RDRP_I01A2
ID RDRP_I01A2 Reviewed; 494 AA.
AC Q809M5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 23-FEB-2022, entry version 59.
DE RecName: Full=RNA-directed RNA polymerase catalytic subunit;
DE EC=2.7.7.48;
DE AltName: Full=Polymerase basic protein 1;
DE Short=PB1;
DE AltName: Full=RNA-directed RNA polymerase subunit P1;
DE Flags: Fragment;
GN Name=PB1;
OS Influenza A virus (strain A/Chicken/Hong Kong/FY150/2001 H5N1 genotype D).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=222142;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9691; Panthera pardus (Leopard) (Felis pardus).
OH NCBI_TaxID=9694; Panthera tigris (Tiger).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12077307; DOI=10.1073/pnas.132268999;
RA Guan Y., Peiris J.S.M., Lipatov A.S., Ellis T.M., Dyrting K.C., Krauss S.,
RA Zhang L.J., Webster R.G., Shortridge K.F.;
RT "Emergence of multiple genotypes of H5N1 avian influenza viruses in Hong
RT Kong SAR.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:8950-8955(2002).
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: Influenza RNA polymerase is composed of three subunits: PB1,
CC PB2 and PA. Interacts (via N-terminus) with PA (via C-terminus).
CC Interacts (via C-terminus) with PB2 (via N-terminus); this interaction
CC is essential for transcription initiation.
CC {ECO:0000250|UniProtKB:P03431}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03431}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P03431}.
CC -!- PTM: Phosphorylated by host PRKCA. {ECO:0000250|UniProtKB:P03431}.
CC -!- SIMILARITY: Belongs to the influenza viruses polymerase PB1 family.
CC {ECO:0000305}.
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DR EMBL; AF509172; AAO53015.1; -; Genomic_DNA.
DR SMR; Q809M5; -.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
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:0039523; P:suppression by virus of host mRNA transcription via inhibition of RNA polymerase II activity; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
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 Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host transcription shutoff by virus; Host cytoplasm;
KW Host gene expression shutoff by virus; Host nucleus;
KW Host-virus interaction; Inhibition of host RNA polymerase II by virus;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW RNA-directed RNA polymerase; Transferase; Viral RNA replication;
KW Viral transcription.
FT CHAIN 1..>494
FT /note="RNA-directed RNA polymerase catalytic subunit"
FT /id="PRO_0000311161"
FT DOMAIN 286..483
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 50..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..256
FT /note="Promoter-binding site"
FT /evidence="ECO:0000250"
FT MOTIF 187..195
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 203..216
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 50..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 494
SQ SEQUENCE 494 AA; 56093 MW; 24F9B0DEB11C9F2A CRC64;
MDVNPTLLFL KVPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGKWTTNTE
TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEKSHP GIFENSCLET MEIVQQTRVD
KLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV MESMDKGEME
ITTHFQRKRR VRDNMTKKMV TQRTIGKKKQ RLNKRSYLIR ALTLNTMTKD AERGKLKRRA
IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF
TITGDNTKWN ENQNPRMFLA MITYITRKQP EWFRNVLSIA PIMFSNKMAR LGKGYMFESK
SMKLRTQIPA EMLASIDLKY FNESTRKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG
VSILNLGQKR YTKTTYWWDG LQSSDDFALI VNAPNHEGIQ AGVDRFYRTC KLVGINMSKK
KSYINRTGTF EFTS
