ID A0A2P1JNT3_9VIRU Unreviewed; 2220 AA. AC A0A2P1JNT3; DT 23-MAY-2018, integrated into UniProtKB/TrEMBL. DT 23-MAY-2018, sequence version 1. DT 08-MAY-2019, entry version 7. DE RecName: Full=RNA-directed RNA polymerase L {ECO:0000256|HAMAP-Rule:MF_04086, ECO:0000256|PIRNR:PIRNR000836}; DE Short=Protein L {ECO:0000256|HAMAP-Rule:MF_04086, ECO:0000256|PIRNR:PIRNR000836}; DE EC=2.7.7.48 {ECO:0000256|HAMAP-Rule:MF_04086, ECO:0000256|PIRNR:PIRNR000836}; DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_04086}; DE AltName: Full=Large structural protein {ECO:0000256|HAMAP-Rule:MF_04086}; DE AltName: Full=Replicase {ECO:0000256|HAMAP-Rule:MF_04086}; DE AltName: Full=Transcriptase {ECO:0000256|HAMAP-Rule:MF_04086}; GN Name=L {ECO:0000256|HAMAP-Rule:MF_04086, ECO:0000313|EMBL:AVO03702.1}; OS Lassa mammarenavirus. OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Negarnaviricota; Polyploviricotina; Ellioviricetes; Bunyavirales; OC Arenaviridae; Mammarenavirus. OX NCBI_TaxID=11620 {ECO:0000313|EMBL:AVO03702.1}; RN [1] {ECO:0000313|EMBL:AVO03702.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Lassa virus/H.sapiens-wt/NGA/2016/ISTH_1123 RC {ECO:0000313|EMBL:AVO03702.1}, and Lassa RC virus/H.sapiens-wt/NGA/2016/ISTH_1250 {ECO:0000313|EMBL:AVO03770.1}; RA Odia I., Ehaine P., Oguzie J.U., Siddle K.J., Mehta S., Barnes K.M., RA Winnicki S.M., Brehio P., Shah R., Chak B., Yozwiak N., Amao A., RA Nosamiefan I., Birren B.W., Park D.J., Folarin O., Okokhere P., RA Sabeti P.C., Happi C.T.; RT "Lassa virus outbreak genomics and epidemiology from Nigeria."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: RNA-dependent RNA polymerase which is responsible for CC replication and transcription of the viral RNA genome. During CC transcription, synthesizes 4 subgenomic RNAs, and assures their CC capping by a cap-snatching mechanism, in which cellular capped CC pre-mRNAs are used to generate primers for viral transcription. CC The 3'-end of subgenomic mRNAs molecules are heterogeneous and not CC polyadenylated. The replicase function is to direct synthesis of CC antigenomic and genomic RNA which are encapsidated and non capped. CC As a consequence of the use of the same enzyme for both CC transcription and replication, these mechanisms need to be well CC coordinated. These processes may be regulated by proteins N and Z CC in a dose-dependent manner. {ECO:0000256|HAMAP-Rule:MF_04086, CC ECO:0000256|PIRNR:PIRNR000836}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA- CC COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, CC ChEBI:CHEBI:83400; EC=2.7.7.48; Evidence={ECO:0000256|HAMAP- CC Rule:MF_04086, ECO:0000256|PIRNR:PIRNR000836, CC ECO:0000256|SAAS:SAAS01176592}; CC -!- SUBUNIT: Homomultimerizes; the oligomeric structure is essential CC for the polymerase activity. Interacts with the nucleocapsid CC protein N. Interacts with protein Z; this interaction inhibits CC viral transcription and replication. {ECO:0000256|HAMAP- CC Rule:MF_04086, ECO:0000256|PIRNR:PIRNR000836}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|HAMAP-Rule:MF_04086, CC ECO:0000256|PIRNR:PIRNR000836}. Host cytoplasm {ECO:0000256|HAMAP- CC Rule:MF_04086, ECO:0000256|PIRNR:PIRNR000836}. CC -!- DOMAIN: The N-terminal domain contains an RNA endonuclease CC activity that plays an essential role in mRNA transcription. This CC activity may be involved in cap snatching. {ECO:0000256|HAMAP- CC Rule:MF_04086}. CC -!- SIMILARITY: Belongs to the arenaviridae RNA polymerase family. CC {ECO:0000256|HAMAP-Rule:MF_04086, ECO:0000256|PIRNR:PIRNR000836}. 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; MH053512; AVO03702.1; -; Genomic_RNA. DR EMBL; MH053587; AVO03770.1; -; Genomic_RNA. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule. DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0075526; P:cap snatching; IEA:UniProtKB-UniRule. DR GO; GO:0039689; P:negative stranded viral RNA replication; IEA:UniProtKB-UniRule. DR HAMAP; MF_04086; ARENA_L; 1. DR InterPro; IPR026382; CapSnatchArena. DR InterPro; IPR007099; RNA-dir_pol_NSvirus. DR InterPro; IPR010453; RNA_pol_arenavir. DR Pfam; PF06317; Arena_RNA_pol; 1. DR Pfam; PF17296; ArenaCapSnatch; 1. DR PIRSF; PIRSF000836; L_ArenaV; 1. DR PROSITE; PS50525; RDRP_SSRNA_NEG_SEG; 1. PE 3: Inferred from homology; KW Cap snatching {ECO:0000256|HAMAP-Rule:MF_04086}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04086, KW ECO:0000256|PIRNR:PIRNR000836}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04086}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04086, KW ECO:0000256|PIRNR:PIRNR000836, ECO:0000256|SAAS:SAAS01176568}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_04086, KW ECO:0000256|PIRNR:PIRNR000836, ECO:0000256|SAAS:SAAS01176569}; KW RNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_04086, KW ECO:0000256|PIRNR:PIRNR000836, ECO:0000256|SAAS:SAAS01176590}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_04086, KW ECO:0000256|PIRNR:PIRNR000836, ECO:0000256|SAAS:SAAS01176594}; KW Viral RNA replication {ECO:0000256|HAMAP-Rule:MF_04086, KW ECO:0000256|PIRNR:PIRNR000836, ECO:0000256|SAAS:SAAS01176589}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04086, KW ECO:0000256|PIRNR:PIRNR000836}. FT DOMAIN 1177 1372 RdRp catalytic. {ECO:0000259|PROSITE: FT PS50525}. FT COILED 5 25 {ECO:0000256|SAM:Coils}. FT COILED 113 133 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 2220 AA; 253956 MW; 1F9C8990C036F77D CRC64; MEEDIANAKD LISKYLADNE KLSRQKLAFL VQTEPRMLLM EGLKLLSLCI EIDSCKANGC EHNTEDKTVE SILSDHGILT PALCFVVPDG YKLTGNVLIL LECFVRSSPA NFEQKYLEDH KKLEQLKNDL ESVGINLIPL IDGRTTFYNE QIPDWVNDKL RDTLFTLLKY SQESNALFEE SEYSRLCESL ALTSGRLSGI ESINVLTDKR AKHFEEIISS CHQGINNKLT SHEVKSLIEE EYQIFRNKLR QGDIENQFVR TDKVRLLEDF KKLYSDKIDT CDDSIEQLTF QFRRASPVLK FLYADLDSGE ERAADSQSEQ MQCWRSFLNK IKSLRILNTR RKLLLIFDVL ILLASRLDRI KHGDGLLAGW LGSCFVSVND RLVSLESTKR DLKRWIDSRK RTRDRNVGVL SPKEERNCEL LAIINRVLTR ATNALREVGI ETNSYGIDFK ILDCDVYDAI MDIEITGITP TISYQKTQED MFPYTLGVID ILDATDLERL SSLSLALINS MKTSSTVKLR QNEFGPSRYQ VVRCKEAYCQ EFFINRMGFK LLYQKTGECS KCYAINNNIT GEVCSFYADP KRFFPSVFSS DVLQKVVDVM VSWIEECTEL SEQLITIKLL TKMILVLILT HPSKRCQKFL QNIRYFVMAF VSDFYHKDLI EKIREDLITE VEYLLYRLVR HLLKIILSEE VVSMMTNRFK FVLNVSYMCH FITKETPDRL TDQIKCFEKF LEPKLEFGHV SVNPKDDASE EELAEMVHNA RRFLSKECCA DAEKIRYKKP GVSKKFISLL VSSFNNGSLF KEKEVKRTLR DPLITSGCAT ALDLASNKSV VVNKYTDGSR ILDYDFNKLT ALAVTQLTEV FARKGKFLLN KQDYDYKIQQ AMSNLVLGSK GGSGDTNNAD LDEILLDGGA SEYFDQLRCT VDNIVSQYRE QPERQQQADC NAPSISDLDK VVEEKLLIRL IKSELSNHMI EDFDREILSE DQYIKICENI YNDADLRSKY FYVGPMNSCP ISELTKAVVT RTFLDQEYFQ CFKSILLVMN GNKLMGRYSH YKSKCLNFKF DTGRLAEDVR ISERESNSEA LSKALSLTNC TTAMLKNLCF YSQESPQSYN STGPDTGRLK FSLSYKEQVG GNRELYIGDL RTKMFTRLIE DYFEALTSQL AGSCLNNEKE FDNAILSMKL NVSSAHVSYS MDHSKWGPMM CPFLFLTIIQ NLILLSDDLQ ADLKGKDYLS TLLTWHMHKM VEIPFNVVSA MMKSYIKSQL GLKKKTTQSV TEDFFNSNFQ IGTVPSHISS ILDMGQGILH NTSDFYALIS ERFINFAVRC VSGGQIDAYT SSDDQISLFD QNLTELLSRD AEEFKTLLEF HYYMSDQLNK FVSPKSAIGR FVAEFKSRFY VWGDEVPLLT KFVAAALHNI KCKEPHQLAE TIDTIIDQSV ANGVPVDLCN QIQKRTLSLL CYAKYPIDPF LLNCETDVRD WVDGNRSYRI MRQIERLIPD ACKKMRSMLR ILFNKLKTGE LHEEFTTNYL SGEHTTSLQN LFKLLGIEPL SDSDLGYHWL NLATHHPLRM VLRQKIIYSG AVNLEDEKVP TIVKTLQNRL SSTFTRGAQK LLSEAINKSA FQSSIASGFV GLCRTLGSKC VRGPNKENLY IRSIQTQLLG TQGVEVVMGD NGIQIWKVSP EVKDGGDTVV TYLRPLLWDY MCITLSTAIE LGAWVLGEPK QAQILDFFKH NPCDYFPLRP TVSKLLEDRV GMSHIIHSLR RLYPSLFEKH ILPFMSDLAS TKMKWSPRIK FLDLCVALDV NCEALSLVSH IVKWKREEHY VVLASELRNS HSRTHEPMME ERVVSTTDAV DNFMRQIYFE SYVRSFVATT RTLGSFTWFP HKTSIPEGEG LQRLGPFSSF IEKAIYKGIE RPMFKFDLMM GYAWIDFDIE PAQINLNQLI ASGLTEELRL DSLEDFFDLL STMPMDSVQF YQTIRYKIKS QDASFKETFS IHLNMIGLVN QCGEFVVNDV QALYSGSVSP CVLSDCWRLA LSGPTFKGRS AWFVESDVVN EFLKDTQQLG DVIPMKLIIN PDKLQFSEFD FTKVGPDNEP VPLVVCRGAL WESDRRVATF SPSIQDQDLE MFVREIGDGS PHLLVGALKS MMSDRLKQRI QWTGVDIVSI LTKQRPLDYA DILSELLESL GEWIDFKGYA LCYSKSKQKV MIQSSGGSLR LKGRTCSELF GPERCVEDIE //