PB2_I83A1
ID PB2_I83A1 Reviewed; 759 AA.
AC P11486; A4GCI5;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 104.
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/Chile/1/1983 H1N1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=380985;
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].
RX PubMed=3214273; DOI=10.1007/bf01311091;
RA Schreier E., Petzold D.R., Michel S., Dittmann S.;
RT "Evolution of influenza polymerase: nucleotide sequence of the PB2 gene of
RT A/Chile/1/83 (H1 N1).";
RL Arch. Virol. 103:179-187(1988).
RN [2]
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 (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RG The NIAID Influenza Genome Sequencing Consortium;
RL Submitted (MAR-2007) 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}.
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; X15283; CAA33357.1; -; Genomic_RNA.
DR EMBL; CY020444; ABO38350.1; -; Viral_cRNA.
DR SMR; P11486; -.
DR PRO; PR:P11486; -.
DR Proteomes; UP000008582; 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 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_0000078815"
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 519
FT /note="N -> S"
SQ SEQUENCE 759 AA; 86006 MW; 3DD8535139EE6442 CRC64;
MERIKELRNL MSQSRTREIL TKTTVDHMAI IKKYTSGRQE KNPSLRMKWM MAMKYPITAD
KRITEMIPER NEQGQTLWSK MNDAGSDRVM ISPLAVTWWN RNGPVASTVH YPKIYKTYFE
KVERLKHGTF GPVHFRNQVK IRRRVDINPG HADLSAKEAQ DVIMEVVFPN EVGARILTSE
SQLTITKEKK EELQNCKISP LMVAYMLERE LVRKTRFLPV AGGTSSVYIE VLHLTQGTCW
EQMYTPGGEV RNDDVDQSLI IAARNIVRRA AVSADPLASL LEMCHSTQIG GTRMVDILRQ
NPTEEQAVDI CKAAMGLRIS SSFSFGGFTF KRTSGSSVKR EEEVLTGNLQ TLKLKVHEGF
EEFTMVGKRA TAILRKATRR LIQLIVSGRD EQSIVEAIVV AMVFSQEDCM IKAVRGDLNF
VNRANQRLNP MHQLLRHFQK DAKVLFQNWG IEPIDNVMGM IGILPDMTPS TEMSMRGVRV
SKMGVDEYSN AERVVVSIDR FLRVRDQRGN VLLSPEEVNE TQGTEKLTIT YSSSMMWEIN
GPESVLVNTY QWIIRNWETV KIQWSQNPTM LYNKMEFEPF QSLVPKAIRG QYSGFVRTLF
QQMRDVLGTF DTTQIIKLLP FAAAPPKQSR MQFSSLTVNV RGSGMRILVR GNSPVFNYNK
TTKRLTVLGK DAGTLTEDPD EGTAGVESAV LRGFLILGKE DRRYGPALSI NELSNLAKGE
KANVLIGQGD VVLVMKRKRD SSILTDSQTA TKRIRMAIN
