L_LATVB
ID L_LATVB Reviewed; 2238 AA.
AC B2MW49;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 53.
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 Latino mammarenavirus (isolate Rat/Bolivia/MARU 1924/1965) (LATV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=45221;
OH NCBI_TaxID=56210; Calomys callosus (Large vesper mouse).
RN [1]
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 [2]
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 [3]
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; EU627612; ACC94300.1; -; Genomic_RNA.
DR RefSeq; YP_001936026.1; NC_010760.1.
DR SMR; B2MW49; -.
DR GeneID; 6334524; -.
DR KEGG; vg:6334524; -.
DR Proteomes; UP000009262; 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 Reference proteome; RNA-directed RNA polymerase; Transferase;
KW Viral RNA replication; Virion.
FT CHAIN 1..2238
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000361640"
FT DOMAIN 1188..1387
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT REGION 26..284
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 1346
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 2238 AA; 256323 MW; 218FA14B9576882D CRC64;
MDDIVNQLFD LLRKHFPARP KVTEQITLVT CQNDAKMILT EGFKLLSLLV ELDSAEANNC
THNSDSLTIE GILRKEGIMS IALPRIVPDG FSLYGNVLIL LETFVRVNPV SFEQKYNQDM
SKLLSLKDDL SLCGITLVPL VDGRTNYYNR FVDDWVIERF RWLLLQLIKF VRESGEEIEE
LEYQRLITSL SKLENQSLGF ENIEKLPQTG LKYRDELKKH MFGNLSSKMK ESEIQENLIN
VLKEFFIKEY KNNKSLHKFV FTNRDGLLAK LDQITHHSEH PVDCMSCSSK LYSIIDKLGT
LKRQPLHSDY HPIYAKMWHS DSLSQAEQIY LKLLSQCNKI KSAKLLNTRR NTLLFLDLIM
VNFIVHSWKQ NPEVLTEYRR CGLMAGQLAL FSNDRYFDLN ELRNKLINKL KNCENWIAKC
VHQLKKQEFV ALDDVLVWAT VPDFESLELI TTSLELKRFK LQYGKDKVDH NEHPIGPLSE
ETFFRNLNVL SSVCLALVNS MKTSFTSKTV INERRASNHF GEVDLIECYC QRFFLSKDLV
GILSYQKTGE KSRCYSISLI SNGELEYIGS FYCDPKRFFL PIFSQIVLLN MSREMMLWLA
DLNLNDSLVG DKLRKLILLI VTNPSKRNQT FLQGLRYFIM AYVNQFHHVE LMDRLIVPVK
SYCESCLQRI SFDIFRLILE GDYDNEHMTR KFKFLLNVSY LCHLITKETP DRLTDQIKCF
EKFMEPKLKF ESVIVNPSLT ENMTEDEEAQ VLKGVDKLLG KSLSCSTDLT SPGVSKTLLS
MCVSSFNRGL LNVNGHLRQD PYRPNFTSTA LDLSSNKSVV VPKLDELGNP ISRYDYELLV
SSCVTNLAEG FKTKGKFKLD INCQEYTIMR NLTNLVLKNE DKSDAKIKGE KPCSFELSQW
METLSEEQLE VLEKLKGDVN IALGKLKEKG RSKSNSTLKE GVKRLDSGNT LAGCADPQQV
LVNLWSEFGV MKQILVEVSL HEIKDFDPDI IPPQMIQKLV FKVNNSNYKS LFFLDSVINP
CPLELLIKNM TTATFDDGEL FECFKYLLIT AGFDQKLGTY EHKNRSRFGF KFEALKVREE
GRMSSRESNS EAIARRLDKS VFTNSALRNL CFYSDESPIS YSHVSPDVGK LKFGLSYKEQ
VGSNRELYVG DLNTKLMTRL IEDFSESVVS NMSYSCLNNE AEFEKAITDM KMCVNLGDMS
LSLDHSKWGP HMSPVIFAAF LQGLDLKYGP SLCKLNTDPI ITLLSWHIHK VVEVPYNVIH
AYVTGMIKRQ LGLMNMSGST ITESFVHRLL KEKREPLSHV MSVIDMGQGI LHNMSDLYGL
VTEQFINYAI HFLFDMNTTS YTSSDDQISM IKIGSGMCNF ESLKVIEEWE TILNFHAFIS
TKFNKFVSPK TVAGTFAAEF KSRFFVWGEE VPLLTKFVSA ALHNVKCKTP VQLSETVDTI
CDQCVANGVS VEIVSYICNR TNRLIRYSGF GEHPFLNVEN LDVKDWVDGS RGYRLQRNIE
LHLESDGCTS FIRQAARKVF SNIKSGKIVE QALVDLVQED GDKAITGFLR SVGVSEEDIA
LLCRIRWINL CAHGDLRLVL RTKLMSSRRI IETEEIPSLI KSIQSKLSKN FVKGAKKILA
ESINKSAFQS SIASGFIGFC QSVGSKCVRT GEGGFYYIKE LKSKVDLYCP CEVCARWKGV
TYCSSSCLKI ESFTRPLMWD YFSLVLSNAC ELGEWVFEDV EYPKDINFLR NPNLFWLVKP
RVSCQIEEKL GLTHILQSIR RNYPQLFETH LSPFMSDFQA GRTLGTMTVK FLDVCVALDL
ANENLGIVKH FLKNRRHDIY IVKQDESSQS HIRCQKSICV DVELTSTQVC QNFMTQLIMS
SLVQPLVLTS SELKKFNWFQ QVLTLETDED VDLGLLTDFA LQVKKFNVDR AMHSEDLSAG
YISSTVSVTT FSLSKPIFLQ QIDSDFIGGT EDRKDFIQMI KSEFTKNSID LQFVIQISHV
KRALRFNLKR TTVYTLIVRT SILKEVILNS LGQEDQSVEL VVDDLELFCS GHDGNHFTLD
AAPLIVQEPL INGNLKFDLV SRLEEEDLTF SYSESLPSFH FNFEKYKHEL CNKFSYHLSG
PVIVDEPLVL DRGVILHGGR KLTTLQFDFS ADRIMQALSE LESLSSRDLF LFNLWVYSDQ
TKSKLYIHQD KLLLLVESYL SELNSSLARY DSWLNLGNYM ICYSKSFKCL MISDTNGRNR
LKGILCRRLI EEEVQDIE
