PB2_THOGV
ID PB2_THOGV Reviewed; 769 AA.
AC Q9YNA4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 29-SEP-2021, entry version 75.
DE RecName: Full=Polymerase basic protein 2;
DE Short=PB2;
DE AltName: Full=RNA-directed RNA polymerase subunit P3;
GN OrderedLocusNames=Segment 1;
OS Thogoto virus (isolate SiAr 126) (Tho).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Thogotovirus.
OX NCBI_TaxID=126796;
OH NCBI_TaxID=34610; Amblyomma variegatum (Tropical bont tick).
OH NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
OH NCBI_TaxID=210652; Mungos mungo (Banded mongoose).
OH NCBI_TaxID=34631; Rhipicephalus appendiculatus (Brown ear tick).
OH NCBI_TaxID=6941; Rhipicephalus microplus (Cattle tick) (Boophilus microplus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10486113; DOI=10.1007/s007050050613;
RA Weber F., Gruber S., Haller O., Kochs G.;
RT "PB2 polymerase subunit of Thogoto virus (Orthomyxoviridae family).";
RL Arch. Virol. 144:1601-1609(1999).
CC -!- FUNCTION: subunit of the RNA-dependent RNA polymerase which is
CC responsible for replication and transcription of virus RNA segments.
CC The transcription of viral mRNAs occurs by a unique mechanism called
CC cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after
CC 10-13 nucleotides by PA. In turn, these short capped RNAs are used as
CC primers by PB1 for transcription of viral mRNAs. During virus
CC replication, PB1 initiates RNA synthesis and copy vRNA into
CC complementary RNA (cRNA) which in turn serves as a template for the
CC production of more vRNAs. {ECO:0000250|UniProtKB:P03428}.
CC -!- SUBUNIT: RNA polymerase is composed of three subunits: PA, PB1 and PB2.
CC {ECO:0000250|UniProtKB:P03431}.
CC -!- SUBCELLULAR LOCATION: Virion. Host nucleus
CC {ECO:0000303|PubMed:10486113}.
CC -!- SIMILARITY: Belongs to the influenza viruses PB2 family. {ECO:0000305}.
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DR EMBL; Y17873; CAA76908.1; -; Genomic_RNA.
DR RefSeq; YP_145810.1; NC_006508.1.
DR PDB; 4CHD; X-ray; 2.40 A; A=543-701.
DR PDB; 4CHE; X-ray; 1.80 A; A=323-486.
DR PDB; 4CHF; X-ray; 3.00 A; A/B=323-486.
DR PDBsum; 4CHD; -.
DR PDBsum; 4CHE; -.
DR PDBsum; 4CHF; -.
DR SMR; Q9YNA4; -.
DR GeneID; 5075739; -.
DR KEGG; vg:5075739; -.
DR Proteomes; UP000008973; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
DR GO; GO:0075526; P:cap snatching; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR InterPro; IPR001591; INV_PB2.
DR Pfam; PF00604; Flu_PB2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cap snatching; Host nucleus; mRNA capping; mRNA processing;
KW Reference proteome; Virion.
FT CHAIN 1..769
FT /note="Polymerase basic protein 2"
FT /id="PRO_0000078849"
FT MOTIF 753..756
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:4CHE"
FT STRAND 333..342
FT /evidence="ECO:0007829|PDB:4CHE"
FT STRAND 345..354
FT /evidence="ECO:0007829|PDB:4CHE"
FT STRAND 357..365
FT /evidence="ECO:0007829|PDB:4CHE"
FT STRAND 367..376
FT /evidence="ECO:0007829|PDB:4CHE"
FT STRAND 379..386
FT /evidence="ECO:0007829|PDB:4CHE"
FT STRAND 389..396
FT /evidence="ECO:0007829|PDB:4CHE"
FT HELIX 404..414
FT /evidence="ECO:0007829|PDB:4CHE"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:4CHE"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:4CHE"
FT HELIX 432..445
FT /evidence="ECO:0007829|PDB:4CHE"
FT HELIX 448..454
FT /evidence="ECO:0007829|PDB:4CHE"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:4CHE"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:4CHE"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:4CHE"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:4CHE"
FT HELIX 548..560
FT /evidence="ECO:0007829|PDB:4CHD"
FT HELIX 563..575
FT /evidence="ECO:0007829|PDB:4CHD"
FT HELIX 582..588
FT /evidence="ECO:0007829|PDB:4CHD"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:4CHD"
FT HELIX 595..608
FT /evidence="ECO:0007829|PDB:4CHD"
FT HELIX 612..614
FT /evidence="ECO:0007829|PDB:4CHD"
FT HELIX 616..629
FT /evidence="ECO:0007829|PDB:4CHD"
FT STRAND 644..647
FT /evidence="ECO:0007829|PDB:4CHD"
FT STRAND 654..656
FT /evidence="ECO:0007829|PDB:4CHD"
FT STRAND 660..667
FT /evidence="ECO:0007829|PDB:4CHD"
FT STRAND 670..673
FT /evidence="ECO:0007829|PDB:4CHD"
FT STRAND 676..680
FT /evidence="ECO:0007829|PDB:4CHD"
SQ SEQUENCE 769 AA; 88043 MW; 5301B3829ADE9595 CRC64;
MDREEPAESE CTLRALVEEY NGACKEAPKE MSKQFTDYNT FKRYTTSKKD HAPQMRLVYS
VRKPWPISMT PSKEIPLVFN GTKLKDTILD LGESKRTRAN IVVPDYWSKY GSQTSLEVVN
AILYAEDLKV QRFFSTEWGE IRYGRMLPFR KPVQACPTIE EVNPASIPHT LLQVFCPQYT
TLDSKRKAHM GAVEKLKRVM EPICKVQTQE SAVHIARSLI DSNKKWLPTV VDHTPRTAEM
AHFLCSKYHY VHTNTQDLSD TRSIDNLCGE LVKRSLKCRC PKETLVANLD KITIQGRPMR
EVLADHDGEL PYLGICRVAM GLSTHHTMKI RSTKFSILNS DHPRIEVKKV FSLSPDVQVT
IPYRRFKGKA KVYFQNDQIQ GYFSCTDRQI DEIKISAPKN APLLEPLLDI CYYGSFIEPG
FEQTFGFYPA GKREFVDSFF MHHSKDHKAF LIHMGLDKDL SLPLSPELNW KEPALSKVCR
VTELDSTVQP YTSATREFVL GETLNVYTQH ENGLELLICP TEIRSTRGPL PPGTNLSGSE
FIDIYQDPFS RAKSLLKSTI LHAERCKEFV GNMLEEYQDP AETTVQSLVP INTWGKSAKR
KLQEEITSDP DWHQCPRKRA KMSYLAIIAG SIQDRDKKQT NVPRAFMLRG SQIEYDMKAT
RGLVVDTTNR IIVGGETVLR EGKGGPEGYV QTGVFEEQPR CYLVDTPDHG LSMGLSRFCV
HSQGRYFQYE KKISIWEETD NIKATIDSQR DLKRRRDIEE MVSKRARIV
