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RNA-directed RNA polymerase L (Protein L) (Large structural protein) (Replicase) (Transcriptase) [Includes: RNA-directed RNA polymerase (EC 2.7.7.48); mRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.56); GDP polyribonucleotidyltransferase (EC 2.7.7.88); Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 (EC 2.1.1.296)]

 A0A0S0HDC5_9MONO        Unreviewed;      2212 AA.
A0A0S0HDC5;
17-FEB-2016, integrated into UniProtKB/TrEMBL.
17-FEB-2016, sequence version 1.
30-AUG-2017, entry version 15.
RecName: Full=RNA-directed RNA polymerase L {ECO:0000256|PIRNR:PIRNR037548};
Short=Protein L {ECO:0000256|PIRNR:PIRNR037548};
AltName: Full=Large structural protein {ECO:0000256|PIRNR:PIRNR037548};
AltName: Full=Replicase {ECO:0000256|PIRNR:PIRNR037548};
AltName: Full=Transcriptase {ECO:0000256|PIRNR:PIRNR037548};
Includes:
RecName: Full=RNA-directed RNA polymerase {ECO:0000256|PIRNR:PIRNR037548};
EC=2.7.7.48 {ECO:0000256|PIRNR:PIRNR037548};
Includes:
RecName: Full=mRNA (guanine-N(7)-)-methyltransferase {ECO:0000256|PIRNR:PIRNR037548};
EC=2.1.1.56 {ECO:0000256|PIRNR:PIRNR037548};
Includes:
RecName: Full=GDP polyribonucleotidyltransferase {ECO:0000256|PIRNR:PIRNR037548};
EC=2.7.7.88 {ECO:0000256|PIRNR:PIRNR037548};
Includes:
RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 {ECO:0000256|PIRNR:PIRNR037548};
EC=2.1.1.296 {ECO:0000256|PIRNR:PIRNR037548};
Name=L {ECO:0000313|EMBL:ALG01626.1};
Zaire ebolavirus.
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Filoviridae; Ebolavirus.
NCBI_TaxID=186538 {ECO:0000313|EMBL:ALG01626.1, ECO:0000313|Proteomes:UP000138653};
[1] {ECO:0000313|Proteomes:UP000105726, ECO:0000313|Proteomes:UP000138653, ECO:0000313|Proteomes:UP000147798}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ebola virus/H.sapiens-wt/LBR/2014/Makona-LIBR10106
{ECO:0000313|EMBL:ALG01626.1},
Ebola virus/H.sapiens-wt/LBR/2014/Makona-LIBR10113
{ECO:0000313|EMBL:ALG01896.1},
Ebola virus/H.sapiens-wt/LBR/2014/Makona-LIBR10168
{ECO:0000313|EMBL:ALG01770.1}, and
Ebola virus/H.sapiens-wt/LBR/2014/Makona-LIBR10179
{ECO:0000313|EMBL:ALG01968.1};
Ladner J.T., Wiley M.R., Mate S., Dudas G., Prieto K., Lovett S.P.,
Beitzel B., Fakoli L., Diclaro J.W., Schoepp R., Fair J., Kuhn J.H.,
Hensley L.E., Park D.J., Sabeti P.C., Rambaut A., Sanchez-Lockhart M.,
Bolay F.K., Kugelman J.R., Palacios G.;
"Evolution and spread of Ebola virus in Liberia, 2014-2015.";
Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|Proteomes:UP000098997, ECO:0000313|Proteomes:UP000102707, ECO:0000313|Proteomes:UP000112221}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Blackley D., Wiley M.R., Ladner J.T., Fallah M., Lo T., Gilbert M.,
Gregory C., Dambrozio J., Coulter S., Mate S., Balogun Z.,
Kugelman J., Nwachukwu W., Prieto K., Yeiah A., Clement P.,
Amigashie F., Kearney B., Wisniewski M., Schroth G., Fakoli L.,
DiClaro J.W., Kuhn J., Hensley L., Jahrling P., Nichol S.,
Massaquoi M., Kateh F., Gasasira A., Bolay F., Monroe S., Laney A.,
Nyenswah T., Christie A., Palacios G.F.;
"Reduced rate of evolution associated with the reemergence Ebola virus
transmission chains.";
Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|EMBL:ALT66736.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Ebola virus/H.sapiens-wt/LBR/2014/Makona-LIBR20001
{ECO:0000313|EMBL:ALT66736.1},
Ebola virus/H.sapiens-wt/LBR/2014/Makona-LIBR20003
{ECO:0000313|EMBL:ALT66754.1},
Ebola virus/H.sapiens-wt/LBR/2014/Makona-LIBR20004
{ECO:0000313|EMBL:ALT66763.1}, and
Ebola virus/H.sapiens-wt/LBR/2014/Makona-LIBR20006
{ECO:0000313|EMBL:ALT66781.1};
Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|EMBL:ALT66736.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Ebola virus/H.sapiens-wt/LBR/2014/Makona-LIBR20001
{ECO:0000313|EMBL:ALT66736.1},
Ebola virus/H.sapiens-wt/LBR/2014/Makona-LIBR20003
{ECO:0000313|EMBL:ALT66754.1},
Ebola virus/H.sapiens-wt/LBR/2014/Makona-LIBR20004
{ECO:0000313|EMBL:ALT66763.1}, and
Ebola virus/H.sapiens-wt/LBR/2014/Makona-LIBR20006
{ECO:0000313|EMBL:ALT66781.1};
PubMed=27386513;
Blackley D.J., Wiley M.R., Ladner J.T., Fallah M., Lo T.,
Gilbert M.L., Gregory C., D'ambrozio J., Coulter S., Mate S.,
Balogun Z., Kugelman J., Nwachukwu W., Prieto K., Yeiah A.,
Amegashie F., Kearney B., Wisniewski M., Saindon J., Schroth G.,
Fakoli L., Diclaro J.W.II., Kuhn J.H., Hensley L.E., Jahrling P.B.,
Stroher U., Nichol S.T., Massaquoi M., Kateh F., Clement P.,
Gasasira A., Bolay F., Monroe S.S., Rambaut A., Sanchez-Lockhart M.,
Scott Laney A., Nyenswah T., Christie A., Palacios G.;
"Reduced evolutionary rate in reemerged Ebola virus transmission
chains.";
Sci. Adv. 2:E1600378-E1600378(2016).
-!- FUNCTION: RNA-directed RNA polymerase that catalyzes the
replication of viral genomic RNA. The template is composed of the
viral RNA tightly encapsidated by the nucleoprotein (N). The
replicase mode is dependent on intracellular N protein
concentration. In this mode, the polymerase replicates the whole
viral genome without recognizing transcriptional signals, and the
replicated genome is not caped or polyadenylated.
{ECO:0000256|PIRNR:PIRNR037548}.
-!- FUNCTION: RNA-directed RNA polymerase that catalyzes the
transcription of viral mRNAs, their capping and polyadenylation.
The template is composed of the viral RNA tightly encapsidated by
the nucleoprotein (N). The viral polymerase binds to the genomic
RNA at the 3' leader promoter, and transcribes subsequently all
viral mRNAs with a decreasing efficiency. The first gene is the
most transcribed, and the last the least transcribed. The viral
phosphoprotein acts as a processivity factor. Capping is
concommitant with initiation of mRNA transcription. Indeed, a GDP
polyribonucleotidyl transferase (PRNTase) adds the cap structure
when the nascent RNA chain length has reached few nucleotides.
Ribose 2'-O methylation of viral mRNA cap precedes and facilitates
subsequent guanine-N-7 methylation, both activities being carried
by the viral polymerase. Polyadenylation of mRNAs occur by a
stuttering mechanism at a slipery stop site present at the end
viral genes. After finishing transcription of a mRNA, the
polymerase can resume transcription of the downstream gene.
{ECO:0000256|PIRNR:PIRNR037548}.
-!- CATALYTIC ACTIVITY: 5'-triphospho-mRNA + GDP = diphosphate +
guanosine 5'-triphospho-mRNA. {ECO:0000256|PIRNR:PIRNR037548}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000256|PIRNR:PIRNR037548,
ECO:0000256|SAAS:SAAS00361115}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
{ECO:0000256|PIRNR:PIRNR037548, ECO:0000256|SAAS:SAAS00847042}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl
5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-
(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-
methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-
ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA].
{ECO:0000256|PIRNR:PIRNR037548}.
-!- SUBCELLULAR LOCATION: Host cytoplasm
{ECO:0000256|SAAS:SAAS00847043}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000256|PIRNR:PIRNR037548}. Host
cytoplasm {ECO:0000256|PIRNR:PIRNR037548}.
-----------------------------------------------------------------------
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EMBL; KT725337; ALG01626.1; -; Viral_cRNA.
EMBL; KT725353; ALG01770.1; -; Viral_cRNA.
EMBL; KT725367; ALG01896.1; -; Viral_cRNA.
EMBL; KT725375; ALG01968.1; -; Viral_cRNA.
EMBL; KU220277; ALT66736.1; -; Viral_cRNA.
EMBL; KU220279; ALT66754.1; -; Viral_cRNA.
EMBL; KU220280; ALT66763.1; -; Viral_cRNA.
EMBL; KU220282; ALT66781.1; -; Viral_cRNA.
Proteomes; UP000098997; Genome.
Proteomes; UP000102707; Genome.
Proteomes; UP000105726; Genome.
Proteomes; UP000112221; Genome.
Proteomes; UP000129202; Genome.
Proteomes; UP000138653; Genome.
Proteomes; UP000147798; Genome.
Proteomes; UP000162493; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
InterPro; IPR026890; Mononeg_mRNAcap.
InterPro; IPR014023; Mononeg_RNA_pol_cat.
InterPro; IPR025786; Mononega_L_MeTrfase.
InterPro; IPR017235; RNA-dir_pol_L_filovirus.
Pfam; PF14318; Mononeg_mRNAcap; 1.
Pfam; PF00946; Mononeg_RNA_pol; 1.
PIRSF; PIRSF037548; RNA_pol_Filoviridae; 1.
TIGRFAMs; TIGR04198; paramyx_RNAcap; 1.
PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
PROSITE; PS51590; SAM_MT_MNV_L; 1.
4: Predicted;
ATP-binding {ECO:0000256|PIRNR:PIRNR037548,
ECO:0000256|SAAS:SAAS00503432}; Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000098997,
ECO:0000313|Proteomes:UP000102707, ECO:0000313|Proteomes:UP000105726,
ECO:0000313|Proteomes:UP000112221};
Host cytoplasm {ECO:0000256|PIRNR:PIRNR037548,
ECO:0000256|SAAS:SAAS00847045};
Methyltransferase {ECO:0000256|PIRNR:PIRNR037548,
ECO:0000256|SAAS:SAAS00847038};
mRNA capping {ECO:0000256|PIRNR:PIRNR037548,
ECO:0000256|SAAS:SAAS00503423};
mRNA processing {ECO:0000256|PIRNR:PIRNR037548,
ECO:0000256|SAAS:SAAS00503423};
Multifunctional enzyme {ECO:0000256|SAAS:SAAS00503427};
Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037548,
ECO:0000256|SAAS:SAAS00503432};
Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR037548,
ECO:0000256|SAAS:SAAS00503441};
RNA-directed RNA polymerase {ECO:0000256|PIRNR:PIRNR037548,
ECO:0000256|SAAS:SAAS00503441};
S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR037548,
ECO:0000256|SAAS:SAAS00503438};
Transferase {ECO:0000256|PIRNR:PIRNR037548,
ECO:0000256|SAAS:SAAS00503441, ECO:0000256|SAAS:SAAS00847038};
Viral RNA replication {ECO:0000256|PIRNR:PIRNR037548,
ECO:0000256|SAAS:SAAS00503417};
Virion {ECO:0000256|PIRNR:PIRNR037548, ECO:0000256|SAAS:SAAS00847034}.
DOMAIN 625 809 RdRp catalytic.
{ECO:0000259|PROSITE:PS50526}.
DOMAIN 1805 2003 Mononegavirus-type SAM-dependent 2'-O-
MTase. {ECO:0000259|PROSITE:PS51590}.
COILED 2082 2109 {ECO:0000256|SAM:Coils}.
SEQUENCE 2212 AA; 252437 MW; 82AE2AE4DEC43F78 CRC64;
MATQHTQYPD ARLSSPIVLD QCDLVTRACG LYSSYSLNPQ LRNCKLPKHI YRLKYDVTVT
KFLSDVPVAT LPIDFIVPIL LKALSGNGFC PVEPRCQQFL DEIIKYTMQD ALFLKYYLKN
VGAQEDCVDD HFQEKILSSI QGNEFLHQMF FWYDLAILTR RGRLNRGNSR STWFVHDDLI
DILGYGDYVF WKIPISLLPL NTQGIPHAAM DWYQTSVFKE AVQGHTHIVS VSTADVLIMC
KDLITCRFNT TLISKIAEVE DPVCSDYPNF KIVSMLYQSG DYLLSILGSD GYKIIKFLEP
LCLAKIQLCS KYTERKGRFL TQMHLAVNHT LEEITEIRAL KPSQAHKIRE 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 RNNPPEGPSS YRGHMGGIEG LQQKLWTSIS
CAQISLVEIK TGFKLRSAVM GDNQCITVLS VFPLETDAGE 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
VVWLKPYEQC PQCSNAKQPG GKPFVSVAVK KHIVSAWPNA SRISWTIGDG IPYIGSRTED
KIGQPAIKPK CPSAALREAI ELASRLTWVT QGSSNSDLLI KPFLEARVNL SVQEILQMTP
SHYSGNIVHR YNDQYSPHSF MANRMSNSAT RLIVSTNTLG EFSGGGQSAR DSNIIFQNVI
NYAVALFDIK FRNTEATDIQ YNRAHLHLTK CCTREVPAQY LTYTSTLDLD LTRYRENELI
YDNNPLKGGL NCNISFDNPF FQGKQLNIIE DDLIRLPHLS GWELAKTIMQ SIISDSNNSS
TDPISSGETR SFTTHFLTYP KIGLLYSFGA FVSYYLGNTI LRTKKLTLDN FLYYLTTQIH
NLPHRSLRIL KPTFKHASVM SRLMSIDPHF SIYIGGAAGD RGLSDAARLF LRTSISSFLT
FVKEWIINRG TIVPLWIVYP LEGQNPTPVN NFLHQIVALL VHDSSRHQAF KTTINDHVHP
HDNLVYTCKS TASNFFHASL AYWRSRHRNS NRKDLTRNSS TGSSTNNSDG HIKRSQEQTT
RDPHDGTERS LVLQMSHEIK RTTIPQENTH QGPSFQSFLS DSACGTANPK LNFDRSRHNV
KSQDHNSASK REGHQIISHR LVLPFFTLSQ GTRQLTSSNE SQTQDEISKY LRQLRSVIDT
TVYCRFTGIV SSMHYKLDEV LWEIENFKSA VTLAEGEGAG ALLLIQKYQV KTLFFNTLAT
ESSIESEIVS GMTTPRMLLP VMSKFHNDQI EIILNNSASQ ITDITNPTWF KDQRARLPRQ
VEVITMDAET TENINRSKLY EAVHKLILHH VDPSVLKAVV LKVFLSDTEG MLWLNDNLAP
FFATGYLIKP ITSSARSSEW YLCLTNFLST TRKMPHQNHL SCKQVILTAL QLQIQRSPYW
LSHLTQYADC DLHLSYIRLG FPSLEKVLYH RYNLVDSKRG PLVSVTQHLA HLRAEIRELT
NDYNQQRQSR TQTYHFIRTA KGRITKLVND YLKFFLIVQA LKHNGTWQAE FKKLPELISV
CNRFYHIRDC NCEERFLVQT LYLHRMQDSE VKLIERLTGL LSLFPDGLYR FD


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