L_MOBVC
ID L_MOBVC Reviewed; 2220 AA.
AC Q27YE5;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=RNA-directed RNA polymerase L {ECO:0000255|HAMAP-Rule:MF_04086};
DE Short=Protein L {ECO:0000255|HAMAP-Rule:MF_04086};
DE EC=2.7.7.48 {ECO:0000255|HAMAP-Rule:MF_04086};
DE AltName: Full=Large structural protein {ECO:0000255|HAMAP-Rule:MF_04086};
DE AltName: Full=Replicase {ECO:0000255|HAMAP-Rule:MF_04086};
DE AltName: Full=Transcriptase {ECO:0000255|HAMAP-Rule:MF_04086};
DE Includes:
DE RecName: Full=cap-snatching endonuclease {ECO:0000255|HAMAP-Rule:MF_04086};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04086};
GN Name=L {ECO:0000255|HAMAP-Rule:MF_04086};
OS Mobala mammarenavirus (isolate Rat/Central African Republic/Acar 3080/1983)
OS (MOBV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=55097;
OH NCBI_TaxID=10111; Praomys (African soft-furred rats).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16494913; DOI=10.1016/j.virol.2006.01.026;
RA Emonet S., Lemasson J.J., Gonzalez J.P., de Lamballerie X., Charrel R.N.;
RT "Phylogeny and evolution of old world arenaviruses.";
RL Virology 350:251-257(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=18602020; DOI=10.1016/j.mib.2008.06.001;
RA Charrel R.N., de Lamballerie X., Emonet S.;
RT "Phylogeny of the genus Arenavirus.";
RL Curr. Opin. Microbiol. 11:362-368(2008).
RN [3]
RP REVIEW.
RX PubMed=28418734; DOI=10.1080/1040841x.2017.1307805;
RA Amroun A., Priet S., de Lamballerie X., Querat G.;
RT "Bunyaviridae RdRps: structure, motifs, and RNA synthesis machinery.";
RL Crit. Rev. Microbiol. 43:753-778(2017).
RN [4]
RP REVIEW.
RX PubMed=31948728; DOI=10.1016/j.tim.2019.12.006;
RA Olschewski S., Cusack S., Rosenthal M.;
RT "The Cap-Snatching Mechanism of Bunyaviruses.";
RL Trends Microbiol. 28:293-303(2020).
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:0000255|HAMAP-Rule:MF_04086}.
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:0000255|HAMAP-Rule:MF_04086};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04086};
CC Note=For endonuclease activity. Binds 2 Mn(2+) ions in the active site.
CC The divalent metal ions are crucial for catalytic activity.
CC {ECO:0000255|HAMAP-Rule:MF_04086};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04086};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04086};
CC Note=For polymerase activity. {ECO:0000255|HAMAP-Rule:MF_04086};
CC -!- SUBUNIT: Homomultimer; the oligomeric structure is essential for the
CC polymerase activity. Interacts with nucleoprotein N. Interacts with
CC protein Z; this interaction inhibits viral transcription and
CC replication. {ECO:0000255|HAMAP-Rule:MF_04086}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04086}. Host
CC cytoplasm {ECO:0000255|HAMAP-Rule:MF_04086}.
CC -!- DOMAIN: The N-terminus contains the endonuclease activity (endoN). The
CC central region contains the RdRp activity. {ECO:0000255|HAMAP-
CC Rule:MF_04086}.
CC -!- MISCELLANEOUS: Classified as His(-) endonuclease since it does not have
CC a histidine upstream of the active site that coordinates the first
CC cation. His(-) endonucleases display very low activity in vitro,
CC although they are clearly active in vivo. {ECO:0000255|HAMAP-
CC Rule:MF_04086}.
CC -!- SIMILARITY: Belongs to the Bunyavirales RNA polymerase family.
CC {ECO:0000255|HAMAP-Rule:MF_04086}.
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DR EMBL; DQ328876; ABC71139.1; -; Genomic_RNA.
DR RefSeq; YP_516229.1; NC_007904.1.
DR SMR; Q27YE5; -.
DR PRIDE; Q27YE5; -.
DR GeneID; 3953123; -.
DR KEGG; vg:3953123; -.
DR Proteomes; UP000140987; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
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; ISS:UniProtKB.
DR GO; GO:0039696; P:RNA-templated viral transcription; ISS:UniProtKB.
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; Host cytoplasm; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW RNA-directed RNA polymerase; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..2220
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000361642"
FT DOMAIN 1174..1370
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT REGION 26..289
FT /note="Endonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT ACT_SITE 115
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT BINDING 51
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT BINDING 89
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT BINDING 89
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT BINDING 1332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for RdRp activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
SQ SEQUENCE 2220 AA; 255250 MW; C2C0DB50EFA05508 CRC64;
MEEQISEVKD IISKYLSNDD RLAKQKLAFL VQSEPKLLLI EGLKLLSLCI EIDSCEANGC
DHNTKELSVE NFLSENRVLC PGLPMVVPDG FKLNGNVLMI LECFVRSSPA NFEQKYREDL
VKLNSLKEDL MTVGITMLPL IDGRTNFQTD RLPEWANERF RTLLFSLLAF SQESSRMFEE
AEYSRLCESL NVSGGKRSGI ENINILSDHR SEHFDELLKL CHVGINNHMS SLDVKREIIQ
EFQAFRNKLQ NGVIERQFLR VNREELIKAF NEMYTLRVGD KPELLDSLLN DYYHSCPLIT
MLYCELPNGK SCQSDISHVR GWRSLLNKVK SLRLINTRRK LMLIFDSILL LAHMKDLSVN
GHLVESEWMG SSFLSVNDRL VSLPATQKDL KTWLQRRTNR LSHSHQSQSA YEVFSTMVNR
VLNKAKEVLL LVNLTFKDYN VDEDILSESS FTEMMSLEVN GVEPTINYEK NPIDRFSYNI
QAMDPDNQSD LKRLSSISLA LVNSMKTSST VKLRQNEHGK LRYKCVRCKE AYYQDFLIEG
HRLMLIYQKT GECSKCYSVN DAVVGELCSF YADPKRYFPA IFSDSVLQEM IDTMISWLTE
CSELKEFIKE IKSLLKMVVM VVLTNPTKRI QKFLQNLRYF TMAYVSEYHH KDLLEKLRED
LITNCEFLLY RITRSILNIV FNVNVTTMIT NRFKFILNLS YLCHLITKET PDRLTDQIKC
FEKFIEPKMK FDSVNVNPLE PADQEELRSL LMSADKFLSK PDCFGDEGIL FKTPGVSRKI
FSMMVSSFNN GSLFKQAELK NGVKDPLVVS GCATALDLAS NKSVVVNKYT DGDRIIEYDY
DKLVATAVCQ LSEVFSRKGK YVLSKEDYDF KIQQIMSDLV IGRSKLHGSE IGLNSCEEVD
EVLIEGGAAD YFDSIKQSVD TVMSKFSWSG SESSATLKSE CSIDDLSLAL QDKAQLRLIR
NELSCHMVED FDVMTLPYDT YEEICKSVYS DPSLRSKYFY LESLESCPLT KMAQAVCTRT
FHDEEYFQCF KSLLLQMNAN KLSGKFNHYK SKCLNFKLDR DRLFNETRIS ERESNSEALS
KALSLTNCTT AALKNLCFYS QESPQSYNSQ GPDTGRLKFS LSYKEQVGGN RELYIGDLRT
KMFTRLIEDY FEALTSQFKG SCLNDEHEFE NAVFSMKFNV SLGLLSYSLD HSKWGPMMTP
FLFLATLQNI NWPSLDTLSD AKSRDYVSSM LSWHIHKLVE VPFNVVTAMM KSFIKSKLGL
KKNLSETMTE RFFFEHFRLG KVPSHISSIL DKGQGILQNT SDFYGLISER FINYCISCLY
EGNVDAFTSS DDQISLFDKS LSDLLEKDPD EFEYILEFHN YLSDQLNKFI SPKSVKGNFA
AEFKSRFFVW GDEVPLLTKF VAASLHNIKC KEPHQLAETI DTIIDQAVAN GVPVKLCNIV
QERTLNLLRY AQYPIDPFLM FCSSDVKDWV DGNRGYRIMR NIEMLEPNGT RKVRSFLRRL
YNNLKTGLLH EEFTAAYLSG DPYQSLAKLS KIFDTEILND EELGLSWLNL SAYYPLRMVL
RQKVIYTGAV NVEEEKLPTI VKTLQNKLSS NFTRGAQKLL SEAINRSAFQ SCIASGFVGL
CRTLGSKCVR GPERENFYIK SIMNQSMMME GVSRELVMGV DVWRVRNPLD NSRAQQKWGN
YFRPILWDYL CIALSTALEI GSWVLGEPKL KSPLPQMKFR PCDYFPMKPS VTRLLEDKVG
FNHIIHSFRR LYPDIFEKHL LPFMSDLAST KMKWSPRVKF LDLCVMLDVN CEAMSLVSHI
VKWKREEHYV ILSDELSISH DRSHESLADE RVVSTEDVSE NFLRQIYFES FARPFVATSR
TLGSFTWFPH KTSLPESEGL ASLGPFGTFI EKVIFKGIER PMYRHDLFSG YAWLDFDFGE
FYINSSKLIQ YGLTEMRYFE DLSEFMSMLS SLKPGSIEIS LTVNFQVKSQ GESLREKFFI
HCKFYGSFDV DGKFEFNNIG VQYSGAINRS AVLDCWRLIL TNSHFLGDKV IWHLNTANIK
DYLKDGSMVG EVVPIEVIIN RDALRLDTLD FERVGPDVNV VPLVVKDGYI FEGDKKLVPF
NPSIHDQDFE ILVKELCIDD KELLKDMIQK MITVRGSQGL QWHSLDIVAV LTKNMPTNYK
DFITESLSVL DSWTGFKGYS LCFSKTKNTL MIHTSEGNLR LKGKLCRKLF DDPVHVEDIE
