RDRP_IPNVS
ID RDRP_IPNVS Reviewed; 844 AA.
AC P22174;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, 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 Infectious pancreatic necrosis virus (strain Sp) (IPNV).
OC Viruses; Riboviria; Orthornavirae; Birnaviridae; Aquabirnavirus.
OX NCBI_TaxID=11005;
OH NCBI_TaxID=8022; Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OH NCBI_TaxID=8028; Salmo.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1901682; DOI=10.1016/0042-6822(91)90887-h;
RA Duncan R., Mason C.L., Nagy E., Leong J.-A., Dobos P.;
RT "Sequence analysis of infectious pancreatic necrosis virus genome segment B
RT and its encoded VP1 protein: a putative RNA-dependent RNA polymerase
RT lacking the Gly-Asp-Asp motif.";
RL Virology 181:541-552(1991).
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: Exists in multiple phosphorylated forms.
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DR EMBL; M58757; AAA46244.1; -; Genomic_RNA.
DR PIR; B37946; RRXSSP.
DR SMR; P22174; -.
DR Proteomes; UP000007213; 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..844
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000221964"
FT DOMAIN 384..588
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 820..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 248..255
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 844 AA; 94089 MW; 0E8D7B9553A7A456 CRC64;
MSDIFNSPQN KASILNALMK STQGDVEDVL IPKRFRPAKD PLDSPQAAAA FLKEHKYRIL
RPRAIPTMVE IETDAALPRL AAMVDDGKLK EMVNVPEGTT AFYPKYYPFH RPDHDDVGTF
GAPDITLLKQ LTFFLLENDF PTGPETLRQV REAIATLQYG SGSYSGQLNR LLAMKGVATG
RNPNKTPLAV GYTNEQMARL MEQTLPINPP KNEDPDLRWA PSWLIQYTGD ASTDKSYLPH
VTAKSSAGLP YIGKTKGDTT AEALVLADSF IRDLGKAATS ADPGAAAKKV LSDFWYLSCG
LLFPKGERYT QKDWDLKTRN IWSAPYPTHL LLSMVSSPVM DESKLNITNT QTPSLYGFSP
FHGGINRIMT IIREHLDQEQ DLVMIYADNI YILQDNTWYS IDLEKGEANC TPQHMQAMMY
YRLTREWTNE DGSPRYNPTW ATFAMYVGPS MVVDSTCLLM NLQLKTTGQG SGNAFTFLNN
HLMSTIVVAE WHKAGRPNPM SKEFMDLEAK TGINFKIERE LKDLRSIIME AVDTAPLDGY
LADGSDLPPR VPGKAVELDL LGWSAVYSRQ LEMFVPVLEN ERLIASVAYP KGLENKSLAR
KPGAEIAYQI VRYEAIRLIG GWNNPLIETA AKHMSLDKRK RLEVKGIDVT GFLDDWNTMS
EFGGDLEGIS LTAPLTNQTL LDINTPETEF DVKDRPPTPR SPGKTLAEVT AAITSGTYKD
PKSAVWRLLD QRTKLRVSTL RDHAHALKPA ASTSDFWGDA TEELAEQQQL LMKANNLLKS
SLTEAREALE TVQSDKIISG KTSPEKNPGT AANPVVAYGE FSEKIPLTPT QKKNAKRREK
QRRN