ID   RDRP_BOOLV              Reviewed;         998 AA.
AC   Q992J0;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   13-SEP-2023, entry version 58.
DE   RecName: Full=RNA-directed RNA polymerase;
DE            Short=RdRp;
DE            EC=2.7.7.48 {ECO:0000250|UniProtKB:Q66929};
DE   AltName: Full=RNA replicase;
DE            Short=Protein A;
OS   Boolarra virus (BoV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Magsaviricetes;
OC   Nodamuvirales; Nodaviridae; Alphanodavirus.
OX   NCBI_TaxID=12286;
OH   NCBI_TaxID=41021; Hepialidae (ghost moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11457991; DOI=10.1099/0022-1317-82-8-1855;
RA   Johnson K.N., Johnson K.L., Dasgupta R., Gratsch T., Ball L.A.;
RT   "Comparisons among the larger genome segments of six nodaviruses and their
RT   encoded RNA replicases.";
RL   J. Gen. Virol. 82:1855-1866(2001).
CC   -!- FUNCTION: RNA-dependent RNA polymerase, which replicates the viral
CC       genome composed of 2 RNA segments, RNA1 and RNA2. Does not need an
CC       exogenous primer. Also possesses a terminal nucleotidyl transferase
CC       (TNTase) activity. The TNTase catalyzes the addition of nucleotide to
CC       the 3'-end of plus- and minus-stranded RNAs, probably to repair the 3'-
CC       end nucleotide loss. Forms the open necked connection to the cytosol of
CC       the virus-induced replication vesicles. Mediates viral RNA1
CC       recruitment. {ECO:0000250|UniProtKB:Q66929}.
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:0000250|UniProtKB:Q66929};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249;
CC         Evidence={ECO:0000250|UniProtKB:Q66929};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q66929};
CC       Note=For RdRP activity. {ECO:0000250|UniProtKB:Q66929};
CC   -!- SUBUNIT: Homododecamer. Forms 2 stacked rings of 35-nm in diameter,
CC       arranged in a crown-like structure at the opening of virus-induced
CC       replication vesicles. Interacts with protein B2.
CC       {ECO:0000250|UniProtKB:Q66929}.
CC   -!- SUBCELLULAR LOCATION: Host mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:Q66929}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q66929}. Note=Part of the 30- to 90-nm
CC       invaginations of the host mitochondrial outer membrane that form the
CC       viral replication complexes vesicules. Has a N-terminal membrane-
CC       spanning mitochondrial anchor. {ECO:0000250|UniProtKB:Q66929}.
CC   -!- DOMAIN: The N-terminus is important for both membrane association and
CC       mitochondrial localization. It may also contain a RNA methyltransferase
CC       (MTase-GTase) capping domain. The C-terminus contains the RNA-dependent
CC       RNA polymerase domain and a structurally disordered region at the very
CC       end. {ECO:0000250|UniProtKB:Q66929}.
CC   -!- MISCELLANEOUS: The viral bipartite genome is composed of RNA1 and RNA2.
CC       {ECO:0000250|UniProtKB:Q66929}.
CC   -!- SIMILARITY: Belongs to the nodaviridae RNA polymerase family.
CC       {ECO:0000305}.
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DR   EMBL; AF329080; AAK15751.1; -; Genomic_RNA.
DR   RefSeq; NP_689439.1; NC_004142.1.
DR   SMR; Q992J0; -.
DR   GeneID; 956656; -.
DR   KEGG; vg:956656; -.
DR   OrthoDB; 155at10239; -.
DR   Proteomes; UP000204043; Genome.
DR   GO; GO:0044193; C:host cell mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   CDD; cd23173; ps-ssRNAv_Nodaviridae_RdRp; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR043647; Noda_Vmethyltr_dom.
DR   Pfam; PF19222; Noda_Vmethyltr; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
PE   3: Inferred from homology;
KW   Host membrane; Host mitochondrion; Host mitochondrion outer membrane;
KW   Membrane; Nucleotidyltransferase; RNA-directed RNA polymerase; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..998
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000222445"
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          44..998
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q66929"
FT   REGION          91..282
FT                   /note="Capping"
FT                   /evidence="ECO:0000250|UniProtKB:Q66929"
FT   REGION          901..998
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        901..936
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        944..958
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        692
FT                   /note="For RdRp/TNTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q66929"
SQ   SEQUENCE   998 AA;  111204 MW;  7FAFFE4FC7329253 CRC64;
     MTIKIILGEH QITRTELLGG IVIVSGCGAV AYCISKFWGY GAIAPYPQSG GNRVTRALQR
     AVIDKTKTPI KTHFYPLDSL RTVTPRRASD NGHAVSGAVR DAARRLINES IETVGGSKFE
     LNPNPNSTMG PRNHFHFAVG DLAQNFRDDQ PAADAFIVGV DVDYYITEPD VLLEHMRPLV
     LHTFNPKKVS GFDADSPFTI NNNLVEYKVS GGAAWVHPVW DWCEAGEFIA SRVRSSWFEW
     LLQLPLRCLG LERVGYHKIH HCRPWTDCPD RALVYTIPQH TVWRFTWIDT EIHTRKLKRI
     TYQDNTKPGW NRLEHVSDNN QLLVSIGREG EHMQITIEKD KLEMLSGLGA TQSVNARLIG
     MGHKDPLYTS MIVQYYTGKK VVLSVAPTVY RPTMPRVHWP VTSDADVPEV SARQYTKPII
     SDCMMMPMIK RWETMSESIE RRVTFVANNK KPSDAVAKIA AEFVSLMNGP FIDLEPLTIE
     ETVERLNKPS QQLQLRAVFE IMGVEPRQVI ESFNKNEPGM KSSRIISAFP DILFIVKVSR
     YTLAYSDAVL HAEHNQHWYY PGRTPVGITD GVCEFVSDCD GQVIETDFSN LDGRVSGWMQ
     RNIAQKAMVQ AFRAEYRDEI ISFMDTIINC PAKAKRFGFR YEPGMGVKSG SPTTTPHNTQ
     YNACVEYTAL KFEYPDANPE DLFSLLGPKC GDDGLARATI QKTINRAAKC YGLELKVEKY
     NPEVGLCFLS RVFVDPLNTP TTIQDPLRTL RKLHITTRDP TIPIADAACD RVEGYLCTDA
     HTPLISEYCR MVQRLYGPKT STRDVREARR SRNKEKPYWL TCDGSWPQHP QDALLMKQIV
     VSRTGIDEDT VDKLIGRFAA MKDVWEPITL ESEESKAAQT IDEEGVAPGS VDESLLKLND
     AKQTRSNSGT SGPHTKGGGS GTGNELPRST KQRAKGPRQS AGLPKQGKAN SKPNGNVAAG
     QAQHGGIPRG KTPSGGKTNA RRAPPKAGAQ PGAPTNPK
//