RDRP_APRVF
ID RDRP_APRVF Reviewed; 1233 AA.
AC Q2Y0E9;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 23-FEB-2022, entry version 38.
DE RecName: Full=RNA-directed RNA polymerase VP2;
DE EC=2.7.7.48;
GN Name=S2;
OS Aedes pseudoscutellaris reovirus (isolate France) (ApRV).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Spinareovirinae; Dinovernavirus.
OX NCBI_TaxID=648170;
OH NCBI_TaxID=316597; Aedes pseudoscutellaris (Mosquito) (Stegomyia pseudoscutellaris).
RN [1]
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 viruses:
RT isolation and characterization of a new virus designated Aedes
RT pseudoscutellaris reovirus assigned to a proposed genus (Dinovernavirus).";
RL Virology 343:212-223(2005).
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:0000250}.
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;
CC -!- SUBUNIT: Interacts with VP6. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the reoviridae RNA-directed RNA polymerase
CC family. {ECO:0000305}.
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DR EMBL; DQ087277; AAZ94069.1; -; Genomic_RNA.
DR RefSeq; YP_443936.1; NC_007667.1.
DR SMR; Q2Y0E9; -.
DR PRIDE; Q2Y0E9; -.
DR GeneID; 5076689; -.
DR KEGG; vg:5076689; -.
DR Proteomes; UP000001676; Genome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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.
PE 3: Inferred from homology;
KW Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW RNA-directed RNA polymerase; Transferase; Viral RNA replication.
FT CHAIN 1..1233
FT /note="RNA-directed RNA polymerase VP2"
FT /id="PRO_0000403276"
FT DOMAIN 1..775
FT /note="RdRp catalytic"
SQ SEQUENCE 1233 AA; 143302 MW; CC2B5C43577F84D2 CRC64;
MATEPNEINL RMTQTRMKQI EDTTFKIRRK HDDMYTYLIN DIEATEMYPD TETPFRMKSS
LNNTYIQVKC QIPKLIMQPP LYNNDMYPLN HNSTNFLEDR PFNYLCNFDW FEFLSRSKDE
LGMHYNMIRD LISMSSQTRY SNIWSNISGI IMYLRQYKRG FALRSILIRL LTYWNNFPFF
DTWDGFKDVL PKTSTAWPLL FYAFMSVAFD YICENISEGD AIVCFQNHLE NAQISYQDTK
LEKKNGYTLW LKYECHNLRV ALTPRYDYTG TVYGNFLKDT TEYIITDEFE ENEIKMKNIL
NPSFYKILQQ LRREIKTVED IIRLLTICYS ARDDRTYYGT LMELAISKAI KPQVAGSIVP
KPIPTSWLQK DPKIVLSAKY PSTSFLSQMQ EFYRRYYPAL QREIDVHALS ASFINFLSTA
SAGVGIELPE EIINMVKDKR LLYLLKKGSG KRVLQEALLV ERYNDLDPII NDFVRLIKIV
VRKQIERRQR GIAGIPNNVL KINQVTYEAN KPFSKIARAP SHGKQSGNAS DIHDLLFYTT
QEDVSHIEVN GKRQMRGIVI SSADVKGMDT HIQINAAMNQ HLGAIEILDG IQYDVGPFRQ
TRAVIQDIQG NVYERNLNGG QQAIAFGLAN FSQTTGINSK YFGQIPNQEG TFPSGLITTS
NHHTQMLTLL IETAATTFTN EFGKSIAIAH LMILGDDVSL MLHGNDKDVN FFMKYLVEKF
SQLGLILERD ESRNFGVFLQ QHVINGRFNG FSNRIAIFTS EDYKTRKSVQ ESCTEYNALI
DDVIFRTYNV RKLLQFQRIH QFVVLSKYIF RVQNYKYEKL KAKLATRLNV FEYDLKPHND
SRENVQNQNM LRFIGIQIPY TYFQCSGGGE IPPESFQRKD GSFTYEYSIY SPKGKWLRKF
LYDISCTIDE PKFRIDDEIM RMYNLDICDF LIQYNMLNIQ EEIRATIIDR ELISKLAMNL
ESLENSNARM ISRRASESLR IMGIKLPANG VYGYQINERL VKVLQNIQQS DYEVKMVGDA
LFTAIMEKFD SHKVRMEKGD RLHNFTLDFS DKSDRLVINK KMIALHNISI SKNMAPYSDA
WMLYTCLNHT YNASSELSTA LAHSQGHFKS FQYDRDMFAE SVKIASKHGI GSLPMELFFE
ASNIRDSAQL KWIEAIKYYI QFKDYLYPYS INPRRLFFIP EQVSSVSSLL NQDNIPADAN
KKALMFRRAY AYVLSHPFRI SGAKAIFVDD RIS