ID   PB2_I02A5               Reviewed;         759 AA.
AC   Q6J859;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 75.
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/Chicken/Hong Kong/96.1/2002 H5N1 genotype Y).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=279803;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9691; Panthera pardus (Leopard) (Felis pardus).
OH   NCBI_TaxID=9694; Panthera tigris (Tiger).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15148370; DOI=10.1073/pnas.0402443101;
RA   Guan Y., Poon L.L.M., Cheung C.Y., Ellis T.M., Lim W., Lipatov A.S.,
RA   Chan K.H., Sturm-Ramirez K.M., Cheung C.L., Leung Y.H.C., Yuen K.Y.,
RA   Webster R.G., Peiris J.S.M.;
RT   "H5N1 influenza: a protean pandemic threat.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:8156-8161(2004).
RN   [2]
RP   SEQUENCE REVISION.
RA   Guan Y., Poon L.L.M., Cheung C.Y., Ellis T.M., Lim W., Lipatov A.S.,
RA   Chan K.H., Sturm-Ramirez K.M., Cheung C.L., Leung Y.H.C., Yuen K.Y.,
RA   Webster R.G., Peiris J.S.M.;
RL   Submitted (MAR-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.
CC       {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). {ECO:0000255|HAMAP-
CC       Rule:MF_04062}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04062}. Host
CC       nucleus {ECO:0000255|HAMAP-Rule:MF_04062}.
CC   -!- SIMILARITY: Belongs to the influenza viruses PB2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_04062}.
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DR   EMBL; AY576389; AAT39038.2; -; Genomic_DNA.
DR   SMR; Q6J859; -.
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: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 nucleus;
KW   Host-virus interaction; Inhibition of host RNA polymerase II by virus;
KW   mRNA capping; mRNA processing; Viral transcription; Virion.
FT   CHAIN           1..759
FT                   /note="Polymerase basic protein 2"
FT                   /id="PRO_0000311152"
FT   MOTIF           736..739
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04062"
FT   SITE            627
FT                   /note="Avian adaptation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04062"
SQ   SEQUENCE   759 AA;  85807 MW;  F11A3FE9D25851FE CRC64;
     MERIKELRDL MSQSRTREIL TKTTVDHMAI IKKYTSGRQE KNPALRMKWM MAMKYPITAD
     KRIIEMIPER NEQGQTLWSK TNDAGSDRVM VSPLAVTWWN RNGPATGTVH YPKVYKTYFE
     KVERLKHGTF GPVHFRNQVK IRRRVDINPG HADLSAKEAQ DVIMEVVFPN EVGARTLTSE
     SQLTITKEKK EELQDCKIAP LMVAYMLERE LVRKTRFLPV AGGTSSVYIE VLHLTQGTCW
     EQMYTPGGEV RNDDVDQSLV IAARNIVRRA TVSADPLASL LEMCHSTQIG GIRMVDILRQ
     NPTEEQAVDI CKAAMGLRIS SSFSFGGFTF KRTSGSSVKK EEEVLTGNLQ TLKIRVHEGY
     EEFTMVGRRA TAILRKATRR LIQLIVSGRD EQSIAEAIIV AMVFSQEECM IKAVRGDLNF
     VNRANQRLNP MHQLLRHFQK DAKVLFQNWG IEPIDNVMGM IGILPDMTPS TEMSLRGVRV
     SKMGVDEYSS TEKVVVSIDR FLRVRDQRGN VLLSPEEVSE TQGTEKLTIT YSSSMMWEIN
     GPESVLVNTY QWIIRNWETV KIQWSQDPTM LYNKMEFEPF QSLVPKAVRG QYSGFVRTLF
     QQMRDVLGTF DTVQIIKLLP FAAAPPEQSR MQFSSLTVNV RGSGMRILIR GNSPVFNYNK
     TTKRLTVLGK DAGALTEDPD EGTAGVESAV LRGFLILGKE DKRYGPALSI SELSNLAKGE
     KANVLIGQGD VVLVMKRKRD SSILTDSQTA TKRIRMAIN