L_MABVR
ID L_MABVR Reviewed; 2327 AA.
AC Q1PDC4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
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 Lake Victoria marburgvirus (strain Ravn-87) (MARV) (Marburg virus (strain
OS Kenya/Ravn/1987)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Marburgvirus.
OX NCBI_TaxID=378809;
OH NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9407; Rousettus aegyptiacus (Egyptian rousette) (Egyptian fruit bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16775337; DOI=10.1128/jvi.00069-06;
RA Towner J.S., Khristova M.L., Sealy T.K., Vincent M.J., Erickson B.R.,
RA Bawiec D.A., Hartman A.L., Comer J.A., Zaki S.R., Stroeher U.,
RA Gomes da Silva F., del Castillo F., Rollin P.E., Ksiazek T.G., Nichol S.T.;
RT "Marburgvirus genomics and association with a large hemorrhagic fever
RT outbreak in Angola.";
RL J. Virol. 80:6497-6516(2006).
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; DQ447649; ABE27074.1; -; Genomic_RNA.
DR SMR; Q1PDC4; -.
DR Proteomes; UP000008239; 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; Reference proteome; RNA-directed RNA polymerase;
KW S-adenosyl-L-methionine; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..2327
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000314972"
FT DOMAIN 628..812
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1921..2118
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
SQ SEQUENCE 2327 AA; 266524 MW; 3F4516E0D40608F1 CRC64;
MQHPTQYPDA RLSSPIILDQ CDLLTRSLGL YSHYSHNPKL RNCRIPYHIY RLRNSTALKT
FLQNCSILTV PFHSIWDHII TSIQHDAINH INDFKYLLPS ELIKYANWDN EFLRVFLNKI
LRLDHAFTNS AKLQCEDFSP KENPYYWGML LLVHLSQLAR RIKGQRGSLR SNWKFIGVDL
ELFGIADFVI FKVPIKAIIR NATSLQASKP GLKTWYRDQN LTPYLCDDEF VVSIASYECF
IMIKDVFIER YNTWEICARA WVEDNEEADY PPLGILRDLY NQGDQIITMY LEDGFKLIKH
LEPLCVSCIQ TYGIFTPRKY WFQSQMIKSY YDELQSLNLK LQIPDNRTEC AQNFIKTIIQ
AKLTPQQYCE LFSLQKHWGH PVLYNDVALD KVKKHAQSTK ILKPKVMFET FCVFKFIVAK
NHYHSQGSWY KTTHDLHLTP YLRQHIVSNS FPSQAEIYQH LWEWYFVEHE PLFSTKIISD
LSIFIKDRAT AVNRECWDSV FDRSVLGYNP PVRFQSKRVP EQFLGQADFS LNQILDFAEK
LEYLAPSYRN FSFSLKEKEL NIGRTFGKLP YRVRNVQTLA EALLADGLAK AFPSNMMVVT
EREQKEALLH QASWHHNSAS IGENAIVRGA SFVTDLEKYN LAFRYEFTRH FIDYCNRCYG
VKNLFDWMHF LIPLCYMHVS DFYSPPHCVT ENNRNNPPDC ANAYHYHLGG IEGLQQKLWT
CISCAQITLV ELKTKLKLKS SVMGDNQCIT TLSLFPIDAP NDYQENEAEL NAARVAVELA
ITTGYSGIFL KPEETFVHSG FIYFGKKQYL NGVQLPQSLK TMARCGPLSD SIFDDLQGSL
ASIGTSFERG ASETRHIFPS RWIAAFHSML AVNLLNQNHL GFPLGFSIDV SCFKKPLTFS
EKLIALITPQ VLGGLSFLNP EKLFYRNISD PLTSGLFQLR NALEFLRKEE LFYILIAKKP
GLADASDFVM NPLGLNVPGS REIITFLRQT VRENITITSQ NRIINSLFHI GSDLEDQRVC
EWLLSSNPVM SRFAADIFSR TPSGKRLQVL GYLEGTRTLL ASRTISLTTE GTMLMRLREL
TKSRWKSWFS YIDALDDDLS ESLEKFICTV DVANFLRAYS WSDVLKGKRL IGATLPCLLE
QFNVKWVNLS EDLKEQFKLS SDLGSPTDLL QYDCNGLHSK GADNAELNYV SCALDRKIVQ
KHPSDNRLAW TIGNRAPYIG SRTEDKIGYP PLRVNCPSAA LKEAIEMVSR LLWVTQGTAD
REKLLIPLLN SRVNLDYQTV LNFLPTHYSG NIVHRYNDQY GQHSFMANRM SNTSTRAIIS
TNTLGKYAGG GQAAVDSNII FQNTINLGVA VLDITLSLSK LSSTSNVSFR LMLSKCCTRH
VPSEYLFFDK PLDVDLNKYM DNELVYDNDP LCSGIKGRLG RVSRSTLSLS LNVSDIGSYD
FPTIAAWTLG ETIIGSIFSD ESSQSTDPIS SGCTKTFVTH FLVYPVESIF YAFGANLIVE
SLSLSRINSI KSLSDLTFLI SSTIRNLSHR SLRILQSTFR HELVLTRLAH HIPLISLMLG
GSAGEKSSSD AVRLFLTASY QNFINNFSCL MRKNQSPLPV WLYFPSEGQQ LKPILKILQR
LSCLLTTKKV QNHRPVADTC FLTDNFWVYP SKSTRTNHYY ASLNYWRDKA NKIKNTSFSH
LINYSFSEPS LHASSISSSQ EVVNLKHTSR LDETPNMSER AQSTNHEPTA LQEVCTEIPY
SEQDPAKSYL LLENTRFRDD QKILRHDQKA ERGEPLSLQV SSRGCLQALT CPHHPSPSQT
TTEPLSMLRN CDAIKAALRS ETNDPRLMSS ILDMRSLKTP MRIESRNTSL LQPSECLSTS
KGKSVLSREQ ASYLYVDCSN ISSISLDSGF RNMSDRNQVQ MLINTYKRDL YTCFDSNQFC
RFTGVVSSMH YKLYDLLPAG KLGKAICLAE GEGSGARLLL KWKETDYLFF NTLATDSQQE
AEILSGRVIP RMLYNIDKLS VLLESRKLIL NNLTIQITDI TNPLWLDSVI QYLPEDSDIL
TMDAETTKEE TREQLYKTII NIWARTSPNI PKTSIIKVFL LDYGGTLFLM KNAIQYYGQV
QLKKPYSSNA KNSEWYLCCG KRRVQRLRVD FPDQVGIFLI CKAMSRQRQA IPYWLKHIEK
NYPASLHEFF ITLGFPSLES SFCHRYTIPF TEGTALFHKV QSYVRQGRQH LHSLMLDYEN
NSPLLDLRNH FICSLRGKIT KYYNDILKLN LVVRAVERGK NWSQLVESLP NMHSVCITHV
DHECIGCERR LLLKLDFVRN TKIAEQKLLN RVIGYILFFP FGFSRPK
