RDRP_IBDV
ID RDRP_IBDV Reviewed; 881 AA.
AC Q9Q6Q5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 69.
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 (IBDV) (Gumboro disease virus).
OC Viruses; Riboviria; Orthornavirae; Birnaviridae; Avibirnavirus.
OX NCBI_TaxID=10995;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Isolate CEF94;
RX PubMed=10600604; DOI=10.1006/viro.1999.0042;
RA Boot H.J., ter Huurne A.A., Peeters B.P.H., Gielkens A.L.;
RT "Efficient rescue of infectious bursal disease virus from cloned cDNA:
RT evidence for involvement of the 3'-terminal sequence in genome
RT replication.";
RL Virology 265:330-341(1999).
RN [2]
RP PROTEIN SEQUENCE OF 19-29.
RA Pan J., Vakharia V.N., Tao Y.J.;
RL Submitted (MAY-2007) to UniProtKB.
RN [3]
RP INTERACTION WITH VP3.
RC STRAIN=Isolate CEF94;
RX PubMed=12388690; DOI=10.1128/jvi.76.22.11301-11311.2002;
RA Tacken M.G., Peeters B.P.H., Thomas A.A.M., Rottier P.J.M., Boot H.J.;
RT "Infectious bursal disease virus capsid protein VP3 interacts both with
RT VP1, the RNA-dependent RNA polymerase, and with viral double-stranded
RT RNA.";
RL J. Virol. 76:11301-11311(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND MUTAGENESIS OF 401-ALA--ASN-403.
RX PubMed=17456597; DOI=10.1073/pnas.0611599104;
RA Pan J., Vakharia V.N., Tao Y.J.;
RT "The structure of a birnavirus polymerase reveals a distinct active site
RT topology.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7385-7390(2007).
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.
CC {ECO:0000269|PubMed:12388690}.
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; AF194429; AAF16083.1; -; mRNA.
DR PDB; 2PGG; X-ray; 2.50 A; A=31-804.
DR PDB; 2PUS; X-ray; 2.40 A; A=1-845.
DR PDB; 2QJ1; X-ray; 3.48 A; A=5-845.
DR PDB; 2R70; X-ray; 2.70 A; A=1-845.
DR PDB; 2R72; X-ray; 3.15 A; A=1-845.
DR PDBsum; 2PGG; -.
DR PDBsum; 2PUS; -.
DR PDBsum; 2QJ1; -.
DR PDBsum; 2R70; -.
DR PDBsum; 2R72; -.
DR SMR; Q9Q6Q5; -.
DR EvolutionaryTrace; Q9Q6Q5; -.
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 1: Evidence at protein level;
KW 3D-structure; Covalent protein-RNA linkage; Direct protein sequencing;
KW GTP-binding; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW RNA-directed RNA polymerase; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..881
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000227880"
FT DOMAIN 398..598
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 846..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 259..266
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MUTAGEN 401..403
FT /note="ADN->GDD: Increases polymerase activity."
FT /evidence="ECO:0000269|PubMed:17456597"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2PUS"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 96..106
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2R70"
FT HELIX 128..139
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:2PGG"
FT HELIX 146..161
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 169..184
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:2PGG"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:2QJ1"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:2R72"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:2PGG"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 271..291
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:2PUS"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 342..356
FT /evidence="ECO:0007829|PDB:2PUS"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:2PUS"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 381..390
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 403..408
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 411..417
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 420..423
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 426..439
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 451..459
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 461..465
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 469..473
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 486..506
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 515..518
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 520..524
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 528..536
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 537..546
FT /evidence="ECO:0007829|PDB:2PUS"
FT TURN 552..554
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 566..570
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 573..578
FT /evidence="ECO:0007829|PDB:2PUS"
FT TURN 579..582
FT /evidence="ECO:0007829|PDB:2PUS"
FT STRAND 583..588
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 590..598
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 613..629
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 631..633
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 635..655
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 659..662
FT /evidence="ECO:0007829|PDB:2PUS"
FT TURN 663..665
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 666..668
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 673..675
FT /evidence="ECO:0007829|PDB:2PUS"
FT TURN 676..678
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 687..694
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 713..720
FT /evidence="ECO:0007829|PDB:2PUS"
FT TURN 721..723
FT /evidence="ECO:0007829|PDB:2R70"
FT TURN 728..730
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 731..741
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 744..746
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 747..760
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 771..782
FT /evidence="ECO:0007829|PDB:2PUS"
FT HELIX 793..801
FT /evidence="ECO:0007829|PDB:2PUS"
SQ SEQUENCE 881 AA; 97911 MW; 3FBB3EDB3B744D7B CRC64;
MSDIFNSPQA RSTISAAFGI KPTAGQDVEE LLIPKVWVPP EDPLASPSRL AKFLRENGYK
VLQPRSLPEN EEYETDQILP DLAWMRQIEG AVLKPTLSLP IGDQEYFPKY YPTHRPSKEK
PNAYPPDIAL LKQMIYLFLQ VPEANEGLKD EVTLLTQNIR DKAYGSGTYM GQATRLVAMK
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 RQRQKESRQQ P
