RDRP_IBDVU
ID RDRP_IBDVU Reviewed; 879 AA.
AC Q82630;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 67.
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 (isolate Chicken/UK/UK661/1989)
OS (IBDV) (Gumboro disease virus).
OC Viruses; Riboviria; Orthornavirae; Birnaviridae; Avibirnavirus.
OX NCBI_TaxID=644440;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8725117; DOI=10.1016/0168-1702(95)01253-2;
RA Brown M.D., Skinner M.A.;
RT "Coding sequences of both genome segments of a European 'very virulent'
RT infectious bursal disease virus.";
RL Virus Res. 40:1-15(1996).
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; X92761; CAA63417.1; -; Genomic_RNA.
DR RefSeq; NP_690839.1; NC_004179.1.
DR SMR; Q82630; -.
DR GeneID; 956510; -.
DR KEGG; vg:956510; -.
DR Proteomes; UP000007249; 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..879
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000378410"
FT DOMAIN 398..598
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 847..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; 97691 MW; 4E4BE23D99674DCB CRC64;
MSDVFNSPQA RSKISAAFGI KPTAGQDVEE LLIPKVWVPP EDPLASPSRL AKFLRENGYK
ILQPRSLPEN EEYETDQILP DLAWMRQIEG PVLKPTLSLP IGDQEYFPKY YPTHRPSKEK
PNAYPPDIAL LKQMIYLFLQ VPEATDNLKD EVTLLTQNIR DKAYGSGTYM GQATRLVAMK
EVATGRNPNK DPLKLGYTFE SIAQLLDITL PVGPPGEDDK PWVPLTRVPS RMLVLTGDVD
GEFEVEDYLP KINLKSSSGL PYVGRTKGET IGEMIAISNQ FLRELSALLK QGAGTKGSNK
KKLLSMLSDY WYLSCGLLFP KAERYDKSTC CTKTRNKWSA QSSTHLMISM ITWPVMSNSP
NNVLNIEGCP SLYKFNPFRG GLNRIVEWIM APDEPKALVY ADNIYIVHSN TWYSIDLEKG
EANCTRQHMQ AAMYYILTRG WSDNGDPMFN QTWATFAMNI APALVVDSSC LIMNLQIKTY
GQGSGNAATF INNHLLSTLV LDQWNLMKQP SPDSEEFKSI EDKLGINFKI ERSIDDIRGK
LRQLVPLAQP GYLSGGVEPE QPSPTVELDL LGWSATYSKD LGIYVPVLDK ERLFCSAAYP
KGVENKSLKS KVGIEQAYKV VRYEALRLVG GWNYPLLNKA CKNNASAARR HLEAKGFPLD
EFLAEWSELS EFGEAFEGFN IKLTVTPESL AELNRPVPPK PPNVNRPVNT GGLKAVSNAL
KTGRYRNEAG LSGLVLLATA RSRLQDAVKA MAEAEKLHKS KPDDPDADWF ERSETLSDLL
EKADIASKVA HSALVETSDA LEAVQSTSVY TPKYPEVKNP QTASHPVVGL HLPAKRATGV
QAALLGAGTS RPMGMEAPTR SKNAVKMAKR RQRQKESRQ