L_JUNIN
ID L_JUNIN Reviewed; 2210 AA.
AC Q6XQI4;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 65.
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 Junin mammarenavirus (JUNV) (Junn mammarenavirus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=2169991;
OH NCBI_TaxID=29095; Akodon azarae (Azara's grass mouse).
OH NCBI_TaxID=10080; Bolomys.
OH NCBI_TaxID=56211; Calomys laucha (Small vesper mouse).
OH NCBI_TaxID=56212; Calomys musculinus (Drylands vesper mouse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=MC2;
RX PubMed=14698659; DOI=10.1016/j.virol.2003.08.016;
RA Charrel R.N., Lemasson J.J., Garbutt M., Khelifa R., De Micco P.,
RA Feldmann H., de Lamballerie X.;
RT "New insights into the evolutionary relationships between arenaviruses
RT provided by comparative analysis of small and large segment sequences.";
RL Virology 317:191-196(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=MC2;
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; AY216507; AAP44543.2; -; Genomic_RNA.
DR SMR; Q6XQI4; -.
DR PRIDE; Q6XQI4; -.
DR Proteomes; UP000127886; 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..2210
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000361638"
FT DOMAIN 1171..1368
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 1329
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 2210 AA; 252871 MW; 97D7A1324309C61B CRC64;
MEESVNEIKN LIRKHFPERQ ELAYQRDIFL SQHHPSSLLL EGFKLLSSLV ELESCEAHAC
QINSDQKFVD VILSDHGILC PTLPKVIPDG FKLTGKTLIL LETFVRVNPD EFEKKWKSDM
SKLLNLKSDL LRAGITLVPV VDGRSSYSNR FLADWVVERV RWLLIDILKK SKFMQEINIE
EQEYQRLIHS LSNTKNQSLG LENIECLKKN SLGYDERLNE SLFVGVRGDI RESVIREELI
KLRFWFKKEI FDKQLGKFKF SQKSNLINDL VSLGSHKDSD VPSCPFCANK LMDVVYSIAS
HPIDEVNMKS QSDENSISID AVERCYLQAL SVCNKVKGLK VFNTRRNTLL FLDLVLLNLL
CDLFKKHDDA IVRLRNAGIV VGQMLMLVND RLLDILEAIK LIRKKLMTSP KWVQMCSRTL
KNSHQDLWSQ LEKLIKHPDM DSMMILAQAL VSDRPVMRYT IDRESEKICR HQPFSSLVEG
EQKKLFRILS SISLALVNSM KTSFSSRLLI NEREYSRYFG NVRLRECYVQ RFHLIKNTFG
LLFYQKTGEK SRCYSIYLSI NGVLEEQGSF YCDPKRFFLP IFSEDVLIEM CEEMTSWLDF
SHELMTMTRP TLRLLVLAVL CSPSKRNQTF LQGLRYFLMA YANQIHHVDL MSKLRVDCMS
GSEVLIQRMA VELFQTILSE GEDADLYFAR RFKYLLNVSY LCHLVTKETP DRLTDQIKCF
EKFIEPKVKF DCVVVNPPLN GSLTLEQEDI MIRGLDRFFS KEAKTSSDTQ IPGVSKEILS
FCISLFNRGR LKVTGELKSN PYRPNITSTA LDLSSNKSVV IPKLDELGNI LSVYDKEKLV
STCVSTMAER FKTKGRYNLD PDSMDYLILK NLTGLVSTGS RTRTNQEELS MMYESLTEDQ
VRAFEGIRND VQMTLAKMAN SEGSKVETTK LKSKNLSVDE RESLESLWAP FGVLREIKAE
VSMHEVKDFD PDVFRSDVYK ELCDAVYLSP FKLTYFLEAP QDICPLGLLL KNLTTIAYQE
DEFFECFKYL LIQGHYDQKL GSYEHRSRSR LGFSSEVLKL KDEVRLSTRE SNSEAIADKL
DKSYFTNAAL RNLCFYSDDS PTEFTSISSN TGNLKFGLSY KEQVGSNREL YVGDLNTKLM
TRLVEDFSEA VGSSMRYTCL NSEKEFERAI CDMKMAVNNG DLSCSYDHSK WGPTMSPALF
LSFLYTLELK NPRDRTKVNL EPVMNILKWH LHKVVEVPIN VAEAYCVGKL KRSLGLMGCD
CTSVGEEFFH QYLQSRDQVP SHIMSVLDMG QGILHNTSDL YGLITEQFLC YALDLLYDVI
PVTYTSSDDQ VSLIKIPCLS DEKCQDRTEL LEMVCFHEFL SSKLNKFISP KSVIGTFVAE
FKSRFFVMGE ETPLLTKFVS AALHNVKCKT PTQLSETIDT ICDQCIANGV STHIVSKISI
RVNQLIRYSG YRETPFGAIE EQDVKDWVDG SRGYRLQRKI EAIFSDDKET MFIRNCARKV
FNDIKKGKIF EENLINLISR GGDEALSGFL QYAGCSEDEI RRTLDYRWVN LASFGDLRLV
LRTKLMTSRR VLEKEEMPTL IKTIQSRLSR NFTKGVKKIL AESINKSAFQ SSVASGFIGF
CKSMGSKCVR DGKGGFLYIK DIFTRIMPCL CEICEKKPKV IYCQKSLQEV NQFSKPILWD
YFSLVLTNAC ELGEWVFSAV KSPQAPLVLC NKNFFWAVKP KAVRQIEDQL GMNHVLHSIR
RNYPKLFEEH LAPFMNDLQV NRSLDSGRLK FLDVCVALDM MNENLGIISH LLKVRDNNVY
IVKQSDCASA HVRQSEYTNW EVGISPQQVC RNFMVQVVLS SMINPLVMST SCLKSFFWFN
EVLDLEDDSQ VDLAELTDFT LSIKNNKVSR AMFVEDIAMG YVVSSFDNIK VFLESVSVDN
ISLLPQEDMI DLHTVLRNVA CQEAVKLKLI IQVEHTRVST KFKLRRKMVY SYTIVSSLRV
DDVSTPELEL NVDAMSQCVS GSEGNHSLLD GALVIASLPL FTGHESFDLA GLFIDAGYAV
TNDDNILSHV KLNFGDFYSE LGNKYAYDLI GPNNPGEPLV LKEGIFYRGN ERLSTYKVEL
SGDVIVKAIG ALEDIDSVET LLCQLWPYLK TTSQTILFQQ EDFVLVYDLH KEQLVRSLDK
FGDWLEFSNF KVAFSRSLND LLVSDPQGQF RLKGVTCRPL KHKVEIKDID
