PB2_INBLE
ID PB2_INBLE Reviewed; 770 AA.
AC Q9QLL6;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 B virus (strain B/Lee/1940).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Betainfluenzavirus.
OX NCBI_TaxID=518987;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10725418; DOI=10.1099/0022-1317-81-4-929;
RA Hiromoto Y., Saito T., Lindstrom S.E., Li Y., Nerome R., Sugita S.,
RA Shinjoh M., Nerome K.;
RT "Phylogenetic analysis of the three polymerase genes (PB1, PB2 and PA) of
RT influenza B virus.";
RL J. Gen. Virol. 81:929-937(2000).
RN [2]
RP FUNCTION, AND INTERACTION WITH HOST ANP32A AND ANP32B.
RC STRAIN=B/Yamagata/PJ/2018;
RX PubMed=33045004; DOI=10.1371/journal.ppat.1008989;
RA Zhang Z., Zhang H., Xu L., Guo X., Wang W., Ji Y., Lin C., Wang Y.,
RA Wang X.;
RT "Selective usage of ANP32 proteins by influenza B virus polymerase:
RT Implications in determination of host range.";
RL PLoS Pathog. 16:e1008989-e1008989(2020).
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 a wide
CC range of cap structures of target pre-RNAs which are subsequently
CC cleaved after 10-13 nucleotides by the viral protein PA. Plays a role
CC in the initiation of the viral genome replication and modulates the
CC activity of the ribonucleoprotein (RNP) complex. {ECO:0000255|HAMAP-
CC Rule:MF_04062, ECO:0000269|PubMed:33045004}.
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 with host
CC ANP32A (via C-terminus) and ANP32B; these interactions promote viral
CC RNA synthesis (PubMed:33045004). {ECO:0000255|HAMAP-Rule:MF_04062,
CC ECO:0000269|PubMed:33045004}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF101982; AAF06851.1; -; Genomic_RNA.
DR RefSeq; NP_056658.1; NC_002205.1.
DR PDB; 5EF9; X-ray; 1.70 A; A=320-485.
DR PDB; 5EFA; X-ray; 1.90 A; A=320-485.
DR PDB; 5EFC; X-ray; 1.90 A; A=320-485.
DR PDB; 6XQA; X-ray; 2.16 A; C/F=550-558.
DR PDBsum; 5EF9; -.
DR PDBsum; 5EFA; -.
DR PDBsum; 5EFC; -.
DR PDBsum; 6XQA; -.
DR SMR; Q9QLL6; -.
DR PRIDE; Q9QLL6; -.
DR GeneID; 956546; -.
DR KEGG; vg:956546; -.
DR Proteomes; UP000008158; Genome.
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 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 nucleus;
KW Host-virus interaction; Inhibition of host RNA polymerase II by virus;
KW mRNA capping; mRNA processing; Reference proteome; Viral transcription;
KW Virion.
FT CHAIN 1..770
FT /note="Polymerase basic protein 2"
FT /id="PRO_0000391500"
FT MOTIF 740..743
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04062"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:5EF9"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:5EF9"
FT STRAND 340..347
FT /evidence="ECO:0007829|PDB:5EF9"
FT STRAND 353..361
FT /evidence="ECO:0007829|PDB:5EF9"
FT STRAND 363..369
FT /evidence="ECO:0007829|PDB:5EF9"
FT STRAND 372..379
FT /evidence="ECO:0007829|PDB:5EF9"
FT STRAND 382..389
FT /evidence="ECO:0007829|PDB:5EF9"
FT HELIX 393..406
FT /evidence="ECO:0007829|PDB:5EF9"
FT HELIX 410..414
FT /evidence="ECO:0007829|PDB:5EF9"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:5EFC"
FT HELIX 432..441
FT /evidence="ECO:0007829|PDB:5EF9"
FT HELIX 444..451
FT /evidence="ECO:0007829|PDB:5EF9"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:5EF9"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:5EF9"
FT STRAND 471..476
FT /evidence="ECO:0007829|PDB:5EF9"
FT STRAND 479..482
FT /evidence="ECO:0007829|PDB:5EF9"
SQ SEQUENCE 770 AA; 88025 MW; F399A58CCD924CD7 CRC64;
MTLAKIELLK QLLRDNEAKT VLRQTTVDQY NIIRKFNTSR IEKNPSLRMK WAMCSNFPLA
LTKGDMANRI PLEYKGIQLK TNAEDIGTKG QMCSIAAVTW WNTYGPIGDT EGFEKVYESF
FLRKMRLDNA TWGRITFGPV ERVRKRVLLN PLTKEMPPDE ASNVIMEILF PKEAGIPRES
TWIHRELIKE KREKLKGTMI TPIVLAYMLE RELVARRRFL PVAGATSAEF IEMLHCLQGE
NWRQIYHPGG NKLTESRSQS MIVACRKIIR RSIVASNPLE LAVEIANKTV IDTEPLKSCL
AALDGGDVAC DIIRAALGLK IRQRQRFGRL ELKRISGRGF KNDEEILIGN GTIQKIGIWD
GEEEFHVRCG ECRGILKKSQ MRMEKLLINS AKKEDMKDLI ILCMVFSQDT RMFQGVRGEI
NFLNRAGQLL SPMYQLQRYF LNRSNDLFDQ WGYEESPKAS ELHGINELMN ASDYTLKGVV
VTKNVIDDFS STETEKVSIT KNLSLIKRTG EVIMGANDVS ELESQAQLMI TYDTPKMWEM
GTTKELVQNT YQWVLKNLVT LKAQFLLGKE DMFQWDAFEA FESIIPQKMA GQYSGFARAV
LKQMRDQEVM KTDQFIKLLP FCFSPPKLRS NGEPYQFLRL MLKGGGENFI EVRKGSPLFS
YNPQTEILTI CGRMMSLKGK IEDEERNRSM GNAVLAGFLV SGKYDPDLGD FKTIEELERL
KPGEKANILL YQGKPVKVVK RKRYSALSND ISQGIKRQRM TVESMGWALS
