ID   RDRP_DXV96              Reviewed;         997 AA.
AC   Q91CD5;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 2.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=RNA-directed RNA polymerase;
DE            Short=RDRP;
DE            EC=2.7.7.48;
DE   AltName: Full=Protein VP1;
GN   Name=VP1;
OS   Drosophila x virus (isolate Chung/1996) (DXV).
OC   Viruses; Riboviria; Orthornavirae; Birnaviridae; Entomobirnavirus.
OX   NCBI_TaxID=654931;
OH   NCBI_TaxID=7227; Drosophila melanogaster (Fruit fly).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12069523; DOI=10.1006/viro.2001.1334;
RA   Shwed P.S., Dobos P., Cameron L.A., Vakharia V.N., Duncan R.;
RT   "Birnavirus VP1 proteins form a distinct subgroup of RNA-dependent RNA
RT   polymerases lacking a GDD motif.";
RL   Virology 296:241-250(2002).
CC   -!- FUNCTION: RNA-dependent RNA polymerase which is found both free and
CC       covalently attached to the genomic RNA. May also contain guanylyl and
CC       methyl transferase activities (By similarity). {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; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC   -!- SUBUNIT: Interacts with VP3 in the cytoplasm. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Note=Minor amounts are
CC       incorporated in the virion. {ECO:0000250}.
CC   -!- PTM: May exist in multiple phosphorylated forms.
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; AF196645; AAL13168.2; -; Genomic_RNA.
DR   RefSeq; NP_690806.1; NC_004169.1.
DR   SMR; Q91CD5; -.
DR   GeneID; 993339; -.
DR   KEGG; vg:993339; -.
DR   Proteomes; UP000000515; Genome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR   GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR007100; RNA-dir_pol_birnavirus.
DR   InterPro; IPR007098; RNA-dir_pol_mononegavirus.
DR   Pfam; PF04197; Birna_RdRp; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50524; RDRP_DSRNA_BIR; 1.
PE   3: Inferred from homology;
KW   Covalent protein-RNA linkage; GTP-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Phosphoprotein; Reference proteome;
KW   RNA-directed RNA polymerase; Transferase; Viral RNA replication; Virion.
FT   CHAIN           1..997
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000378412"
FT   DOMAIN          420..616
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          950..997
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        950..967
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         256..263
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   997 AA;  112779 MW;  2CE74CA091D9AC29 CRC64;
     MSDIFNQQGL KSKFSNIVKN EGQGDSDIRE VFNELARPQA EVGRDIEYSE LSQALNDNSV
     KVFRPQPYDE LVNIPFIEAA SPRMMALYGE LLDSKDVSLP VGSGLHIPTY KPGHEVTPPL
     LTLPNSLSYE YMHYIANSAN DTWDKQIYET LKELLVAQAT NRFSTGSLLG QVKRVAAGQD
     VAYGRKGHHK NKSFKEMGIT PYRVMEWLDE YMPISDDEPE ITLSNTLDWL VYTPEEAELM
     GVPDSLPDIT QSSAAGLPWL GKKKGEVAVS ALITANMLIK DVSQLLKENL FTGSNNPLDP
     KKEGVAEVTT KNPRRAADQF SRQVLDRIIK EYSYTMMGLL FPKGERYAIA DHLTKTRNIW
     SASYVTHLIG STISDQPAKR MLNVLTSTSR TPSLAKFSPT QGGMEALINI ILNATDIVEL
     VYADNAYIYY PNEDIWYSID LTKGEANCTR DVAMTTAMYL LTRGWTSKQG TPIYNYTWAY
     LALYGIPYMT VDSISVLKNF QIKNPGQGSG NPWTFLNNHV LTTILMNKWS EIGKPQPSPD
     VIEKLASMTG IDFKVELVVT NFREKLIAAS RHSIPTSNRV EPRTIVEMDM LGWDVTHTEF
     GFTPVLSKER LFKSIACPQP PSSTFQTSVA KQVHKYIQNV ALLYVGAWAY PCIAQTIEGY
     ALNHWNTINI MIRNKEYDLD KAIGKAVEAS PFSEVISLLS LDRPMHEQNY AQVLYQQKTI
     EKKEAKPKVS NPLYKRDKET YHEYTTRMAR MRINDDMVGP QWEPIINLVT KLYPREATGE
     NQKSRESMTR VKIRGLLENM ERQLESNGRS MDVWYNAYLT GKKPSGVDKK LATLLVLLAP
     KRTKKLPSGV YQKLLGYPPI DKSPVPSLTS DEAYLYDTNS LEYNRIAYVS KLNEDDITVY
     ANKYMVYSST LLSNLLPDKV DWPELRSMNV EGASDPYQVK GYKKKELKPR FGEEILDDEP
     TGKKSSSEKR RLQRKGQKAK LQRQAATGTT FVRKPLN