PB2_I68A6
ID PB2_I68A6 Reviewed; 759 AA.
AC P03429;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 108.
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/Northern Territory/60/1968 H3N2) (Influenza A
OS virus (strain NT60)) (Influenza A virus (strain A/NT/60/1968 H3N2)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=384505;
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=6828387; DOI=10.1093/nar/11.5.1555;
RA Jones K.L., Huddleston J.A., Brownlee G.G.;
RT "The sequence of RNA segment 1 of influenza virus A/NT/60/68 and its
RT comparison with the corresponding segment of strains A/PR/8/34 and
RT A/WSN/33.";
RL Nucleic Acids Res. 11:1555-1566(1983).
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; J02140; AAA43613.1; -; Genomic_RNA.
DR PIR; A93458; P3IV68.
DR PDB; 6QNW; X-ray; 3.31 A; C/F/I/L=1-759.
DR PDB; 6QPG; X-ray; 3.34 A; C/F/I/L=1-759.
DR PDB; 6QX3; EM; 3.79 A; C=1-756.
DR PDB; 6QX8; EM; 4.07 A; C/G=1-759.
DR PDB; 6QXE; EM; 4.15 A; C/G=1-759.
DR PDB; 6RR7; EM; 3.01 A; C=1-759.
DR PDBsum; 6QNW; -.
DR PDBsum; 6QPG; -.
DR PDBsum; 6QX3; -.
DR PDBsum; 6QX8; -.
DR PDBsum; 6QXE; -.
DR PDBsum; 6RR7; -.
DR SMR; P03429; -.
DR IntAct; P03429; 3.
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_0000078833"
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:6RR7"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6QNW"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 61..65
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:6QNW"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 180..192
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 252..272
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 306..314
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 391..405
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 430..437
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 443..447
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:6QNW"
FT STRAND 458..463
FT /evidence="ECO:0007829|PDB:6QNW"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 471..478
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:6QPG"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 536..539
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 542..555
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 557..563
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 569..572
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:6QNW"
FT HELIX 578..581
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:6QNW"
FT HELIX 589..605
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 612..618
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 619..621
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 634..640
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 643..651
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 654..658
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 660..662
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 664..667
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 670..674
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 688..699
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 702..704
FT /evidence="ECO:0007829|PDB:6QNW"
FT HELIX 710..712
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 713..715
FT /evidence="ECO:0007829|PDB:6QPG"
FT TURN 717..719
FT /evidence="ECO:0007829|PDB:6QNW"
FT STRAND 722..726
FT /evidence="ECO:0007829|PDB:6RR7"
FT TURN 727..729
FT /evidence="ECO:0007829|PDB:6RR7"
FT STRAND 730..736
FT /evidence="ECO:0007829|PDB:6RR7"
FT HELIX 746..749
FT /evidence="ECO:0007829|PDB:6QNW"
FT HELIX 750..752
FT /evidence="ECO:0007829|PDB:6QNW"
FT TURN 753..755
FT /evidence="ECO:0007829|PDB:6QNW"
SQ SEQUENCE 759 AA; 86046 MW; FD736AA1B3DDCFC9 CRC64;
MERIKELRNL MSQSRTREIL TKTTVDHMAI IKKYTSGRQE KNPSLRMKWM MAMKYPITAD
KRITEMVPER NEQGQTLWSK MSDAGSDRVM VSPLAVTWWN RNGPMTSTVH YPKVYKTYFE
KVERLKHGTF GPVHFRNQVK IRRRVDINPG HADLSAKEAQ DVIMEVVFPN EVGARILTSE
SQLTITKEKK EELQDCKISP LMVAYMLERE LVRKTRFLPV AGGTSSVYIE VLHLTQGTCW
EQMYTPGGEV RNDDVDQSLI IAARNIVRRA AVSADPLASL LEMCHSTQIG GTRMVDILRQ
NPTEEQAVDI CKAAMGLRIS SSFSFGGFTF KRTSGSSIKR EEELLTGNLQ TLKIRVHDGY
EEFTMVGKRA TAILRKATRR LVQLIVSGRD EQSVAEAIIV AMVFSQEDCM IKAVRGDLNF
VNRANQRLNP MHQLLRHFQK DAKVLFQNWG IEHIDNVMGM IGVLPDMTPS TEMSMRGIRV
SKMGVDEYSS TERVVVSIDR FLRVRDQRGN VLLSPEEVSE TQGTEKLTIT YSSSMMWEIN
GPESVLVNTY QWIIRNWETV KIQWSQNPTM LYNKMEFEPF QSLVPKAIRG QYSGFVRTLF
QQMRDVLGTF DTTQIIKLLP FAAAPPKQSR MQFSSLTVNV RGSGMRILVR GNSPAFNYNK
TTKRLTILGK DAGTLIEDPD EGTSGVESAV LRGFLILGKE DRRYGPALSI NELSNLAKGE
KANVLIGQGD VVLVMKRKRD SSILTDSQTA TKRIRMAIN
