L_PIRVV
ID L_PIRVV Reviewed; 2210 AA.
AC Q6RSS2;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
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 Pirital mammarenavirus (isolate Rat/Venezuela/VAV-488/1995) (PIRV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=49891;
OH NCBI_TaxID=134742; Sigmodon alstoni.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15084402; DOI=10.1016/j.virusres.2004.01.032;
RA Cajimat M.N., Fulhorst C.F.;
RT "Phylogeny of the Venezuelan arenaviruses.";
RL Virus Res. 102:199-206(2004).
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; AY494081; AAS72554.1; -; Genomic_RNA.
DR RefSeq; YP_025093.1; NC_005897.1.
DR SMR; Q6RSS2; -.
DR PRIDE; Q6RSS2; -.
DR GeneID; 2943174; -.
DR KEGG; vg:2943174; -.
DR Proteomes; UP000009266; 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..2210
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000361645"
FT DOMAIN 1163..1359
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT REGION 26..285
FT /note="Endonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT ACT_SITE 114
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 88
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT BINDING 88
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT BINDING 101
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04086"
FT BINDING 1319
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; 253470 MW; 4552633F41DC58DA CRC64;
MEEHVNELHD LVRKWVSDDE NFAEQKAIFL SQTKLRAITI EGLKLLSTIV EVDSCQKNSC
IHNREKTLNS ILRDNKIVCP TLPEIVPDGY RLIGDVLILL EVFVRSNQES FEKKYEQDYT
KLMQVKKDLQ SHGITLVPMI DGRSSYYVEF MPDWVVEKIR WHLIKLMDLL KEDGESVEEL
EYERLVSSLS ALENQSLGLE SLLSIKERGI EYIDRLTKIM YGNLNNNMSV DECKGEILRI
YQNFRQLFDQ GQFKPKYRKT DREFILKTLR EHGLIKCAIM SEEDSCKNCM IHMFKVLTII
KQSFVSNKNI ESSFILKEYN QLLSVCNKVK SLKVLNTRRG TLMVLDLIML NKLLSLIKIY
GIKAALTILR MQCIPAVNDR LLSIDFLISI YERKMIKSPK WLEKVHGKLK RVVQDCMFKA
LEDYLVEIDF DTWFSIKDEL LMTQQFKPSI CYRSSKGCVC NAETLKNLSM MTEEDFLSYL
KILSSLSLSL VNSMKTSSAP KSKINQANDF YGIVHCEEVY FQGFGDNNAC TLLYQKTGEK
SRCYSVAFSD NEQQIDYGSK ISFYADPKRF FLPIMSQDVL NRMCNEMLSW LDFLSDDNIK
VVADLLRKLI LCVLCTPSKR VQVYLQGFRY LIMAYVNEIH CNDLFAKLEV DALTASERQV
MIWMDDLTRI VLEMSKEADM AKSFKFILNL SYLCHLITKE TPDRLTDQIK CFEKFLEPKL
KFGSLMVNPD STPELTSEQE DQVCEGLHRL LNKKIFSKCE NIPGVSKELV SLCSSLFNSS
NLEVKPLLNH DPLTPSFTST ALDLSSNKSV VVPKLNEIGE TLTEYDFGKI VSSVVVDLTE
HFKTKGKYKL DPRDLRFRIF KKLSSLVEVN PTKKSNRKSE SGEVVAPDES FMDELTEEQQ
LMLSEIEVKV SKTFEGMSKD ELNRKQSKEK GAEAHLKRLW SKEVRDKISS ETSLHEVKDF
DVQLFPFDTY EELVTIVFND KSAHDFYFLE KYLNPCPLDM LMKNLTLKAF NEGDFFECFK
YILIASEFDN KIGRYDHKIR TRLGLKDPAL KIREEARIST RESNSESIAK RLDKSFFTNS
SLRNLCFYSD ESPTTRTGVA TDVGKLKFGL SYKEQVGGNR ELYVGDLNTK LITRLVEDYA
ESICSNMKYT CLNSESEFER ALLDMKSVVR QGGFAVSMDH SKWGPHMSPA IFAQLLRCLK
FRLKDGSEID KKAVLNILYW HLHKIVEVPF NVVQAFMSGF VKRGLGLMDR GGATLSEEFM
FGFFEKGVVP SHLSSVVDMG QGILHNMSDL YGLITEQFIN YVLDFCYNVS MTSYTSSDDE
IMLSTSSALN HEDGSLNVDV ALEILEFHNF LSDKLNKFVS PKTVAGTFAS EFKSRFFIWS
QEVPLLTKFV AAALHNIKAK APNQLAETVD TILDQCVANG VSIEIVGAIS KRTNSLVCYS
GHPLNPFLCL EESDVRDWVD GSRGYRLQRS IENIFPDDLC PNLIRDACRK VFHRIQSGKI
EEEFLVASIQ GSPDECLNSM LTIADVDEDI KKDLAGYRWL NLRAYGDLRL VLRTKLMSST
RTLQREEIPS LVRSVQSKLS KNFVRGAKRI LTDAINKSAF QSCISSGFIG VCKSMGSKCV
RDNTGGFVYI KEITKHVMPH TTSYCPYCKP SKNIYCEDAL RSVSEYSRPI FWDYFSLVLS
NACELGNWVF GAPILPKTVF HLDNPNHFWP IKPSSQTELE DKVGMNHVLY SIRRNYPSIF
DEHISPYMSD LNMLRLSWVQ KIKFLDLCVA LDMSSECLGI ISHIMRRKRE ELYIVKQQEL
SMSHTRESTN LESGLSLEPQ EVCKNFLLQV LFDSMVNPVL LTTSQFRKYF WYGEVLQLPN
DASHHLAQFT QFILDCKQLN SSRAMTLDDL DVGYVTSRVK RTTTFVALST FITSLDWENR
HEYKSFQELI LSSPCDVFKF EFSMTFSHIR SSHKFRYERC TSYILKVHVV FDKRVLNSNM
LEDQSLLITP HSVEYFVSQS GGNHISLDGV GLLPLDPLIS GKEVLNIDDV LRHEDVNFSA
ESPLFSKMRF DFKPFLKELK NKFSYKLIGP DIIMEPLVLD KGQIKEGSRI VSQLKLRLDF
KAVFVALGCL EEESRSTFIS NLFMYIGSLR GEEHRISMTE SNLVQLIDNY PQVFDSMLDA
TNDWLNCGSF SLCKSKSLGC VMIADERGPF KLKGVNCRRL LPDSQAVEID
