ID PB2_I61A1 Reviewed; 759 AA. AC B3EUR6; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 1. DT 24-JAN-2024, entry version 57. 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/Swine/Wisconsin/1/1961 H1N1). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus; OC Alphainfluenzavirus influenzae; Influenza A virus. OX NCBI_TaxID=383533; 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., Kim M., Zaborsky J., Overton L., Djuric K., Sarmiento M., RA Sitz J., Katzel D., Webster R.G., Hoffmann E., Krauss S., Naeve C., RA Bolotov P., Bao Y., Sanders R., Dernovoy D., Kiryutin B., Lipman D.J., RA Tatusova T.; RT "The NIAID influenza genome sequencing project."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RG The NIAID Influenza Genome Sequencing Consortium; RL Submitted (JUN-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}. 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; CY032220; ACD85164.1; -; Viral_cRNA. DR SMR; B3EUR6; -. DR PRO; PR:B3EUR6; -. DR Proteomes; UP000007769; 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_0000373037" 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; 85831 MW; 945D02A0A0226450 CRC64; MERIKELRDL MLQSRTREIL TRTTVDHMAI IKKYTSGRQE KNPALRMKWM MAMKYPITAD KRIIETIPER NEQGQTLWSR TSDAGSDRVM VSPLAVTWWN RNGPTASTVH YPKVYRTYFE KVERLKHGTF GPVHFRNQVK IRRRVDINPG HADLSAKEAQ DVIMEVVFPN EVGARILTSE SQLMITKEKK EELQECKISP LMVAYMLERE LVRKTRFLPV AGGTSSVYIE VLHLTQGACW EQLYTPGGEV RNDDVDQSLI IAARSIVRRA TVSADPLASL LEMCHSTQIG GVRMVDILRQ NPTEEQAVDI CKAAMGLRIS SSFSFGGFTF KRTSGSSTKK EEEVLTGNLQ TLKIRVHEGY EEFTMVGKRA TAILRKATRR LVQLIVSGRD EQSIAEAIIV AMVFSQEDCM IKAVRGDLNF VNRANQRLNP MHQLLRHFQK DAKVLFQNWG IEPIDNVMGM VGILPDLTPS TEMSMRGVRI SKMGVDEYSS TERVVVSIDR FLRVRDQQGN VLLSPEEVSE TQGTEKLTIT YSSSMMWEVN GPESVLVNTY QWIIRNWETV KIQWSQDPTM LYNKMEFEPF QSLVPKAARG QYSGFVRTLF QQMRDVLGTF DTVQIIKLLP FAAAPPKQSR MQFSSLTVNV RGSGMRILIR GNSPVFNYNK GTKRLTVLGK DAGALTENPD EGTTGVESAV LRGFLILGRE DRRYGPALSI NELSSLAKGE KANVLIGQGD VVLVMKRKRD SSILTDSQTA TKRIRMAIN //