ID E9KMS1_9INFA Unreviewed; 759 AA. AC E9KMS1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 08-JUN-2016, entry version 18. DE RecName: Full=Polymerase basic protein 2 {ECO:0000256|RuleBase:RU361246, ECO:0000256|SAAS:SAAS00118352}; GN Name=PB2 {ECO:0000256|RuleBase:RU361246, ECO:0000313|EMBL:ADD21402.1}; OS Influenza A virus (A/Hong Kong/415742/2009(H1N1)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. OX NCBI_TaxID=735355 {ECO:0000313|EMBL:ADD21402.1}; RN [1] {ECO:0000313|EMBL:ADD21402.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Hong Kong/415742/2009 {ECO:0000313|EMBL:ADD21402.1}; RX PubMed=20660098; DOI=10.1258/ebm.2010.010071; RA Zheng B., Chan K.H., Zhang A.J., Zhou J., Chan C.C., Poon V.K., RA Zhang K., Leung V.H., Jin D.Y., Woo P.C., Chan J.F., To K.K., Chen H., RA Yuen K.Y.; RT "D225G mutation in hemagglutinin of pandemic influenza H1N1 (2009) RT virus enhances virulence in mice."; RL Exp. Biol. Med. (Maywood) 235:981-988(2010). RN [2] {ECO:0000313|EMBL:ADD21402.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Hong Kong/415742/2009 {ECO:0000313|EMBL:ADD21402.1}; RA Zheng B.J., Chan K.H., Zhang A.J.X., Zhou J., Jin D.Y., Woo P.C.Y., RA Tse H., Chan J.F.W., To K.K.W., Chen H.L., Yuen K.Y.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Plays an essential role in transcription initiation and CC cap-stealing mechanism, in which cellular capped pre-mRNAs are CC used to generate primers for viral transcription. CC {ECO:0000256|RuleBase:RU361246}. CC -!- FUNCTION: Plays an essential role in transcription initiation and CC cap-stealing mechanism, in which cellular capped pre-mRNAs are CC used to generate primers for viral transcription. Binds the cap of CC the target pre-RNA which is subsequently cleaved after 10-13 CC nucleotides by PA. Plays a role in the initiation of the viral CC genome replication and modulates the activity of the CC ribonucleoprotein (RNP) complex. In addition, participates in the CC inhibition of type I interferon induction through interaction with CC the host mitochondrial antiviral signaling protein MAVS. CC {ECO:0000256|SAAS:SAAS00161294}. CC -!- SUBUNIT: Influenza RNA polymerase is composed of three subunits: CC PB1, PB2 and PA. {ECO:0000256|RuleBase:RU361246, CC ECO:0000256|SAAS:SAAS00118334}. CC -!- SUBUNIT: Influenza RNA polymerase is composed of three subunits: CC PB1, PB2 and PA. Interacts (via N-terminus) with PB1 (via C- CC terminus). Interacts with nucleoprotein NP (via N-terminus). CC Interacts (via N-terminus) with host MAVS (via N-terminus); this CC interaction inhibits host innate immune response. CC {ECO:0000256|SAAS:SAAS00161291}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|RuleBase:RU361246}. Host CC nucleus {ECO:0000256|RuleBase:RU361246}. Host mitochondrion CC {ECO:0000256|RuleBase:RU361246}. CC -!- SIMILARITY: Belongs to the influenza viruses PB2 family. CC {ECO:0000256|RuleBase:RU361246, ECO:0000256|SAAS:SAAS00584119}. 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; GU931811; ADD21402.1; -; Viral_cRNA. 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:0019012; C:virion; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:InterPro. DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW. DR GO; GO:0075526; P:cap snatching; IEA:UniProtKB-KW. DR GO; GO:0039545; P:suppression by virus of host MAVS activity; IEA:UniProtKB-KW. DR GO; GO:0039523; P:suppression by virus of host RNA polymerase II activity; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. DR InterPro; IPR001591; RNA_pol_PB2_orthomyxovir. DR Pfam; PF00604; Flu_PB2; 1. DR ProDom; PD001667; RNA_pol_PB2_orthomyxovir; 1. PE 3: Inferred from homology; KW Cap snatching {ECO:0000256|SAAS:SAAS00477284}; KW Eukaryotic host gene expression shutoff by virus KW {ECO:0000256|SAAS:SAAS00477208}; KW Eukaryotic host transcription shutoff by virus KW {ECO:0000256|SAAS:SAAS00477383}; KW Host gene expression shutoff by virus {ECO:0000256|SAAS:SAAS00477173}; KW Host mitochondrion {ECO:0000256|RuleBase:RU361246}; KW Host nucleus {ECO:0000256|RuleBase:RU361246}; KW Host-virus interaction {ECO:0000256|SAAS:SAAS00477422}; KW Inhibition of host innate immune response by virus KW {ECO:0000256|SAAS:SAAS00477452}; KW Inhibition of host MAVS by virus {ECO:0000256|SAAS:SAAS00477114}; KW Inhibition of host RLR pathway by virus KW {ECO:0000256|SAAS:SAAS00477196}; KW Inhibition of host RNA polymerase II by virus KW {ECO:0000256|SAAS:SAAS00477256}; KW mRNA capping {ECO:0000256|RuleBase:RU361246, KW ECO:0000256|SAAS:SAAS00477228}; KW mRNA processing {ECO:0000256|RuleBase:RU361246, KW ECO:0000256|SAAS:SAAS00476958}; KW Viral immunoevasion {ECO:0000256|SAAS:SAAS00477196}; KW Viral transcription {ECO:0000256|SAAS:SAAS00477398}; KW Virion {ECO:0000256|RuleBase:RU361246}. SQ SEQUENCE 759 AA; 85879 MW; 37964DF830D4BD7A CRC64; MERIKELRDL MSQSRTREIL TKTTVDHMAI IKKYTSGRQE KNPALRMKWM MAMRYPITAD KRIMDMIPER NEQGQTLWSK TNDAGSDRVM VSPLAVTWWN RNGSTTSTVH YPKVYKTYFE KVERLKHGTF GPVHFRNQVK IRRRVDTNPG HADLSAKEAQ DVIMEVVFPN EVGARILTSE SQLAITKEKK EELQDCKIAP LMVAYMLERE LVRKTRFLPV AGGTGSVYIE VLHLTQGTCW EQMYTPGGEV RNDDVDQSLI IAARNIVRRA AVSADPLASL LEMCHSTQIG GVRMVDILRQ NPTEEQAVDI CKAAIGLRIS SSFSFGGFTF KRTSGSSVKK EEEVLTGNLQ TLKIRVHEGY EEFTMVGRRA TAILRKATRR LIQLIVSGRD EQSIAEAIIV AMVFSQEDCM IKAVRGDLNF VNRANQRLNP MHQLLRHFQK DAKVLFQNWG IESIDNVMGM IGILPDMTPS TEMSLRGIRV SKMGVDEYSS TERVVVSIDR FLRVRDQRGN VLLSPEEVSE TQGTERLTIT YSSSMMWEIN GPESVLVNTY QWIIRNWEIV KIQWSQDPTM LYNKMEFEPF QSLVPKATRS RYSGFVRTLF QQMRDVLGTF DTVQIIKLLP FAAAPPEQSR MQFSSLTVNV RGSGLRILVR GNSPVFNYNK ATKRLTVLGK DAGALTEDPD EGTSGVESAV LRGFLILGKE DKRYGPALSI NELSNLAKGE KANVLIGQGD VVLVMKRKRN SSILTDSQTA TKRIRMAIN //