L_EBOSU
ID L_EBOSU Reviewed; 2210 AA.
AC Q5XX01;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
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 Human/Uganda/Gulu/2000) (SEBOV) (Sudan Ebola
OS virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX NCBI_TaxID=386033;
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].
RX PubMed=16139097; DOI=10.1016/j.virusres.2005.03.028;
RA Sanchez A., Rollin P.E.;
RT "Complete genome sequence of an Ebola virus (Sudan species) responsible for
RT a 2000 outbreak of human disease in Uganda.";
RL Virus Res. 113:16-25(2005).
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; AY729654; AAU43890.1; -; Genomic_RNA.
DR RefSeq; YP_138527.1; NC_006432.1.
DR PDB; 6YU8; X-ray; 1.84 A; A=1741-2046.
DR PDBsum; 6YU8; -.
DR SMR; Q5XX01; -.
DR PRIDE; Q5XX01; -.
DR ABCD; Q5XX01; 1 sequenced antibody.
DR GeneID; 3160771; -.
DR KEGG; vg:3160771; -.
DR Proteomes; UP000000277; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Host cytoplasm; Hydrolase; Methyltransferase;
KW mRNA capping; 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_0000245049"
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 1694..1736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 1757..1762
FT /evidence="ECO:0007829|PDB:6YU8"
FT HELIX 1777..1793
FT /evidence="ECO:0007829|PDB:6YU8"
FT HELIX 1812..1817
FT /evidence="ECO:0007829|PDB:6YU8"
FT TURN 1818..1820
FT /evidence="ECO:0007829|PDB:6YU8"
FT STRAND 1825..1831
FT /evidence="ECO:0007829|PDB:6YU8"
FT HELIX 1836..1843
FT /evidence="ECO:0007829|PDB:6YU8"
FT STRAND 1848..1853
FT /evidence="ECO:0007829|PDB:6YU8"
FT HELIX 1873..1878
FT /evidence="ECO:0007829|PDB:6YU8"
FT HELIX 1879..1883
FT /evidence="ECO:0007829|PDB:6YU8"
FT STRAND 1888..1892
FT /evidence="ECO:0007829|PDB:6YU8"
FT HELIX 1906..1910
FT /evidence="ECO:0007829|PDB:6YU8"
FT HELIX 1911..1913
FT /evidence="ECO:0007829|PDB:6YU8"
FT STRAND 1919..1923
FT /evidence="ECO:0007829|PDB:6YU8"
FT HELIX 1934..1946
FT /evidence="ECO:0007829|PDB:6YU8"
FT TURN 1950..1952
FT /evidence="ECO:0007829|PDB:6YU8"
FT STRAND 1955..1961
FT /evidence="ECO:0007829|PDB:6YU8"
FT HELIX 1965..1974
FT /evidence="ECO:0007829|PDB:6YU8"
FT HELIX 1976..1978
FT /evidence="ECO:0007829|PDB:6YU8"
FT STRAND 1979..1986
FT /evidence="ECO:0007829|PDB:6YU8"
FT STRAND 1996..2004
FT /evidence="ECO:0007829|PDB:6YU8"
FT HELIX 2016..2036
FT /evidence="ECO:0007829|PDB:6YU8"
SQ SEQUENCE 2210 AA; 251294 MW; 9FCCAF21F7AA0078 CRC64;
MMATQHTQYP DARLSSPIVL DQCDLVTRAC GLYSEYSLNP KLKTCRLPKH IYRLKYDTIV
LRFISDVPVA TIPIDYIAPM LINVLADSKN VPLEPPCLSF LDEIVNYTVQ DAAFLNYYMN
QIKTQEGVIT DQLKQNIRRV IHKNRYLSAL FFWHDLAILT RRGRMNRGNV RSTWFVTNEV
VDILGYGDYI FWKIPIALLP MNTANVPHAS TDWYQPNIFK EAIQGHTHII SVSTAEVLIM
CKDLVTSRFN TLLIAELARL EDPVSADYPL VDNIQSLYNA GDYLLSILGS EGYKIIKYLE
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 YFGKKQYLNG IQLPQSLKTA ARMAPLSDAI FDDLQGTLAS
IGTAFERSIS ETRHILPCRV AAAFHTYFSV RILQHHHLGF HKGSDLGQLA INKPLDFGTI
ALSLAVPQVL GGLSFLNPEK CLYRNLGDPV TSGLFQLKHY LSMVGMSDIF HALIAKSPGN
CSAIDFVLNP GGLNVPGSQD LTSFLRQIVR RSITLSARNK LINTLFHASA DLEDELVCKW
LLSSTPVMSR FAADIFSRTP SGKRLQILGY LEGTRTLLAS KMISNNAETP ILERLRKITL
QRWNLWFSYL DHCDPALMEA IQPIKCTVDI AQILREYSWA HILDGRQLIG ATLPCIPEQF
QTTWLKPYEQ CVECSSTNNS SPYVSVALKR NVVSAWPDAS RLGWTIGDGI PYIGSRTEDK
IGQPAIKPRC PSAALREAIE LTSRLTWVTQ GSANSDQLIR PFLEARVNLS VQEILQMTPS
HYSGNIVHRY NDQYSPHSFM ANRMSNTATR LMVSTNTLGE FSGGGQAARD SNIIFQNVIN
FAVALYDIRF RNTCTSSIQY HRAHIHLTNC CTREVPAQYL TYTTTLNLDL SKYRNNELIY
DSDPLRGGLN CNLSIDSPLM KGPRLNIIED DLIRLPHLSG WELAKTVLQS IISDSSNSST
DPISSGETRS FTTHFLTYPK IGLLYSFGAL ISFYLGNTIL CTKKIGLTEF LYYLQNQIHN
LSHRSLRIFK PTFRHSSVMS RLMDIDPNFS IYIGGTAGDR GLSDAARLFL RIAISTFLSF
VEEWVIFRKA NIPLWVIYPL EGQRSDPPGE FLNRVKSLIV GTEDDKNKGS ILSRSGEKCS
SNLVYNCKST ASNFFHASLA YWRGRHRPKK TIGATNATTA PHIILPLGNS DRPPGLDLNR
NNDTFIPTRI KQIVQGDSRN DRTTTTRFPP KSRSTPTSAT EPPTKMYEGS TTHQGKLTDT
HLDEDHNAKE FPSNPHRLVV PFFKLTKDGE YSIEPSPEES RSNIKGLLQH LRTMVDTTIY
CRFTGIVSSM HYKLDEVLWE YNKFESAVTL AEGEGSGALL LIQKYGVKKL FLNTLATEHS
IESEVISGYT TPRMLLPIMP KTHRGELEVI LNNSASQITD ITHRDWFSNQ KNRIPNDADI
ITMDAETTEN LDRSRLYEAV YTIICNHINP KTLKVVILKV FLSDLDGMCW INNYLAPMFG
SGYLIKPITS SAKSSEWYLC LSNLLSTLRT TQHQTQANCL HVVQCALQQQ VQRGSYWLSH
LTKYTTSRLH NSYIAFGFPS LEKVLYHRYN LVDSRNGPLV SITRHLALLQ TEIRELVTDY
NQLRQSRTQT YHFIKTSKGR ITKLVNDYLR FELVIRALKN NSTWHHELYL LPELIGVCHR
FNHTRNCTCS ERFLVQTLYL HRMSDAEIKL MDRLTSLVNM FPEGFRSSSV
