ID   L_GOGV                  Reviewed;        2066 AA.
AC   J7H8Q3;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=RNA-directed RNA polymerase L;
DE            Short=Protein L;
DE            EC=2.7.7.48 {ECO:0000250|UniProtKB:I0DF35};
DE   AltName: Full=Large structural protein;
DE   AltName: Full=Replicase;
DE   AltName: Full=Transcriptase;
DE   Includes:
DE     RecName: Full=cap-snatching endonuclease;
DE              EC=3.1.-.- {ECO:0000250|UniProtKB:Q6GWS6};
GN   Name=L; OrderedLocusNames=Segment L;
OS   Alethinophid 1 reptarenavirus (isolate AlRrV1/Boa/USA/BC/2009) (Golden Gate
OS   virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Ellioviricetes; Bunyavirales; Arenaviridae; Reptarenavirus.
OX   NCBI_TaxID=1223562;
OH   NCBI_TaxID=8574; Boa constrictor (Boa).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22893382; DOI=10.1128/mbio.00180-12;
RA   Stenglein M.D., Sanders C., Kistler A.L., Ruby J.G., Franco J.Y.,
RA   Reavill D.R., Dunker F., Derisi J.L.;
RT   "Identification, characterization, and in vitro culture of highly divergent
RT   arenaviruses from bosysa constrictors and annulated tree boas: candidate
RT   etiological agents for snake inclusion body disease.";
RL   MBio 3:1-12(2012).
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).
CC   -!- FUNCTION: RNA-dependent RNA polymerase, which is responsible for the
CC       replication and transcription of the viral RNA genome. During
CC       transcription, synthesizes subgenomic RNAs and assures their capping by
CC       a cap-snatching mechanism, which involves the endonuclease activity
CC       cleaving the host capped pre-mRNAs. These short capped RNAs are then
CC       used as primers for viral transcription. The 3'-end of subgenomic mRNAs
CC       molecules are heterogeneous and not polyadenylated. The replicase
CC       function is to direct synthesis of antigenomic and genomic RNA which
CC       are encapsidated and non capped. As a consequence of the use of the
CC       same enzyme for both transcription and replication, these mechanisms
CC       need to be well coordinated. {ECO:0000250|UniProtKB:P14240}.
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|PROSITE-ProRule:PRU00539};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q6GWS6};
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:0000250|UniProtKB:Q6GWS6};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P14241};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P14241};
CC       Note=For polymerase activity. {ECO:0000250|UniProtKB:P14241};
CC   -!- SUBUNIT: Homomultimer; the oligomeric structure is essential for the
CC       polymerase activity. Interacts with nucleoprotein N.
CC       {ECO:0000250|UniProtKB:P27316}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P14241}. Host
CC       cytoplasm {ECO:0000250|UniProtKB:P14241}.
CC   -!- DOMAIN: The N-terminus contains the endonuclease activity (endoN). The
CC       central region contains the RdRp activity.
CC       {ECO:0000250|UniProtKB:P14240}.
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.
CC       {ECO:0000250|UniProtKB:Q6GWS6}.
CC   -!- SIMILARITY: Belongs to the Arenaviridae RNA polymerase family.
CC       {ECO:0000305}.
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DR   EMBL; JQ717263; AFP93553.1; -; Genomic_RNA.
DR   RefSeq; YP_006590089.1; NC_018482.1.
DR   SMR; J7H8Q3; -.
DR   GeneID; 13466435; -.
DR   KEGG; vg:13466435; -.
DR   Proteomes; UP000134698; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-directed 5'-3' 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   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   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..2066
FT                   /note="RNA-directed RNA polymerase L"
FT                   /id="PRO_0000443035"
FT   DOMAIN          1131..1331
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          32..205
FT                   /note="Endonuclease"
FT                   /evidence="ECO:0000250|UniProtKB:Q6GWS6"
FT   REGION          808..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        120
FT                   /note="For endonuclease activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6GWS6"
FT   BINDING         54
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6GWS6"
FT   BINDING         92
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6GWS6"
FT   BINDING         92
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6GWS6"
FT   BINDING         107
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6GWS6"
FT   BINDING         1293
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic; for RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:I0DF35"
SQ   SEQUENCE   2066 AA;  236976 MW;  11E636D3D0B7D11B CRC64;
     MSSICPEDSE LERLKGLVLE VLSYERDLYR PGWISNTAGE MAMNAIKLRS TIHELNCCRD
     TGLKHNNDLK EMNELFDEAI GSHETVKTIV PDGYLIDKNN NVLTVLEVST RTEPSDQTKK
     VQLDRLKYDG FENLLRPLGW TLNVITISEK KPRIGRIPEI LMFKLLSTSL SILSYTTDIC
     NWISEEDYLE LKKSLTSYDF RTLTEEFKGQ RLLFDIESAE DPYKDLFDWM LKNSEKLPFS
     LNWEGPKITE MIQDFKREDK QLRLLEIMRS AVTGLNFRTN HLSLLNKLKS LNLLNTRRKQ
     NKVYDYIALM LFVRDSEIHD FPKGWFPSVN DRLVRVDSVD SPLSVYKKLV ERMIKSLQSL
     QNEVGSKQKL GELKILIKFL EESSNNFIEP PVLKTMYFGL PARVLVPQPS LCLKIINDVP
     YEPQTTIVTS DETDTIEKVA LNLILSQKTR STPRASMSEE FFFQSVNGCL LLYKCTGEGQ
     KAFSILCKSY KQGELRYSFY SFNINPSRLF PLIFSAKPIA NLVDQLIMLI NPICEDAERL
     QETIKRQESV NEFLISSEYS DKQIDDLKVK VTYLIYGILT TPTKRLQIEL QSQRYYIMDT
     LSIIHHKDLK AKVIGNCITY DEYYLRDLAH GLINEILSCK NIGLFLKVTW ALNISYLCHL
     ITKETPDRLS DLRDCYEKFF KPKFQFMSNM IYDCKSVDEL VERMEQEVND FIQCEEPSFE
     TKPFLYEPIL ADFLKWISTE KFNGIDGEQL LNPKDYLTSN IDVLDLTSNK STFKRSKNHH
     MNDVLDQQYD TEKLLKRVIS ERLHKRITKS TKAGDDPSTA KSFKSGGESV KERNWKAGGE
     KRKKTRLAYE EFLGIVQGLI VETDSEEDLN DFLLQINKCL HEIDDELKKM NPKEINDLQK
     TKYCLVLDVI RELLGPEVCD LVRSTCYSTK LSDLPTDLLR KEAYERIVGE TMSRAPLEFP
     RNVDTIDVTN ISAGMVVTKY ELKEFFSSFK FLLLWAGFNN FQGTYDHRSG PQSSFLSISN
     KYRGESMLST RVTNSEALQD RLIAIKYGAP TLRNILFSTL NLEMKNSEIG PNNKPLQFGL
     AIKEQVGGPR ELYVGDSDTK LITRVLEETS RNIGNRLNNS CLNSDKKFSN FMKRIARSFF
     ENEIVLSMDH SKWGPFNSPL QYHLMFEAME SINDTDGRRL DFSFAKTILK WHLFKAVETP
     QILAEDVILS SLDVSLGRRD RQIGKERTFE TFMVDAVLSN KPVPSQIHSW FDMGQGILHH
     TSDLYGSLAS EYITKKIKEI FGVRSSTMNT SDDMVLLFHI KYKNEDSNQK DELLLITNFL
     CLVSNCLNKH ISPKFCCSPL VGEFKSHFEV EATMVPLFTK FFAASINNFR CKTPMELFNT
     CDAIVEQGIC NGMSLKVADS LKGRMVEMLG WLGYVADPLM KPVESRQQDW LEGCLSYRKL
     RSLESWLMDL GIGKLKLDVL KLELLKVIKE LRESSIAPSV AYNKMVDISK SELGEITLWF
     PTLNGEFKLI VRSKLNLGTT INETCENLLI KKLINHYSRY SKQGLGLLIA EGLERSAFQS
     SVVTGFIGLS ISLSGACIRK GDGTFLTLKE SKNVVKPVAE VFPSLVMQSV CAVGDWVCGV
     ESEMDKQMNK SIYMRTSLVN TAEFRFGLDE LTAAIEMTMP DLFDKYLKDI VPPDKRLLMR
     HSWKVRPEME LLIECANKGL SIFDGRIDRQ EEAVVLVDYY EPGRLLRRTM KLEKRGPERT
     ARKGLQAIVN RMILDSILEP KIIDKTMVMD ATKLAPYEGS MEDLKSHGES GVRRYIQQVL
     LGRESHYRQK EDEPNEITSS NVVVYGRGTP EFPLEDGTWL RGAKLGTSNP IKLQCCLQQI
     SNDLKIQATL ITHTGRAHYQ DFMFLKRVII SDSDFDEPEI LDTLEFRDVV VVENSKPNGK
     PCFLFMGCVI PLESDLVGSI MTHMSEAEWE ELWKLVRTYF ITRMKGEISC LPKARFDALW
     GMVSRIFGYS TVEKVVTMGF HQLDSFAEFL TFTDRVFTTK GPTLVFHRLK GLLVSYPAGP
     LLYKGHRLML YKDWASGTPE PETLED