ID PB2_I77AA Reviewed; 759 AA. AC A4GBY7; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 1. DT 24-JAN-2024, entry version 77. 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/Brazil/11/1978 H1N1). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus; OC Alphainfluenzavirus influenzae; Influenza A virus. OX NCBI_TaxID=393560; 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 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 [2] 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; CY020300; ABO38075.1; -; Viral_cRNA. DR BMRB; A4GBY7; -. DR SMR; A4GBY7; -. DR PRO; PR:A4GBY7; -. DR Proteomes; UP000008025; 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_0000373039" 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; 85993 MW; 4922CF11CF5A034B CRC64; MERIKELRNL MSQSRTREIL TKTTVDHMAI IKKYTSGRQE KNPSLRMKWM MAMKYPITAD KRITEMIPER NEQGQTLWSK MNDAGSDRVM VSPLAVTWWN RNGPVTSTVH YPKIYKTYFE KVERLKHGTF GPVHFRNQVK IRRRVDINPG HADLSAKEAQ DVIMEVVFPN EVGARILTSE SQLTITKEKK EELQNCKISP LLVAYMLERE LVRKTRFLPV AGGTSSVYIE VLHLTQGTCW EQMYTPGGEV RNDDVDQSLI IAARNIVRRA AVSADPLASL LEMCHSTQIG GTRMVDILRQ NPTEEQAVDI CKAAMGLRIS SSFSFGGFTF KRTSGSSVKR EEEVLTGNLQ TLKIKVHEGY EEFTMVGKRA TAILRKATRR LIQLIVSGRD EQSIVEAIVV AMVFSQEDCM IKAVRGDLNF VNRANQRLNP MHQLLRHFQK DAKVLFQNWG IEPIDNVMGM IGILPDMTPS TEMSMRGVRV SKMGVDEYSN AERVVVSIDR FLRVRDQRGN VLLSPEEVSE TQGTEKLTIT YSSSMMWEIN GPESVLVNTY QWIIRNWETV KIQWSQNPTM LYNKMEFEPF QSLVPKAIRG QYSGFVRTLF QQMRDVLGTF DTTQIIKLLP FAAAPPKQSR MQFSSLTVNV RGSGMRILVR GNSPVFNYNK TTKRLTVLGK DAGTLTEDPD EGTAGVESAV LRGFLILGKE DRRYGPALSI NELSNLAKGE KANVLIGQGD VVLVMKRKRD SSILTDSQTA TKRIRMAIN //