ID   RDRP_AQRVC              Reviewed;        1274 AA.
AC   Q8JU61;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   05-JUN-2019, entry version 52.
DE   RecName: Full=RNA-directed RNA polymerase VP2;
DE            EC=2.7.7.48;
GN   Name=S2;
OS   Aquareovirus C (isolate Golden shiner/USA/GSRV/1977) (AQRV-C).
OC   Viruses; Riboviria; Reoviridae; Spinareovirinae; Aquareovirus.
OX   NCBI_TaxID=185783;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12124458;
RA   Attoui H., Fang Q., Mohd Jaafar F., Cantaloube J.F., Biagini P.,
RA   de Micco P., de Lamballerie X.;
RT   "Common evolutionary origin of aquareoviruses and orthoreoviruses
RT   revealed by genome characterization of Golden shiner reovirus, Grass
RT   carp reovirus, Striped bass reovirus and golden ide reovirus (genus
RT   Aquareovirus, family Reoviridae).";
RL   J. Gen. Virol. 83:1941-1951(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=16171838; DOI=10.1016/j.virol.2005.08.028;
RA   Attoui H., Mohd Jaafar F., Belhouchet M., Biagini P., Cantaloube J.F.,
RA   de Micco P., de Lamballerie X.;
RT   "Expansion of family Reoviridae to include nine-segmented dsRNA
RT   viruses: isolation and characterization of a new virus designated
RT   Aedes pseudoscutellaris reovirus assigned to a proposed genus
RT   (Dinovernavirus).";
RL   Virology 343:212-223(2005).
CC   -!- FUNCTION: RNA-directed RNA polymerase that is involved in
CC       transcription and genome replication. Following infection, it
CC       catalyzes the synthesis of fully conservative plus strands. After
CC       core assembly, which consists in recruitment of one capped plus-
CC       strand for each genomic segments and polymerase complexes, the
CC       polymerase switches mode and catalyzes the synthesis of
CC       complementary minus-strands (By similarity). {ECO:0000255|PROSITE-
CC       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:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
CC         ChEBI:CHEBI:83400; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00539};
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the reoviridae RNA-directed RNA polymerase
CC       family. {ECO:0000305}.
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DR   EMBL; AF403399; AAM92745.1; -; Genomic_RNA.
DR   RefSeq; NP_938061.1; NC_005167.1.
DR   SMR; Q8JU61; -.
DR   PRIDE; Q8JU61; -.
DR   GeneID; 2648330; -.
DR   KEGG; vg:2648330; -.
DR   Proteomes; UP000006713; 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; IPR012915; RdRP_5.
DR   InterPro; IPR007097; RNA-dir_pol_reovirus.
DR   Pfam; PF07925; RdRP_5; 1.
DR   PROSITE; PS50523; RDRP_DSRNA_REO; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome;
KW   RNA-directed RNA polymerase; Transferase; Viral RNA replication;
KW   Virion.
FT   CHAIN         1   1274       RNA-directed RNA polymerase VP2.
FT                                /FTId=PRO_0000404172.
FT   DOMAIN      561    798       RdRp catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00539}.
SQ   SEQUENCE   1274 AA;  141581 MW;  34C11609EF1B3D72 CRC64;
     MEELFNALPQ PLQQLSLALA GEIPLTDHIF EQAASTWHVQ PRSLTYKLLD HIPFSTPVVV
     PPSIYHSLDW SKCFAVNQDR VERVPTIDDP DDVYVPNSDI GPLLTSLHTI PDYGFLHPAI
     ENDATTLRAE RARCASTFYK IASSQARQVK LDPIRMLGFL LLVQARPRVP SGLVTDQPTR
     RDPTQSPALH AIWQVMQYYK VAGVYYAPAL VVPSGAIWWI PPPGKRNVVS VQYLLTDLIN
     LAILAHMTDM SPTLELTGVL MYLRAASSHS HAYTLLQMKS VFPALSLRSM YRNKGFGGKA
     PAIEWTEPRS KYKFRWTGVT QLHDGLRPRS PSMDVPTLEV LTKYELVDIG HIIIRERNAH
     PRHNHDSVRF VRDVMALTSG MYLVRQPTMS VLREYSQVPD IKDPIPPSAW TGPIGNVRYL
     LPSVQGPARH LYDTWRAAAR QIAQDPQWHD PLNQAIMRAQ YVTARGGSSA SLKFALKVTG
     IVLPEYDDSK VKKSSKIYQA AQIARIAFML LIAAIHAEVT MGIRNQVQRR ARSIMPLNVI
     QQAISAPHTL VANYINKHMN LSTTSGSVVT DKVIPLILYA STPPNTVVNV DIKACDASIT
     YNYFLSVICG AMHEGFEVGN ADAAFMGVPS TIVSDRRSSV APYSRPISGL QTMVQHLADL
     YAAGFRYSVS DAFSSGNKFS FPTSTFPSGS TATSTEHTAN NSTMMEYFLN VHAPSHVKSA
     SLKRILTDMT IQRNYVCQGD DGILLLPHEA ASKISADDMN ELLTCLRDYG QLFGWNYDID
     WSDTAEYLKL YALMGCRIPN TSRHPPVGKE YAAPQTDEIW PSLIDIVIGH HLNGVTDVLN
     WREWLRFSWA FACYSSRGGY TNPKGQSFSA QYPWWTFVYL GIPPILLPGQ TPFIHSCYMP
     PGDQGMFSIL NGWRDWLISH ASTTLPPLRH NHPVWGLSDV PSLLSQFGVY AGYHAAQHYR
     RPKPAPETAS SDSINQITSD LTEYLFYDSA LKARVMKGRY NWERLSSSLS LNVGSRVPSL
     FDVPGKWVAA GRDAEKPPPS SVEDMFTSLN RCIRRPTHSF SRLLELYLRV HVTLGESIPL
     AIDPDVPQVA GADPANDDHW FKYTCLGDIP SATRNYFGES LFVGRVVSGL DVEAVDATLL
     RLKILGAPPE AFIAVLNGIG MSDSEAHQIA GRISLANAQL VQIARVVHLS IPSSWMTLNT
     GPYIHHHAYD FKPGITQPSA KSRDKSIWMS PILKLLCTSY AMTVAGPVRT SIVTEIDGSA
     AALSGNLRVW MRDV
//