PB2_I75A3
ID PB2_I75A3 Reviewed; 759 AA.
AC P31345;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 116.
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/Victoria/3/1975 H3N2).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=392809;
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.
RX PubMed=2773594; DOI=10.1016/0168-1702(89)90012-9;
RA de la Luna S., Martinez C., Ortin J.;
RT "Molecular cloning and sequencing of influenza virus A/Victoria/3/75
RT polymerase genes: sequence evolution and prediction of possible functional
RT domains.";
RL Virus Res. 13:143-156(1989).
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 -!- INTERACTION:
CC P31345; P52294: KPNA1; Xeno; NbExp=3; IntAct=EBI-6051231, EBI-358383;
CC P31345; P52293: Kpna2; Xeno; NbExp=3; IntAct=EBI-6051231, EBI-3043908;
CC P31345; O00629: KPNA4; Xeno; NbExp=3; IntAct=EBI-6051231, EBI-396343;
CC P31345; O60684: KPNA6; Xeno; NbExp=3; IntAct=EBI-6051231, EBI-359923;
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 PIR; B60008; B60008.
DR PDB; 2GMO; NMR; -; A=678-759.
DR PDB; 2JDQ; X-ray; 2.20 A; D/E=678-759.
DR PDB; 2VQZ; X-ray; 2.30 A; A/B/D/E/F=318-483.
DR PDB; 2VY6; X-ray; 1.95 A; A=538-753.
DR PDB; 2VY7; X-ray; 1.53 A; A=538-693.
DR PDB; 2VY8; X-ray; 1.20 A; A=538-693.
DR PDB; 4NCE; X-ray; 2.30 A; A=318-483.
DR PDB; 4NCM; X-ray; 2.82 A; A=318-483.
DR PDB; 4P1U; X-ray; 2.52 A; A=318-483.
DR PDB; 4UAD; X-ray; 2.42 A; E=683-759.
DR PDB; 4UAE; X-ray; 2.70 A; F=678-759.
DR PDB; 4UAF; X-ray; 1.70 A; E=678-759.
DR PDB; 6EUV; X-ray; 2.70 A; A/C/F/I=247-536.
DR PDB; 6EUY; X-ray; 3.00 A; A/B/C=247-536.
DR PDBsum; 2GMO; -.
DR PDBsum; 2JDQ; -.
DR PDBsum; 2VQZ; -.
DR PDBsum; 2VY6; -.
DR PDBsum; 2VY7; -.
DR PDBsum; 2VY8; -.
DR PDBsum; 4NCE; -.
DR PDBsum; 4NCM; -.
DR PDBsum; 4P1U; -.
DR PDBsum; 4UAD; -.
DR PDBsum; 4UAE; -.
DR PDBsum; 4UAF; -.
DR PDBsum; 6EUV; -.
DR PDBsum; 6EUY; -.
DR SMR; P31345; -.
DR DIP; DIP-29297N; -.
DR IntAct; P31345; 7.
DR EvolutionaryTrace; P31345; -.
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_0000078840"
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 253..270
FT /evidence="ECO:0007829|PDB:6EUV"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6EUV"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:6EUV"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:6EUV"
FT HELIX 306..314
FT /evidence="ECO:0007829|PDB:6EUV"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6EUV"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:2VQZ"
FT STRAND 328..335
FT /evidence="ECO:0007829|PDB:2VQZ"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:2VQZ"
FT STRAND 351..359
FT /evidence="ECO:0007829|PDB:2VQZ"
FT STRAND 361..366
FT /evidence="ECO:0007829|PDB:2VQZ"
FT STRAND 368..377
FT /evidence="ECO:0007829|PDB:2VQZ"
FT STRAND 380..390
FT /evidence="ECO:0007829|PDB:2VQZ"
FT HELIX 391..404
FT /evidence="ECO:0007829|PDB:2VQZ"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:2VQZ"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:4NCE"
FT HELIX 430..440
FT /evidence="ECO:0007829|PDB:2VQZ"
FT HELIX 443..448
FT /evidence="ECO:0007829|PDB:2VQZ"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:2VQZ"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:2VQZ"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:2VQZ"
FT STRAND 478..481
FT /evidence="ECO:0007829|PDB:2VQZ"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:6EUV"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:6EUV"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:6EUV"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:6EUY"
FT HELIX 541..555
FT /evidence="ECO:0007829|PDB:2VY8"
FT HELIX 557..566
FT /evidence="ECO:0007829|PDB:2VY8"
FT HELIX 568..572
FT /evidence="ECO:0007829|PDB:2VY8"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:2VY8"
FT HELIX 578..583
FT /evidence="ECO:0007829|PDB:2VY8"
FT TURN 586..588
FT /evidence="ECO:0007829|PDB:2VY8"
FT HELIX 589..607
FT /evidence="ECO:0007829|PDB:2VY8"
FT HELIX 612..618
FT /evidence="ECO:0007829|PDB:2VY8"
FT HELIX 619..622
FT /evidence="ECO:0007829|PDB:2VY8"
FT STRAND 634..638
FT /evidence="ECO:0007829|PDB:2VY8"
FT STRAND 645..651
FT /evidence="ECO:0007829|PDB:2VY8"
FT STRAND 654..659
FT /evidence="ECO:0007829|PDB:2VY8"
FT TURN 660..663
FT /evidence="ECO:0007829|PDB:2VY8"
FT STRAND 664..667
FT /evidence="ECO:0007829|PDB:2VY8"
FT STRAND 670..674
FT /evidence="ECO:0007829|PDB:2VY8"
FT HELIX 688..691
FT /evidence="ECO:0007829|PDB:4UAF"
FT STRAND 694..699
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 702..704
FT /evidence="ECO:0007829|PDB:4UAF"
FT HELIX 710..713
FT /evidence="ECO:0007829|PDB:4UAF"
FT STRAND 721..726
FT /evidence="ECO:0007829|PDB:4UAF"
FT TURN 727..729
FT /evidence="ECO:0007829|PDB:4UAF"
FT STRAND 730..738
FT /evidence="ECO:0007829|PDB:4UAF"
FT TURN 745..747
FT /evidence="ECO:0007829|PDB:4UAF"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:2GMO"
SQ SEQUENCE 759 AA; 86125 MW; 22DD5C3A573DA870 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 RNDDIDQSLI IAARNIVRRA SVSADPLASL LEMCHSTQIG GTRMVDILRQ
NPTEEQAVDI CKAAMGLRIS SSFSFGGFTF KRTSGSSIKR EEEVLTGNLQ TLKIRVHEGY
EEFTMVGKRA TAILRKATRR LVQLIVSGRD EQSIAEAIIV AMVFSQEDCM IKAVRGDLNF
VNRANQRLNP MHQLLRHFQK DAKVLFQNWG IEHIDNVMGM VGVLPDMTPS TEMSMRGIRV
SKMGVDEYSS TERVVVSIDR FLRVRDQRGN VLLSPEEVSE THGTERLTIT YSSSMMWEIN
GPESVLVNTY QWIIRNWETV KIQWSQNPTM LYNKMEFEPF QSLVPKAIRG QYSGFVRTLF
QQMRDVLGTF DTTQIIKLLP FAAAPPKQSR MQFSSLTVNV RGSGMRILVR GNSPVFNYNK
TTKRLTILGK DAGTLIEDPD ESTSGVESAV LRGFLILGKE DRRYGPALSI NELSNLAKGE
KANVLIGQGD VVLVMKRKRD SSILTDSQTA TKRIRMAIN
