ID   PB2_I56A3               Reviewed;         759 AA.
AC   P26107;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 94.
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/Equine/Prague/1/1956 H7N7).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=380337;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9796; Equus caballus (Horse).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9709; Phocidae (true seals).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2398532; DOI=10.1128/jvi.64.10.4893-4902.1990;
RA   Gorman O.T., Donis R.O., Kawaoka Y., Webster R.G.;
RT   "Evolution of influenza A virus PB2 genes: implications for evolution of
RT   the ribonucleoprotein complex and origin of human influenza A virus.";
RL   J. Virol. 64:4893-4902(1990).
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; M73519; AAA43140.1; -; Genomic_RNA.
DR   SMR; P26107; -.
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_0000078824"
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;  85836 MW;  F6BF456BF02923F4 CRC64;
     MERIKELRDL MSQSRTREIL TTTTVDHMAI IKRYTSGRQE KNPALRMKWM MAMKYPITAD
     KRIMEMIPER NEQGQTLWSK TNDAGSDRIM VSPLAVTWWN RNGPTAVTTH YPKVYKTYFE
     KVERLKNGTF GPVHFRNQIK IRRRVDTNPG HADLSAKEAQ DVIMEVVFPN EVGAQLLTSE
     SQLKITQEKK EELQDCKIAP LMVAYMLERE LVRKTRFLPV AGGTSSVYIE VLHLTQGTCW
     EQMYAPGGEV RNDDIDQSLI IAARNIVRRA TVSTDPLASL LEMCHSTQIG GIRMVDILKQ
     NPTEEQAVDI CKAAMGLKIS SSFSFGGFTF KRTSGTSVRR EEEILTGNLQ TLKIQIHEGY
     EEFTIVGKRA TAILRKATQR LVQLIISGKD EQSIAEAIIV AMVFSQEDCM IKAVRGDLNF
     MNRANQRLNP MHQLLRHFQK DAKILFQNWG IEPIDNIMGM TGILPDMTPS TEMSLRGIRI
     SKTGVDEYSS TERIVVSIDR FLRVRDQRGN VLLSPEEVSE TQGTEKLTIT YSSSMMWEIN
     GPESILVNTY QWIIKNWETV KIQWSQDPTI LYNKIEFEPF QSLIPKAARA QYSGFVRTLF
     QQMRDVLGTF DTVQIIKLLP FAAAPPEQSR IQFSSLTVNV RGSGMRILIR GNSPVFNYNK
     TTKRLTVLGK DAGALMNDPD EGTTGIESAV LRGFLILGKE NKRYGPALSI SELGNLAKGE
     KANVLIGQGD VVLVMKRKRD SSILTDSQTA TKRIRMATN