR RSAHQTHKAC LGVIRDALQA QVQRGVYWLS
HIAQYATKNL HCEYICLGFP PLEKVLYHRY NLVDTGLGPL SSVIRHLTNL QAEIRDLVLD
YTLMRESRTQ TYHFIKTAKG RITKLVNDFL KFSLIVQALK NNSSWYTELK KLPEVINVCN
RFYHTHSCEC QEKFFVQTLY LQRLRDAEIK LIERLTGLMR FYPEGLIYSN HT
