ID   RDRP_I78A7              Reviewed;         758 AA.
AC   Q2VNE5;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   23-FEB-2022, entry version 57.
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/Memphis/2/1978 H3N2).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=383580;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9721; Cetacea (whales).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9709; Phocidae (true seals).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V.,
RA   Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H.,
RA   Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y.,
RA   Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
RT   "The NIAID influenza genome sequencing project.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CY006697; ABB96327.1; -; Genomic_RNA.
DR   SMR; Q2VNE5; -.
DR   Proteomes; UP000007555; 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   RNA-directed RNA polymerase; Transferase; Viral RNA replication;
KW   Viral transcription.
FT   CHAIN           1..758
FT                   /note="RNA-directed RNA polymerase catalytic subunit"
FT                   /id="PRO_0000279604"
FT   DOMAIN          286..483
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04065"
FT   REGION          50..76
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   758 AA;  86607 MW;  15B7F1610BCBFDDA CRC64;
     MDVNPTLLFL KIPAQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHQYS EKGKWTTNTE
     TGAPQLNPID GPLPEDNEPS GYAQTDCVLE AMAFLEESHP GIFENSCLET MEVVQQTRVD
     RLTQGRQTYD WTLNRNQPAA TALANTIEVF RSNGLTANES GRLIDFLKDV MESMDKEEIE
     ITTHFQRKRR VRDNMTKKMV TQRTIGKKKQ RVNKRSYLIR ALTLNTMTKD AERGKLKRRA
     IATPGMQIRG FVYFVETLAR SICEKLEQSG LPVGGNEKKA KLANVVRKMM TNSQDTELSF
     TITGDNTKWN ENQNPRMFLA MITYITKNQP EWFRNILSIA PIMFSNKMAR LGKGYMFESK
     RMKLRTQIPA EMLASIDLKY FNESTRKKIE KIRPLLIDGT ASLSPGMMMG MFNMLSTVLG
     VSILNLGQKK YTKTTYWWDG LQSSDDFALI VNAPNHEGIQ AGVDRFYRTC KLVGINMSKK
     KSYINRTGTF EFTSFFYRYG FVANFSMELP SFGVSGINES ADMSIGVTVI KNNMINNDLG
     PATAQMALQL FIKDYRYTYR CHRGDTQIQT RRSFELKKLW EQTRSKAGLL VSDGGPNLYN
     IRNLHIPEVC LKWELMDEDY QGRLCNPLNP FVSHKEIESV NNAVVMPAHG PAKSMEYDAV
     ATTHSWIPKR NRSILNTSQR GILEDEQMYQ KCCNLFEKFF PSSSYRRPVG ISSMVEAMVS
     RARIDARIDF ESGRIKKEEF SEIMKICSTI EELRRQKQ