ID   RDRP_IBDVB              Reviewed;         879 AA.
AC   A7L9Z4;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 40.
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   Avian infectious bursal disease virus (strain Chicken/Cuba/Soroa/1998)
OS   (IBDV) (Gumboro disease virus).
OC   Viruses; Riboviria; Orthornavirae; Birnaviridae; Avibirnavirus.
OX   NCBI_TaxID=645118;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
OH   NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=10400796; DOI=10.1128/jvi.73.8.6973-6983.1999;
RA   Lombardo E., Maraver A., Caston J.R., Rivera J., Fernandez-Arias A.,
RA   Serrano A., Carrascosa J.L., Rodriguez J.F.;
RT   "VP1, the putative RNA-dependent RNA polymerase of infectious bursal
RT   disease virus, forms complexes with the capsid protein VP3, leading to
RT   efficient encapsidation into virus-like particles.";
RL   J. Virol. 73:6973-6983(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12551984; DOI=10.1128/jvi.77.4.2459-2468.2003;
RA   Maraver A., Clemente R., Rodriguez J.F., Lombardo E.;
RT   "Identification and molecular characterization of the RNA polymerase-
RT   binding motif of infectious bursal disease virus inner capsid protein
RT   VP3.";
RL   J. Virol. 77:2459-2468(2003).
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.
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DR   EMBL; EF688065; ABS18957.1; -; mRNA.
DR   SMR; A7L9Z4; -.
DR   Proteomes; UP000007429; 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   2: Evidence at transcript level;
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..879
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000378411"
FT   DOMAIN          398..598
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          846..879
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..879
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         259..266
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   879 AA;  97685 MW;  E08D0F214C1A3AAB CRC64;
     MSDVFNSPQA RSTISAAFGI KPTAGQDVEE LLIPKVWVPP EDPLASPSRL AKFLRENGYK
     VLQPRSLPEN EEYETDQILP DLAWMRQIEG AVLKPTLSLP IGDQEYFPKY YPTHRPSKEK
     PNAYPPDIAL LKQMIYLFLQ VPEANEGLKD EVTLLTQNIR DKAYGSGTYM GQANRLVAMK
     EVATGRNPNK DPLKLGYTFE SIAQLLDITL PVGPPGEDDK PWVPLTRVPS RMLVLTGDVD
     GDFEVEDYLP KINLKSSSGL PYVGRTKGET IGEMIAISNQ FLRELSTLLK QGAGTKGSNK
     KKLLSMLSDY WYLSCGLLFP KAERYDKSTW LTKTRNIWSA PSPTHLMISM ITWPVMSNSP
     NNVLNIEGCP SLYKFNPFRG GLNRIVEWIL APEEPKALVY ADNIYIVHSN TWYSIDLEKG
     EANCTRQHMQ AAMYYILTRG WSDNGDPMFN QTWATFAMNI APALVVDSSC LIMNLQIKTY
     GQGSGNAATF INNHLLSTLV LDQWNLMRQP RPDSEEFKSI EDKLGINFKI ERSIDDIRGK
     LRQLVLLAQP GYLSGGVEPE QSSPTVELDL LGWSATYSKD LGIYVPVLDK ERLFCSAAYP
     KGVENKSLKS KVGIEQAYKV VRYEALRLVG GWNYPLLNKA CKNNAGAARR HLEAKGFPLD
     EFLAEWSELS EFGEAFEGFN IKLTVTSESL AELNKPVPPK PPNVNRPVNT GGLKAVSNAL
     KTGRYRNEAG LSGLVLLATA RSRLQDAVKA KAEAEKLHKS KPDDPDADWF ERSETLSDLL
     EKADIASKVA HSALVETSDA LEAVQSTSVY TPKYPEVKNP QTASNPVVGL HLPAKRATGV
     QAALLGAGTS RPMGMEAPTR SKNAVKMAKR RQRQKESRQ