ID A0A9E9KU74_9VIRU Unreviewed; 2228 AA. AC A0A9E9KU74; DT 03-MAY-2023, integrated into UniProtKB/TrEMBL. DT 03-MAY-2023, sequence version 1. DT 08-NOV-2023, entry version 4. DE RecName: Full=RNA-directed RNA polymerase L {ECO:0000256|ARBA:ARBA00018602, ECO:0000256|PIRNR:PIRNR000836}; DE Short=Protein L {ECO:0000256|PIRNR:PIRNR000836}; DE EC=2.7.7.48 {ECO:0000256|ARBA:ARBA00012494, ECO:0000256|PIRNR:PIRNR000836}; OS WENV Rattus norvegicus mammarenavirus. OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus. OX NCBI_TaxID=3014462 {ECO:0000313|EMBL:WAU17171.1}; RN [1] {ECO:0000313|EMBL:WAU17171.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Hainan40 {ECO:0000313|EMBL:WAU17171.1}; RA Xie Q., Zhu C., Tan W.; RL Submitted (SEP-2022) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: RNA-dependent RNA polymerase, which is responsible for the CC replication and transcription of the viral RNA genome using antigenomic CC RNA as an intermediate. During transcription, synthesizes subgenomic CC RNAs and assures their capping by a cap-snatching mechanism, which CC involves the endonuclease activity cleaving the host capped pre-mRNAs. CC These short capped RNAs are then used as primers for viral CC transcription. The 3'-end of subgenomic mRNAs molecules are CC heterogeneous and not polyadenylated. The replicase function is to CC direct synthesis of antigenomic and genomic RNA which are encapsidated CC and non capped. 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 in a CC dose-dependent manner. {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:14527, Rhea:RHEA- CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; CC EC=2.7.7.48; Evidence={ECO:0000256|ARBA:ARBA00024517, CC ECO:0000256|PIRNR:PIRNR000836}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- SUBUNIT: Homomultimer; the oligomeric structure is essential for the CC polymerase activity. {ECO:0000256|PIRNR:PIRNR000836}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|PIRNR:PIRNR000836}. Host CC cytoplasm {ECO:0000256|PIRNR:PIRNR000836}. CC -!- SIMILARITY: Belongs to the Bunyavirales RNA polymerase family. CC {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; OP562167; WAU17171.1; -; Genomic_RNA. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0044423; C:virion component; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0075526; P:cap snatching; IEA:UniProtKB-KW. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR Gene3D; 3.30.70.2640; Arenavirus RNA polymerase; 1. DR Gene3D; 1.20.1440.300; RNA-directed RNA polymerase L, helical domain; 1. DR InterPro; IPR026382; CapSnatch_arenavir. DR InterPro; IPR048006; CapSnatch_bunyavir. DR InterPro; IPR007099; RNA-dir_pol_NSvirus. DR InterPro; IPR010453; RNA_pol_arenavir. DR NCBIfam; TIGR04202; capSnatchArena; 1. 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|ARBA:ARBA00022715}; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200, KW ECO:0000256|PIRNR:PIRNR000836}; Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000836}; KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR000836}; KW RNA-directed RNA polymerase {ECO:0000256|PIRNR:PIRNR000836, KW ECO:0000313|EMBL:WAU17171.1}; Transferase {ECO:0000256|PIRNR:PIRNR000836}; KW Viral RNA replication {ECO:0000256|PIRNR:PIRNR000836}; KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|PIRNR:PIRNR000836}. FT DOMAIN 1177..1373 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50525" SQ SEQUENCE 2228 AA; 255102 MW; D7B5EBA4C58BA19C CRC64; MEEILTEARR LVGCHFPQME QIARQKALFL AQREPKFTLI EGLKLLSLCI EIDSCRSNAC DHNSESLSVE VLLFRNNILC PSLPYVVPDG FKLKGNVLIL LECFVRSNPA NFQQKYTEDL TKLESLRIDL GRAGVQLIPI VDGKTSFYTS IVPDWVCERF RHLLFKLLEY EQESNSEFEE SEYQRLCESL SQNTSRLSGV DSLNILADHR SRHYEDIIQK CHVGINSSLS AREIRERVTM IFQTFRNRLR SQTVKHHFVK VNSEQLLKSF SELYESELSN AVDTMDSIRS EFNIVSPIIK FLYMRIPKES EKEEEIQTNG PNTLICGLRS MLNKVKSMKV LNTRRKMLLL FDTFILMAHI RYFKERSLYA EAEWLGSSFC SVNDRLVSLD ETVQSLTKWV RARQRNHSKK LPERVTPTLN QVFQDMMRST YKKIESALDY ICMKPESYGV SFGALEIDIE ELVAFKKDGV QPTMSYEALQ AKETPYHVEM MSVQSDDDFR VLSSLCLSIV NSMKTSSVPK LRQNEMGASR YKVVRCREAF YQDLITRVGC FKLLYQKTGE SSKCYAINDE KSGEICSFYA DPKRYFLPIF SHEVLPETVR TMMSWLDGCE ELKEHLADIH WLTKAIVILI LCQPSKRSQR FLQNLRYFVM AMVSEYHHVK LMEKLREPLI TKCEYYLYRL IRKLLTVLFD PSVKSLLTNR FKYMLNVSYF CHLITKETPD RLTDQIKCFE KFLEPKIDFG SCFINPSDVI TDDELDTLSY GLDQFLAKPD ISDSAGITHG KPGINKEIFS LMVSSFNAGL LFKESEMRGD FVDPLISSGC ATALDLASNK SVVVNKFTEG GRVLEYDINK LTSAAVCELT ETFSKKGKYL LNKDDYEYKV QRVISKLVTK GTTGTSVKEQ EDVGIDDVFE GESKEFFYCV KQRVDNILAN YQPGMKLQDT QPHQATLSDL SEFVSDPVKQ RLIMSELSTH MVEDFDPNLL DESFYERFCK SVHDSAFKER YFYDTSLGPC PISLISRSVA SRFFEAGEYF QCFKSVLLQM GGNRFSGKFM HHKHNNVNFK FDHSKLLDDV RISERESNSE ALSKALSLSN CTSAALKNLC FYSEESPESF TSVGPNTGRL KFSLSYKEQV GGNRELYIGD LRTKMYTRLI EDYFEAFTKH FRGSCLNDEK EFENALIAMR LSVSLAQLSY SLDHSKWGPM MCPFLFLMLI QNIDLKSPSA LEGIKSRDLI STLLCWHIHK MVEVPYNVIS AMMRSYIKRN LGVMNSDHMT STEAFIFNEF EIGVVPSHIS SVLDMGQGIL HNTSDFYGLV TEKFINYCLR LVSDGSVGSY TSSDDQISLF DSELTSLHDK SEEDFLCLLE FHNYLSDMLN KFISPKSVVG RFVAEFKSRF FVWGEEVPLL TKFVSASLHN VKCKEPHQLA ETIDTIIDQS VANGVPVKLC NMMQDRTLAL LRYAKYPLDP FLLFNKSDVK DWVDGTRGYR IMRNIENICP DQTGKIRSML RMLYNKLKVG ELHEEFTAVY LSSEPKESIN KLMALVGKEL LTDDDLSLCW LNLSTHHPLR MVLRQKVIYP SVINVEEEKV PTIIKTMQNK LSSHFTRGAQ KLLSEAINKS AFQSSIASGF VGLCRTLGSK CVRDSNRGVH HIKSILEQLT TVSNVSHDQI NGWDIWRVSN HSSNADNSGH DWVLTLLRPI LWDYLCIALS TALEIGPWVL GDPKPKFEVK IRNKRSCDYF LLRPQNTRIL EDKVSMNHLI HSVRRMYPEM FEKHLLPYMS DLAATKMKWS PRIKFLDLCV VLDVNCEALS LISHVVKWKR SEHYVVLMSE LQESHDRQHV TLLDERVVST ENVSDNFMKQ ILFESFIRPI VVTSRTLGSF TWFPHKSAIP QGEGLGRLGP LSSFVEKVIF KGIERPMYEY DLSSGFSWVD LDVKPSIITA AELTRLKITE AGVFDDFWDL WSFIIQNSNE GFRVMKTIHV SVRSKGGSGS KNFFIHLQFN GSVDPLRMEV TMTLSEASYS GNVDLIFLES IWTLILTDPN FSSSCVSWYF STETISDAIR NGAQVLGDLV LVDVGLERES LKLSGIEFER VGPDWEPVPL VLRDGYLWEG ERKLVPLIVE LHTDDLKVFI QELHEDHGQL LLESLACLSK TQLAQRVSFI HMDVIDALET VCGEAKGMLV LTEVMSQVGD WVDFKGNSIC YSKSKGELMR QTPGGSLRLK GRLCEPFTQA TVDVKEID //