ID PB2_I18A0 Reviewed; 759 AA. AC Q3HM41; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 24-JAN-2024, entry version 76. 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/Brevig Mission/1/1918 H1N1) (Influenza A virus OS (strain A/South Carolina/1/1918 H1N1)). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus; OC Alphainfluenzavirus influenzae; Influenza A virus. OX NCBI_TaxID=88776; OH NCBI_TaxID=8782; Aves. OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9823; Sus scrofa (Pig). RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=16208372; DOI=10.1038/nature04230; RA Taubenberger J.K., Reid A.H., Lourens R.M., Wang R., Jin G., Fanning T.G.; RT "Characterization of the 1918 influenza virus polymerase genes."; RL Nature 437:889-893(2005). 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 -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Polymerase basic protein 2; CC IsoId=Q3HM41-1; Sequence=Displayed; CC Name=PB2-S1 {ECO:0000250|UniProtKB:P03427}; CC IsoId=P0DOG7-1; Sequence=External; CC -!- MISCELLANEOUS: South Carolina isolate has been sequenced from formalid CC fixed-lung tissues of a 21-year-old male which died in 1918 at Ft. CC Jackson, SC. Brevig Mission isolate has been sequenced from lung CC tissues of an Inuit woman buried in the permafrost in a gravesite near CC Brevig Mission, Alaska. This sample was recovered by John Hultin, CC retired pathologist. 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; DQ208309; ABA55038.1; -; mRNA. DR PDB; 7NHA; EM; 2.91 A; C=1-759. DR PDB; 7NHC; EM; 2.87 A; C=1-759. DR PDB; 7NHX; EM; 3.23 A; C=1-759. DR PDB; 7NI0; EM; 3.32 A; C=1-759. DR PDB; 7NIK; EM; 6.20 A; C=1-759. DR PDB; 7NIL; EM; 5.01 A; C=1-759. DR PDB; 7NIR; EM; 6.70 A; C=1-759. DR PDB; 7NIS; EM; 5.96 A; C=1-759. DR PDB; 7NJ3; EM; 4.48 A; C=1-759. DR PDB; 7NJ4; EM; 5.84 A; C=1-759. DR PDB; 7NJ5; EM; 4.63 A; C=1-759. DR PDB; 7NJ7; EM; 4.82 A; C=1-759. DR PDB; 7NK1; EM; 4.22 A; C=1-759. DR PDB; 7NK2; EM; 4.84 A; C=1-759. DR PDB; 7NK4; EM; 5.32 A; C=1-759. DR PDB; 7NK6; EM; 6.72 A; C=1-759. DR PDB; 7NK8; EM; 5.34 A; C=1-759. DR PDB; 7NKA; EM; 4.07 A; C=1-759. DR PDB; 7NKC; EM; 4.46 A; C=1-759. DR PDB; 7NKI; EM; 4.67 A; C=1-759. DR PDB; 7NKR; EM; 5.60 A; C=1-759. DR PDBsum; 7NHA; -. DR PDBsum; 7NHC; -. DR PDBsum; 7NHX; -. DR PDBsum; 7NI0; -. DR PDBsum; 7NIK; -. DR PDBsum; 7NIL; -. DR PDBsum; 7NIR; -. DR PDBsum; 7NIS; -. DR PDBsum; 7NJ3; -. DR PDBsum; 7NJ4; -. DR PDBsum; 7NJ5; -. DR PDBsum; 7NJ7; -. DR PDBsum; 7NK1; -. DR PDBsum; 7NK2; -. DR PDBsum; 7NK4; -. DR PDBsum; 7NK6; -. DR PDBsum; 7NK8; -. DR PDBsum; 7NKA; -. DR PDBsum; 7NKC; -. DR PDBsum; 7NKI; -. DR PDBsum; 7NKR; -. DR SMR; Q3HM41; -. DR PRO; PR:Q3HM41; -. DR Proteomes; UP000008430; 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 1: Evidence at protein level; KW 3D-structure; Alternative splicing; 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_0000310573" 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 HELIX 2..12 FT /evidence="ECO:0007829|PDB:7NHC" FT HELIX 14..22 FT /evidence="ECO:0007829|PDB:7NHC" FT TURN 25..27 FT /evidence="ECO:0007829|PDB:7NHC" FT HELIX 28..33 FT /evidence="ECO:0007829|PDB:7NHC" FT HELIX 43..50 FT /evidence="ECO:0007829|PDB:7NHC" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:7NHC" FT STRAND 57..59 FT /evidence="ECO:0007829|PDB:7NHC" FT HELIX 63..66 FT /evidence="ECO:0007829|PDB:7NHC" FT STRAND 78..82 FT /evidence="ECO:0007829|PDB:7NHC" FT STRAND 84..87 FT /evidence="ECO:0007829|PDB:7NHA" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:7NHC" FT HELIX 93..102 FT /evidence="ECO:0007829|PDB:7NHC" FT HELIX 108..110 FT /evidence="ECO:0007829|PDB:7NHA" FT HELIX 111..114 FT /evidence="ECO:0007829|PDB:7NHC" FT HELIX 116..126 FT /evidence="ECO:0007829|PDB:7NHC" FT STRAND 129..135 FT /evidence="ECO:0007829|PDB:7NHC" FT STRAND 141..146 FT /evidence="ECO:0007829|PDB:7NHC" FT HELIX 156..167 FT /evidence="ECO:0007829|PDB:7NHC" FT HELIX 169..171 FT /evidence="ECO:0007829|PDB:7NHC" FT HELIX 180..191 FT /evidence="ECO:0007829|PDB:7NHC" FT HELIX 200..211 FT /evidence="ECO:0007829|PDB:7NHC" FT STRAND 215..220 FT /evidence="ECO:0007829|PDB:7NHC" FT HELIX 226..229 FT /evidence="ECO:0007829|PDB:7NHC" FT HELIX 232..235 FT /evidence="ECO:0007829|PDB:7NHC" FT STRAND 238..245 FT /evidence="ECO:0007829|PDB:7NHC" FT HELIX 252..272 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 273..275 FT /evidence="ECO:0007829|PDB:7NHX" FT HELIX 276..285 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 286..289 FT /evidence="ECO:0007829|PDB:7NI0" FT HELIX 294..300 FT /evidence="ECO:0007829|PDB:7NHX" FT HELIX 306..314 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 331..334 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 342..345 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 351..354 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 361..366 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 371..377 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 380..386 FT /evidence="ECO:0007829|PDB:7NHX" FT HELIX 391..405 FT /evidence="ECO:0007829|PDB:7NHX" FT HELIX 408..411 FT /evidence="ECO:0007829|PDB:7NHX" FT HELIX 430..437 FT /evidence="ECO:0007829|PDB:7NHX" FT TURN 438..440 FT /evidence="ECO:0007829|PDB:7NHX" FT HELIX 443..449 FT /evidence="ECO:0007829|PDB:7NHX" FT HELIX 457..459 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 465..467 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 471..478 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 496..498 FT /evidence="ECO:0007829|PDB:7NI0" FT STRAND 507..509 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 511..513 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 529..531 FT /evidence="ECO:0007829|PDB:7NI0" FT TURN 538..540 FT /evidence="ECO:0007829|PDB:7NHX" FT HELIX 542..555 FT /evidence="ECO:0007829|PDB:7NHX" FT HELIX 557..563 FT /evidence="ECO:0007829|PDB:7NHX" FT HELIX 569..572 FT /evidence="ECO:0007829|PDB:7NHX" FT HELIX 578..582 FT /evidence="ECO:0007829|PDB:7NHX" FT HELIX 588..605 FT /evidence="ECO:0007829|PDB:7NHX" FT HELIX 612..618 FT /evidence="ECO:0007829|PDB:7NHX" FT HELIX 619..621 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 622..624 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 634..640 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 643..651 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 660..662 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 664..667 FT /evidence="ECO:0007829|PDB:7NHX" FT STRAND 670..674 FT /evidence="ECO:0007829|PDB:7NHX" SQ SEQUENCE 759 AA; 85938 MW; CCF3E21D026468F9 CRC64; MERIKELRDL MSQSRTREIL TKTTVDHMAI IKKYTSGRQE KNPALRMKWM MAMKYPITAD KRIMEMIPER NEQGQTLWSK TNDAGSDRVM VSPLAVTWWN RNGPTTSAVH YPKIYKTYFE KVERLKHGTF GPVHFRNQVK IRRRVDINPG HADLSAKEAQ DVIMEVVFPN EVGARILTSE SQLTITKEKK EELQDCKISP LMVAYMLERE LVRKTRFLPV AGGTSSVYIE VLHLTQGTCW EQMYTPGGEV RNDDVDQSLI IAARNIVRRA TVSADPLASL LEMCHSTQIG GIRMVDILRQ NPTEEQAVDI CKAAMGLRIS SSFSFGGFTF KRTSGSSVKR EEEVLTGNLQ TLKIRVHEGY EEFTMVGRRA TAILRKATRR LIQLIVSGRD EQSIAEAIIV AMVFSQEDCM IKAVRGDLNF VNRANQRLNP MHQLLRHFQK DAKVLFQNWG IEPIDNVMGM IGILPDMTPS TEMSMRGVRV SKMGVDEYSS TERVVVSIDR FLRVRDQRGN VLLSPEEVSE TQGTEKLTIT YSSSMMWEVN GPESVLVNTY QWIIRNWETV KIQWSQNPTM LYNKMEFEPF QSLVPKAARG QYSGFVRTLF QQMRDVLGTF DTVQIIKLLP FAAAPPKQSR MQFSSLTVNV RGSGMRILVR GNSPVFNYNK ATKRLTVLGK DAGALTEDPD EGTAGVESAV LRGFLILGKE DRRYGPALSI NELSNLAKGE KANVLIGQGD VVLVMKRKRD SSILTDSQTA TKRIRMAIN //