ID   RDRP_AQRVG              Reviewed;        1274 AA.
AC   B2BNE0;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   29-SEP-2021, entry version 41.
DE   RecName: Full=RNA-directed RNA polymerase VP2;
DE            EC=2.7.7.48;
GN   Name=S2;
OS   Aquareovirus G (isolate American grass carp/USA/PB01-155/-) (AQRV-G).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Spinareovirinae; Aquareovirus.
OX   NCBI_TaxID=648234;
OH   NCBI_TaxID=7959; Ctenopharyngodon idella (Grass carp) (Leuciscus idella).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=18191982; DOI=10.1016/j.virol.2007.12.006;
RA   Mohd Jaafar F., Goodwin A.E., Belhouchet M., Merry G., Fang Q.,
RA   Cantaloube J.F., Biagini P., de Micco P., Mertens P.P., Attoui H.;
RT   "Complete characterisation of the American grass carp reovirus genome
RT   (genus Aquareovirus: family Reoviridae) reveals an evolutionary link
RT   between aquareoviruses and coltiviruses.";
RL   Virology 373:310-321(2008).
CC   -!- FUNCTION: RNA-directed RNA polymerase that is involved in transcription
CC       and genome replication. Following infection, it catalyzes the synthesis
CC       of fully conservative plus strands. After core assembly, which consists
CC       in recruitment of one capped plus-strand for each genomic segments and
CC       polymerase complexes, the polymerase switches mode and catalyzes the
CC       synthesis of complementary minus-strands (By similarity).
CC       {ECO:0000255|PROSITE-ProRule:PRU00539}.
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   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the reoviridae RNA-directed RNA polymerase
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EF589099; ABV01040.1; -; Genomic_RNA.
DR   RefSeq; YP_001837095.1; NC_010585.1.
DR   SMR; B2BNE0; -.
DR   GeneID; 6218800; -.
DR   KEGG; vg:6218800; -.
DR   Proteomes; UP000001674; Genome.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR012915; RdRP_5.
DR   InterPro; IPR007097; RNA-dir_pol_reovirus.
DR   Pfam; PF07925; RdRP_5; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50523; RDRP_DSRNA_REO; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   RNA-directed RNA polymerase; Transferase; Viral RNA replication; Virion.
FT   CHAIN           1..1274
FT                   /note="RNA-directed RNA polymerase VP2"
FT                   /id="PRO_0000404173"
FT   DOMAIN          550..798
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ   SEQUENCE   1274 AA;  141975 MW;  3803AF205C265808 CRC64;
     MEDLFNALPQ PLQQLSLALA GEIPLNDELF QAAASTWHTR QRSETYHLLD RLRFSTPIVT
     PQAIYRDLPW RNCYRINQDR VERIPTTNAS DDVYVPNSDI STLLSPLFSI PTYGTLHPSI
     EKDALELRAD SARCASTFYK IASSQARQVK LDPTRMLEFL LLLVATPRVN SGLDTDQPSM
     RDPTKSPALH AIWQIMQYYK VDSKYHAPAL IVSTGAVWWI PPPGKRNVVS VQYLLTDLVN
     LAIIARMTDM HPTLGLCAAR VYIQAATTDS YTHTLLKLKG VFPALSIHSM YRQKGFGGKA
     PDIQWTEPRT KYQFKWVGVT HLHDGLRPRA PVRDEAVRKL LTEYQLADIM APIVEMRNQH
     KHHDHDSVRF VRDVMALTSG MYLVRQPTMS VLQEYSQVPD IKQPIPPSAW TGTVGNVRYL
     NKDVTGPARW LYNTWREAAQ EIAQDRTWHD PVNQFIMGSQ YVTARGGSGS SLKHSLTVTG
     LVLPEFSESS VKRSSKIYQA AQIARIPFTL LTAAIHAEVV MAIRNQVQRR ARSIMPLNVV
     QQAVSAPHTL VANYINKHMN MSTTSGSVVT DKVVPLLLYA STPPRTVVNV DIKACDASIT
     YDYFLSLICG AMHEGFEVGD NHASFMGVPS SIIMDKRSAL APYSRTVSGL QTMVQHLSQM
     YANGFRYSVT DAFSSGNKFS FPTSTFPSGS TATSTEHTAN NSTMMSYFLA VHAPQHIKSP
     NMKRVLSDMT IQRNYVCQGD DGVLLLPDEA ASKISAEDMD ELLTCLKDYG TSFGWVYDID
     WSDSAEYLKL FALCGCRVPN VSRHPPVGKE YASPTTDEIW PSLIDIVVGH HLNGVMDLMN
     WREWLRFSWA FACYASRGAY TDKYGETHIA QYPWWTFVYL GIPPILLPGQ TPFIHSLFMP
     PGDQAMFAIL NNWRDLISTN TTTTFPPLKH PHHTWHLADV PTLLDSYGVY AGYHAAQHPR
     RPVAQPETAN SESIEQITGA LTDYLLYDPI LKARVNTGRH NWSQLSQSIG LNIGGRVPSL
     MDVPGKWVAA GREAEKPPPS AIVYMFKSLN RTIRRPSKHF SKLLELYIRV KVVLGAPKPL
     AIDPDIPQVA GADPHNDDPW FKYVGLGDIP TSTRRYFGES LFVGRVVSGL DVEAVDAALL
     RLKILGAPPA AYIALLNGIG MSNSEANQIA GRVSLANAQT VQIGRVVNLS TPSSWMTLDT
     APYIQYHTYD FKPGVTNPSA QSREKFIWLS PILKLLCATA AMSIAGPVRE AYVLDIHGSA
     ASLSGNFREW MRAA