L_EBOSM
ID L_EBOSM Reviewed; 2210 AA.
AC Q66802;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 103.
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 Sudan ebolavirus (strain Maleo-79) (SEBOV) (Sudan Ebola virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX NCBI_TaxID=128949;
OH NCBI_TaxID=77231; Epomops franqueti (Franquet's epauleted fruit bat).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Sanchez A., Trappier S., Nichol S.T.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; U23458; AAA79970.1; -; Genomic_RNA.
DR SMR; Q66802; -.
DR PRIDE; Q66802; -.
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..2210
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000222168"
FT DOMAIN 626..810
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1802..2000
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT REGION 1693..1740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1693..1736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2210 AA; 251258 MW; F50E6B624951AEA4 CRC64;
MMATQHTQYP DARLSSPIVL DQCDLVTRAC GLYSEYSLNP KLRTCRLPKH IYRLKYDAIV
LRFISDVPVA TIPIDYIAPM LINVLADSKN APLEPPCLSF LDEIVNYTVQ DAAFLNYYMN
QIKTQEGVIT DQLKQNIRRV IHKNRYLSAL FFWHDLSILT RRGRMNRGNV RSTWFVTNEV
VDILGYGDYI FWKIPIALLP MNSANVPHAS TDWYQPNIFK EAIQGHTHII SVSTAEVLIM
CKDLVTSRFN TLLIAELARL EDPVSADYPL VDDIQSLYNA GDYLLSILGS EGYQIIKYLE
PLCLAKIQLC SQYTERKGRF LTQMHLAVIQ TLRELLLNRG LKKSQLSKIR EFHQLLLRLR
STPQQLCELF SIQKHWGHPV LHSEKAIQKV KNHATVLKAL RPIIIFETYC VFKYSVAKHF
FDSQGTWYSV ISDRCLTPGL NSYIRRNQFP PLPMIKDLLW EFYHLDHPPL FSTKIISDLS
IFIKDRATAV EQTCWDAVFE PNVLGYSPPY RFNTKRVPEQ FLEQEDFSIE SVLQYAQELR
YLLPQNRNFS FSLKEKELNV GRTFGKLPYL TRNVQTLCEA LLADGLAKAF PSNMMVVTER
EQKESLLHQA SWHHTSDDFG EHATVRGSSF VTDLEKYNLA FRYEFTAPFI KYCNQCYGVR
NVFDWMHFLI PQCYMHVSDY YNPPHNVTLE NREYPPEGPS AYRGHLGGIE GLQQKLWTSI
SCAQISLVEI KTGFKLRSAV MGDNQCITVL SVFPLESSPN EQERCAEDNA ARVAASLAKV
TSACGIFLKP DETFVHSGFI YFGPKQYLNG IQLPQSLKTA ARMAPLSDAI FDDLQGTLAS
IGTAFERSIS ETRHILPSRV AAAFHTYFSV RILQHHHLGF HKGSDLGQLA INKPLDFGTI
ALSLAVPQVL GGLSFLNPEK CLYRNLGDPV TSGLFQLKHY LSMVGMSDIF HALVAKSPGN
CSAIDFVLNP GGLNVPGSQD LTSFLRQIVR RSITLSARNK LINTLFHASA DLEDELVCKW
LLSSTPVMSR FAADIFSRTP SGKRLQILGY LEGTRTLLAS KMISNNAETP ILERLRKITL
QRWNLWFSYL DHCDSALMEA IQPIRCTVDI AQILREYSWA HILGGRQLIG ATLPCIPEQF
QTTWLKPYEQ CVECSSTNNS SPYVSVALKR NVVSAWPDAS RLGWTIGDGI PYIGSRTEDK
IGQPAIKPRC PSAALREAIE LTSRLTWVTQ GSANSDQLIR PFLEARVNLS VQEILQMTPS
HYSGNIVHRY NDQYSPHSFM ANRMSNTATR LMVSTNTLGE FSGGGQAARD SNIIFQNVIN
FAVALYDIRF RNTCTSSIQY HRAHIHLTDC CTREVPAQYL TYTTTLNLDL SKYRNNELIY
DSEPLRGGLN CNLSIDSPLM KGPRLNIIED DLIRLPHLSG WELAKTVLQS IISDSSNSST
DPISSGETRS FTTHFLTYPK IGLLYSFGAL ISFYLGNTIL CTKKIGLTEF LYYLQNQIHN
LSHRSLRIFK PTFRHSSVMS RLMDIDPNFS IYIGGTAGDR GLSDAARLFL RIAISTFLSF
VEEWVIFRKA NIPLWVVYPL EGQRPDPPGE FLNRVKSLIV GIEDDKNKGS ILSRSEEKCS
SNLVYNCKST ASNFFHASLA YWRGRHRPKK TIGATKATTA PHIILPLGNS DRPPGLDLNQ
SNDTFIPTRI KQIVQGDSRN DRTTTTRLPP QSRSTPTSAT EPPTKIYEGS TTYRGKSTDT
HLDEGHNAKE FPFNPHRLVV PFFKLTKDGE YSIEPSPEES RSNIKGLLQH LRTMVDTTIY
CRFTGIVSSM HYKLDEVLWE YNKFESAVTL AEGEGSGALL LIQKYGVKKL FLNTLATEHS
IESEVISGYT TPRMLLSVMP RTHRGELEVI LNNSASQITD ITHRDWFSNQ KNRIPNDVDI
ITMDAETTEN LDRSRLYEAV YTIICNHINP KTLKVVILKV FLSDLDGMCW INNYLAPMFG
SGYLIKPITS SARSSEWYLC LSNLLSTLRT TQHQTQANCL HVVQCALQQQ VQRGSYWLSH
LTKYTTSRLH NSYIAFGFPS LEKVLYHRYN LVDSRNGPLV SITRHLALLQ TEIRELVTDY
NQLRQSRTQT YHFIKTSKGR ITKLVNDYLR FELVIRALKN NSTWHHELYL LPELIGVCHR
FNHTRNCTCS ERFLVQTLYL HRMSDAEIKL MDRLTSLVNM FPEGFRSSSV
