PB2_I72A2
ID PB2_I72A2 Reviewed; 759 AA.
AC Q67296; Q1K9E4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 105.
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/Udorn/307/1972 H3N2).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=381517;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9721; Cetacea (whales).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9709; Phocidae (true seals).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1413525; DOI=10.1016/0042-6822(92)90221-a;
RA Lawson C.M., Subbarao E.K., Murphy B.R.;
RT "Nucleotide sequence changes in the polymerase basic protein 2 gene of
RT temperature-sensitive mutants of influenza A virus.";
RL Virology 191:506-510(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Mbawuike I.N., Zhang Y., Yamada R.E., Nino D., Bui H.-H., Sette A.,
RA Couch R.B.;
RT "Complete genome sequencing and analysis of selected influenza virus
RT vaccine strains spanning six decades (1933-1999).";
RL Submitted (APR-2006) 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}.
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DR EMBL; M91712; AAA43594.1; -; Genomic_RNA.
DR EMBL; DQ508926; ABF21239.1; -; Genomic_RNA.
DR PDB; 5WL0; X-ray; 2.40 A; A=241-741.
DR PDBsum; 5WL0; -.
DR SMR; Q67296; -.
DR IntAct; Q67296; 25.
DR PRO; PR:Q67296; -.
DR Proteomes; UP000153055; 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-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: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: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 1: Evidence at protein level;
KW 3D-structure; 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_0000078839"
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 CONFLICT 44
FT /note="S -> L (in Ref. 1; AAA43594)"
FT CONFLICT 290
FT /note="G -> R (in Ref. 1; AAA43594)"
FT CONFLICT 526
FT /note="R -> K (in Ref. 1; AAA43594)"
FT HELIX 253..272
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 276..286
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 306..314
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 328..335
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 351..359
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 361..366
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 368..377
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 380..390
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 391..405
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 408..412
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 430..440
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 443..447
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 478..483
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 534..540
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 541..555
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 557..566
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 568..572
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 578..582
FT /evidence="ECO:0007829|PDB:5WL0"
FT TURN 586..588
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 589..605
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 612..618
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 619..622
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 634..640
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 643..651
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:5WL0"
FT TURN 660..663
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 664..667
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 670..674
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 686..691
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 694..699
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 702..704
FT /evidence="ECO:0007829|PDB:5WL0"
FT HELIX 710..712
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 721..725
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 727..729
FT /evidence="ECO:0007829|PDB:5WL0"
FT STRAND 731..736
FT /evidence="ECO:0007829|PDB:5WL0"
SQ SEQUENCE 759 AA; 86071 MW; E5EFE93E3BB07DF7 CRC64;
MERIKELRNL MSQSRTREIL TKTTVDHMAI IKKYTSGRQE KNPSLRMKWM MAMKYPITAD
KRITEMVPER NEQGQTLWSK MSDAGSDRVM VSPLAVTWWN RNGPVTSTVH YPKVYKTYFD
KVERLKHGTF GPVHFRNQVK IRRRVDINPG HADLSAKEAQ DVIMEVVFPN EVGARILTSE
SQLTITKEKK EELQDCKISP LMVAYMLERE LVRKTRFLPV AGGTSSVYIE VLHLTQGTCW
EQMYTPGGEV RNDDVDQSLI IAARNIVRRA AVSADPLASL LEMCHSTLIG GTRMVDILRQ
NPTEEQAVDI CKAAMGLRIS SSFSFGGFTF KRTSGSSIKR EEEVLTGNLQ TLKIRVHEGY
EEFTMVGKRA TAILRKATRR LVQLIVSGRD EQSIAEAIIV AMVFSQEDCM IKAVRGDLNF
VNRANQRLNP MHQLLRHFQK DAKVLFQNWG IEHIDNVMGM VGVLPDMTPS TEMSMRGIRV
SKMGVDEYSS TERVVVSIDR FLRVRDQRGN VLLSPEEVSE TQGTERLTIT YSSSMMWEIN
GPESVLVNTY QWIIRNWETV KIQWSQNPTM LYNKMEFEPF QSLVPKAIRG QYSGFVRTLF
QQMRDVLGTF DTTQIIKLLP FAAAPPKQSR MQFSSLTVNV RGSGMRILVR GNSPVFNYNK
TTKRLTILGK DAGTLIEDPD ESTSGVESAV LRGFLILGKE DRRYGPALSI NELSNLAKGE
KANVLIGQGD VVLVMKRKRD SSILTDSQTA TKRIRMAIN
