RDRP_IBDVA
ID RDRP_IBDVA Reviewed; 878 AA.
AC P12918;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 Australian 002-73) (IBDV)
OS (Gumboro disease virus).
OC Viruses; Riboviria; Orthornavirae; Birnaviridae; Avibirnavirus.
OX NCBI_TaxID=10997;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2831661; DOI=10.1016/0042-6822(88)90258-9;
RA Morgan M.M., Macreadie I.G., Harley V.R., Hudson P.J., Azad A.A.;
RT "Sequence of the small double-stranded RNA genomic segment of infectious
RT bursal disease virus and its deduced 90-kDa product.";
RL Virology 163:240-242(1988).
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; M19336; AAA89177.1; -; Genomic_RNA.
DR PIR; A28649; RRXSIB.
DR SMR; P12918; -.
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..878
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000221962"
FT DOMAIN 397..597
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 845..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 258..265
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 878 AA; 97274 MW; 6B67C1E0AC193D1F CRC64;
MSDVFNSPQA RTKISAAFGI KPTAGQDVEE LLIPKVWVPP EDPLASPSRL AKFLRENGYK
ILQPRSLPEN EEYETDQILP DLAWMRQIEG AVLKPTLSLH WGPRVLPKVL LNSPPEQGKA
QCVPTRHCTT QADIYLFLQV PEATESLKDE VTLLTQNIRD KAYGSGTYMG QATRLVAMKE
VATGRNPNKD PLKLGYTFES IAQLLDITLP VGPPGEDDKP WVPLTRVPSR MLVLTGDVDG
DFEVEDYLPK INLKSSSGLP YVGRTKGETI GEMIAISNQF LRELSALLKQ GAGTKGSNKK
KLLSMLSDYW YLSCGLLFPK AERYDKSTWL TKTRNIWSAP SPTHLMISMI TWPVMSNSPN
NVLNIEGCPS LYKFNPFRGG LNRIVEWILA PEEPKALVYA DNIYIVHSNT WYSIDLEKGE
ANCTRQHMQA AMYYILTRGW SDNGDPMFNQ TWASFAMNIA PALVVDSSCL IMNLQIKSYG
QGSGNAATFI NNHLLSTLVL DQWNLMKQPN PDSEEFKSIE DKLGINFKIE RSIDDIRGKL
RQLVPLAQPG YLSGGVEPEQ SSPTVELDLL GWSATYSKDL GIYVPVLDKE RLFCSAAYPK
GVENKSLKSK VGIEQAYKVV RYEALRLVGG WNYPLLNKAC KNNASAARRH LEAKGFPLDE
FLAEWSELSE FGETFEGFNI KLTVTRENLA ELNKPVPPKP PNVNRPVNTG GLKAVSNALK
TGRYRNEAGL SGLVLLATAR SRLQDAVKAK AEAEKLHKSK PDDPDADWFE RSETLSDLLE
KADVASKVAH SALVETSDAL EAVQSSSVYT PKYPEVKNPQ TASNPVVGLH LPAKRATGVQ
AALLGAGTSR PMGMEAPTRS KNAVKMAKRA QRQKESRQ