ID   PB2_I06A0               Reviewed;         759 AA.
AC   B4URE6;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=Polymerase basic protein 2 {ECO:0000255|HAMAP-Rule:MF_04062};
DE   AltName: Full=RNA-directed RNA polymerase subunit P3 {ECO:0000255|HAMAP-Rule:MF_04062};
GN   Name=PB2 {ECO:0000255|HAMAP-Rule:MF_04062};
OS   Influenza A virus (strain A/Russia:St.Petersburg/8/2006 H1N1).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC   Alphainfluenzavirus influenzae; Influenza A virus.
OX   NCBI_TaxID=518998;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Spiro D., Halpin R., Boyne A., Bera J., Ghedin E., Hostetler J.,
RA   Fedorova N., Hine E., Overton L., Djuric K., Sarmiento M., Sitz J.,
RA   Katzel D., Manojkumar R., Devis R., Fulvini A., Silverman J., Le J.,
RA   Kilbourne E.D., Pokorny B., Bucher D., Orff E., Minieri J., Onodera S.,
RA   Huang L., Bao Y., Sanders R., Dernovoy D., Kiryutin B., Lipman D.J.,
RA   Tatusova T.;
RT   "The NIAID influenza genome sequencing project.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RG   The NIAID Influenza Genome Sequencing Consortium;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an essential role in transcription initiation and cap-
CC       stealing mechanism, in which cellular capped pre-mRNAs are used to
CC       generate primers for viral transcription. Recognizes and binds the 7-
CC       methylguanosine-containing cap of the target pre-RNA which is
CC       subsequently cleaved after 10-13 nucleotides by the viral protein PA.
CC       Plays a role in the initiation of the viral genome replication and
CC       modulates the activity of the ribonucleoprotein (RNP) complex. In
CC       addition, participates in the inhibition of type I interferon induction
CC       through interaction with and inhibition of the host mitochondrial
CC       antiviral signaling protein MAVS. {ECO:0000255|HAMAP-Rule:MF_04062}.
CC   -!- SUBUNIT: Influenza RNA polymerase is composed of three subunits: PB1,
CC       PB2 and PA. Interacts (via N-terminus) with PB1 (via C-terminus).
CC       Interacts with nucleoprotein NP (via N-terminus). Interacts (via N-
CC       terminus) with host MAVS (via N-terminus); this interaction inhibits
CC       host innate immune response. {ECO:0000255|HAMAP-Rule:MF_04062}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04062}. Host
CC       nucleus {ECO:0000255|HAMAP-Rule:MF_04062}. Host mitochondrion
CC       {ECO:0000255|HAMAP-Rule:MF_04062}.
CC   -!- SIMILARITY: Belongs to the influenza viruses PB2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_04062}.
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DR   EMBL; CY034131; ACF54597.1; -; Viral_cRNA.
DR   SMR; B4URE6; -.
DR   PRO; PR:B4URE6; -.
DR   Proteomes; UP000008081; Genome.
DR   GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-UniRule.
DR   GO; GO:0075526; P:cap snatching; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:DNA-templated transcription; 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:0039545; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   Gene3D; 3.30.30.90; Polymerase Basic Protein 2, C-terminal domain; 1.
DR   HAMAP; MF_04062; INV_PB2; 1.
DR   InterPro; IPR049110; Flu_PB2_2nd.
DR   InterPro; IPR049114; Flu_PB2_6th.
DR   InterPro; IPR049115; Flu_PB2_C.
DR   InterPro; IPR048298; Flu_PB2_CAP-bd.
DR   InterPro; IPR049111; Flu_PB2_middle.
DR   InterPro; IPR049106; Flu_PB2_N.
DR   InterPro; IPR001591; INV_PB2.
DR   InterPro; IPR049113; PB2_helical.
DR   InterPro; IPR037258; PDB2_C.
DR   Pfam; PF20947; Flu_PB2_1st; 1.
DR   Pfam; PF20948; Flu_PB2_2nd; 1.
DR   Pfam; PF20949; Flu_PB2_3rd; 1.
DR   Pfam; PF20950; Flu_PB2_4th; 1.
DR   Pfam; PF00604; Flu_PB2_5th; 1.
DR   Pfam; PF20951; Flu_PB2_6th; 1.
DR   Pfam; PF20952; Flu_PB2_7th; 1.
DR   SUPFAM; SSF160453; PB2 C-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Cap snatching; Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host transcription shutoff by virus;
KW   Host gene expression shutoff by virus; Host mitochondrion; Host nucleus;
KW   Host-virus interaction; Inhibition of host innate immune response by virus;
KW   Inhibition of host MAVS by virus; Inhibition of host RLR pathway by virus;
KW   Inhibition of host RNA polymerase II by virus; mRNA capping;
KW   mRNA processing; Viral immunoevasion; Viral transcription; Virion.
FT   CHAIN           1..759
FT                   /note="Polymerase basic protein 2"
FT                   /id="PRO_0000373028"
FT   MOTIF           736..739
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04062"
FT   SITE            627
FT                   /note="Mammalian adaptation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04062"
SQ   SEQUENCE   759 AA;  86095 MW;  10D2D1608AE536D2 CRC64;
     MERIKELRNL MSQSRTREIL TKTTVDHMAI IKKYTSGRQE KNPALRMKWM MAMKYPITAD
     KRITEMIPER NEQGQTLWSK MNDAGSDRVM VSPLAVTWWN RNGPITNTVH YPKIYKTYFE
     RVERLKHGTF GPVHFRNQVK IRRRVDINPG HADLSAKEAQ DVIMEVVFPN EVGARILTSE
     SQLTITKEKK EELQDCKISP LMVAYMLERE LVRKTRFLPV AGGTSSVYIE VLHLTQGTCW
     EQMYTPGGEV RNDDVDQSLI IAARNIVRRA AVSADPLASL LEMCHSTQIG GIRMVDILRQ
     NPTEEQAVDI CKAAMGLRIS SSFSFGGFTF KRTSGSSVKR EEEVLTGNLQ TLKIRVHEGY
     EEFTMVGRRA TAILRKATRR LIQLIVSGRD EQSIAEAIIV AMVFSQEDCM IKAVRGDLNF
     VNRANQRLNP MHQLLRHFQK DAKVLFQNWG VEPIDNVMGM IGILPDMTPS IEMSMRGVRI
     SKMGVDEYSS TERVVVSIDR FLRIRDQRGN VLLSPEEVSE TQGTEKLTIT YSSSMMWEIN
     GPESVLVNTY QWIIRNWETV KIQWSQNPTM LYNKMEFEPF QSLVPKAIRG QYSGFVRTLF
     QQMRDVLGTF DTAQIIKLLP FAAAPPKQSR MQFSSFTVNV RGSGMRILVR GNSPVFNYNK
     ATKRLTVLGK DAGTLTEDPD EGTAGVESAV LRGFLILGKE DKRYGPALSI NELSNLAKGE
     KANVLIGQGD VVLVMKRKRD SSILTDSQTA TKRIRMAIN
//