PB2_I18A0
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 03-AUG-2022, entry version 71.
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.
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}.
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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-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; 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
