RDRP_QRFVE
ID RDRP_QRFVE Reviewed; 777 AA.
AC D0QX26;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 23-FEB-2022, entry version 40.
DE RecName: Full=RNA-directed RNA polymerase catalytic subunit;
DE EC=2.7.7.48;
GN Name=PB1; OrderedLocusNames=Segment 1;
OS Quaranfil virus (isolate QrfV/Tick/Afghanistan/EG_T_377/1968) (QRFV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Quaranjavirus.
OX NCBI_TaxID=1559362;
OH NCBI_TaxID=6939; Ixodidae (hardbacked ticks).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=19726499; DOI=10.1128/jvi.00677-09;
RA Presti R.M., Zhao G., Beatty W.L., Mihindukulasuriya K.A., da Rosa A.P.,
RA Popov V.L., Tesh R.B., Virgin H.W., Wang D.;
RT "Quaranfil, Johnston Atoll, and Lake Chad viruses are novel members of the
RT family Orthomyxoviridae.";
RL J. Virol. 83:11599-11606(2009).
CC -!- FUNCTION: RNA-dependent RNA polymerase which is responsible for
CC replication and transcription of virus RNA segments. The transcription
CC of viral mRNAs occurs by a unique mechanism called cap-snatching. 5'
CC methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides
CC by PA. In turn, these short capped RNAs are used as primers by PB1 for
CC transcription of viral mRNAs. During virus replication, PB1 initiates
CC RNA synthesis and copy vRNA into complementary RNA (cRNA) which in turn
CC serves as a template for the production of more vRNAs.
CC {ECO:0000250|UniProtKB:P03431}.
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: RNA polymerase is composed of three subunits: PA, PB1 and PB2.
CC {ECO:0000250|UniProtKB:P03431}.
CC -!- SIMILARITY: Belongs to the influenza viruses polymerase PB1 family.
CC {ECO:0000305}.
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DR EMBL; FJ861695; ACY56282.1; -; Genomic_RNA.
DR SMR; D0QX26; -.
DR Proteomes; UP000029941; Genome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR InterPro; IPR007099; RNA-dir_pol_NSvirus.
DR InterPro; IPR001407; RNA_pol_PB1_influenza.
DR Pfam; PF00602; Flu_PB1; 1.
DR PROSITE; PS50525; RDRP_SSRNA_NEG_SEG; 1.
PE 3: Inferred from homology;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW RNA-directed RNA polymerase; Transferase; Viral RNA replication.
FT CHAIN 1..777
FT /note="RNA-directed RNA polymerase catalytic subunit"
FT /id="PRO_0000443068"
FT DOMAIN 313..512
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ SEQUENCE 777 AA; 88189 MW; F0A1A8291E0F4A6F CRC64;
MERLNSFLVS TLIRDGMSRE EKEKLVGPYP VGIENTGLGA VSFLYKYVNV PPLAVGAPAP
KTAESVLRSF EYNRLPDNGK GLRPRQYWME TDGPYPYDVT CANFHLSAAQ EMHKSFLREH
HAVIDKVTEA MYQRLKTTNA DILTKGKQTW DPINKRSVPS AAAFKEITTV LRTYLKLVGF
SVLDFVEAFH RMLMLPEMVY NRRVNAEKTV RKRKGGVITL EKKAVVVLET VHLTRNEDVR
ETVMGWATAF CSYLKSKERG KLKRRAIASA NPILRMFLWI VEELHLELGK QEEMVSSTIS
IGGEEKRAKI IATPDGLSLN EFNIQATEDA TKWNECLAPE NFCLMHEIWW SHSIREEMGL
PKPPESAEIM RQIFQQAFYL LSHKRIYLGK GHLIHNQTRA ALLQWKEDHE KYMNEKTLEW
FRKIKEHLDS EGYVKAPFGM LMGMLNAGST TLALPATKWR LQPGMDCKTV RSSDDSMTVF
SGKTRQLLME NINRFYDNLK LLGINISQKK TRFFQLKFGE YTSAYQDGDF TAQYGVGTAA
LRPEGSNPPD DFHSVASQTA TSLRSGTVNF VGAQFRLGIG VDNVRRLYKI DRTPGKRQGV
PDSALVLSDG GPSPWNFSNC HLPELALKWI THEQNPQATR YLERVMNPNN PFTADAAEIT
SFSRELNTLV ETSLELPRNL FHTLKRFNAT QKSLLRKGDN DFMKSCNLAM QLFEEVIPAS
LLQVPSGPQP MSQVMADVLR AQASALRSVG VHFTEEEMEE IRGALNTLEH DSNIDFE