RDRP_I68A5
ID RDRP_I68A5 Reviewed; 757 AA.
AC P16506;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 23-FEB-2022, entry version 97.
DE RecName: Full=RNA-directed RNA polymerase catalytic subunit {ECO:0000255|HAMAP-Rule:MF_04065};
DE EC=2.7.7.48 {ECO:0000255|HAMAP-Rule:MF_04065};
DE AltName: Full=Polymerase basic protein 1 {ECO:0000255|HAMAP-Rule:MF_04065};
DE Short=PB1 {ECO:0000255|HAMAP-Rule:MF_04065};
DE AltName: Full=RNA-directed RNA polymerase subunit P1 {ECO:0000255|HAMAP-Rule:MF_04065};
GN Name=PB1 {ECO:0000255|HAMAP-Rule:MF_04065};
OS Influenza A virus (strain A/Korea/426/1968 H2N2).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=488241;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2795713; DOI=10.1128/jvi.63.11.4603-4608.1989;
RA Kawaoka Y., Krauss S., Webster R.G.;
RT "Avian-to-human transmission of the PB1 gene of influenza A viruses in the
RT 1957 and 1968 pandemics.";
RL J. Virol. 63:4603-4608(1989).
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:0000255|HAMAP-Rule:MF_04065}.
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|HAMAP-Rule:MF_04065};
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. {ECO:0000255|HAMAP-
CC Rule:MF_04065}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04065}.
CC Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04065}.
CC -!- PTM: Phosphorylated by host PRKCA. {ECO:0000255|HAMAP-Rule:MF_04065}.
CC -!- SIMILARITY: Belongs to the influenza viruses polymerase PB1 family.
CC {ECO:0000255|HAMAP-Rule:MF_04065}.
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DR EMBL; M25935; AAA43644.1; -; Genomic_RNA.
DR RefSeq; YP_308851.1; NC_007375.1.
DR SMR; P16506; -.
DR GeneID; 3655105; -.
DR KEGG; vg:3655105; -.
DR Proteomes; UP000200640; Genome.
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-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0039523; P:suppression by virus of host mRNA transcription via inhibition of RNA polymerase II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:UniProtKB-UniRule.
DR GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
DR HAMAP; MF_04065; INFV_RDRP; 1.
DR InterPro; IPR007099; RNA-dir_pol_NSvirus.
DR InterPro; IPR001407; RNA_pol_PB1_influenza.
DR Pfam; PF00602; Flu_PB1; 1.
DR PIRSF; PIRSF000827; RdRPol_OMV; 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 Reference proteome; RNA-directed RNA polymerase; Transferase;
KW Viral RNA replication; Viral transcription.
FT CHAIN 1..757
FT /note="RNA-directed RNA polymerase catalytic subunit"
FT /id="PRO_0000078756"
FT DOMAIN 286..483
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
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:0000255|HAMAP-Rule:MF_04065"
FT MOTIF 187..195
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
FT MOTIF 203..216
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
FT COMPBIAS 50..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 757 AA; 86368 MW; 452390A46C9CD3A1 CRC64;
MDVNPTLLFL KVPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGKWTTNTE
TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCLET MEVIQQTRVD
KLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV IESMDKEEME
ITTHFQRKRR VRDNMTKKMV TQRTIGKKKQ RLNKRSYLIR ALTLNTMTKD AERGKLKRRA
IATPGMQIRG FVHFVETLAR NICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF
TITGDNTKWN ENQNPRVFLA MITYITRNQP EWFRNVLSIA PIMFSNKMAR LGKGYMFESK
SMKLRTQIPA EMLASIDLKY FNESTRKKIE KIRPLLIDGT VSLSPGMMMG MFNMLSTVLG
VSILNLGQKK YTKTTYWWDG LQSSDDFALI VNAPNHEGIQ AGVNRFYRTC KLVGINMSKK
KSYINRTGTF EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG
PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFELKKLW EQTRSKAGLL VSDGGSNLYN
IRNLHIPEVC LKWELMDEDY QGRLCNPLNP FVSHKEIESV NNAVVMPAHG PAKSMEYDAV
ATTHSWTPKR NRSILNTSQR GILEDEQMYQ KCCNLFEKFF PSSSYRRPVG ISSMVEAMVS
RARIDARIDF ESGRIKKEEF AEIMKICSTI EELRRQK
