ID   L_EBOZM                 Reviewed;        2212 AA.
AC   Q05318; O39794; Q773N0; Q8JS59; Q9DQD1;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   16-JUN-2009, entry version 56.
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   Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus).
OC   Viruses; ssRNA negative-strand viruses; Mononegavirales; Filoviridae;
OC   Ebola-like viruses.
OX   NCBI_TaxID=128952;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=77231; Epomops franqueti (Franquet's epauleted bat).
OH   NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   MEDLINE=99171703; PubMed=10073695;
RA   Volchkov V.E., Volchkova V.A., Chepurnov A.A., Blinov V.M.,
RA   Netesov S.V., Feldmann H.;
RT   "Characterization of the L gene and 5' trailer region of Ebola
RT   virus.";
RL   J. Gen. Virol. 80:355-362(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-54.
RX   MEDLINE=94055391; PubMed=8237108; DOI=10.1016/0168-1702(93)90063-S;
RA   Sanchez A., Kiley M.P., Holloway B.P., Auperin D.D.;
RT   "Sequence analysis of the Ebola virus genome: organization, genetic
RT   elements, and comparison with the genome of Marburg virus.";
RL   Virus Res. 29:215-240(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Wilson J.A., Kondig J.P., Kuehne A.I., Hart M.K.;
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
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 transcriptase
CC       stutters on a specific sequence, resulting on a cotranscriptional
CC       editing of the glycoprotein (GP) mRNA. 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: Virion. Host cytoplasm.
CC   -!- SIMILARITY: Contains 1 RdRp catalytic domain.
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DR   EMBL; X67110; CAA47483.1; -; Genomic_RNA.
DR   EMBL; AF272001; AAG40171.1; -; Genomic_RNA.
DR   EMBL; AF086833; AAD14589.1; -; Genomic_RNA.
DR   EMBL; L11365; AAB81007.1; -; Genomic_RNA.
DR   EMBL; AY142960; AAN37511.1; -; Genomic_RNA.
DR   EMBL; AF499101; AAM76038.1; -; Genomic_RNA.
DR   RefSeq; NP_066251.1; -.
DR   GeneID; 911824; -.
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   2212       Large structural protein.
FT                                /FTId=PRO_0000222167.
FT   DOMAIN      625    809       RdRp catalytic.
FT   VARIANT     820    820       T -> A.
FT   VARIANT     934    934       F -> L.
FT   VARIANT    1532   1532       I -> V.
SQ   SEQUENCE   2212 AA;  252724 MW;  5B07EDDC370E2934 CRC64;
     MATQHTQYPD ARLSSPIVLD QCDLVTRACG LYSSYSLNPQ LRNCKLPKHI YRLKYDVTVT
     KFLSDVPVAT LPIDFIVPVL LKALSGNGFC PVEPRCQQFL DEIIKYTMQD ALFLKYYLKN
     VGAQEDCVDE HFQEKILSSI QGNEFLHQMF FWYDLAILTR RGRLNRGNSR STWFVHDDLI
     DILGYGDYVF WKIPISMLPL NTQGIPHAAM DWYQASVFKE AVQGHTHIVS VSTADVLIMC
     KDLITCRFNT TLISKIAEIE DPVCSDYPNF KIVSMLYQSG DYLLSILGSD GYKIIKFLEP
     LCLAKIQLCS KYTERKGRFL TQMHLAVNHT LEEITEMRAL KPSQAQKIRE FHRTLIRLEM
     TPQQLCELFS IQKHWGHPVL HSETAIQKVK KHATVLKALR PIVIFETYCV FKYSIAKHYF
     DSQGSWYSVT SDRNLTPGLN SYIKRNQFPP LPMIKELLWE FYHLDHPPLF STKIISDLSI
     FIKDRATAVE RTCWDAVFEP NVLGYNPPHK FSTKRVPEQF LEQENFSIEN VLSYAQKLEY
     LLPQYRNFSF SLKEKELNVG RTFGKLPYPT RNVQTLCEAL LADGLAKAFP SNMMVVTERE
     QKESLLHQAS WHHTSDDFGE HATVRGSSFV TDLEKYNLAF RYEFTAPFIE YCNRCYGVKN
     VFNWMHYTIP QCYMHVSDYY NPPHNLTLEN RDNPPEGPSS YRGHMGGIEG LQQKLWTSIS
     CAQISLVEIK TGFKLRSAVM GDNQCITVLS VFPLETDADE QEQSAEDNAA RVAASLAKVT
     SACGIFLKPD ETFVHSGFIY FGKKQYLNGV QLPQSLKTAT RMAPLSDAIF DDLQGTLASI
     GTAFERSISE TRHIFPCRIT AAFHTFFSVR ILQYHHLGFN KGFDLGQLTL GKPLDFGTIS
     LALAVPQVLG GLSFLNPEKC FYRNLGDPVT SGLFQLKTYL RMIEMDDLFL PLIAKNPGNC
     TAIDFVLNPS GLNVPGSQDL TSFLRQIVRR TITLSAKNKL INTLFHASAD FEDEMVCKWL
     LSSTPVMSRF AADIFSRTPS GKRLQILGYL EGTRTLLASK IINNNTETPV LDRLRKITLQ
     RWSLWFSYLD HCDNILAEAL TQITCTVDLA QILREYSWAH ILEGRPLIGA TLPCMIEQFK
     VFWLKPYEQC PQCSNAKQPG GKPFVSVAVK KHIVSAWPNA SRISWTIGDG IPYIGSRTED
     KIGQPAIKPK CPSAALREAI ELASRLTWVT QGSSNSDLLI KPFLEARVNL SVQEILQMTP
     SHYSGNIVHR YNDQYSPHSF MANRMSNSAT RLIVSTNTLG EFSGGGQSAR DSNIIFQNVI
     NYAVALFDIK FRNTEATDIQ YNRAHLHLTK CCTREVPAQY LTYTSTLDLD LTRYRENELI
     YDSNPLKGGL NCNISFDNPF FQGKRLNIIE DDLIRLPHLS GWELAKTIMQ SIISDSNNSS
     TDPISSGETR SFTTHFLTYP KIGLLYSFGA FVSYYLGNTI LRTKKLTLDN FLYYLTTQIH
     NLPHRSLRIL KPTFKHASVM SRLMSIDPHF SIYIGGAAGD RGLSDAARLF LRTSISSFLT
     FVKEWIINRG TIVPLWIVYP LEGQNPTPVN NFLYQIVELL VHDSSRQQAF KTTISDHVHP
     HDNLVYTCKS TASNFFHASL AYWRSRHRNS NRKYLARDSS TGSSTNNSDG HIERSQEQTT
     RDPHDGTERN LVLQMSHEIK RTTIPQENTH QGPSFQSFLS DSACGTANPK LNFDRSRHNV
     KFQDHNSASK REGHQIISHR LVLPFFTLSQ GTRQLTSSNE SQTQDEISKY LRQLRSVIDT
     TVYCRFTGIV SSMHYKLDEV LWEIESFKSA VTLAEGEGAG ALLLIQKYQV KTLFFNTLAT
     ESSIESEIVS GMTTPRMLLP VMSKFHNDQI EIILNNSASQ ITDITNPTWF KDQRARLPKQ
     VEVITMDAET TENINRSKLY EAVYKLILHH IDPSVLKAVV LKVFLSDTEG MLWLNDNLAP
     FFATGYLIKP ITSSARSSEW YLCLTNFLST TRKMPHQNHL SCKQVILTAL QLQIQRSPYW
     LSHLTQYADC ELHLSYIRLG FPSLEKVLYH RYNLVDSKRG PLVSITQHLA HLRAEIRELT
     NDYNQQRQSR TQTYHFIRTA KGRITKLVND YLKFFLIVQA LKHNGTWQAE FKKLPELISV
     CNRFYHIRDC NCEERFLVQT LYLHRMQDSE VKLIERLTGL LSLFPDGLYR FD
//