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   16-JUN-2009, entry version 23.
DE   RecName: Full=Large structural protein;
DE            Short=Protein L;
DE   AltName: Full=Transcriptase;
DE   AltName: Full=Replicase;
DE   Includes:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48;
DE   Includes:
DE     RecName: Full=mRNA (guanine-N(7)-)-methyltransferase;
DE              EC=2.1.1.56;
DE   Includes:
DE     RecName: Full=mRNA guanylyltransferase;
DE              EC=2.7.7.-;
GN   Name=L;
OS   Lake Victoria marburgvirus (strain Angola/2005) (MARV).
OC   Viruses; ssRNA negative-strand viruses; Mononegavirales; Filoviridae;
OC   Marburgvirus.
OX   NCBI_TaxID=378830;
OH   NCBI_TaxID=9407; Rousettus aegyptiacus (Egyptian rousette) (Egyptian fruit bat).
OH   NCBI_TaxID=9534; Cercopithecus aethiops (Green monkey) (Grivet).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Ang0126, Isolate Ang0214, Isolate Ang0215,
RC   Isolate Ang0754, Isolate Ang1379c, Isolate Ang1381, and
RC   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.,
RA   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: Displays RNA-directed RNA polymerase, mRNA guanylyl
CC       transferase, mRNA (guanine-N(7)-)-methyltransferase and poly(A)
CC       synthetase activities. The viral mRNA guanylyl transferase
CC       displays a different biochemical reaction than the cellular
CC       enzyme. The template is composed of the viral RNA tightly
CC       encapsidated by the nucleoprotein (N). Functions either as
CC       transcriptase or as replicase. The transcriptase synthesizes
CC       subsequently subgenomic RNAs, assuring their capping and
CC       polyadenylation by a stuttering mechanism. The replicase mode is
CC       dependent on intracellular N protein concentration. In this mode,
CC       the polymerase replicates the whole viral genome without
CC       recognizing the transcriptional signals (By similarity).
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
CC       adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm. Virion (By similarity).
CC   -!- SIMILARITY: Contains 1 RdRp catalytic domain.
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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   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006370; P:mRNA capping; IEA:UniProtKB-KW.
DR   GO; GO:0006410; P:transcription, RNA-dependent; IEA:UniProtKB-KW.
DR   InterPro; IPR017235; RNA-dir_RNA_pol_filovir.
DR   InterPro; IPR014023; RNA_pol_cat.
DR   InterPro; IPR001016; RNA_pol_L_viral.
DR   Pfam; PF00946; Paramyx_RNA_pol; 1.
DR   PIRSF; PIRSF037548; RNA_pol_Filoviridae; 1.
DR   PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Methyltransferase;
KW   mRNA capping; mRNA processing; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; RNA replication;
KW   RNA-directed RNA polymerase; S-adenosyl-L-methionine; Transferase;
KW   Virion.
FT   CHAIN         1   2331       Large structural protein.
FT                                /FTId=PRO_0000314970.
FT   DOMAIN      628    812       RdRp catalytic.
FT   COMPBIAS   1362   1365       Poly-Ser.
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
//