PB2_I68A4
ID PB2_I68A4 Reviewed; 759 AA.
AC Q91MB1; Q91MB0;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 97.
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/Hong Kong/1/1968 H3N2).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=506350;
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].
RC STRAIN=A/Hong Kong/1/68, and Isolate MA20c;
RX PubMed=11371620; DOI=10.1073/pnas.111165798;
RA Brown E.G., Liu H., Kit L.C., Baird S., Nesrallah M.;
RT "Pattern of mutation in the genome of influenza A virus on adaptation to
RT increased virulence in the mouse lung: identification of functional
RT themes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6883-6888(2001).
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; AF348170; AAK51712.1; -; Genomic_RNA.
DR EMBL; AF348171; AAK51713.1; -; Genomic_RNA.
DR PDB; 4EQK; X-ray; 1.95 A; A=318-483.
DR PDBsum; 4EQK; -.
DR SMR; Q91MB1; -.
DR PRO; PR:Q91MB1; -.
DR Proteomes; UP000142359; 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-directed 5'-3' 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: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:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 3.30.30.90; -; 1.
DR HAMAP; MF_04062; INV_PB2; 1.
DR InterPro; IPR001591; INV_PB2.
DR InterPro; IPR037258; PDB2_C.
DR Pfam; PF00604; Flu_PB2; 1.
DR SUPFAM; SSF160453; SSF160453; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cap snatching;
KW 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_0000279634"
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"
FT VARIANT 701
FT /note="D -> N (in strain: Isolate MA20c)"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:4EQK"
FT STRAND 328..335
FT /evidence="ECO:0007829|PDB:4EQK"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:4EQK"
FT STRAND 351..359
FT /evidence="ECO:0007829|PDB:4EQK"
FT STRAND 361..366
FT /evidence="ECO:0007829|PDB:4EQK"
FT STRAND 368..377
FT /evidence="ECO:0007829|PDB:4EQK"
FT STRAND 380..390
FT /evidence="ECO:0007829|PDB:4EQK"
FT HELIX 391..404
FT /evidence="ECO:0007829|PDB:4EQK"
FT HELIX 408..413
FT /evidence="ECO:0007829|PDB:4EQK"
FT HELIX 430..440
FT /evidence="ECO:0007829|PDB:4EQK"
FT HELIX 443..449
FT /evidence="ECO:0007829|PDB:4EQK"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:4EQK"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:4EQK"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:4EQK"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:4EQK"
SQ SEQUENCE 759 AA; 86102 MW; 3AF8639FF65305FB CRC64;
MERIKELRNL MSQSRTREIL TKTTVDHMAI IKKYTSGRQE KNPSLRMKWM MAMKYPITAD
KRITEMVPER NEQGQTLWSK MSDAGSDRVM VSPLAVTWWN RNGPMTSTVH YPKVYKTYFE
KVERLKHGTF GPVHFRNQVK IRRRVDINPG HADLSAKEAQ DVIMEVVFPN EVGARILTSE
SQLTITKEKK EELQDCKISP LMVAYMLERE LVRKTRFLPV AGGTSSVYIE VLHLTQGTCW
EQMYTPGGEV RNDDVDQSLI IAARNIVRRA AVSADPLASL LEMCHSTQIG GTRMVDILRQ
NPTEEQAVDI CKAAMGLRIS SSFSFGGFTF KRTSGSSIKR EEELLTGNLQ TLKIRVHEGY
EEFTMVGKRA TAILRKATRR LVQLIVSGRD EQSVAEAIIV AMVFSQEDCM IKAVRGDLNF
VNRANQRLNP MHQLLRHFQK DAKVLFQNWG IEHIDNVMGM IGVLPDMTPS TEMSMRGIRV
SKMGVDEYSS TERVVVSIDR FLRVRDQRGN VLLSPEEVSE TQGTEKLTIT YSSSMMWEIN
GPESVLVNTY QWIIRNWETV KIQWSQNPTM LYNKMEFEPF QSLIPKAIRG QYSGFVRTLF
QQMRDVLGTF DTTQIIKLLP FAAAPPKQSR MQFSSLTVNV RGSGMRILVR GNSPVFNYNK
TTKRLTILGK DAGTLIEDPD EGTSGVESAV LRGFLILGKE DRRYGPALSI NELSNLAKGE
KANVLIGQGD VVLVMKRKRD SSILTDSQTA TKRIRMAIN
