ID   RDRP_IBDV5              Reviewed;         525 AA.
AC   P31817;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   29-SEP-2021, entry version 75.
DE   RecName: Full=RNA-directed RNA polymerase;
DE            Short=RDRP;
DE            EC=2.7.7.48;
DE   AltName: Full=Protein VP1;
DE   Flags: Fragment;
GN   Name=VP1;
OS   Avian infectious bursal disease virus (strain 52/70) (IBDV) (Gumboro
OS   disease virus).
OC   Viruses; Riboviria; Orthornavirae; Birnaviridae; Avibirnavirus.
OX   NCBI_TaxID=10996;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
OH   NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Bayliss C.D.;
RL   Thesis (1980), University College of Wales, United Kingdom.
RN   [2]
RP   FUNCTION.
RX   PubMed=2157806; DOI=10.1099/0022-1317-71-4-977;
RA   Spies U., Muller H.;
RT   "Demonstration of enzyme activities required for cap structure formation in
RT   infectious bursal disease virus, a member of the birnavirus group.";
RL   J. Gen. Virol. 71:977-981(1990).
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       ECO:0000269|PubMed:2157806}.
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; D12610; BAA02135.1; -; Genomic_RNA.
DR   PIR; PS0378; RRXSI5.
DR   SMR; P31817; -.
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; RNA-directed RNA polymerase;
KW   Transferase; Viral RNA replication; Virion.
FT   CHAIN           <1..>525
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000221961"
FT   DOMAIN          72..272
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   NON_TER         1
FT   NON_TER         525
SQ   SEQUENCE   525 AA;  57979 MW;  1B7ECF35CE49EE06 CRC64;
     KSTWLTKTRN IWSAPSPTHL MISMITWPVM SNSPNNVLNI EGCPSLYKFN PFRGGLNRIV
     EWILAPEEPK ALVYADNIYI VHSNTWYSID LEKGEANCTR QHMQAAMYYI LTRGWSDNGD
     PMFNQTWATF AMNIAPALVV DSSCLIMNLQ IKTYGQGSGN AATFINNHLL STLVLDQWNL
     MRQPRPDSEE FKSIEDKLGI NFKIERSIDD IRGKLRQLVP LAQPGYLSGG VEPEQSSPTV
     ELDLLGWSAT YSKDLGIYVP VLDKERLFCS AAYPKGVENK SLKSKVGIEQ AYKVVRYEAL
     RLVGGWNYPL LNKACKNNAG AARRHLEAKG FPLDEFLAEW SELSEFGEAF EGFNIKLTVT
     SESLAELNKP VPPKPPNVNR PVNTGGLKAV SNALKTGRYR NEAGLSGLVL LATARSRLQD
     AVKAKAEAEK LHKSKPDDPD ADWFERSETL SDLLEKADIA SKVAHSALVE TSDALEAVQS
     TSVYTPKYPE VKNPQTASNP VVGLHLPAKR ATGVQAALLG AGTSR