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PB2_I02A6
ID   PB2_I02A6               Reviewed;         759 AA.
AC   Q6DNL8;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 81.
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/Chicken/Hong Kong/YU22/2002 H5N1 genotype Z).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=284177;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9691; Panthera pardus (Leopard) (Felis pardus).
OH   NCBI_TaxID=9694; Panthera tigris (Tiger).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15241415; DOI=10.1038/nature02746;
RA   Li K.S., Guan Y., Wang J., Smith G.J.D., Xu K.M., Duan L., Rahardjo A.P.,
RA   Puthavathana P., Buranathai C., Nguyen T.D., Estoepangestie A.T.S.,
RA   Chaisingh A., Auewarakul P., Long H.T., Hanh N.T.H., Webby R.J.,
RA   Poon L.L.M., Chen H., Shortridge K.F., Yuen K.Y., Webster R.G.,
RA   Peiris J.S.M.;
RT   "Genesis of a highly pathogenic and potentially pandemic H5N1 influenza
RT   virus in eastern Asia.";
RL   Nature 430:209-213(2004).
RN   [2]
RP   SEQUENCE REVISION.
RA   Li K.S., Guan Y., Wang J., Smith G.J.D., Xu K.M., Duan L., Rahardjo A.P.,
RA   Puthavathana P., Buranathai C., Nguyen T.D., Estoepangestie A.T.S.,
RA   Chaisingh A., Auewarakul P., Long H.T., Hanh N.T.H., Lim W., Webby R.J.,
RA   Poon L.L.M., Chen H., Shortridge K.F., Yuen K.Y., Webster R.G.,
RA   Peiris J.S.M.;
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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.
CC       {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). {ECO:0000255|HAMAP-
CC       Rule:MF_04062}.
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}.
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DR   EMBL; AY651734; AAT73565.2; -; Genomic_RNA.
DR   PDB; 5EG9; X-ray; 2.30 A; A/B=318-420, A/B=428-483.
DR   PDBsum; 5EG9; -.
DR   SMR; Q6DNL8; -.
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; Viral transcription; Virion.
FT   CHAIN           1..759
FT                   /note="Polymerase basic protein 2"
FT                   /id="PRO_0000311153"
FT   MOTIF           736..739
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04062"
FT   SITE            627
FT                   /note="Avian adaptation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04062"
FT   STRAND          323..325
FT                   /evidence="ECO:0007829|PDB:5EG9"
FT   STRAND          328..335
FT                   /evidence="ECO:0007829|PDB:5EG9"
FT   STRAND          338..345
FT                   /evidence="ECO:0007829|PDB:5EG9"
FT   STRAND          351..359
FT                   /evidence="ECO:0007829|PDB:5EG9"
FT   STRAND          361..366
FT                   /evidence="ECO:0007829|PDB:5EG9"
FT   STRAND          368..377
FT                   /evidence="ECO:0007829|PDB:5EG9"
FT   STRAND          380..390
FT                   /evidence="ECO:0007829|PDB:5EG9"
FT   HELIX           391..405
FT                   /evidence="ECO:0007829|PDB:5EG9"
FT   HELIX           408..411
FT                   /evidence="ECO:0007829|PDB:5EG9"
FT   HELIX           430..440
FT                   /evidence="ECO:0007829|PDB:5EG9"
FT   HELIX           443..449
FT                   /evidence="ECO:0007829|PDB:5EG9"
FT   STRAND          451..453
FT                   /evidence="ECO:0007829|PDB:5EG9"
FT   STRAND          461..463
FT                   /evidence="ECO:0007829|PDB:5EG9"
FT   STRAND          469..475
FT                   /evidence="ECO:0007829|PDB:5EG9"
FT   STRAND          478..480
FT                   /evidence="ECO:0007829|PDB:5EG9"
SQ   SEQUENCE   759 AA;  85832 MW;  918725B103736E24 CRC64;
     MERIKELRDL MSQSRTREIL TKTTVDHMAI IKKYTSGRQE KNPALRMKWM MAMKYPITAD
     KRIIEMIPER NEQGQTLWSK TNDAGSDRVM VSPLAVTWWN RNGPTTSAVH YPKVYKTYFE
     KVERLKHGTF GPVHFRNQVK IRRRVDINPG HADLSAKEAQ DVIMEVVFPN EVGARILTSE
     SQLTITKEKK EELQDCKIAP LMVAYMLERE LVRKTRFLPV AGGTSSVYIE VLHLTQGTCW
     EQMYTPGGEV RNDDVDQSLI IAARNIVRRA TVSADPLASL LEMCHSTQIG GIRMVDILRQ
     NPTEEQAVDI CKAAMGLRIS SSFSFGGFTF KRTSGSSVKK EEEVLTGNLQ TLKIRVHEGY
     EEFTMVGRRA TAILRKATRR LIQLIVSGRD EQSIAEAIIV AMVFSQEDCM IKAVRGDLNF
     VNRANQRLNP MHQLLRHFQK DAKVLFQNWG IEPIDNVMGM IGILPDMTPS TEMSLRGVRV
     SKMGVDEYSS TERVVVSIDR FLRVRDQRGN VLLSPEEVSE TQGTEKLTIT YSSSMMWEIN
     GPESVLVNTY QWIIRNWETV KIQWSQDPTM LYNKMEFEPF QSLVPKAARG QYSGFVRTLF
     QQMRDVLGTF DTVQIIKLLP FAAAPPEQSR MQFSSLTVNV RGSGMRILVR GNSPVFNYNK
     ATKRLTVLGK DAGALTEDPD EGTAGVESAV LRGFLILGKE DKRYGPALSI NELSNLAKGE
     KANVLIGQGD VVLVMKRKRD SSILTDSQTA TKRIRMAIN
 
 
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