L_MABVA
ID L_MABVA Reviewed; 2331 AA.
AC Q1PD54;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
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 Angola/2005) (MARV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Marburgvirus.
OX NCBI_TaxID=378830;
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].
RC STRAIN=Isolate Ang0126, Isolate Ang0214, Isolate Ang0215, Isolate Ang0754,
RC Isolate Ang1379c, Isolate Ang1381, and Isolate Ang1386;
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}.
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DR EMBL; DQ447653; ABE27018.1; -; Genomic_RNA.
DR EMBL; DQ447654; ABE27025.1; -; Genomic_RNA.
DR EMBL; DQ447655; ABE27032.1; -; Genomic_RNA.
DR EMBL; DQ447656; ABE27039.1; -; Genomic_RNA.
DR EMBL; DQ447657; ABE27046.1; -; Genomic_RNA.
DR EMBL; DQ447658; ABE27053.1; -; Genomic_RNA.
DR EMBL; DQ447659; ABE27060.1; -; Genomic_RNA.
DR SMR; Q1PD54; -.
DR Proteomes; UP000008242; Genome.
DR Proteomes; UP000097432; Genome.
DR Proteomes; UP000102513; Genome.
DR Proteomes; UP000115353; Genome.
DR Proteomes; UP000130744; Genome.
DR Proteomes; UP000168007; Genome.
DR Proteomes; UP000171838; 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; IPR001611; Leu-rich_rpt.
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; PS51450; LRR; 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..2331
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000314970"
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 2331 AA; 266716 MW; B1BCB816FC42C37D CRC64;
MQHPTQYPDA RLSSPIILDQ CDLLARSLGL YSHYSHNPKL RNCRIPHHIY RLRNSTALKT
FLQNCSILTV PFHSIWDHIL TSIQYDAINH VDDFKYLLPS ELVKYANWDN EFLKAYLNKI
LGLNHVFPTS ARSQCEDFSP KENPYYWGML LLVHLSQLAR RIKGQRGSLR SNWKFIGTDL
ELFGIADFVI FKVPVKTIIR NAVSLQASKP GLRVWYRDQN LTPYLCDDEF IVSVASYECF
IMIKDVFIER YNTWEICARA WLEDSDGADY PPLDVLGELY NQGDQIIAMY LEDGFKLIKH
LEPLCVSCIQ THGIFTPRKY WFQSQMIKSY YDELCCLNLK LQISDNKAEC AQNFIKTIIQ
AKLTPQQYCE LFSLQKHWGH PVLYNDVALD KVKKHAQSTK ILKPKVMFET FCVFKFIVAK
NHYHSQGSWY KTTHDLHLTP YLRQHIVSNS FPSQAEIYQH LWEWYFVEHE PLFSTKIISD
LSIFIKDRAT AVNQECWDSV FDRSVLGYNP PVRFQSKRVP EQFLGQADFS LNQILDFAEK
LEYLAPSYRN FSFSLKEKEL NIGRTFGKLP YRVRNVQTLA EALLADGLAK AFPSNMMVVT
EREQKEALLH QASWHHNSAS IGENAIVRGA SFVTDLEKYN LAFRYEFTRH FIDYCNRCYG
VKNLFDWMHF LIPLCYMHVS DFYSPPHCVT EDNRNNPPDC ANAYHYHLGG IEGLQQKLWT
CISCAQITLV ELKTKLKLKS SVMGDNQCIT TLSLFPVDAP NDYQENEAEL NAARVAVELA
ITTGYSGIFL KPEETFVHSG FIYFGKKQYL NGVQLPQSLK TMARCGPLSD SIFDDLQGSL
ASIGTSFERG TSETRHIFPS RWIASFHSML AINLLNQNHL GFPLGFNIDI SCFKKPLTFS
EKLIALITPQ VLGGLSFLNP EKLFYRNISD PLTSGLFQLK NALEFLEKEE LFYILIAKKP
GLADASDFVM NPLGLNVPGS REIITFLRQT VRENITITSQ NRIINSLFHI GSDLEDQRVC
EWLLSSNPVM SRFAADIFSR TPSGKRLQVL GYLEGTRTLL ASRTISLTTE GTMLMKLREL
TRNRWKSWFS YIDALDDDLS ESLEKFTCTV DVANFLRAYS WSDVLKGKRL IGATLPCLLE
QFKVKWINLS EDLREQFNLS SDAESTINFL PYDCKELRLG GSNDTELNYV SCALDRKVVQ
KHPSVNRLAW TIGNRAPYIG SRTEDKIGYP PLRVNCPSAA LKEAIEMVSR LLWVTQGTAD
REKLLIPLLN SRVNLDYQTV LNFLPTHYSG NIVHRYNDQY GQHSFMANRM SNTSTRAIIS
TNTLGKYAGG GQAAIDSNII FQNTINLGVA VLDIALSLAK LSSSSNVTFR LMLSKCCTRH
VPSEYLFFDK PLDVDLNKYM DNELVYDNDP LCSGIKGRLG RVSRSTLSLS LNVSDIGSYD
FPTIAAWTLG ETIVGSIFSD ESSQSTDPIS SGCTKTFVTH FLVYPVESIF YAFGANLIVE
SLSLNRIKSI KNLSDLTFLI SSTIRNLSHR SLRILQSTFR HELVLTRLAH HIPLISLMLG
GSAGEKSSSD AVRLFLTASY QNFINNFSCL IKKGQSSLPV WLYFPSEGQQ LKPILKILQR
LSDLFSPDKV QKRKILADTC YPVDSFWVYP SKSTRTNHYY ASLNYWRDKA NKVKNTPFSH
LINCSFLELS SHTISVPSNQ QMTNSKYIVH PENIPETNAR TELMNYGSTT LQGMDIKMPL
SEQNLVENCR PSKGIRCKDN QKIIKHDQRY GKKESSSQQM LPKDNMQTPA YIHGSSPSQT
IIKSLDVHED FDASKVILNS ETNNPNLTDC TLNTKFLTTL TGTEILGTSP LQPSRYSSTS
KERSLLSREQ ASYLYVDCSN IPSISLDPGF RNMSDQNQVQ MLINAYKRDL HACFDSNQFC
RFTGVVSSMH YKLYDLLPPG ELRKAICLAE GEGSGARLLL KWKETDYLFF NTLATDSQQE
AEILSGRVIP RMLYNIDKLS VLLESRRLIL NNLTIQITDI TNPLWLDSVI QYLPEDSDIL
TMDAETTKDE TREQLYKTIV NIWTRTSPNI PKISIIKVFL LDYEGTLFLM RNAIQYYGQV
QLKKPYSSNA KNSEWYLCCG KRRIQRLQID FSDQVGIFLI CKAMSRQRQA IPYWLKHIEK
NYPASLHEFF LTLGFPSLES SFCHRYTIPF SEGKALFHKV QSYVRQGKQH LHSLMLDYEN
NSPLLDLRNH FICSLRGKIT KYYNDILKLN LVIKAVEKGK NWSQLVETLP NMHSVCIVHV
DHECFGCEKR LLLKLDFIRN TKIAEQKLLN RVIGYILFFP FGLFKSGSLR A
